RU2813924C2 - Neoantigens and their use - Google Patents

Abstract

FIELD: biotechnology.

SUBSTANCE: invention relates to a method of obtaining a population of immunoreactive T-cells containing a T-cell receptor (TCR) specific for the peptide:MHC complex, where the peptide of the peptide:MHC complex is a mutant GATA3 peptide sequence. The method involves bringing a population of immune cells into contact with a polynucleotide containing a sequence encoding a polypeptide containing the said mutant GATA3 peptide sequence, or a polypeptide containing the said mutant GATA3 peptide sequence. The immune cell population is a population of immune cells lacking cells expressing CD14 and CD25, and wherein the immune cell population includes a population of FMS-like receptor tyrosine kinase ligand 3 (FLT3L) stimulated antigen presenting cells (APCs) and a population of T-cells.

EFFECT: invention is effective for obtaining a population of immunoreactive T-cells for cancer immunotherapy.

9 cl, 54 dwg, 44 tbl, 41 ex

Description

CROSS REFERENCE

This application claims priority to provisional US Application No. 62/687,191, filed June 19, 2018, US Provisional Application No. 62/702,567, filed July 24, 2018, US Provisional Application No. 62/726,804, filed September 4, 2018, US Provisional Application No. 62/ 789,162, filed January 7, 2019, US Provisional Application No. 62/801,981, filed February 6, 2019, US Provisional Application No. 62/800,700, filed February 4, 2019, and US Provisional Application No. 62/800,792, filed February 4, 2019, each is incorporated herein by reference in its entirety.

BACKGROUND OF THE ART

Cancer immunotherapy is the use of the immune system to treat cancer. Immunotherapy takes advantage of the fact that cancer cells often have molecules on their surface that can be detected by the immune system, known as tumor antigens, which are often proteins or other macromolecules (such as carbohydrates). Active immunotherapy directs the immune system to attack tumor cells by targeting tumor antigens. Passive immunotherapy enhances existing antitumor responses and includes the use of monoclonal antibodies, lymphocytes and cytokines. Tumor vaccines typically consist of tumor antigens and immunostimulatory molecules (eg, adjuvants, cytokines, or TLR ligands) that work together to induce antigen-specific cytotoxic T cells (CTLs) that recognize and lyse tumor cells. One of the critical barriers to the development of curative and tumor-specific immunotherapies is the identification and selection of highly specific and limited tumor antigens to avoid autoimmunity.

Tumor neoantigens, which arise from genetic changes (eg, inversions, translocations, deletions, missense mutations, splice site mutations, etc.) in malignant cells, represent the most tumor-specific class of antigens and can be patient-specific or cross-reactive. Tumor neoantigens are unique to the tumor cell because the mutation and its corresponding protein are present only in the tumor. They also avoid central tolerance and are therefore more likely to be immunogenic. Thus, tumor neoantigens are excellent targets for immune recognition, including through both humoral and cellular immunity. However, tumor neoantigens are rarely used in cancer vaccines or immunogenic compositions due to technical difficulties in identifying them, selecting optimized antigens, and producing neoantigens for use in the vaccine or immunogenic composition. Accordingly, there is still a need to develop additional anticancer therapeutic agents.

INCLUSION AS LINKS

All publications, patents and patent applications mentioned in this specification are incorporated herein by reference to the same extent as if each individual publication, patent or patent application had been specifically and individually indicated to be incorporated by reference.

SUMMARY OF THE INVENTION

In one aspect, the invention provides a pharmaceutical composition comprising (a) at least one polypeptide or a pharmaceutically acceptable salt thereof comprising a first mutant GATA3 peptide sequence and a second mutant GATA3 peptide sequence, wherein (i) each of the first mutant GATA3 peptide sequence and a second the GATA3 mutant peptide sequence contains at least 8 contiguous amino acids of SEQ ID NO: 1, and (ii) the C-terminal sequence of the first GATA3 mutant peptide sequence overlapping with the N-terminal sequence of the second GATA3 mutant peptide sequence; wherein at least 8 continuous amino acids of SEQ ID NO: 1 contain at least one amino acid with the sequence: PGRPLQTHVLPEPHLALQPLQPHADHAHADAPAIQPVLWTTPPLQHGHRHGLEPCSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFAT LQRSSLWCLCSNH (SEQ ID NO: 2), or (b) at least one polynucleotide containing a sequence encoding at least one polypeptide .

In some embodiments, the first mutant GATA3 peptide sequence or the second mutant GATA3 peptide sequence contains at least 8 contiguous amino acids of SEQ ID NO: 2. In some embodiments, the first mutant GATA3 peptide sequence and the second mutant peptide sequence contain at least 8 contiguous amino acids amino acids SEQ ID NO: 2.

In some embodiments, the at least 8 contiguous amino acid sequences of SEQ ID NO: 2 comprise at least 8 contiguous amino acid sequences: PGRPLQTHVLPEPHLALQPLQPHADHAHADAPAIQPVLWTTPPLQHGHRHGL (SEQ ID NO: 3).

In some embodiments, the at least 8 contiguous amino acids of SEQ ID NO: 2 contain at least one amino acid of the sequence: EPCSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 4).

In some embodiments, at least one of the first GATA3 mutant peptide sequence and the second GATA3 mutant peptide sequence contains at least 14 mutant amino acids. In some embodiments, the at least one polypeptide contains at least 3 mutant GATA3 peptide sequences. In some embodiments, the at least one polypeptide comprises at least two polypeptides. In some embodiments, the at least one polypeptide further comprises a third mutant GATA3 peptide sequence, wherein the third mutant GATA3 peptide sequence comprises at least 8 contiguous amino acids of SEQ ID NO: 1, wherein at least 8 contiguous amino acids of SEQ ID NO: 1 comprise at least one amino acid of SEQ ID NO: 2. In some embodiments, the third GATA3 mutant peptide contains at least 8 contiguous amino acids of SEQ ID NO: 2.

In some embodiments, the at least one polypeptide contains at least one mutant GATA3 peptide sequence that binds or is predicted to bind to a protein encoded by the HLA-A02:01 allele, the HLA-A24:02 allele, the HLA-A03:01 allele, HLA-B07:02 allele and/or HLA-B08:01 allele. In some embodiments, the at least one polypeptide comprises at least one mutant GATA3 peptide sequence that binds or is predicted to bind to a protein encoded by: (a) the HLA-A02:01 allele and the HLA-A24:02 allele, (b ) HLA-A02:01 allele and HLA-B08:01 allele, (c) HLA-A24:02 allele and HLA-B08:01 allele, or (d) HLA-A02:01 allele, HLA-A24:02 allele and HLA-B08:01 allele. In some embodiments, (a) the first mutant GATA3 peptide sequence binds to or is predicted to bind to a protein encoded by the HLA-A02:01 allele, HLA-A24:02 allele, HLA-A03:01 allele, HLA-B07:02 allele, or HLA-B08:01 allele; and (b) the second GATA3 peptide sequence binds to or is predicted to bind to a protein encoded by the HLA-A02:01 allele, HLA-A24:02 allele, HLA-A03:01 allele, HLA-B07:02 allele, or HLA-B08:01 allele; wherein the first mutant GATA3 peptide sequence binds or is predicted to bind to a protein encoded by an HLA allele different from that of the second mutant GATA3 peptide sequence.

In some embodiments, at least one of the first mutant GATA3 peptide sequence and the second mutant GATA 3 peptide sequence binds to a protein encoded by the HLA allele with an affinity of less than 500 nM.

In some embodiments, at least one of the first GATA3 mutant peptide sequence and the second mutant peptide sequence binds to a protein encoded by the HLA allele with stability greater than 1 hour.

In some embodiments, the at least one polypeptide contains at least one of the following sequences: (a) TLQRSSLWCL (SEQ ID NO: 5), VLPEPHLAL (SEQ ID NO: 6), HVLPEPHLAL (SEQ ID NO: 7), ALQPLQPHA (SEQ ID NO: 8), AIQPVLWTT (SEQ ID NO: 9), APAIQPVLWTT (SEQ ID NO: 10), SMLTGPPARV (SEQ ID NO: 11), MLTGPPARV (SEQ ID NO: 12), and/or YMFLKAESKI (SEQ ID NO: 13), and/or (b) MFLKAESKI (SEQ ID NO: 14) and/or YMFLKAESKI (SEQ ID NO: 15), and/or (c) VLWTTPPLQH (SEQ ID NO: 16), YMFLKAESK (SEQ ID NO: 17) and/or KIMFATLQR (SEQ ID NO: 18), and/or (d) FATLQRSSL (SEQ ID NO: 19), EPHLALQPL (SEQ ID NO: 20), QPVLWTTPPL (SEQ ID NO: 21), GPPARVPAV (SEQ ID NO: 22), MFATLQRSSL (SEQ ID NO: 23), KPKRDGYMF (SEQ ID NO: 24) and/or KPKRDGYMFL (SEQ ID NO: 25), and/or (e) IMKPKRDGYM (SEQ ID NO: 26), MFATLQRSSL (SEQ ID NO: 27), FLKAESKIMF (SEQ ID NO: 28), LHFCRSSIM (SEQ ID NO: 29), EPHLALQPL (SEQ ID NO: 30), FATLQRSSL (SEQ ID NO: 31), ESKIMFATL ( SEQ ID NO: 32), FLKAESKIM (SEQ ID NO: 33) and/or YMFLKAESKI (SEQ ID NO: 34).

In some embodiments, at least one polypeptide contains at least two of the following sequences: (a) TLQRSSLWCL (SEQ ID NO: 35), VLPEPHLAL (SEQ ID NO: 36), HVLPEPHLAL (SEQ ID NO: 37), ALQPLQPHA (SEQ ID NO: 38), AIQPVLWTT (SEQ ID NO: 39), APAIQPVLWTT (SEQ ID NO: 40), SMLTGPPARV (SEQ ID NO: 41), MLTGPPARV (SEQ ID NO: 42), and/or YMFLKAESKI (SEQ ID NO: 43), and/or (b) MFLKAESKI (SEQ ID NO: 44) and/or YMFLKAESKI (SEQ ID NO: 45), and/or (c) VLWTTPPLQH (SEQ ID NO: 46), YMFLKAESK (SEQ ID NO: 47) and/or KIMFATLQR (SEQ ID NO: 48), and/or (d) FATLQRSSL (SEQ ID NO: 49), EPHLALQPL (SEQ ID NO: 50), QPVLWTTPPL (SEQ ID NO: 51), GPPARVPAV (SEQ ID NO: 52), MFATLQRSSL (SEQ ID NO: 53), KPKRDGYMF (SEQ ID NO: 54) and/or KPKRDGYMFL (SEQ ID NO: 55), and/or (e) IMKPKRDGYM (SEQ ID NO: 56), MFATLQRSSL (SEQ ID NO: 57), FLKAESKIMF (SEQ ID NO: 58), LHFCRSSIM (SEQ ID NO: 59), EPHLALQPL (SEQ ID NO: 60), FATLQRSSL (SEQ ID NO: 61), ESKIMFATL ( SEQ ID NO: 62), FLKAESKIM (SEQ ID NO: 63) and/or YMFLKAESKI (SEQ ID NO: 64).

In some embodiments, the mutant GATA3 peptide sequences comprise (a) a first mutant GATA3 peptide sequence from (a) and a second mutant GATA3 peptide sequence from (b), (b) a first mutant GATA3 peptide sequence from (a) and a second mutant GATA3 peptide sequence from (c), (c) the first mutant GATA3 peptide sequence from (a) and the second mutant GATA3 peptide sequence from (d), (d) the first mutant GATA3 peptide sequence from (a) and the second mutant GATA3 peptide sequence from (e) , (e) the first mutant GATA3 peptide sequence from (b) and the second mutant GATA3 peptide sequence from (c), (f) the first mutant GATA3 peptide sequence from (b) and the second mutant GATA3 peptide sequence from (d), (g) first mutant GATA3 peptide sequence from (b) and second mutant GATA3 peptide sequence from (e), (h) first mutant GATA3 peptide sequence from (c) and second mutant GATA3 peptide sequence from (d), (i) first mutant GATA3 peptide sequence sequence from (c) and the second mutant GATA3 peptide sequence from (e), or (j) the first mutant GATA3 peptide sequence from (d) and the second mutant GATA3 peptide sequence from (e).

In some embodiments, the first mutant GATA3 peptide sequences and the second mutant GATA3 peptide sequence comprise a peptide from Table 5 and/or Table 6. In some embodiments, the first mutant GATA3 peptide sequence comprises a first neo-epitope of a GATA3 protein and the second mutant GATA3 peptide sequence comprises a second neoepitope of a mutant GATA protein, wherein the first mutant GATA3 peptide sequence is different from the second mutant GATA3 peptide sequence, and where the first neoepitope contains at least one mutant amino acid, and the second neoepitope contains the same mutant amino acid.

In some embodiments, each of the first mutant GATA3 peptide sequence and the second mutant GATA3 peptide sequence comprising at least eight contiguous amino acids represented by the formula: [Xaa]F-[Xaa]N-[Xaa]C or [Xaa]N-[ Xaa]C-[Xaa]F, where each Xaa is an amino acid, where each of [Xaa]N and [Xaa]C contains an amino acid sequence encoded by different parts of the GATA3 gene, where [Xaa]F is any amino acid sequence, where [Xaa ]N is encoded in the non-wild type reading frame of the GATA3 gene, where [Xaa]C contains at least one mutant amino acid and is encoded in the non-wild type reading frame of the GATA3 gene, where N is an integer from 0-100, where C is an integer from 1-100, where F is an integer from 0-100, where the sum of N and M is at least 8.

In some embodiments, each Xaa of [Xaa]F is a lysine residue, and F is an integer from 1-100, 1-10, 9, 8, 7, 6, 5, 4, 3, 2, or 1. In some In embodiments, F is 3, 4, or 5.

In some embodiments, each of the mutant GATA3 peptide sequences is present at a concentration of at least 50 μg/ml to 400 μg/ml. In some embodiments, the first mutant GATA3 peptide sequences and the second mutant GATA3 peptide sequence comprise a sequence from Table 1 or 2. In some embodiments, the composition further comprises an immunomodulatory agent or adjuvant. In some embodiments, the adjuvant is polyICLC.

In one aspect, the invention relates to a pharmaceutical composition comprising: one or more mutant GATA3 peptide sequences, wherein the one or more mutant GATA3 peptide sequences comprises a sequence selected from the group consisting of ESKIMFATLQRSSL (SEQ ID NO: 65), KPKRDGYMFLKAESKI (SEQ ID NO : 66), SMLTGPPARVPAVPFDLH (SEQ ID NO: 67), EPCSMLTGPPARVPAVPFDLH (SEQ ID NO: 68), LHFCRSSIMKPKRDGYMFLKAESKI (SEQ ID NO: 69), GPPARVPAVPFDLHFCRSSIMKPKRD (SEQ ID NO: 70), and KPKRDGYMFLKAESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 71).

In some embodiments, the one or more mutant GATA3 peptide sequences are ESKIMFATLQRSSL (SEQ ID NO: 72). In some embodiments, the one or more mutant GATA3 peptide sequences are KPKRDGYMFLKAESKI (SEQ ID NO: 73). In some embodiments, the one or more mutant GATA3 peptide sequences are SMLTGPPARVPAVPFDLH (SEQ ID NO: 74). In some embodiments, the one or more mutant GATA3 peptide sequences are EPCSMLTGPPARVPAVPFDLH (SEQ ID NO: 75). In some embodiments, the one or more mutant GATA3 peptide sequences are LHFCRSSIMKPKRDGYMFLKAESKI (SEQ ID NO: 76). In some embodiments, the one or more mutant GATA3 peptide sequences are GPPARVPAVPFDLHFCRSSIMKPKRD (SEQ ID NO: 77). In some embodiments, the one or more mutant GATA3 peptide sequences are KPKRDGYMFLKAESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 78).

In some embodiments, the pharmaceutical composition contains a pH modifier present at a concentration of 0.1 mM to 1 mM. In some embodiments, the pharmaceutical composition contains a pH modifier present at a concentration of 1 mM to 10 mM.

In one aspect, the invention relates to a method for synthesizing a GATA3 peptide, wherein the peptide comprises a sequence of at least two contiguous amino acids selected from the group consisting of Xaa-Cys, Xaa-Ser and Xaa-Thr, where Xaa is any amino acid, wherein the method includes: (a) combining at least one di-peptide or derivative thereof with an amino acid or derivative thereof of a GATA3 peptide or derivative thereof to produce a pseudo-proline containing GATA3 peptide or derivative thereof, wherein the dipeptide or derivative thereof contains a pseudo-proline group, (b) combining one or more selected amino acids, small peptides or derivatives thereof with a pseudo-proline containing GATA3 peptide or a derivative thereof, and (c) cleaving the pseudo-proline containing GATA3 peptide or a derivative thereof from the resin. In some embodiments, the method includes deprotecting a pseudo-proline containing GATA3 peptide, or a derivative thereof.

In some embodiments, the amino acid or derivative thereof with which the at least one dipeptide or derivative thereof is combined is selected from the group consisting of Ala, Cys, Asp, Glu, Phe, Gly, Ile, Lys, Leu, Met, Asn, Pro, Gln, Arg, Ser, Thr, Trp, Tyr, His and Val. In some embodiments, one or more selected amino acids, small peptides, or derivatives thereof, optionally conjugated to a pseudo-proline containing GATA3 peptide or derivative thereof, comprises Fmoc-Ala-OH∙H2O, Fmoc-Cys(Trt)-OH, Fmoc -Asp(OtBu)-OH, Fmoc-Asp(OMpe)-OH, Fmoc-Glu(OtBu)-OH, Fmoc-Phe-OH, Fmoc-Gly-OH, Fmoc-Ile-OH, Fmoc-Lys(Boc) -OH, Fmoc-Leu-OH, Fmoc-Met-OH, Fmoc-Asn(Trt)-OH, Fmoc-Pro-OH, Fmoc-Gln(Trt)-OH, Fmoc-Arg(Pbf)-OH, Fmoc- Ser(tBu)-OH, Fmoc-Thr(tBu)-OH, Fmoc-Trp(Boc)-OH, Fmoc-Tyr(tBu)-OH, Fmoc-Val-OH, Fmoc-His(Trt)-OH and Fmoc -His(Boc)-OH.

In some embodiments, the N-terminal amino acid or derivative thereof of the GATA3 peptide or derivative thereof is selected from the group consisting of Fmoc-Ala-OH∙H2O, Fmoc-Cys(Trt)-OH, Fmoc-Asp(OtBu)-OH, Fmoc -Asp(OMpe)-OH, Fmoc-Glu(OtBu)-OH, Fmoc-Phe-OH, Fmoc-Gly-OH, Fmoc-Ile-OH, Fmoc-Lys(Boc)-OH, Fmoc-Leu-OH, Fmoc-Met-OH, Fmoc-Asn(Trt)-OH, Fmoc-Pro-OH, Fmoc-Gln(Trt)-OH, Fmoc-Arg(Pbf)-OH, Fmoc-Ser(tBu)-OH, Fmoc- Thr(tBu)-OH, Fmoc-Trp(Boc)-OH, Fmoc-Tyr(tBu)-OH, Fmoc-Val-OH, Fmoc-His(Trt)-OH and Fmoc-His(Boc)-OH.

In some embodiments, the pseudo-proline group is (a) Fmoc-Ser(tBu)-Ser(psi(Me,Me)pro)-OH, (b) Fmoc-Ala-Thr(psi(Me,Me)pro) -OH, (c) Fmoc-Glu(OtBu)-Ser(psi(Me,Me)pro)-OH, (d) Fmoc-Leu-Thr(psi(Me,Me)pro)-OH, (e) Fmoc -Leu-Cys(psi(Dmp,H)pro)-OH. In some embodiments, (a) Xaa-Ser is Ser-Ser, (b) Xaa-Ser is Glu-Ser, (c) Xaa-Thr is Ala-Thr, (d) Xaa-Thr is Leu-Thr, or ( e) Xaa-Cys is Leu-Cys.

In one aspect, the invention relates to a method of treating a subject with cancer, comprising administering to the subject a subject pharmaceutical composition according to any of the aspects described above.

In one aspect, the invention relates to a method for identifying a cancer subject as a candidate for therapy, where the method includes identifying the subject as expressing a protein encoded by the HLA-A02:01 allele, HLA-A24:02 allele, HLA-A03:01 allele, HLA-B07: 02 allele and/or HLA-B08:01 allele, where the therapeutic agent contains (a) at least one polypeptide containing one or more mutant GATA3 peptide sequences, where each of the one or more mutant GATA3 peptide sequences contains at least one mutant amino acid and is a fragment of at least 8 contiguous amino acids of a mutant GATA3 protein resulting from a mutation in the GATA3 gene of a cancer cell; or (b) at least one polynucleotide comprising a sequence encoding at least one polypeptide, wherein each of the one or more mutant GATA3 peptide sequences or portions thereof binds to a protein encoded by the HLA-A02:01 allele, HLA-A24:02 allele, HLA-A03:01 allele, HLA-B07:02 allele and/or HLA-B08:01 allele. In some embodiments, the method further includes administering a therapeutic agent to a subject.

In one aspect, the invention relates to a method of treating a cancer subject, comprising administering to the subject a pharmaceutical composition comprising: (a) at least one polypeptide comprising a first mutant GATA3 peptide sequence and a second mutant GATA3 peptide sequence, wherein (i) the first mutant GATA3 peptide sequence and the second mutant GATA3 peptide sequence each contains at least 8 contiguous amino acids of SEQ ID NO: 1, and (ii) the C-terminal sequence of the first mutant GATA3 peptide sequence overlaps with the N-terminal sequence of the second mutant GATA3 peptide sequence; wherein at least 8 contiguous amino acids of SEQ ID NO: 1 contain at least one amino acid with the sequence PGRPLQTHVLPEPHLALQPLQPHADHAHADAPAIQPVLWTTPPLQHGHRHGLEPCSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFAT LQRSSLWCLCSNH (SEQ ID NO: 2), or (b) at least one polynucleotide containing a sequence encoding at least at least one polypeptide wherein the HLA alleles expressed by the subject are unknown at the time of administration.

In some embodiments, the at least 8 contiguous amino acids of SEQ ID NO: 1 contain at least one amino acid with the sequence: PGRPLQTHVLPEPHLALQPLQPHADHAHADAPAIQPVLWTTPPLQHGHRHGLEPCSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFAT LQRSSLWCLCSNH (SEQ ID NO: 2).

In some embodiments, the cancer is selected from the group consisting of melanoma, ovarian cancer, lung cancer, prostate cancer, breast cancer, colorectal cancer, endometrial cancer, and chronic lymphocytic leukemia (CLL). In some embodiments, the subject has breast cancer resistant to anti-estrogen therapy, MSI breast cancer, metastatic breast cancer, Her2 negative breast cancer, Her2 positive breast cancer, ER negative breast cancer, ER positive breast cancer, PR positive breast cancer, PR negative breast cancer, or any combination of the two.

In some embodiments, the breast cancer expresses a mutation in the estrogen receptor. In some embodiments, the method of the aspects described above further includes administering at least one additional therapeutic agent or modality. In some embodiments, the at least one additional therapeutic agent or modality is surgery, a checkpoint inhibitor, an antibody or fragment thereof, a chemotherapeutic agent, radiation, a vaccine, a small molecule, a T cell, a vector and APC, a polynucleotide, an oncolytic virus or any combination thereof. In some embodiments, the at least one additional therapeutic agent is an anti-PD-1 agent and an anti-PD-L1 agent, an anti-CTLA-4 agent, an anti-CD40 agent, letrozole, fulvestrant, a PI3 kinase inhibitor and/or an CDK 4/6. In some embodiments, the at least one additional therapeutic agent is palbociclib, ribociclib, abemaciclib, seliciclib, dinaciclib, milciclib, roniciclib, atuveciclib, briciclib, riviciclib, seliciclib, trilaciclib, voruciclib, or any combination thereof.

In some embodiments, the at least one additional therapeutic agent is palbociclib (PD0332991); abemaciclib (LY2835219); ribociclib (LEE 011); varuciclib (P1446A-05); Fascaplysin; arciriaflavin; 2-bromo-12,13-dihydro-5H-indolo[2,3-a]pyrrolo[3,4-c]carbazole-5,7(6H)-dione; 3-aminothioacridone (3-ATA), trans-4-((6-(ethylamino)-2-((1-(phenylmethyl)-1H-indol-5-yl)amino)-4-pyrimidinyl)amino)cyclohexano ( CINK4); 1,4-dimethoxyacridine-9(10H)-thione (NSC 625987); 2-methyl-5-(p-tolylamino)benzo[d]thiazole-4,7-dione (riuvidine); flavopiridol (alvocidib); seliciclib; dinaciclib; milciclib; roniciclib; atuveciclib; briciclib; riviciclib; trilaciclib (G1T28); or any combination thereof.

In some embodiments, the at least one additional therapeutic agent is Wortmannin, Demethoxyviridine, LY294002, Hibiscon C, Idelalisib, Copanlisib, Duvelisib, Tazelisib, Perifosine, Buparlisib, Duvelisib, Alpelisib (BYL719), Umbralisib, (TGR 1202), Copanlisib ( BAY 80-6946), PX-866, Dactolisib, CUDC-907, BDPX-696, voxtalisib (SAR245409, XL765), CUDC-907, ME-401, IPI-549, SF1126, RP6530, INK1117, pictilisib (GDC-0941 ), XL147 (SAR245408), palomide 529, GSK1059615, ZSTK474, PWT33597, IC87114, TG100–115, CAL263, RP6503, PI-103, GNE-477 or AEZS-136.

In some embodiments, the cancer is recurrent or metastatic breast cancer. In some embodiments, the subject is a subject who has experienced disease progression following endocrine therapy in combination with a CDK 4/6 inhibitor; or where the subject has not previously received systemic therapy. In some embodiments, the method includes determining the mutation status of an estrogen receptor gene in a cell of the subject. In some embodiments, the cells are isolated cells or cells enriched for estrogen receptor expression.

In some aspects, the invention provides a composition comprising at least one polypeptide comprising one or more mutant GATA3 peptide sequences, each of the one or more mutant GATA3 peptide sequences contains at least one mutant amino acid, and is a fragment of at least 8 contiguous amino acids of the mutant GATA3 protein, which occurs when there is a mutation in the GATA3 gene of a cancer cell; at least one polynucleotide containing a sequence encoding at least one polypeptide; one or more APCs containing at least one polypeptide; or a T cell receptor (TCR) specific for a neoepitope of at least one polypeptide in complex with an HLA protein.

In some embodiments, the one or more mutant GATA3 peptide sequences comprises two or more mutant GATA3 peptide sequences. In some embodiments, each of the one or more mutant GATA3 peptide sequences contains at least 8 contiguous amino acids of SEQ ID NO: 1 or 2.

In some aspects, the invention provides a composition comprising at least one polypeptide comprising two or more mutant GATA3 peptide sequences, wherein each of the two or more mutant GATA3 peptide sequences contains at least 8 contiguous amino acids of SEQ ID NO: 1, and C- the terminal sequence of the first GATA3 peptide sequence overlaps with the N-terminal sequence of the second GATA3 peptide sequence; at least one polynucleotide containing a sequence encoding at least one polypeptide of one or more APCs containing at least one polypeptide; or a T cell receptor (TCR) specific for a neoepitope of at least one polypeptide in complex with an HLA protein.

In some embodiments, the mutant GATA3 peptide sequence comprises a fragment of a mutant GATA3 protein resulting from a frameshift mutation in the GATA3 gene of a cancer cell. In some embodiments, the at least 8 contiguous amino acids comprise at least one amino acid encoded by the GATA3 neoORF sequence. In some embodiments, the mutation in the cancer cell's GATA3 gene is a frameshift mutation. In some embodiments, the mutation in the cancer cell's GATA3 gene is a missense mutation, a splice site mutation, or a gene fusion mutation. In some embodiments, each of the mutant GATA3 peptide sequences comprises at least 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26 , 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39 or 40 mutant amino acids.

In some embodiments, the at least one polypeptide contains at least 3, 4, 5, 6, 7, 8, 9, or 10 mutant GATA3 peptide sequences. In some embodiments, the at least one polypeptide contains at least two polypeptides, or the at least one polynucleotide contains at least two polynucleotides. In some embodiments, at least one of one or more GATA3 peptide sequences or at least one of two or more GATA3 peptide sequences comprises at least 9, 10, 11, 12, 13, 14, 15, 16, 17 , 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, or 40 continuous amino acids of protein GATA3. In some embodiments, at least two of the GATA3 peptide sequences comprise at least 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25 , 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39 or 40 continuous amino acids of the GATA3 protein.

In some embodiments, each of the GATA3 peptide sequences contains at least 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, The 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, or 40 contiguous amino acids of the GATA3 protein. In some embodiments, at least one of the two or more mutant GATA3 peptide sequences contains at least 8 contiguous amino acids of SEQ ID NO: 2. In some embodiments, at least 3, 4, 5, 6, 7, 8, 9, or 10 of the two or more mutant GATA3 peptide sequences contain at least 8 contiguous amino acids of SEQ ID NO: 2. In some embodiments, each of one of the two or more mutant GATA3 peptide sequences contains at least 8 contiguous amino acids of SEQ ID NO: 2. NO: 2. In some embodiments, at least one of the two or more mutant GATA3 peptide sequences contains at least 8 contiguous amino acids of SEQ ID NO: 3.

In some embodiments, at least one of the at least 8 contiguous amino acids is an amino acid of SEQ ID NO: 4. In some embodiments, a contiguous amino acid of at least 8 contiguous amino acids is not an amino acid of SEQ ID NO: 4. In some embodiments, a contiguous amino acid of at least 8 contiguous amino acids is not an amino acid of SEQ ID NO: 4. In embodiments, the at least one polypeptide comprises at least one mutant GATA3 peptide sequence that binds or is predicted to bind to a protein encoded by the HLA-A02:01 allele, HLA-A24:02 allele, HLA-A03:01 allele, HLA -B07:02 allele and/or HLA-B08:01 allele. In some embodiments, the at least one polypeptide contains at least one mutant GATA3 peptide sequence that binds or is predicted to bind to a protein encoded by: the HLA-A02:01 allele and the HLA-A24:02 allele; HLA-A02:01 allele and HLA-B08:01 allele; HLA-A24:02 allele and HLA-B08:01 allele; or HLA-A02:01 allele, HLA-A24:02 allele and HLA-B08:01 allele.

In some embodiments, two or more mutant GATA3 peptide sequences comprise a first mutant GATA3 peptide sequence that binds or is predicted to bind to a protein encoded by the HLA-A02:01 allele, the HLA-A24:02 allele, the HLA-A03:01 allele, HLA-B07:02 allele or HLA-B08:01 allele; and a second GATA3 peptide sequence that binds or is predicted to bind to a protein encoded by the HLA-A02:01 allele, HLA-A24:02 allele, HLA-A03:01 allele, HLA-B07:02 allele, or HLA-B08:01 allele ; wherein the first mutant GATA3 peptide sequence binds or is predicted to bind to a protein encoded by an HLA allele different from that of the second mutant GATA3 peptide sequence.

In some embodiments, the at least one polypeptide contains at least one mutant GATA3 peptide sequence that binds to a protein encoded by the HLA allele with an affinity of less than 10 μM, less than 1 μM, less than 500 nM, less than 400 nM, less than 300 nM, less than 250 nM, less than 200 nM, less than 150 nM, less than 100 nM, or less than 50 nM. In some embodiments, the at least one polypeptide contains at least one mutant GATA3 peptide sequence that binds to a protein encoded by the HLA allele with stability greater than 24 hours, greater than 12 hours, greater than 9 hours, greater than 6 hours, greater than 5 hours, more than 4 hours, more than 3 hours, more than 2 hours, more than 1 hour, more than 45 minutes, more than 30 minutes, more than 15 minutes or more than 10 minutes. In some embodiments, the HLA allele is selected from the group consisting of HLA-A02:01, HLA-A24:02, HLA-A03:01, HLA-B07:02, HLA-B08:01, and any combination thereof.

In some embodiments, the at least one polypeptide contains at least one of the following sequences: TLQRSSLWCL (SEQ ID NO: 79), VLPEPHLAL (SEQ ID NO: 80), HVLPEPHLAL (SEQ ID NO: 81), ALQPLQPHA (SEQ ID NO: 82), AIQPVLWTT (SEQ ID NO: 83), APAIQPVLWTT (SEQ ID NO: 84), SMLTGPPARV (SEQ ID NO: 85), MLTGPPARV (SEQ ID NO: 86), and/or YMFLKAESKI (SEQ ID NO: 87); and/or MFLKAESKI (SEQ ID NO: 88) and/or YMFLKAESKI (SEQ ID NO: 89), VLWTTPPLQH (SEQ ID NO: 90), YMFLKAESK (SEQ ID NO: 91) and/or KIMFATLQR (SEQ ID NO: 92 ); and/or FATLQRSSL (SEQ ID NO: 93), EPHLALQPL (SEQ ID NO: 94), QPVLWTTPPL (SEQ ID NO: 95), GPPARVPAV (SEQ ID NO: 96), MFATLQRSSL (SEQ ID NO: 97), KPKRDGYMF ( SEQ ID NO: 98) and/or KPKRDGYMFL(SEQ ID NO: 99) and/or IMKPKRDGYM (SEQ ID NO: 100), MFATLQRSSL (SEQ ID NO: 101), FLKAESKIMF (SEQ ID NO: 102), LHFCRSSIM (SEQ ID NO: 103), EPHLALQPL (SEQ ID NO: 104), FATLQRSSL (SEQ ID NO: 105), ESKIMFATL (SEQ ID NO: 106), FLKAESKIM (SEQ ID NO: 107) and/or YMFLKAESKI (SEQ ID NO: 108).

In some embodiments, two or more mutant GATA3 peptide sequences comprise at least two of the following sequences: TLQRSSLWCL (SEQ ID NO: 109), VLPEPHLAL (SEQ ID NO: 110), HVLPEPHLAL (SEQ ID NO: 111), ALQPLQPHA ( SEQ ID NO: 112), AIQPVLWTT (SEQ ID NO: 113), APAIQPVLWTT (SEQ ID NO: 114), SMLTGPPARV (SEQ ID NO: 115), MLTGPPARV (SEQ ID NO: 116), and/or YMFLKAESKI (SEQ ID NO: 117); and/or MFLKAESKI (SEQ ID NO: 118) and/or YMFLKAESKI (SEQ ID NO: 119), VLWTTPPLQH (SEQ ID NO: 120), YMFLKAESK (SEQ ID NO: 121) and/or KIMFATLQR (SEQ ID NO: 122 ); and/or FATLQRSSL (SEQ ID NO: 123), EPHLALQPL (SEQ ID NO: 124), QPVLWTTPPL (SEQ ID NO: 125), GPPARVPAV (SEQ ID NO: 126), MFATLQRSSL (SEQ ID NO: 127), KPKRDGYMF ( SEQ ID NO: 128) and/or KPKRDGYMFL (SEQ ID NO: 129) and/or IMKPKRDGYM (SEQ ID NO: 130), MFATLQRSSL (SEQ ID NO: 131), FLKAESKIMF (SEQ ID NO: 132), LHFCRSSIM (SEQ ID NO: 133), EPHLALQPL (SEQ ID NO: 134), FATLQRSSL (SEQ ID NO: 135), ESKIMFATL (SEQ ID NO: 136), FLKAESKIM (SEQ ID NO: 137) and/or YMFLKAESKI (SEQ ID NO: 138).

In some embodiments, the mutant GATA3 peptide sequences comprise at least two of the following sequences: EPCSMLTGPPARVPAVPFDLH (SEQ ID NO: 139), SMLTGPPARVPAVPFDLH (SEQ ID NO: 140), GPPARVPAVPFDLHFCRSSIMKPKRD (SEQ ID NO: 141), DLHFCRSSIMKPKRDGYMFLKAESKI (SEQ ID NO : 142), KPKRDGYMFLKAESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 143), FLKAESKIMFATLQRS (SEQ ID NO: 144) and KPKRDGYMFLKAESKI (SEQ ID NO: 145).

In some embodiments, the mutant GATA3 peptide sequences comprise at least two of their Table 5 and/or Table 6 sequences. In some embodiments, the first mutant GATA3 peptide sequence of the two or more mutant GATA3 peptide sequences comprises a first neo-epitope of a GATA3 protein, and a second the GATA3 mutant peptide sequence comprises a second neo-epitope of a GATA3 mutant protein, wherein the first GATA3 mutant peptide sequence is different from the GATA3 mutant peptide sequence, and where the first neo-epitope contains at least one mutant amino acid, and the second neo-epitope contains the same mutant amino acid.

In some aspects, the invention provides a composition comprising at least one polypeptide comprising one or more mutant GATA3 peptide sequences, wherein the at least one polypeptide is represented by the formula [Xaa]F-[Xaa]N-[Xaa]C, wherein each Xaa independently is any amino acid where [Xaa]N-[Xaa]C represents one or more mutant GATA3 peptide sequences, where [Xaa]N and [Xaa]C each contain a contiguous amino acid sequence encoded by different parts of the GATA3 gene, where [ Xaa]N is encoded by a non-wild type reading frame, where [Xaa]C contains at least one mutant amino acid and is encoded by a non-wild type reading frame, where N is an integer from 0-100, where C is an integer from 1-100, where F is an integer from 0-100, where the sum of N and M is at least 8.

In some embodiments, each of the mutant GATA3 peptide sequences, at least eight contiguous amino acids, is represented by the formula [Xaa]F-[Xaa]N-[Xaa]C or [Xaa]N-[Xaa]C-[Xaa]F , where each Xaa is an amino acid, where each of [Xaa]N and [Xaa]C contains an amino acid sequence encoded by different parts of the GATA3 gene, where [Xaa]F is any amino acid sequence, where [Xaa]N is encoded in a non-wild-type reading frame type of GATA3 gene, where [Xaa]C contains at least one mutant amino acid and is encoded in the reading frame of a non-wild type GATA3 gene, where N is an integer from 0-100, where C is an integer from 1-100, where F is an integer from 0-100, where the sum of N and M is at least 8. In some embodiments, each Xaa of [Xaa]F is a lysine residue, and F is an integer from 1-100, 1-10, 9, 8, 7, 6, 5, 4, 3, 2, or 1. In some embodiments, F is 3, 4, or 5.

In some embodiments, the at least one mutant amino acid comprises at least 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26 , 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39 or 40 continuous mutant amino acids. In some embodiments, each of the mutant GATA3 peptide sequences is present at a concentration of at least 1 μg/ml, at least 10 μg/ml, at least 25 μg/ml, at least 50 μg/ml, at least 100 µg/ml, at least 200 µg/ml, at least 250 µg/ml, at least 300 µg/ml or at least 400 µg/ml. In some embodiments, each of the mutant GATA3 peptide sequences is present at a concentration of at most 5000 μg/ml, at most 2500 μg/ml, at most 1000 μg/ml, at most 750 μg/ml, at most 500 μg/ml, at most greater than 400 µg/ml, or at most 300 µg/ml. In some embodiments, each of the mutant GATA3 peptide sequences is present at a concentration of 10 μg/ml to 5000 μg/ml, 10 μg/ml to 4000 μg/ml, 10 μg/ml to 3000 μg/ml, 10 μg/ml to 2000 mcg/ml, 10 mcg/ml up to 1000 mcg/ml, 25 mcg/ml up to 500 mcg/ml, 50 mcg/ml up to 500 mcg/ml, 100 mcg/ml up to 500 mcg/ml, 200 mcg/ml up to 500 µg/ml, 200 µg/ml to 400 µg/ml or 3000 µg/ml to 400 µg/ml.

In some embodiments, the composition further includes an immunomodulatory agent or adjuvant. In some embodiments, the adjuvant is polyICLC. In some aspects, the invention relates to a pharmaceutical composition comprising a composition described herein and a pharmaceutically acceptable excipient. In some embodiments, the pharmaceutical composition contains a pH modifier present at a concentration of less than 1 mM or greater than 1 mM. In some embodiments, the pharmaceutical composition is a vaccine composition. In some embodiments, the pharmaceutical composition is aqueous.

In some embodiments, one or more of at least one polypeptide is bound by pI>5 and HYDRO >-6, pI>8 and HYDRO >-8, pI<5 and HYDRO >-5, pI>9 and HYDRO <-8 , pI >7 and HYDRO value >-5.5, pI < 4.3 and -4≥HYDRO≥-8, pI>0 and HYDRO<-8, pI>0 and HYDRO >-4, or pI>4, 3 and -4≥HYDRO≥-8, pI>0 and HYDRO>-4, or pI>4.3 and HYDRO≤-4, pI>0 and HYDRO>-4, or pI>4.3 and -4≥ HYDRO≥-9, 5≥pI ≥12 and -4≥HYDRO≥-9.

In some embodiments, the pH modifier is a base. In some embodiments, the pH modifier is a weak acid base conjugate. In some embodiments, the pH modifier is a pharmaceutically acceptable salt. In some embodiments, the pH modifier is a dicarboxylate or tricarboxylate. In some embodiments, the pH modifier is citric acid and/or citrate. In some embodiments, the citrate is disodium citrate and/or trisodium citrate. In some embodiments, the pH modifier is succinic acid and/or succinate. In some embodiments, the succinate is disodium succinate and/or monosodium succinate. In some embodiments, the succinate is succinate hexahydrate. In some embodiments, the pH modifier is present at a concentration of 0.1 mM - 10 mM. In some embodiments, the pH modifier is present at a concentration of 0.1 mM - 5 mM. In some embodiments, the pH modifier is present at a concentration of 0.1 mM - 1 mM. In some embodiments, the pH modifier is present at a concentration of 1 mM - 10 mM. In some embodiments, the pH modifier is present at a concentration of 1 mM - 5 mM.

In some embodiments, the pharmaceutically acceptable carrier comprises a liquid. In some embodiments, the pharmaceutically acceptable carrier comprises water. In some embodiments, the pharmaceutically acceptable carrier contains sugar. In some embodiments, the sugar contains dextrose or mannitol. In some embodiments, dextrose or mannitol is present at a concentration of 1-10% w/v. In some embodiments, the sugar contains trehalose. In some embodiments, the sugar comprises sucrose. In some embodiments, the pharmaceutically acceptable carrier comprises dimethyl sulfoxide (DMSO).

In some embodiments, DMSO is present at a concentration of 0.1% - 10%, 0.5% - 5%, 1% - 5%, 2% - 5%, 2% - 4%, or 2% - 4%. In some embodiments, the pharmaceutically acceptable carrier does not contain dimethyl sulfoxide (DMSO). In some embodiments, the pharmaceutical composition is lyophilizable. In some embodiments, the pharmaceutical composition further comprises an immunomodulator or adjuvant. In some embodiments, the immunomodulator or adjuvant is selected from the group consisting of poly-ICLC, 1018 ISS, aluminum salts, Amplivax, AS15, BCG, CP-870,893, CpG7909, CyaA, ARNAX, STING agonists, dSLIM, GM-CSF, IC30 , IC31, Imiquimoda, ImuFact IMP321, IS Patch, ISS, ISCOMATRIX, Juvlmmune, LipoVac, MF59, monophosphoryl lipid A, Montanida IMS 1312, Montanida ISA 206, Montanida ISA 50V, Montanida ISA-51, OK-432, OM-174, OM -197-MP-EC, ONTAK, PepTel®, vector systems, PLGA microparticles, resiquimod, SRL172, Virosomes and other virus-like particles, YF-17D, VEGF trap, R848, beta-glucan, Pam3Cys, and Aquila's QS21 stimulon.

In some embodiments, the immunomodulator or adjuvant comprises poly-ICLC. In some embodiments, the ratio of poly-ICLC to peptides in the pharmaceutical composition is from 2:1 to 1:10 v:v. In some embodiments, the ratio of poly-ICLC to peptides in the pharmaceutical composition is about 1:1, 1:1.5, 1:2, 1:3, 1:4, or 1:5 v:v. In some embodiments, the ratio of poly-ICLC to peptides in the pharmaceutical composition is about 1:3 v/v.

In some aspects, the invention relates to a method for synthesizing a GATA3 peptide, wherein the peptide comprises a sequence of at least two contiguous amino acids selected from the group consisting of Xaa-Cys, Xaa-Ser and Xaa-Thr, where Xaa is any amino acid, where the method includes : combining at least one di-peptide or derivative thereof with an amino acid or derivative thereof of a GATA3 peptide or derivative thereof to produce a pseudo-proline containing GATA3 peptide or derivatives thereof, wherein the dipeptide or derivative thereof contains a pseudo-proline group; combining one or more selected amino acids, small peptides or derivatives thereof with a pseudo-proline containing GATA3 peptide or derivative thereof; and cleaving the pseudo-proline containing GATA3 peptide or derivative thereof from the resin.

In some embodiments, the method includes deprotecting a pseudo-proline containing GATA3 peptide or derivative thereof. In some embodiments, the GATA3 peptide is a peptide from at least one polypeptide of a composition described herein or a pharmaceutical composition. In some embodiments, the N-terminal amino acid or derivative thereof of the GATA3 peptide or derivative thereof is attached to the resin. In some embodiments, the resin is Wang's resin or 2-chlorotrityl resin (2-Cl-Trt resin). In some embodiments, the coupling starting material is Fmoc-His(Trt)-Wang resin, H-His(Trt)-2Cl-Trt resin, Fmoc-Asp(OtBu)-Wang resin, Fmoc-Ile-Wang resin, Fmoc -Ser(tBu)-Wang resin or Fmoc-Leu-Wang resin. In some embodiments, the amino acid or derivative thereof to which at least one dipeptide or derivative thereof is conjugated is selected from the group consisting of Ala, Cys, Asp, Glu, Phe, Gly, Ile, Lys, Leu, Met, Asn , Pro, Gln, Arg, Ser, Thr, Trp, Tyr, His and Val.

In some embodiments, one or more selected amino acids, small peptides, or derivatives thereof, optionally conjugated to a pseudo-proline containing GATA3 peptide or derivative thereof, comprises Fmoc-Ala-OH∙H2O, Fmoc-Cys(Trt)-OH, Fmoc -Asp(OtBu)-OH, Fmoc-Asp(OMpe)-OH, Fmoc-Glu(OtBu)-OH, Fmoc-Phe-OH, Fmoc-Gly-OH, Fmoc-Ile-OH, Fmoc-Lys(Boc) -OH, Fmoc-Leu-OH, Fmoc-Met-OH, Fmoc-Asn(Trt)-OH, Fmoc-Pro-OH, Fmoc-Gln(Trt)-OH, Fmoc-Arg(Pbf)-OH, Fmoc- Ser(tBu)-OH, Fmoc-Thr(tBu)-OH, Fmoc-Trp(Boc)-OH, Fmoc-Tyr(tBu)-OH, Fmoc-Val-OH, Fmoc-His(Trt)-OH and Fmoc -His(Boc)-OH.

In some embodiments, the N-terminal amino acid or derivative thereof of the GATA3 peptide or derivative thereof is selected from the group consisting of Fmoc-Ala-OH∙H2O, Fmoc-Cys(Trt)-OH, Fmoc-Asp(OtBu)-OH, Fmoc -Asp(OMpe)-OH, Fmoc-Glu(OtBu)-OH, Fmoc-Phe-OH, Fmoc-Gly-OH, Fmoc-Ile-OH, Fmoc-Lys(Boc)-OH, Fmoc-Leu-OH, Fmoc-Met-OH, Fmoc-Asn(Trt)-OH, Fmoc-Pro-OH, Fmoc-Gln(Trt)-OH, Fmoc-Arg(Pbf)-OH, Fmoc-Ser(tBu)-OH, Fmoc- Thr(tBu)-OH, Fmoc-Trp(Boc)-OH, Fmoc-Tyr(tBu)-OH, Fmoc-Val-OH, Fmoc-His(Trt)-OH and Fmoc-His(Boc)-OH.

In some embodiments, the pseudo-proline group is Fmoc-Ser(tBu)-Ser(psi(Me,Me)pro)-OH. In some embodiments, the pseudo-proline group is Fmoc-Ala-Thr(psi(Me,Me)pro)-OH. In some embodiments, the pseudo-proline group is Fmoc-Glu(OtBu)-Ser(psi(Me,Me)pro)-OH. In some embodiments, the pseudo-proline group is Fmoc-Leu-Thr(psi(Me,Me)pro)-OH. In some embodiments, the pseudo-proline group is Fmoc-Leu-Cys(psi(Dmp,H)pro)-OH.

In some embodiments, Xaa-Ser is Ser-Ser. In some embodiments, Xaa-Ser is Glu-Ser. In some embodiments, Xaa-Thr is Ala-Thr. In some embodiments, Xaa-Thr is Leu-Thr. In some embodiments, Xaa-Cys is Leu-Cys.

In some aspects, the invention relates to a method of treating a cancer subject, comprising administering to the subject a pharmaceutical composition described in the present invention.

In some aspects, the invention relates to a method for identifying a cancer subject as a candidate for therapy, where the method includes identifying the subject as expressing a protein encoded by the HLA-A02:01 allele, the HLA-A24:02 allele, the HLA-A03:01 allele, the HLA-B07: 02 allele and/or HLA-B08:01 allele, where the therapeutic agent contains at least one polypeptide containing one or more mutant GATA3 peptide sequences, where each of the one or more mutant GATA3 peptide sequences contains at least one mutant amino acid and is a fragment at least 8 contiguous amino acids of a mutant GATA3 protein resulting from a mutation in the GATA3 gene of a cancer cell; at least one polynucleotide containing a sequence encoding at least one polypeptide; one or more APCs containing at least one polypeptide; or a T cell receptor (TCR) specific for at least one polypeptide in complex with an HLA protein; wherein each of one or more mutant GATA3 peptide sequences, or a portion thereof, binds to a protein encoded by the HLA-A02:01 allele, the HLA-A24:02 allele, the HLA-A03:01 allele, the HLA-B07:02 allele, and/or the HLA- B08:01 allele. In some embodiments, the method further includes administering a therapeutic agent to a subject.

In some aspects, the invention relates to a method of treating a cancer subject, comprising administering to the subject a composition comprising: at least one polypeptide comprising one or more mutant GATA3 peptide sequences, wherein each of the one or more mutant GATA3 peptide sequences contains at least one mutant amino acid and is a fragment of at least 8 contiguous amino acids of a mutant GATA3 protein resulting from a mutation in the GATA3 gene of a cancer cell; at least one polynucleotide containing a sequence encoding at least one polypeptide; one or more APCs containing at least one polypeptide; or a T cell receptor (TCR) specific for a neoepitope of at least one polypeptide in complex with an HLA protein; wherein the mutant GATA3 peptide or portion thereof binds to a protein encoded by the HLA-A02:01 allele, the HLA-A24:02 allele, the HLA-A03:01 allele, the HLA-B07:02 allele, and/or the HLA-B08:01 allele; wherein the subject is identified as expressing the HLA-A02:01 allele, the HLA-A24:02 allele, the HLA-A03:01 allele, the HLA-B07:02 allele, and/or the HLA-B08:01 allele.

In some aspects, the invention relates to a method of treating a cancer subject, comprising administering to the subject a composition comprising at least one polypeptide comprising two or more mutant GATA3 peptide sequences, wherein each of the two multiple mutant GATA3 peptide sequences contains at least 8 contiguous amino acids SEQ ID NO: 1, and the C-terminal sequence of the first GATA3 peptide sequence overlaps with the N-terminal sequence of the second GATA3 peptide sequence; at least one polynucleotide containing a sequence encoding at least one polypeptide; one or more APCs containing at least one polypeptide; or a T cell receptor (TCR) specific for a neo-epitope of at least one polypeptide in complex with an HLA protein; wherein the HLA alleles expressed by the subject are unknown at the time of administration.

In some embodiments, an immune response is induced in a subject. In some embodiments, the immune response is a humoral response. In some embodiments, mutant GATA3 peptide sequences are administered simultaneously, separately, or sequentially. In some embodiments, the first peptide is administered sequentially after a period of time sufficient for the second peptide to activate the second T cells. In some embodiments, the cancer is selected from the group consisting of melanoma, ovarian cancer, lung cancer, prostate cancer, breast cancer, colorectal cancer, endometrial cancer, and chronic lymphocytic leukemia (CLL). In some embodiments, the subject has breast cancer resistant to anti-estrogen therapy, MSI breast cancer, metastatic breast cancer, Her2 negative breast cancer, Her2 positive breast cancer, ER negative breast cancer, ER positive breast cancer, PR positive breast cancer, PR negative breast cancer, or any combination of the two. In some embodiments, the breast cancer expresses a mutation in the estrogen receptor. In some embodiments, the method further includes administering at least one additional therapeutic agent or modality.

In some embodiments, the at least one additional therapeutic agent or modality is surgery, a checkpoint inhibitor, an antibody or fragment thereof, a chemotherapeutic agent, radiation, a vaccine, a small molecule, a T cell, a vector and APC, a polynucleotide, an oncolytic virus or any combination thereof. In some embodiments, the at least one additional therapeutic agent is an anti-PD-1 agent and an anti-PD-L1 agent, an anti-CTLA-4 agent, an anti-CD40 agent, letrozole, fulvestrant, a PI3 kinase inhibitor and/or an inhibitor CDK 4/6. In some embodiments, the at least one additional therapeutic agent is selected from the group consisting of palbociclib (PD0332991); abemaciclib (LY2835219); ribociclib (LEE 011); voruciclib (P1446A-05); Fascaplysina; arciriaflavin; 2-bromo-12,13-dihydro-5H-indolo[2,3-a]pyrrolo[3,4-c]carbazole-5,7(6H)-dione; 3-aminothioacridone (3-ATA), trans-4-((6-(ethylamino)-2-((1-(phenylmethyl)-1H-indol-5-yl)amino)-4-pyrimidinyl)amino)cyclohexano ( CINK4); 1,4-dimethoxyacridine-9(10H)-thione (NSC 625987); 2-methyl-5-(p-tolylamino)benzo[d]thiazole-4,7-dione (riuvidine); and flavopiridol (alvocidib); seliciclib; dinaciclib; milciclib; roniciclib; atuveciclib; briciclib; riviciclib; trilaciclib (G1T28); or any combination thereof.

In some embodiments, the additional therapeutic agent is administered before, simultaneously with, or after the administration of the mutant GATA3 peptide sequences. In some embodiments, administration includes subcutaneous or intravenous administration. In some embodiments, the cancer is recurrent or metastatic breast cancer. In some embodiments, the subject is a subject who has experienced disease progression following endocrine therapy in combination with a CDK 4/6 inhibitor.

A mutation common to CLL and some lymphomas is a change from cysteine to serine at position (C481S) in the BTK (Bruton's tyrosine kinase) gene. The mutation is located in a region having the amino acid sequence: IFIITEYMANG S LLNYLREMRHR (SEQ ID NO: 146), the mutated serine is underlined. This change produces a variety of binding peptides that are bound by a range of HLA molecules.

In one aspect, the invention relates to a composition comprising a polypeptide comprising one or more mutant BTK peptide sequences from a C481S mutant BTK protein, one or more mutant BTK peptide sequences comprising at least 8 contiguous amino acids of the mutant BTK protein, wherein the amino acid sequences of the peptides are: ANGSLLNY (SEQ ID NO: 147); ANGSLLNYL (SEQ ID NO: 148); ANGSLLNYLR (SEQ ID NO: 149); EYMANGSL (SEQ ID NO: 150); EYMANGSLLN (SEQ ID NO: 151); EYMANGSLLNY (SEQ ID NO: 152); GSLLNYLR (SEQ ID NO: 153); GSLLNYLREM (SEQ ID NO: 154); ITEYMANGS (SEQ ID NO: 155); ITEYMANGSL (SEQ ID NO: 156); ITEYMANGSLL (SEQ ID NO: 157); MANGSLLNYL (SEQ ID NO: 158); MANGSLLNYLR (SEQ ID NO: 159); NGSLLNYL (SEQ ID NO: 160); NGSLLNYL (SEQ ID NO: 161); SLLNYLREMR(SEQ ID NO: 162); TEYMANGSLL (SEQ ID NO: 163); TEYMANGSLLNY (SEQ ID NO: 164); YMANGSLL(SEQ ID NO: 165); or YMANGSLLN (SEQ ID NO: 166),listed in the table 34.

In some embodiments, one or more mutant BTK peptide sequences comprise: (a) ANGSLLNY (SEQ ID NO: 167) and binds or is predicted to bind to a protein encoded by the HLA-A36:01 allele, (b) ANGSLLNYL (SEQ ID NO : 168) and binds or is predicted to bind to a protein encoded by an HLA allele selected from the group consisting of HLA-C15:02, HLA-C08:01, HLA-C06:02, HLA-A02:04, HLA-C12: 02, HLA-B44:02, HLA-C17:01 and HLA-B38:01, (c) ANGSLLNYLR (SEQ ID NO: 169) and binds to or is predicted to bind to the protein encoded by the HLA-A74:01 allele, or HLA -A31:01 allele, (d) EYMANGSL (SEQ ID NO: 170) and binds or is predicted to bind to a protein encoded by an HLA allele selected from the group consisting of HLA-C14:02, HLA-C14:03 and HLA- A24:02, (e) EYMANGSLLN (SEQ ID NO: 171) and binds to or is predicted to bind to a protein encoded by the HLA-A24:02 allele or HLA-A23:01 allele, (f) EYMANGSLLNY (SEQ ID NO: 172) and binds or is predicted to bind to the protein encoded by the HLA-A29:02 allele, (g) GSLLNYLR (SEQ ID NO: 173) and binds to or is predicted to bind to the protein encoded by the HLA-A31:01 allele or the HLA-A74:01 allele , (h) GSLLNYLREM (SEQ ID NO: 174) and binds to or is predicted to bind to a protein encoded by the HLA-B58:02 allele or HLA-B57:01 allele, (i) ITEYMANGS (SEQ ID NO: 175) and binds to or is predicted to bind to the protein encoded by the HLA-A01:01 allele, (j) ITEYMANGSL (SEQ ID NO: 176) and is believed to bind to or is predicted to bind to the protein encoded by the HLA-A01:01 allele, (k) ITEYMANGSLL (SEQ ID NO : 177) and binds or is predicted to bind to a protein encoded by the HLA-A01:01 allele, (l) MANGSLLNYL (SEQ ID NO: 178) and binds to or is predicted to bind to a protein encoded by an HLA allele selected from the group consisting of HLA -C17:01, HLA-C02:02, HLA-B35:01, HLA-C03:03, HLA-C08:01, HLA-B35:03, HLA-C12:02, HLA-C01:02, HLA-C03 :04 and HLA-C08:02, (m) MANGSLLNYLR (SEQ ID NO: 179) and binds or is predicted to bind to the protein encoded by the HLA-A33:03 allele or HLA-A74:01 allele, (n) NGSLLNYL (SEQ ID NO: 180) and binds or is predicted to bind to a protein encoded by the HLA-B14:02 allele, (o) NGSLLNYL (SEQ ID NO: 181) and binds or is predicted to bind to a protein encoded by an HLA allele selected from the group, consisting of: HLA-A68:01, HLA-A33:03, HLA-A31:01 and HLA-A74:01, (p) SLLNYLREMR (SEQ ID NO: 182) and binds to or is predicted to bind to the protein encoded by HLA- A74:01 allele or HLA-A31:01 allele, (q) TEYMANGSLL (SEQ ID NO: 183) and binds or is predicted to bind to a protein encoded by an HLA allele selected from the group consisting of: HLA-B40:01, HLA -B44:03, HLA-B49:01, HLA-B44:02 and HLA-B40:02, (r) TEYMANGSLLNY (SEQ ID NO: 184) and binds or is predicted to bind to the protein encoded by the HLA-B44:03 allele , (s) YMANGSLL (SEQ ID NO: 185) and binds or is predicted to bind to a protein encoded by an HLA allele selected from the group consisting of HLA-B15:09, HLA-C03:04, HLA-C03:03, HLA -C17:01, HLA-C03:02, HLA-C14:03, HLA-C14:02, HLA-C04:01, HLA-C02:02, HLA-A01:01, or (t) YMANGSLLN (SEQ ID NO : 186) and binds or is predicted to bind to the protein encoded by the HLA-A29:02 allele or the HLA-A01:01 allele.

In some embodiments, one or more mutant BTK peptide sequences are specific for a recognized T cell receptor in complex with an HLA protein. In some embodiments, the composition contains two or more mutant BTK peptide sequences.

In one aspect, the invention relates to a composition comprising: at least one polypeptide comprising one or more mutant BTK peptide sequences, each having at least 8 contiguous amino acids from a C481S mutant BTK protein, one or more mutant BTK peptide sequences selected from table 34, further containing three or more amino acid residues that are heterologous to the mutant BTK protein associated with the N-terminus or C-terminus of the mutant BTK peptide sequence, where three or more amino acid residues improve the processing of mutant BTK peptide sequences within the cell and/or improve epitope presentation of mutant BTK peptide sequences. In some embodiments, the three or more amino acid residues that are heterologous to the mutant BTK protein comprise an amino acid sequence from CMV-pp65, HIV, MART-1, or a non-viral, non-BTK endogenous peptide.

In some embodiments, three or more amino acid residues that are heterologous to the mutant BTK protein comprise at least 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16 , 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39 or 40 amino acids.

In some embodiments, the three or more amino acid residues that are heterologous to the mutant BTK protein comprise at most 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 50, 60, 70, 80, 90 or 100 amino acids.

In one aspect, the invention relates to a composition comprising: at least one polypeptide of the formula (N-terminus Xaa) _N -(Xaa _BTK ) _P -(Xaa-C-terminus) _C, where P is an integer greater than 7; (Xaa _BTK ) _P is a mutant BTK peptide sequence containing at least 8 contiguous amino acids selected from the sequence IFIITEYMANGSLLNYLREMRHR (SEQ ID NO: 187) of a mutant BTK protein containing a C481S mutant amino acid; N is equal to (i) 0 or (ii) an integer greater than 2; (N-terminus Xaa) _N is any amino acid sequence heterologous to the mutant BTK protein; C is equal to (i) 0 or (ii) an integer greater than 2; (Xaa-C-terminus) _C is any amino acid sequence heterologous to the mutant BTK protein; and both N and C are 0.

In some embodiments, the (N-terminus Xaa) _N and/or (Xaa-C-terminus) _C comprises the amino acid sequence of CMV-pp65, HIV, MART-1, or a non-viral, non-BTK endogenous protein or peptide.

In some embodiments, N and/or C is an integer greater than 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39 or 40.

In some embodiments, N and/or C is an integer less than 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 50, 60, 70, 80, 90 or 100 In some embodiments, the composition is any of items 8-10, where N is 0. In some embodiments, 8-10, where C is 0.

In one aspect, the invention provides a composition comprising a polynucleotide sequence encoding the polypeptide of claim 1. In one aspect, the composition contains a polynucleotide sequence encoding one or more peptide sequences of any of the mutant BTK peptides described above and in Tables 34 and Table 36. In some embodiments, the at least one polypeptide contains at least 3, 4, 5, 6, 7, 8, 9, or 10 mutant BTK peptide sequences. In some embodiments, at least one of the mutant BTK peptide sequences comprises at least 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, or 40 continuous amino acids of the mutant BTK protein. In some embodiments, at least 2, 3, 4, 5, 6, 7, 8, 9, or 10 BTK mutant peptide sequences comprise at least 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39 or 40 continuous amino acids of the mutant BTK protein. In some embodiments, each of the mutant BTK peptide sequences, or each of two or more BTK peptide sequences, contains at least 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39 or 40 continuous amino acids of the mutant BTK protein. In some embodiments, the at least one polypeptide contains at least one mutant BTK peptide sequence that binds or is predicted to bind to a protein encoded by the HLA alleles listed in Table 35 with an affinity of 150 nM or less and/or a half-life of 2 hours or more. In some embodiments, the mutant BTK peptide sequences comprise (a) a first mutant BTK peptide sequence selected from Table 34 that binds or is predicted to bind to a protein encoded by the HLA allele; and (b) a second BTK peptide having a C481S mutation, wherein the first mutant BTK peptide sequence and the second mutant BTK peptide sequence are not identical.

In some embodiments, the at least one polypeptide contains at least one mutant BTK peptide sequence that binds to a protein encoded by the HLA allele with an affinity of less than 10 μM, less than 1 μM, less than 500 nM, less than 400 nM , less than 300 nM, less than 250 nM, less than 200 nM, less than 150 nM, less than 100 nM or less than 50 nM.

In some embodiments, the at least one polypeptide contains at least one mutant BTK peptide sequence that binds to a protein encoded by the HLA allele with stability greater than 24 hours, greater than 12 hours, greater than 9 hours, greater than 6 hours, greater than 5 hours , more than 4 hours, more than 3 hours, more than 2 hours, more than 1 hour, more than 45 minutes, more than 30 minutes, more than 15 minutes or more than 10 minutes.

In some embodiments, the (N-terminus of Xaa) _N comprises the amino acid sequence IDIIMKIRNA (SEQ ID NO: 188), FFFFFFFFFFFFFFFFFFFFIIFFIFFWMC (SEQ ID NO: 189), FFFFFFFFFFFFFFFFFFFFFFFFAAFWFW (SEQ ID NO: 190), IFFIFFIIFFFFFFFFFFFFIIIIIIIWEC (SEQ ID NO: 191) , FIFFFIIFFFFFIFFFFFIFIIIIIIFWEC (SEQ ID NO: 192), TEY, WQAGILAR (SEQ ID NO: 193), HSYTTAE (SEQ ID NO: 194), PLTEEKIK (SEQ ID NO: 195), GALHFKPGSR (SEQ ID NO: 196), RRANKDATAE ( SEQ ID NO: 197), KAFISHEEKR (SEQ ID NO: 198), TDLSSRFSKS (SEQ ID NO: 199), FDLGGGTFDV (SEQ ID NO: 200), CLLLHYSVSK (SEQ ID NO: 201) or MTEYKLVVV (SEQ ID NO: 202 ). In some embodiments, (C-terminus Xaa) _C comprises the amino acid sequence KKNKKDDIKD (SEQ ID NO: 203), AGNDDDDDDDDDDDDDDDDDKKDKDDDDDD (SEQ ID NO: 204), AGNKKKKKKKNNNNNNNNNNNNNNNNNNNNNN (SEQ ID NO: 205), AGRDDDDDDDDDDDDDDDDDDDDDDDDDDD (SEQ ID NO: 20) 6) , GKSALTIQL (SEQ ID NO: 207), GKSALTI (SEQ ID NO: 208), QGQNLKYQ (SEQ ID NO: 209), ILGVLLLI (SEQ ID NO: 210), EKEGKISK (SEQ ID NO: 211), AASDFIFLVT (SEQ ID NO: 212), KELKQVASPF (SEQ ID NO: 213), KKKLINEKKE (SEQ ID NO: 214), KKCDISLQFF (SEQ ID NO: 215), KSTAGDTHLG (SEQ ID NO: 216), ATFYVAVTVP(SEQ ID NO: 217), LTIQLIQNHFVDEYDPTIEDSYRKQVVIDG (SEQ ID NO: 218) or TIQLIQNHFVDEYDPTIEDSYRKQVVIDGE (SEQ ID NO: 219).

In some embodiments, at least one of the mutant BTK peptide sequences comprises a mutant amino acid that is not encoded by the genome of the subject's cancer cell.

In some embodiments, each of the mutant BTK peptide sequences is present at a concentration of at least 1 μg/ml, at least 10 μg/ml, at least 25 μg/ml, at least 50 μg/ml, or at least 100 mcg/ml. In some embodiments, each of the mutant BTK peptide sequences is present at a concentration of at most 5000 μg/ml, at most 2500 μg/ml, at most 1000 μg/ml, at most 750 μg/ml, at most 500 μg/ml, at most greater than 400 µg/ml or at most 300 µg/ml. In some embodiments, each of the mutant BTK peptide sequences is present at a concentration of 10 μg/ml to 5000 μg/ml, 10 μg/ml to 4000 μg/ml, 10 μg/ml to 3000 μg/ml, 10 μg/ml to 2000 mcg/ml, 10 mcg/ml up to 1000 mcg/ml, 25 mcg/ml up to 500 mcg/ml, or 50 mcg/ml up to 300 mcg/ml. In some embodiments, the composition further comprises an immunomodulatory agent or adjuvant. In some embodiments, the adjuvant is polyICLC.

In one aspect, the invention relates to a pharmaceutical composition comprising: (a) a composition as described above, and (b) a pharmaceutically acceptable excipient. In some embodiments, the pharmaceutical composition further comprises a pH modifier. In some embodiments, the pharmaceutical composition is a vaccine composition. In some embodiments, the pharmaceutical composition is aqueous. In some embodiments, a pharmaceutical composition comprising one or more of at least one polypeptide is linked via (a) pI>5 and HYDRO >-6, (b) pI>8 and HYDRO >-8, (c) pI< 5 and HYDRO >-5, (d) pI>9 and HYDRO <-8, (e) pI >7 and HYDRO value >-5.5, (f) pI < 4.3 and -4≥HYDRO≥-8 , (g) pI>0 and HYDRO<-8, pI>0 and HYDRO >-4, or pI>4,3 and -4≥HYDRO≥-8, (h) pI>0 and HYDRO>-4, or pI>4.3 and HYDRO≤-4, (i) pI>0 and HYDRO>-4, or pI>4.3 and -4≥HYDRO≥-9, (j) 5≥pI ≥12 and -4≥ HYDRO≥-9.

In some embodiments, the pH modifier is a base. In some embodiments, the pH modifier is a weak acid base conjugate. In some embodiments, the pH modifier is a pharmaceutically acceptable salt. In some embodiments, the pH modifier is a dicarboxylate or tricarboxylate. In some embodiments, the pH modifier is citric acid and/or citrate. In some embodiments, the citrate is disodium citrate and/or trisodium citrate. In some embodiments, the pH modifier is succinic acid and/or succinate. In some embodiments, the succinate is disodium succinate and/or monosodium succinate. In some embodiments, the succinate is disodium succinate hexahydrate. In some embodiments, the pH modifier is present at a concentration of 0.1 mM - 1 mM. In some embodiments, the pharmaceutically acceptable carrier comprises a liquid. In some embodiments, the pharmaceutically acceptable carrier comprises water.

In some embodiments, the pharmaceutically acceptable carrier contains sugar. In some embodiments, the sugar contains dextrose. In some embodiments, dextrose is present at a concentration of 1-10% w/v. In some embodiments, the sugar contains trehalose. In some embodiments, the sugar comprises sucrose.

In some embodiments, the pharmaceutically acceptable carrier comprises dimethyl sulfoxide (DMSO). In some embodiments, DMSO is present at a concentration of 0.1% to 10%, 0.5% to 5%, or 1% to 3%. In some embodiments, the pharmaceutically acceptable carrier does not contain dimethyl sulfoxide (DMSO). In some embodiments, the pharmaceutical composition is lyophilizable. In some embodiments, the pharmaceutical composition further comprises an immunomodulator or adjuvant. In some embodiments, the immunomodulator or adjuvant is selected from the group consisting of poly-ICLC, 1018 ISS, aluminum salts, Amplivax, AS15, BCG, CP-870,893, CpG7909, CyaA, ARNAX, STING agonists, dSLIM, GM-CSF, IC30 , IC31, Imiquimoda, ImuFact IMP321, IS Patch, ISS, ISCOMATRIX, Juvlmmune, LipoVac, MF59, monophosphoryl lipid A, Montanida IMS 1312, Montanida ISA 206, Montanida ISA 50V, Montanida ISA-51, OK-432, OM-174, OM -197-MP-EC, ONTAK, PepTel®, vector systems, PLGA microparticles, resiquimod, SRL172, Virosomes and other virus-like particles, YF-17D, VEGF trap, R848, beta-glucan, Pam3Cys, and Aquila's QS21 stimulon.

In some embodiments, the immunomodulator or adjuvant comprises poly-ICLC. In some embodiments, the ratio of poly-ICLC to peptides in the pharmaceutical composition is from 2:1 to 1:10 v:v. In some embodiments, the ratio of poly-ICLC to peptides in the pharmaceutical composition is about 1:1, 1:2, 1:3, 1:4, or 1:5 v:v. In some embodiments, the ratio of poly-ICLC to peptides in the pharmaceutical composition is about 1:3 v/v.

In one aspect, the invention relates to a method of treating cancer in a subject, comprising administering to the subject a pharmaceutical composition described above.

In one aspect, the invention relates to a method of treating cancer in a subject, where the method includes: administering to a subject in need thereof a composition containing a peptide having a sequence selected from Table 34, 36 or 37, left column; where the subject expresses a protein encoded by any of the HLA alleles listed in the right column corresponding to the peptide in the table. In some embodiments, the invention provides a method of treating cancer in a subject, comprising: administering to a subject in need thereof a composition comprising one or more mutant BTK peptides, or one or more nucleic acids encoding one or more mutant BTK peptides, wherein each the mutant BTK peptide contains at least 8 contiguous amino acids of a mutant BTK protein containing a C481S mutation, wherein at least one of one or more peptides binds to a protein encoded by an HLA allele listed in Table 34, 36 or 37 that is expressed by the subject. In some embodiments, the peptide binds to an HLA protein with an affinity of 150 nM or less and/or a half-life of 2 hours or more.

In one aspect, the invention provides a method of treating cancer in a subject, comprising administering to a subject in need thereof a first and a second peptide or a nucleic acid encoding the first and second peptides, wherein the first peptide has an amino acid sequence selected from: Tables 34, 36 or 37 ; and the second peptide has an amino acid sequence selected from any of Tables 34, 36, or 37.

In some embodiments, an immune response is induced in a subject. In some embodiments, the immune response is a humoral response.

In some embodiments, one or more mutant BTK peptides are administered simultaneously, separately, or sequentially.

In some embodiments, the second peptide is administered sequentially after a period of time sufficient for the first peptide to activate the second T cell.

In some embodiments, the cancer is selected from the group consisting of certain types of lymphoma and certain types of leukemia. In some embodiments, the cancer is acute lymphoblastic leukemia (ALL), mantle cell lymphoma (MCL), chronic lymphocytic lymphoma, or B-cell non-Hodgkin lymphoma.

In some embodiments, the method further includes administering at least one additional therapeutic agent or modality.

In some embodiments, the at least one additional therapeutic agent or modality is surgery, a checkpoint inhibitor, an antibody or fragment thereof, a chemotherapeutic agent, radiation, a vaccine, a small molecule, a T cell, a vector and APC, a polynucleotide, an oncolytic virus or any combination thereof.

In some embodiments, the at least one additional therapeutic agent is an anti-PD-1 agent and an anti-PD-L1 agent, an anti-CTLA-4 agent, or an anti-CD40 agent. In some embodiments, the additional therapeutic agent is administered before, simultaneously with, or after the administration of the mutant BTK peptide sequences.

In one aspect, the invention relates to a method of treating cancer in a subject, comprising the steps of: (a) identifying a first protein expressed by the subject, wherein the first protein is encoded by a first HLA allele of the subject, and wherein the first HLA allele is an HLA allele presented in one of Tables 34, 37 or 38, (b) administering to the subject (i) a first mutant BTK peptide, wherein the first mutant BTK peptide is a peptide to the first HLA allele shown in any of Tables 34, 36, or 37; or (ii) a polynucleic acid encoding the first mutant BTK peptide.

In one aspect, the invention relates to a method for identifying a cancer subject as a candidate for therapy, where the method includes identifying the subject as expressing a protein encoded by an HLA from one of Tables 34, 36, or 37, wherein the therapeutic agent is a mutant BTK peptide or a nucleic acid encoding a mutant BTK a peptide, wherein the mutant BTK peptide contains at least 8 contiguous amino acids of the mutant BTK protein containing a mutation at C481, wherein the peptide (i) contains the C481S mutation, (ii) contains a peptide sequence from any of Tables 34, 36, or 37, and (iii) binds to the corresponding HLA-encoded protein from any of Tables 34, 36, or 37.

In some aspects, the invention provides a composition comprising a polypeptide comprising one or more mutant EGFR peptide sequences from a T790M mutant EGFR protein, one or more mutant EGFR peptide sequences containing at least 8 contiguous amino acids selected from the group consisting of: LIMQLMPF ( SEQ ID NO: 220), TVQLIMQL (SEQ ID NO: 221), TSTVQLIMQL (SEQ ID NO: 222), TVQLIMQLM (SEQ ID NO: 223), VQLIMQLM (SEQ ID NO: 224), STVQLIMQL (SEQ ID NO: 225 ) and LTSTVQLIM (SEQ ID NO: 226).

In some embodiments, one or more mutant EGFR peptide sequences are specific for a recognized T cell receptor in complex with an HLA protein.

In some embodiments, the composition contains a mixture of two or three or more mutant EGFR peptide sequences. In some embodiments, the composition contains at least 2, 3, 4, 5, 6, 7, 8, 9, or 10 mutant EGFR peptide sequences. In some embodiments, at least 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, or 40 contiguous amino acids of the mutant EGFR protein.

In some aspects, the invention provides a composition comprising at least one polypeptide comprising one or more mutant EGFR peptide sequences from a T790M mutant EGFR protein, one or more mutant EGFR peptide sequences containing at least 8 contiguous amino acids selected from the group consisting of from: LIMQLMPF (SEQ ID NO: 227), TVQLIMQL (SEQ ID NO: 228), TSTVQLIMQL (SEQ ID NO: 229), TVQLIMQLM (SEQ ID NO: 230), VQLIMQLM (SEQ ID NO: 231), STVQLIMQL (SEQ ID NO: 232) and LTSTVQLIM (SEQ ID NO: 233), further containing three or more amino acid residues that are heterologous to the mutant EGFR protein, connected to the N-terminus or C-terminus of the mutant EGFR peptide sequence, where three or more amino acid residues improve processing of mutant EGFR peptide sequences within the cell and/or improve epitope presentation of mutant EGFR peptide sequences.

In some embodiments, the three or more amino acid residues that are heterologous to the mutant EGFR protein comprise an amino acid sequence from CMV-pp65, HIV, MART-1, or a non-viral, non-EGFR endogenous peptide.

In some embodiments, three or more amino acid residues that are heterologous to the mutant EGFR protein comprise at least 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16 , 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39 or 40 amino acids.

In some embodiments, three or more amino acid residues that are heterologous to the mutant EGFR protein are linked to the N-terminus or C-terminus of two or more mutant EGFR peptide sequences comprising at most 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 50, 60, 70, 80, 90 or 100 amino acids.

In some embodiments, (Xaa-C-terminus) _C is any amino acid sequence heterologous to the mutant EGFR protein; and both N and C are not equal to 0.

In some embodiments, the (N-terminus Xaa) _N and/or (Xaa-C-terminus) _C comprises the amino acid sequence of CMV-pp65, HIV, MART-1, or a non-viral, non-EGFR endogenous protein or peptide.

In some embodiments, N and/or C is an integer greater than 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39 or 40.

In some embodiments, N and/or C is an integer less than 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 50, 60, 70, 80, 90 or 100 In some embodiments, N is 0. In some embodiments, C is 0.

In one aspect, the invention provides a composition comprising a polynucleotide sequence encoding a polypeptide as described above. In one embodiment, the composition contains a polynucleotide sequence encoding one or more mutant EGFR peptide sequences disclosed in the present invention.

In some embodiments, a composition comprising one or more mutant EGFR peptide sequences further comprises one or more mutant EGFR peptides selected from Table 40A-40D.

In some embodiments, at least one polypeptide comprising at least 3, 4, 5, 6, 7, 8, 9, or 10 mutant EGFR peptide sequences.

In some embodiments, at least one of the mutant EGFR peptide sequences comprises at least 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, or 40 contiguous amino acids of the mutant EGFR protein. In some embodiments, at least 2, 3, 4, 5, 6, 7, 8, 9, or 10 mutant EGFR peptide sequences comprise at least 9, 10, 11, 12, 13, 14, 15, 16, 17 , 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39 or 40 continuous amino acids of the mutant EGFR squirrel. In some embodiments, each of the mutant EGFR peptide sequences, or each of two or more EGFR peptide sequences, comprises at least 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39 or 40 continuous amino acids of the mutant EGFR protein.

In some embodiments, the at least one polypeptide contains at least one mutant EGFR peptide sequence that binds or is predicted to bind to a protein encoded by an HLA allele listed in Table 41 with an affinity of 150 nM or less and/or a half-life of 2 hours or more.

In some embodiments, the mutant EGFR peptide sequences comprise a first mutant EGFR peptide sequence that is selected from the group consisting of STVQLIMQL (SEQ ID NO: 234), LIMQLMPF (SEQ ID NO: 235), LTSTVQLIM (SEQ ID NO: 236), TVQLIMQL (SEQ ID NO: 237), TSTVQLIMQL (SEQ ID NO: 238), TVQLIMQLM (SEQ ID NO: 239) and VQLIMQLM (SEQ ID NO: 240) and a second mutant EGFR peptide sequence having a T790M mutation.

In some embodiments, the mutant EGFR peptide sequences comprise: (a) a first mutant EGFR peptide sequence that is selected from the group consisting of STVQLIMQL (SEQ ID NO: 241), LIMQLMPF (SEQ ID NO: 242), LTSTVQLIM (SEQ ID NO: : 243), TVQLIMQL (SEQ ID NO: 244), TSTVQLIMQL (SEQ ID NO: 245), TVQLIMQLM (SEQ ID NO: 246) and VQLIMQLM (SEQ ID NO: 247), wherein the first mutant EGFR peptide sequence binds to or is predicted to binds to protein encoded by HLA-A68:02, HLA-C15:02, HLA-A25:01, HLA-B57:03, HLA-C12:02, HLA-C03:02, HLA-A26:01, HLA-C12 :03, HLA-C06:02, HLA-C03:03, HLA-B52:01, HLA-A30:01, HLA-C02:02, HLA-C12:03, HLA-A11:01, HLA-A32:01 , HLA-A02:04, HLA-A68:01, HLA-B15:09, HLA-C17:01, HLA-C03:04, HLA-B08:01, HLA-A01:01, HLA-B42:01, HLA -B57:01, HLA-B15:01, HLA-B14:02, HLA-B37:01, HLA-A36:01, HLA-C15:02, HLA-B15:09, HLA-C12:02, HLA-B38 :01, HLA-C03:03, HLA-A02:03, HLA-B58:02, HLA-C08:01, HLA-B35:01, HLA-B40:01 and/or HLA-B35:03 allele; and (b) a second EGFR peptide sequence containing the T790M mutation, where the first and second peptides are not identical.

In some embodiments, the at least one polypeptide contains at least one mutant EGFR peptide sequence that binds to a protein encoded by the HLA allele with an affinity of less than 10 μM, less than 1 μM, less than 500 nM, less than 400 nM , less than 300 nM, less than 250 nM, less than 200 nM, less than 150 nM, less than 100 nM, or less than 50 nM.

In some embodiments, the at least one polypeptide contains at least one mutant EGFR peptide sequence that binds to a protein encoded by the HLA allele with stability greater than 24 hours, greater than 12 hours, greater than 9 hours, greater than 6 hours, greater than 5 hours , more than 4 hours, more than 3 hours, more than 2 hours, more than 1 hour, more than 45 minutes, more than 30 minutes, more than 15 minutes or more than 10 minutes.

In some embodiments, the (N-terminus of Xaa) _N comprises the amino acid sequence IDIIMKIRNA (SEQ ID NO: 248), FFFFFFFFFFFFFFFFFFFFIIFFIFFWMC (SEQ ID NO: 249), FFFFFFFFFFFFFFFFFFFFFFFFAAFWFW (SEQ ID NO: 250), IFFIFFIIFFFFFFFFFFFFIIIIIIIWEC (SEQ ID NO: 251) , FIFFFIIFFFFFIFFFFFIFIIIIIIFWEC (SEQ ID NO: 252), TEY, WQAGILAR (SEQ ID NO: 253), HSYTTAE (SEQ ID NO: 254), PLTEEKIK (SEQ ID NO: 255), GALHFKPGSR (SEQ ID NO: 256), RRANKDATAE ( SEQ ID NO: 257), KAFISHEEKR (SEQ ID NO: 258), TDLSSRFSKS (SEQ ID NO: 259), FDLGGGTFDV (SEQ ID NO: 260), CLLLHYSVSK (SEQ ID NO: 261) or MTEYKLVVV (SEQ ID NO: 262 ).

In some embodiments, (C-terminus Xaa) _C comprises the amino acid sequence KKNKKDDIKD (SEQ ID NO: 263), AGNDDDDDDDDDDDDDDDDDKKDKDDDDDD (SEQ ID NO: 264), AGNKKKKKKKNNNNNNNNNNNNNNNNNNNNNN (SEQ ID NO: 265), AGRDDDDDDDDDDDDDDDDDDDDDDDDDDD (SEQ ID NO: 26) 6) , GKSALTIQL (SEQ ID NO: 267), GKSALTI (SEQ ID NO: 268), QGQNLKYQ (SEQ ID NO: 269), ILGVLLLI (SEQ ID NO: 270), EKEGKISK (SEQ ID NO: 271), AASDFIFLVT (SEQ ID NO: 272), KELKQVASPF (SEQ ID NO: 273), KKKLINEKKE (SEQ ID NO: 274), KKCDISLQFF (SEQ ID NO: 275), KSTAGDTHLG (SEQ ID NO: 276), ATFYVAVTVP (SEQ ID NO: 277), LTIQLIQNHFVDEYDPTIEDSYRKQVVIDG (SEQ ID NO: 278) or TIQLIQNHFVDEYDPTIEDSYRKQVVIDGE (SEQ ID NO: 279).

In some embodiments, at least one of the mutant EGFR peptide sequences comprises a mutant amino acid that is not encoded by the genome of the subject's cancer cell.

In some embodiments, the mutant EGFR peptide sequences are present at a concentration of at least 1 μg/ml, at least 10 μg/ml, at least 25 μg/ml, at least 50 μg/ml, or at least 100 μg /ml.

In some embodiments, each of the mutant EGFR peptide sequences is present at a concentration of at most 5000 μg/ml, at most 2500 μg/ml, at most 1000 μg/ml, at most 750 μg/ml, at most 500 μg/ml, at most greater than 400 µg/ml or at most 300 µg/ml.

In some embodiments, each of the mutant EGFR peptide sequences is present at a concentration of 10 μg/ml to 5000 μg/ml, 10 μg/ml to 4000 μg/ml, 10 μg/ml to 3000 μg/ml, 10 μg/ml to 2000 mcg/ml, 10 mcg/ml up to 1000 mcg/ml, 25 mcg/ml up to 500 mcg/ml, or 50 mcg/ml up to 300 mcg/ml.

In some embodiments, the composition further comprises an immunomodulatory agent or adjuvant. In some embodiments, the adjuvant is polyICLC.

In one aspect, the invention relates to a pharmaceutical composition comprising:

(a) a composition comprising at least one polypeptide containing at least one mutant EGFR peptide sequence as described above, and (b) a pharmaceutically acceptable excipient.

In some embodiments, the pharmaceutical composition further comprises a pH modifier.

In some embodiments, the pharmaceutical composition is a vaccine composition.

In some embodiments, the pharmaceutical composition is aqueous.

In some embodiments, one or more of at least one polypeptide is linked through pI>5 and HYDRO >-6, pI>8 and HYDRO >-8, pI<5 and HYDRO >-5, pI>9 and HYDRO <- 8, pI >7 and HYDRO value >-5.5, pI <4.3 and -4≥HYDRO≥-8, pI>0 and HYDRO<-8, pI>0 and HYDRO >-4, or pI>4 ,3 and -4≥HYDRO≥-8, pI>0 and HYDRO>-4 or pI>4,3 and HYDRO≤-4, pI>0 and HYDRO>-4, or pI>4,3 and -4≥ HYDRO≥-9, 5≥pI≥12 and -4≥HYDRO≥-9.

In some embodiments, the pharmaceutical composition contains a pH modifier that is a base.

In some embodiments, the pH modifier is a conjugate base of a weak acid.

In some embodiments, the pH modifier is a pharmaceutically acceptable salt.

In some embodiments, the pH modifier is a dicarboxylate or tricarboxylate.

In some embodiments, the pH modifier is citric acid and/or citrate.

In some embodiments, the citrate is disodium citrate and/or trisodium citrate.

In some embodiments, the pH modifier is succinic acid and/or succinate.

In some embodiments, the succinate is disodium succinate and/or monosodium succinate.

In some embodiments, the succinate is disodium succinate hexahydrate.

In some embodiments, the pH modifier is present at a concentration of 0.1 mM - 1 mM.

In some embodiments, the pharmaceutical composition comprises a pharmaceutically acceptable carrier comprising a liquid.

In some embodiments, the pharmaceutically acceptable carrier comprises water.

In some embodiments, the pharmaceutically acceptable carrier contains sugar.

In some embodiments, the sugar contains dextrose.

In some embodiments, dextrose is present at a concentration of 1-10% w/v.

In some embodiments, the sugar contains trehalose.

In some embodiments, the sugar comprises sucrose.

In some embodiments, the pharmaceutically acceptable carrier comprises dimethyl sulfoxide (DMSO).

In some embodiments, DMSO is present at a concentration of 0.1% to 10%, 0.5% to 5%, or 1% to 3%.

In some embodiments, the pharmaceutically acceptable carrier does not contain dimethyl sulfoxide (DMSO).

In some embodiments, the pharmaceutical composition is lyophilizable.

In some embodiments, the pharmaceutical composition further comprises an immunomodulator or adjuvant.

In some embodiments, the immunomodulator or adjuvant is selected from the group consisting of poly-ICLC, 1018 ISS, aluminum salts, Amplivax, AS15, BCG, CP-870,893, CpG7909, CyaA, ARNAX, STING agonists, dSLIM, GM-CSF, IC30 , IC31, Imiquimoda, ImuFact IMP321, IS Patch, ISS, ISCOMATRIX, Juvlmmune, LipoVac, MF59, monophosphoryl lipid A, Montanida IMS 1312, Montanida ISA 206, Montanida ISA 50V, Montanida ISA-51, OK-432, OM-174, OM -197-MP-EC, ONTAK, PepTel®, vector systems, PLGA microparticles, resiquimod, SRL172, Virosome and other virus-like particles, YF-17D, VEGF trap, R848, beta-glucan, Pam3Cys and Aquila's QS21 stimulon.

In some embodiments, the immunomodulator or adjuvant comprises poly-ICLC. In some embodiments, the ratio of poly-ICLC to peptides in the pharmaceutical composition is from 2:1 to 1:10 v:v. In some embodiments, the ratio of poly-ICLC to peptides in the pharmaceutical composition is about 1:1, 1:2, 1:3, 1:4, or 1:5 v:v. In some embodiments, the ratio of poly-ICLC to peptides in the pharmaceutical composition is about 1:3 v/v.

In one aspect, the invention relates to a method of treating cancer in a subject, comprising administering to the subject a pharmaceutical composition described above.

In one aspect, the invention provides a method of treating cancer in a subject, comprising administering to a subject in need thereof, a composition comprising one or more mutant EGFR peptides, or one or more nucleic acids encoding one or more mutant EGFR peptides, wherein each mutant EGFR peptide contains at least 8 contiguous amino acids of a mutant EGFR protein containing the T790M mutation, where one or more mutant EGFR peptides have the amino acid sequence shown in table 40A-40D; wherein at least one of the one or more peptides binds with an affinity of 150 nM or less and/or a half-life of 2 hours or more to a protein encoded by, binds to, or is predicted to bind to a protein encoded by HLA-A68:02, HLA-C15 :02, HLA-A25:01, HLA-B57:03, HLA-C12:02, HLA-C03:02, HLA-A26:01, HLA-C12:03, HLA-C06:02, HLA-C03:03 , HLA-B52:01, HLA-A30:01, HLA-C02:02, HLA-C12:03, HLA-A11:01, HLA-A32:01, HLA-A02:04, HLA-A68:01, HLA -B15:09, HLA-C17:01, HLA-C03:04, HLA-B08:01, HLA-A01:01, HLA-B42:01, HLA-B57:01, HLA-B15:01, HLA-B14 :02, HLA-B37:01, HLA-A36:01, HLA-C15:02, HLA-B15:09, HLA-C12:02, HLA-B38:01, HLA-C03:03, HLA-A02:03 , HLA-B58:02, HLA-C08:01, HLA-B35:01, HLA-B40:01 and/or HLA-B35:03 allele; and where said allele is expressed by the subject.

In one aspect, the invention relates to a method of treating a cancer subject, wherein the method includes: administering to a subject in need thereof a polypeptide comprising a mutant EGFR peptide sequence, or a polynucleotide encoding a mutant EGFR peptide, wherein (a) the mutant EGFR peptide has the sequence LIMQLMPF (SEQ ID NO: 280) and the subject expresses a protein encoded by the HLA-C03:02 allele, (b) the mutant EGFR peptide has the sequence LTSTVQLIM (SEQ ID NO: 281) and the subject expresses a protein encoded by an HLA allele selected from the group consisting of: HLA-C12:03, HLA-C15:02, HLA-B57:01, HLA-B57:01, HLA-A36:01, HLA-C12:02, HLA-C03:03 and HLA-B58:02, (c ) the mutant EGFR peptide has the sequence QLIMQLMPF (SEQ ID NO: 282) and the subject expresses a protein encoded by the HLA-A26:01 allele, (d) the mutant EGFR peptide has the sequence STVQLIMQL (SEQ ID NO: 283) and the subject expresses a protein encoded by the HLA allele selected from the group consisting of: HLA-A68:02, HLA-C15:02, HLA-A25:01, HLA-B57:03, HLA-C12:02, HLA-A26:01, HLA-C12:03 , HLA-C06:02, HLA-C03:03, HLA-A30:01, HLA-C02:02, HLA-A11:01, HLA-A32:01, HLA-A02:04, HLA-A68:01, HLA -B15:09, HLA-C03:04, HLA-B38:01, HLA-B57:01, HLA-A02:03, HLA-C08:01, HLA-B35:01 and HLA-B40:01, (e) the mutant EGFR peptide has the sequence STVQLIMQLM (SEQ ID NO: 284) and the subject expresses the protein encoded by the HLA-B57:01 allele, (f) the mutant EGFR peptide has the sequence TSTVQLIMQL (SEQ ID NO: 285) and the subject expresses the protein encoded by the HLA- C15:02 allele, (g) the mutant EGFR peptide has the sequence TVQLIMQL (SEQ ID NO: 286) and the subject expresses a protein encoded by an HLA allele selected from the group consisting of: HLA-C17:01, HLA-B08:01, HLA -B42:01, HLA-B14:02, HLA-B37:01, HLA-B15:09, (h) the mutant EGFR peptide has the sequence TVQLIMQLM (SEQ ID NO: 287) and the subject expresses the protein encoded by HLA-B35:03 allele, or (i) the mutant EGFR peptide has the sequence VQLIMQLM (SEQ ID NO: 288) and the subject expresses a protein encoded by an HLA allele selected from the group consisting of HLA-B52:01, HLA-B14:02 and HLA-B37: 01.

In some embodiments, the method further includes administering a second polypeptide composition comprising at least one mutant EGFR peptide, wherein the second mutant EGFR peptide is selected from Table 40A-40D.

In one aspect, the invention relates to a method of treating cancer in a subject, where the method includes the steps of (a) identifying a first protein expressed by the subject, where the first protein is encoded by the first HLA allele of the subject, and where the first HLA allele is an HLA allele presented in any of Tables 41 -43; and (b) administering to the subject (i) a first mutant EGFR peptide, wherein the first mutant EGFR peptide is a peptide to the first HLA allele shown in any of Tables 42Ai and ii, 42B or 43, or (ii) a polynucleic acid encoding the first mutant EGFR peptide. In some embodiments, a method of treating cancer in a subject includes the steps of: identifying one or more specific HLA subtypes expressed in the subject; administering to a subject a composition comprising one or more mutant EGFR peptides described in the present invention, such as one or more peptide bonds with at least one HLA subtype expressed by the subject with an affinity of 150 nM or less and/or a half-life of 2 hours or more .

In one aspect, the invention provides a method of treating cancer in a subject, wherein the method includes the steps of (a) identifying the subject as expressing a protein encoded by an HLA-B57:01 allele of the subject's genome; (b) administering to the subject a composition comprising a peptide having the sequence STVQLIMQLM (SEQ ID NO: 289). In one embodiment, the method includes the steps of (a) identifying whether a subject expresses a protein encoded by an HLA-A26:01 allele of the subject's genome; (b) administering to a subject a composition comprising a peptide having the sequence QLIMQLMPF (SEQ ID NO: 290).

In some embodiments, an immune response is induced in a subject. In one embodiment, the immune response is a humoral response.

In some embodiments, one or more mutant EGFR peptide sequences are administered simultaneously, separately, or sequentially. In some embodiments, the second peptide is sequentially administered after a period of time sufficient for the first peptide to activate the second T cells.

In some embodiments, the cancer is selected from the group consisting of, selected from the group consisting of glioblastoma, adenocarcinoma of the lung, non-small cell lung cancer, squamous cell lung cancer, kidney cancer, head and neck cancer, ovarian cancer, cervical cancer, bladder cancer , stomach cancer, breast cancer, colon cancer, endometrial cancer and esophageal cancer.

In some embodiments, the method further includes administering at least one additional therapeutic agent or modality.

In some embodiments, the at least one additional therapeutic agent or modality is surgery, a checkpoint inhibitor, an antibody or fragment thereof, a chemotherapeutic agent, radiation, a vaccine, a small molecule, a T cell, a vector and APC, a polynucleotide, an oncolytic virus or any combination thereof. In some embodiments, the at least one additional therapeutic agent is an anti-PD-1 agent and an anti-PD-L1 agent, an anti-CTLA-4 agent, or an anti-CD40 agent. In some embodiments, the additional therapeutic agent is administered before, simultaneously with, or after the administration of the mutant EGFR peptide sequences.

In one aspect, the invention relates to a method for identifying a cancer subject as a candidate for therapy, where the method includes identifying the subject as a subject expressing a block encoded by an HLA from one of Tables 41, 42Ai, 42Aii, 42B, or 43, wherein the therapeutic agent is a mutant EGFR peptide or a nucleic acid encoding a mutant EGFR peptide, where the mutant EGFR peptide contains at least 8 contiguous amino acids of a mutant EGFR protein containing a mutation at T790, where the peptide (i) contains the T790M mutation, (ii) contains a peptide sequence from any of Tables 42Ai, 42Aii, 42B, 43, and 44 and (iii) binds to the corresponding HLA-encoded protein from one of tables 42Ai, 42Aii, 42B, 43, and 44.

In one aspect, the invention provides a method for identifying a subject as a candidate for therapy, where the method includes determining that the subject expresses a protein encoded by the HLA-B57:01 allele, wherein the therapeutic agent comprises a mutant EGFR peptide having the amino acid sequence STVQLIMQLM (SEQ ID NO: 291).

In one aspect, the invention relates to a method for identifying a subject as a candidate for therapy, where the method includes determining that the subject expresses a protein encoded by the HLA-A26:01 allele, wherein the therapeutic agent comprises a mutant EGFR peptide having the amino acid sequence QLIMQLMPF (SEQ ID NO: 292).

BRIEF DESCRIPTION OF THE DRAWINGS

The features of the present disclosure are set forth in detail in the accompanying claims. A better understanding of the characteristics and advantages of the present disclosure will be obtained with reference to the following detailed description, which sets forth illustrative embodiments employing the principles of the disclosure and the accompanying drawings, in which:

In FIG. 1 shows a typical workflow for identifying GATA3 epitopes that can induce CD8+ and/or CD4+ T cells.

In FIG. 2 shows a typical workflow for determining whether epitopes are processed and presented (top) and whether epitopes are recognized by T cells (bottom). This workflow confirms that GATA3 neoantigens have been processed and presented (determined by mass spectrometry), and GATA3 neoantigens bound to the HLA multimer can be recognized by the recombinant T cell receptor (TCR) expressed in the Jurkat cell line.

In FIG. Figure 3 shows a typical flow diagram for determining GATA3 neoORF epitopes by mass spectrometry. Batch lysis is performed to isolate the peptide, and an HLA class I pan antibody (W6/32) is used for immunoprecipitation.

In FIG. Figure 4 shows a typical flow diagram for GATA3 antigen-specific expansion of CD8+ T cells.

In FIG. Figure 5 shows a summary of experiments showing that GATA3-predicted epitopes for HLA-A02 (left), HLA-B07 (middle), and HLA-B08 (right) can be determined by mass spectrometry. In FIG. 5 discloses "HLA-A*02:01" defined peptide sequences as SEQ ID NOS 3824-3826, "HLA-B*07:02" defined peptide sequences as SEQ ID NOS 3827-3828, "HLA-B*08:01""defined peptide sequences as SEQ ID NO: 3829 and construct sequences as 3830-3832, all respectively in order of appearance.

In FIG. Figure 6 shows GATA3 neoORF. The shaded region represents a portion of the GATA3 neoORF sequence common to all patients (common region) and common to some patients (variable region).

In FIG. 7A shows the GATA3 neoORF sequence (SEQ ID NO: 2) with variable region sequence (SEQ ID NO: 3) and common region sequences (SEQ ID NO: 4).

In FIG. 7B is a diagram showing the GATA3 sequence (SEQ ID NO: 1) with the neoORF sequence (SEQ ID NO: 2) and that 3 predicted HLA-02:01 epitopes, 2 predicted HLA-B07:02 epitopes, and 1 predicted HLA-B08: 01 epitopes are determined by mass spectrometry. These data indicate that the epitopes are targetable.

In FIG. Figure 7C shows an example of an overlapping peptide (OLP) peptide design scheme throughout the GATA3 neoORF region. In FIG. 7C disclosed SEQ ID NO: 3853.

In FIG. 7D shows the exemplary amino acid sequence of the GATA3 neo ORF variable region (SEQ ID NO: 3)

In FIG. 7E shows the exemplary amino acid sequence of the general region of the GATA3 neo ORF (SEQ ID NO: 4)

FIG. 8 is a graph depicting the number of GATA3 neoORF therapeutic class I epitopes versus the proportion of patients containing these epitopes. Most patients have 4-5 epitopes.

In FIG. 9A depicts exemplary results showing antigen-specific CD8 ⁺ T cell responses to the indicated peptide (SEQ ID NO: 3834) using a PBMC sample from a human donor.

In FIG. 9B depicts exemplary results showing antigen-specific CD8 ⁺ T cell responses to the indicated peptide (SEQ ID NO: 3835) using a PBMC sample from human donors.

In FIG. 9C depicts exemplary results showing antigen-specific CD8 ⁺ T cell responses to the indicated peptides using a PBMC sample from human donors. In FIG. 9C discloses the "A02:01" sequence as SEQ ID NOS 3836-3837, the "A03:01" sequence as SEQ ID NO: 3838, the "A11:01" sequence as SEQ ID NO: 3839, the "B07:02" sequence as SEQ ID NOS 3840-3841 and "B08:01" sequence as SEQ ID NO: 3842, all respectively in order of appearance.

In FIG. 10A depicts exemplary results showing antigen-specific CD8 ⁺ T cell responses to the indicated peptides (SEQ ID NOS 3843-3845, respectively, in order of appearance) using a PBMC sample from human donors.

In FIG. 10B depicts exemplary results showing antigen-specific CD8 ⁺ T cell responses to the indicated peptides (SEQ ID NOS 3846-3848, respectively, in order of appearance) using a PBMC sample from human donors.

In FIG. 11 depicts FACS analysis of antigen-specific induction of IFNγ and TNFα levels of CD4+ cells from a healthy HLA-A02:01 donor stimulated with APCs loaded with or without GATA3 neoORF peptide.

In FIG. 12A shows that the indicated peptides were soluble at the indicated peptide concentrations in pharmaceutical compositions with 5 mM or 0.25 mM succinate, no DMSO, 5% dextrose in water (5DW) and no polyICLC.

In FIG. 12B shows that the indicated peptides were soluble at the indicated peptide concentrations in pharmaceutical compositions with 5 mM or 0.25 mM succinate, no DMSO, 5% dextrose in water (5DW) and polyICLC.

In FIG. 12C shows that the indicated peptides were soluble at the indicated peptide concentrations in pharmaceutical compositions with 5 mM or 0.25 mM succinate, no DMSO, 5% dextrose in water (5DW) and polyICLC with the indicated peptide:polyICLC ratio.

In FIG. 13 shows the amino acid sequence of the general region of GATA3 frameshift mutations (SEQ ID NO: 4).

In FIG. Figure 14 shows the Kaplan-Meier survival curve for patients in the MSK-IMPACT breast cancer dataset.

In FIG. 15 shows a simulated analysis of presented epitopes per patient.

In FIG. 16 shows an alignment of wild type GATA3 (SEQ ID NO: 3849) and mutation (SEQ ID NO: 3850) nucleotide sequences.

In FIG. 17 shows the wild-type GATA3 alignment and the amino acid sequence mutation. In FIG. 17 describe SEQ ID NOS 3851-3853, respectively, in order of appearance.

In FIG. 18 shows the GATA3 mutation-encoded plasmid map.

In FIG. 19 shows a multi-alignment region of the mutated GATA3 gene and DNA sequencing data of the mutated GATA3 plasmid construct. In FIG. 19 disclosed are SEQ ID NOS 3854-3856, respectively, in order of appearance.

In FIG. Figure 20 shows restriction enzyme digestion of the GATA3 mutation plasmid with AflII.

In FIG. 21 shows MHC class I and MHC class II GATA3 expression of transduced HEK 293T cells.

In FIG. 22A-22D show the HLA-A02 and MHC-ABC expression profile of HLA-A02.01, HLA-B07.02 and HLA-B08.01 transfected GATA3 HEK293T cells.

In FIG. 22A shows non-GATA3 HEK293T cells.

In FIG. 22B shows HLA-A02.01 GATA3 transfected HEK293T cells.

In FIG. 22C shows HLA-B07.02 GATA3 transfected HEK293T cells.

In FIG. 22D shows HLA-B08.01 GATA3 transfected HEK293T cells.

In FIG. 23 shows the determination of predicted peptide epitopes derived from the general region of the GATA3 neoORF stably expressed in HEK293T cells. Light gray and black sequence indicate the variable and common regions of GATA3 neoORF, respectively. In FIG. 23 disclosed SEQ ID NO: 3857.

In FIG. 24A shows the MS/MS spectrum for the endogenously processed peptide epitope SMLTGPPARV (SEQ ID NO: 293) (bottom) and its corresponding synthetic peptide (top).

In FIG. 24B shows a solid plot of MS/MS spectral compatibility. In FIG. 24B is disclosed by "SMLTGPPARV" as SEQ ID NO: 3858.

In FIG. 25A shows the MS/MS spectrum for the endogenously processed MLTGPPARV peptide epitope (SEQ ID NO: 294) (bottom) and its corresponding synthetic peptide (top).

In FIG. 25B shows a solid plot of spectral compatibility. In FIG. 25B is disclosed by "MLTGPPARV" as SEQ ID NO: 3859.

In FIG. 26A shows the MS/MS spectrum for the endogenously processed peptide epitope KPKRDGYMF (SEQ ID NO: 295) (bottom) and its corresponding synthetic peptide (top).

In FIG. 26B shows a solid spectral compatibility plot. In FIG. 26B is disclosed by "KPKRDGYMF" as SEQ ID NO: 3860.

In FIG. 27A shows the MS/MS spectrum for the endogenously processed peptide epitope KPKRDGYMFL (SEQ ID NO: 296) (bottom) and its corresponding synthetic peptide (top).

In FIG. 27B shows a solid plot of spectral compatibility. In FIG. 27B is disclosed by "KPKRDGYMFL" as SEQ ID NO: 3861.

In FIG. 28A shows the MS/MS spectrum for the endogenously processed peptide epitope ESKImFATL (SEQ ID NO: 297) (bottom) and its corresponding synthetic peptide (top).

In FIG. 28B shows a solid plot of spectral compatibility. In FIG. 28B is disclosed by "ESKImFATL" as SEQ ID NO: 3862.

In FIG. 29A shows typical induction of CD8+ responses with a GATA3 neoORF specific peptide (FLT-mDC GATA3 Stim2 multimer). In FIG. 29A is disclosed by "MLTGPPARV" as SEQ ID NO: 3863.

In FIG. 29 B shows a negative control without induction of CD8+ responses in PBMCs and dendritic cells. In FIG. 29B are disclosed to "MLTGPPARV" as SEQ ID NO: 3864.

In FIG. 30A shows the induction of antigen-specific CD4 T cells in the absence of peptide.

In FIG. 30B shows the induction of antigen-specific CD4 T cells with a GATA3 neoORF specific peptide.

In FIG. 31A-31D show GATA3 specific CD8+ T cells via multimer staining.

In FIG. 31A shows GATA3 specific CD8+ T cells observed at an average of 1.16% positive after long-term stimulation for healthy donor HD47.

In FIG. 31B shows GATA3 specific CD8+ T cells observed at an average of 1.29% positive after long-term stimulation for a healthy HD50 donor.

In FIG. 31C shows GATA3 specific CD8+ T cells observed at an average of 1.9% positive after long-term stimulation for a healthy HD51 donor.

In FIG. 31D shows GATA3 specific CD8+ T cells observed at an average of 4.5% positive after long-term stimulation for a healthy HD51 donor at a different peptide concentration than FIG. 31C.

In FIG. 32 shows a comparison of the Caspase-3 positive proportion of living target cells. 4 different GATA3-induced PBMCs from healthy donors 1-4 were co-cultured with GATA3 mutation-transduced HEK 293T cells (GATA3Trd) or non-transduced HEK 293T cells (NoTRd293T) as a negative control group.

In FIG. 33 shows a significant difference between GATA3 transduced HEK293T cells and non-transduced HEK293T cells.

In FIG. 34 shows the difference in CD107a expression of CD8+ T cells co-cultured with GATA3 transduced HEK293T cells and non-transduced HEK293T cells.

In FIG. 35 shows the difference in IFN-γ concentration under coculture conditions between GATA3 transduced HEK293T cells and non-transduced HEK293T cells with GATA3 induced T cells.

In FIG. 36 shows an overview of GATA3 specific TCR cloning. Details are described in example 26.

In FIG. 37 shows exemplary methods for generating GATA3 specific TCRs in transduced Jurkat and PBMC. Details are described in example 26.

In FIG. 38 shows an overview of functional analysis with TCR-transduced Jurkat.

In FIG. 39 shows GATA3 specific CD8+ T cells through multimer staining for sorting.

In FIG. 40 shows a GATA3 specific TCR construct for a lentivirus.

In FIG. 41A shows a multi-alignment of GATA3 TCR alpha sequence and wild-type DNA sequence. In FIG. 41A are described in SEQ ID NOS 3865-3868, respectively, in order of appearance.

In FIG. 41B shows a multi-alignment of GATA3 TCR beta sequence and wild type DNA sequence. In FIG. 41B are described in SEQ ID NOS 3869-3872, respectively, in order of appearance.

In FIG. 42 shows restriction enzyme digestion of the GATA3 TCR plasmid with AflII.

In FIG. 43 shows GATA3 specific TCR transduced Jurkat stained with GATA3 multimer PE and GATA3 multimer BV650.

In FIG. 44 shows a GATA3 specific TCR peptide titration assay.

In FIG. 45 shows the IL-2 GATA3 specific TCR release assay of transduced Jurkat cells and GATA3 mutation of transduced target cells.

In FIG. 46 shows the stereochemistry of a typical GATA3 neo ORF peptide. The peptide consists of 14 amino acids and the sequence ESKIMFATLQRSSL (SEQ ID NO: 298). The peptide has a molecular formula of C ₇₀ H ₁₁₉ N ₁₉ O ₂₂ S and a molecular weight of 1610.89 g/mol. The peptide is in the form of a trifluoroacetic acid (TFA) salt.

In FIG. 47 shows the stereochemistry of a typical GATA3 neo ORF peptide. The peptide consists of 16 amino acids and the sequence KPKRDGYMFLKAESKI (SEQ ID NO: 299). The peptide has a molecular formula of C ₈₇ H ₁₄₃ N ₂₃ O ₂₃ S and a molecular weight of 1911.30 g/mol. The peptide is in the form of a trifluoroacetic acid (TFA) salt.

In FIG. 48 shows the stereochemistry of a typical GATA3 neo ORF peptide. The peptide consists of 18 amino acids and the sequence SMLTGPPARVPAVPFDLH (SEQ ID NO: 300). The peptide has a molecular formula of C ₈₇ H ₁₃₇ N ₂₃ O ₂₃ S and a molecular weight of 1905.25 g/mol. The peptide is in the form of a trifluoroacetic acid (TFA) salt.

In FIG. 49 shows the stereochemistry of a typical GATA3 neo ORF peptide. The peptide consists of 21 amino acids and the sequence EPCSMLTGPPARVPAVPFDLH (SEQ ID NO: 301). The peptide has a molecular formula of C ₁₀₀ H ₁₅₆ N ₂₆ O ₂₈ S ₂ and a molecular weight of 2234.62 g/mol. The peptide is in the form of a trifluoroacetic acid (TFA) salt.

In FIG. 50 shows the stereochemistry of a typical GATA3 neo ORF peptide. The peptide consists of 25 amino acids and the sequence LHFCRSSIMKPKRDGYMFLKAESKI (SEQ ID NO: 302). The peptide has a molecular formula of C ₁₃₄ H ₂₁₇ N ₃₇ O ₃₄ S ₃ and a molecular weight of 2986.62 g/mol. The peptide is in the form of a trifluoroacetic acid (TFA) salt.

In FIG. 51 shows the stereochemistry of a typical GATA3 neo ORF peptide. The peptide consists of 26 amino acids of the sequence GPPARVPAVPFDLHFCRSSIMKPKRD (SEQ ID NO: 303). The peptide has a molecular formula of C ₁₃₁ H ₂₀₉ N ₃₉ O ₃₃ S ₂ and a molecular weight of 2922.47 g/mol. The peptide is in the form of a trifluoroacetic acid (TFA) salt.

In FIG. 52 shows the stereochemistry of a typical GATA3 neo ORF peptide. The peptide consists of 33 amino acids and the sequence KPKRDGYMFLKAESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 304). The peptide has a molecular formula of C ₁₇₃ H ₂₇₄ N ₄₈ O ₄₆ S ₄ and a molecular weight of 3890.63 g/mol. The peptide is in the form of a trifluoroacetic acid (TFA) salt.

In FIG. 53 shows BTK antigen peptide-specific CD8+ T cell responses using PBMC samples from human donors.

In FIG. 54 shows EGFR antigen peptide-specific CD8 ⁺ T cell responses using PBMC samples from human donors.

DETAILED DESCRIPTION

GATA3 is a gene overexpressed in breast cancer and one of the most frequently mutated genes in these cancers. The most common classes of mutations in this gene are insertions or deletions between nucleotides encoding amino acids 393 and 445 (the natural stop codon). When they shift the open reading frame by +1 frame, they produce an extended new reading frame (“neoORF”), resulting in at least 61 and no more than 113 amino acids that are not normally expressed in healthy cells. 61 amino acids are common to all patients (conserved region), while each patient has 0-52 additional amino acids (variable region). Therefore, the epitopes that are processed and presented from this neoORF are neoantigens that are common to all patients who harbor this same class of mutations. GATA3 neoORFs appear to be an adverse prognostic factor in breast cancer. Wild-type GATA3 is an overexpressed gene, and GATA3 neoORF retains this expression. GATA3 neoORF is translated and associated with increased risk of breast cancer.

In some embodiments, overlapping long peptides (OLPs) that cover the entire neoORF can be used to treat cancer. In some aspects, the OLPs described in the present invention have been designed to include epitopes at the ends of the peptides that simplify the processing and presentation process (since only one cleavage agent is required). In some aspects, short peptides (eg, amino acids 9-11) can be administered to a subject for cancer treatment that bind to MHC class I protein. The approaches described in the present invention can be used to target multiple antigens without the need to select patients based on their HLA composition.

In some embodiments, the peptides described in the present invention may contain a modification that may enhance immunogenicity (eg, lipidation). In some embodiments, a polynucleotide encoding a polypeptide encoded by the entire GATA3 neoORF (eg, a polybody) is provided. In some embodiments, cell therapy, such as engineered T cells expressing TCR-targeted specific epitopes, can be used to treat cancer subjects.

Synthetic long peptides (SLPs) that cover the general region of the GATA3 protein are disclosed here. These peptides are soluble in the formulations described in the present invention and are compatible with polyICLC for sc. injections. High purities and synthetic yields of one or more such peptides can be achieved by adopting pseudo-proline building blocks during solid-phase peptide synthesis (SPPS). Purification conditions for each of these peptides were also developed.

The present invention describes new immunotherapeutic agents and their use based on the discovery of neoantigens that occur after mutation events unique to an individual's tumor. Therefore, the present disclosure described in the present invention provides peptides, polynucleotides encoding peptides, and peptide binding agents that can be used, for example, to stimulate an immune response in a tumor-associated antigen or neoepitope, to create an immunogenic composition or an anticancer vaccine for use in treatment of the disease.

The following description and examples illustrate in detail embodiments of the present disclosure. It should be understood that this present description is not limited to the specific embodiments described in the present invention, and may itself vary. Those skilled in the art will appreciate that there are numerous variations and modifications of this present disclosure that are intended to be included within its scope.

All terms are intended to be understood as they would be understood by one skilled in the art. Unless otherwise defined, all technical and scientific terms used in the present invention have the same meaning as commonly understood by one skilled in the art to which the description pertains.

The section headings used in the present invention are for organizational purposes only and should not be construed as limiting the claimed subject matter.

Although various features of the present disclosure may be described in the context of a single embodiment, features may also be provided separately or in any suitable combination. Conversely, although the present disclosure may be described in the present invention in the context of separate embodiments for the sake of clarity, the present disclosure may also be implemented in a single embodiment.

The following definitions are in addition to those in the art and are specific to the current application and are not intended to apply to any related or unrelated case, such as any jointly owned patent or application. Although any methods and materials similar and equivalent to those described in the present invention may be practiced to test the present disclosure, the preferred materials and methods are described in the present invention. Accordingly, the terminology used herein is intended to describe specific embodiments only and is not intended to be limiting.

Definitions

The terminology used herein is intended to describe specific cases only and is not intended to be limiting. In this application, the use of the singular includes the plural unless specifically stated otherwise. The singular forms used herein also include the plural unless the context clearly indicates otherwise.

In this application, the use of “or” means “and/or” unless otherwise indicated. The terms “and/or” and “any combination thereof” and their grammatical equivalents as used herein may be used interchangeably. These terms can convey that any combination is specifically considered. For illustrative purposes only, the following phrases “A, B and/or C” or “A, B, C or any combination thereof” may mean “A individually; B individually; C individually; and B; B and C; and C; and A, B and C." The term "or" may be used together or separately unless the context specifically relates to the individual use.

The term “about” or “approximately” may mean within the acceptable range of error for a particular value as determined by one skilled in the art, which will depend in part on how the value is measured or determined, that is, on the limitations of the measurement system. For example, "about" may mean within 1 or more than 1 standard deviation of practice in the art. Alternatively, "about" may mean a range of up to 20%, up to 10%, up to 5%, or up to 1% of a given value. Alternatively, especially in relation to biological systems or processes, the term may mean within an order of magnitude, within a 5-fold, and more preferably, within a 2-fold. Where specific values are described in the application and claims, unless otherwise indicated, the term "about" means within the acceptable range of error for the specific value.

In this specification and claims, the words "comprising" (and any form of the word "comprising", such as "contain" and "comprises"), "having" (and any form of the word "having", such as "have" and "has "), "including" (and any form of the word "including" such as "include" and "includes") or "containing" (and any form of the word "containing" such as "contains" and "contain") are inclusive or open and do not exclude additional, not listed elements or steps of the method. It is intended that any embodiment discussed in this specification may be implemented with respect to any method or composition of the present disclosure, and vice versa. In addition, the compositions of the present description can be used to achieve the methods of the present description.

Reference in the specification to “certain embodiments,” “an embodiment,” “one embodiment,” or “other embodiments” means that the particular feature, structure, or characteristic described in connection with the embodiments is included in at least some of the embodiments implementation, but not necessarily all embodiments of the present description. To facilitate understanding of this specification, certain terms and phrases are defined below.

The “major histocompatibility complex” or “MHC” is a cluster of genes that play a role in controlling cellular interactions responsible for physiological immune responses. In humans, the MHC complex is also known as the human leukocyte antigen (HLA) complex. A detailed description of the MHC and HLA complexes is given in Paul, Fundamental Immunology, ^3rd Ed., Raven Press, New York (1993). “Major histocompatibility complex (MHC) proteins or molecules”, “MHC molecules”, “MHC proteins” or “HLA proteins” should be understood as proteins capable of binding peptides generated by the proteolytic cleavage of protein antigens and presentation of potential lymphocytic epitopes ( e.g. T -cell epitope and B-cell epitope), transporting them to the cell surface and presenting them there to specific cells, in particular cytotoxic T lymphocytes, T helper cells or B cells. The major histocompatibility complex in the genome contains a genetic region whose gene products, expressed on the cell surface, are important for the binding and presentation of endogenous and/or foreign antigens and, therefore, for the regulation of immunological processes. The major histocompatibility complex is classified into two groups of genes encoding for different proteins, namely MHC class I molecules and MHC class II molecules. The cell biology and expression profiles of the two MHC classes are tailored to these distinct roles.

“Human leukocyte antigen” or “HLA” is a class I or class II major histocompatibility complex (MHC) protein (see, e.g. , Stites, et al., Immunology, ^8th Ed., Lange Publishing, Los Altos, Calif. ( 1994).

“Polypeptide”, “peptide” and their grammatical equivalents as used herein refer to a polymer of an amino acid residue, typically L-amino acids, linked to each other, typically by peptide bonds between the α-amino and carboxyl groups of adjacent amino acids. Polypeptides and peptides include, but are not limited to, “mutant peptides,” “neoantigen peptides,” and “neoantigen peptides.” Polypeptides or peptides may be of varying lengths, either in their neutral (uncharged) forms, which are salts, or free from or contain modifications such as glycosylation, side chain oxidation or phosphorylation, provided that the modification does not destroy biological activity polypeptides described in the present invention. A “mature protein” is a protein that is full length and which optionally includes glycosylation or other modifications typical of the protein in a given cellular environment. The polypeptides and proteins described in the present invention (including functional parts and functional variants thereof) may contain synthetic amino acids in place of one or more naturally occurring amino acids. Such synthetic amino acids are known in the art and include, for example, aminocyclohexanecarboxylic acid, norleucine, α-amino n-decanoic acid, homoserine, S-acetylaminomethylcysteine, trans-3- and trans-4-hydroxyproline, 4-aminophenylalanine, 4-nitrophenylalanine , 4-chlorophenylalanine, 4-carboxyphenylalanine, β-phenylserine, β-hydroxyphenylalanine, phenylglycine, α-naphthylalanine, cyclohexylalanine, cyclohexylglycine, indoline-2-carboxylic acid, 1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid, aminomalonic acid , aminomalonic acid monoamide, N'-benzyl-N'-methyllysine, N',N'-dibenzyllysine, 6-hydroxylysine, ornithine, α-aminocyclopentanecarboxylic acid, α-aminocyclohexanecarboxylic acid, α-aminocycloheptanecarboxylic acid, α-(2-amino -2-norbornane)carboxylic acid, α,γ-diaminobutyric acid, α,β-diaminopropionic acid, homophenylalanine and α-tert-butylglycine. The present description further contemplates that the expression of the polypeptides described in the present invention in the engineered cell may be associated with post-translational modifications of one or more amino acids of the polypeptide constructs. Non-limiting examples of post-translational modifications include phosphorylation, acylation, including acetylation and formylation, glycosylation (including N-linked and O-linked), amidation, hydroxylation, alkylation, including methylation and ethylation, ubiquitination, addition of pyrrolidone carboxylic acid, disulfide bridge formation, sulfonation, myristoylation, palmitoylation, isoprenylation, farnesylation, geranylation, glyation, lipoylation and iodination.

The peptide or polypeptide may contain at least one flanking sequence. The term “flanking sequence” as used herein refers to a fragment or region of a peptide that is not part of an epitope.

An “immunogenic” peptide or “immunogenic” epitope or “peptide epitope” is a peptide that contains an allele-specific motif such that the peptide will bind an HLA molecule and induce a cell-mediated or humoral response, such as a cytotoxic T lymphocyte (CTL) response ( eg , CD8 ⁺ )), helper T lymphocyte (Th ( eg , CD4 ⁺ )) and/or B lymphocyte. Thus, the immunogenic peptides described in the present invention are capable of binding a suitable HLA molecule and then inducing a CTL (cytotoxic) response, or HTL (and humoral) response, to the peptide.

“Neoantigen” refers to tumor antigens that arise from tumor-specific changes in proteins. Neoantigens include, but are not limited to, tumor antigens that arise from, for example, protein sequence substitutions, frameshift mutations, polypeptide fusions, in-frame deletions, insertions, expression of endogenous retroviral polypeptides, and tumor-specific overexpression of polypeptides.

The term “residue” refers to an amino acid residue or amino acid residue mimetic introduced into a peptide or protein through an amide bond or amide bond mimetic, and a nucleic acid (DNA or RNA) that encodes the amino acid or amino acid mimetic.

A “neoepitope,” “tumor-specific neoepitope,” or “tumor antigen” refers to an epitope or region of an antigenic determinant that is not present in the reference, such as a non-disease cell, e.g. , a non-cancer cell or primary cell, but found in a disease cell, e.g. cancer cell. This includes situations where the corresponding epitope is found in a normal non-diseased cell or primary cell, but, due to one or more mutations in a diseased cell, for example a cancer cell, the sequence of the epitope is changed so as to produce a neo-epitope. The term “neoepitope” in the present invention refers to the region of an antigenic determinant in a peptide or neoantigenic peptide. The neoepitope may comprise at least one “anchor residue” and at least one “anchor residue flanking region”. The neo-epitope may further comprise a “separation region”. The term “anchor residue” refers to an amino acid residue that binds to specific pockets on HLA, which causes specific interaction with HLA. In some cases, the anchor residue may be in the canonical anchor position. In other cases, the anchor residue may be in a non-canonical anchor position. Neoepitopes can bind to HLA molecules through primary and secondary anchor residues projecting into pockets in the peptide binding cavities. In peptide binding cavities, certain amino acids constitute pockets in which the corresponding side chains of the anchor residues of the present neoepitopes are located. Peptide binding preferences exist among different alleles of both HLA I and HLA II molecules. HLA class I molecules bind short neoepitopes, the N- and C-termini of which are anchored in pockets located at the ends of the neoepitope binding cavities. Although most HLA class I binding neoepitopes are approximately 9 amino acids long, longer neoepitopes can be accommodated by bulging their central portion, which causes binding of neoepitopes of approximately 8–12 amino acids. Neo-epitopes that bind to HLA class II proteins are not limited in size and can range from approximately 16-25 amino acids. The neoepitope binding cavity in the HLA class II molecule is open at both ends, allowing the binding of relatively long peptides. This core segment of 9 amino acid residues is most conducive to neoepitope recognition; the flanking regions of the anchor residue are also important for the specificity of the peptide to the HLA class II allele. In some cases, the flanking region of the anchor residue is N-terminal residues. In another case, the flanking region of the anchor residue is the C-terminal residues. In yet another case, the flanking region of the anchor residue is both N-terminal residues and C-terminal residues. In some cases, the flanking region of the anchor residue is flanked by at least two anchor residues. The flanking region of the anchor residue flanked by the anchor residues is the “separation region.”

"Reference" can be used to correlate and compare results obtained in the methods of the present description on a tumor sample. Typically, the “reference” may be derived from one or more normal samples, in particular samples that are not affected by cancer, or from a patient or one or more different individuals, for example healthy individuals, in particular individuals of the same species. The "link" can be determined empirically by testing a sufficiently large number of normal samples.

An “epitope” is the collective characteristic of a molecule, such as primary, secondary and tertiary peptide structure, and charge, which together form a site recognized by, for example, an immunoglobulin, T-cell receptor, HLA molecule or chimeric antigen receptor. Alternatively, an epitope may be defined as a set of amino acid residues that are involved in recognition by a particular immunoglobulin, or, in the context of T cells, residues that are required for recognition by T cell receptor proteins, chimeric antigen receptors and/or major histocompatibility complex (MHC) receptors. ). A “T cell epitope” should be understood to mean a peptide sequence that can be bound by MHC class I or class II molecules in the form of MHC peptide-presenting molecules or MHC complex, and then, in this form, be recognized and bound by T cells such as as T lymphocytes or T helper cells. Epitopes can be obtained by isolation from a natural source, or they can be synthesized according to standard protocols in the art. Synthetic epitopes may contain artificial amino acid residues, “amino acid mimetics,” such as D isomers of naturally occurring L amino acid residues or non-naturally occurring amino acid residues such as cyclohexylalanine. In the present description, epitopes may be referred to in some cases as peptides or peptide epitopes. It should be understood that proteins or peptides that contain an epitope or analogue described in the present invention, as well as additional amino acid(s), are still included within the scope of the present description. In certain embodiments, the peptide contains an antigen fragment. In certain embodiments, there is a limitation on the length of the peptide of the present disclosure. A length-limited embodiment exists when the protein or peptide containing an epitope described in the present invention contains a region ( ie , a contiguous series of amino acid residues) having 100% identity to the parent sequence. To avoid defining an epitope from reads, for example on complete natural molecules, there is a limit on the length of any region that has 100% identity with the original peptide sequence. Thus, for a peptide containing an epitope described in the present invention and a region with 100% identity to the original peptide sequence, the region with 100% identity to the original peptide sequence typically has a length of: less than or equal to 600 amino acid residues, less than or equal to 500 amino acid residues, less than or equal to 400 amino acid residues, less than or equal to 250 amino acid residues, less than or equal to 100 amino acid residues, less than or equal to 85 amino acid residues, less than or equal to 75 amino acid residues, less than or equal to 65 amino acid residues residues, and less than or equal to 50 amino acid residues. In certain embodiments, an “epitope” described in the present invention consists of a peptide having a region of less than 51 amino acid residues that has 100% identity with the original peptide sequence, in any increment of 5 amino acid residues; for example 50, 49, 48, 47, 46, 45, 44, 43, 42, 41, 40, 39, 38, 37, 36, 35, 34, 33, 32, 31, 30, 29, 28, 27, 26 , 25, 24, 23, 22, 21, 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2 or 1 amino acid residues.

The nomenclature used to describe peptides or proteins follows the general practice of having an amino group on the left (amino or N terminus) and a carboxyl group on the right (carboxy or C terminus) of each amino acid residue. When amino acid positions are mentioned in a peptide epitope, they are numbered in the amino to carboxyl direction, where position one is located at the amino terminus of the epitope, or the peptide or protein of which it may be a member. In the formula representing selected specific embodiments of the present disclosure, the amino and carboxyl terminal groups, although not specifically shown, are in the form that they would take at physiological pH unless otherwise indicated. In an amino acid structure formula, each residue is usually represented by standard three-letter or one-letter symbols. The L-form of an amino acid residue is represented by a capital letter or a capital letter of a tri-letter symbol, and the D-form for those amino acid residues that have D-forms is represented by a single lowercase letter or a lowercase tri-letter symbol. However, if three-letter symbols or full names are used without capitalization, they may refer to L amino acid residues. Glycine has no asymmetric carbon atom and is simply designated “Gly” or “G.” The amino acid sequences of the peptides provided in the present invention are generally designated using standard alphabetic symbols. (A, Alanine; C, Cysteine; D, Aspartic acid; E, Glutamic acid; F, Phenylalanine; G, Glycine; H, Histidine; I, Isoleucine; K, Lysine; L, Leucine; M, Methionine; N, Asparagine ; P, Proline; Q, Glutamine; R, Arginine; S, Serine; T, Threonine; V, Valine; W, Tryptophan; and Y, Tyrosine.)

The term “mutation” refers to a change or difference in the nucleic acid sequence (nucleotide substitution, addition or deletion) compared to the reference. A “somatic mutation” can occur in any cell of the body except germ cells (sperm and eggs), and is therefore passed on to children. These changes (but not always) cause cancer or other diseases. In some embodiments, the mutation is a non-nonsense mutation. The term “non-nonsense mutation” refers to a mutation, such as a nucleotide substitution, that is not caused by an amino acid change, such as an amino acid substitution in the translation product. A “frameshift” occurs when a mutation interrupts the normal phase of codon periodicity of a gene (also known as the “reading frame”), causing translation of a non-natural protein sequence. For different mutations in a gene, it is possible to achieve the same altered reading frame.

A “conservative” amino acid substitution is one in which one amino acid residue is replaced by another amino acid residue that has a similar side chain. Families of amino acid residues having similar side chains are defined in the art, including basic side chains ( e.g. lysine, arginine, histidine), acidic side chains ( e.g. aspartic acid, glutamic acid), unchanged polar side chains ( e.g. glycine, asparagine, glutamine, serine, threonine, tyrosine, cysteine), non-polar side chains ( e.g. alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine, tryptophan), beta-branched side chains ( e.g. threonine, valine , isoleucine) and aromatic side chains ( eg tyrosine, phenylalanine, tryptophan, histidine). For example, replacing phenylalanine with tyrosine is a conservative substitution. Methods for identifying nucleotide and amino acid conservative substitutions that do not eliminate peptide function are well known in the art.

In the present invention, the term “affinity” refers to a measure of the strength of binding between two members of a binding pair, for example, an HLA binding peptide and an HLA class I or II. K _D is the dissociation constant and is measured in molarity units. The affinity constant is the reciprocal of the dissociation constant. Affinity constant is sometimes used as a general term to describe this chemical structural unit. It is a direct measure of binding energy. Affinity can be determined experimentally, for example by surface plasmon resonance (SPR) using commercially available Biacore SPR units. Affinity can also be expressed as inhibitory concentration 50 (IC ₅₀ ), that is, the concentration at which 50% of the peptide is replaced, ln(IC ₅₀ ) refers to the natural logarithm of IC ₅₀ . K _off refers to the dissociation rate constant, for example for the dissociation of HLA binding peptide and HLA class I or II. In this description, the results of “binding data” can be expressed as “IC ₅₀ . “IC ₅₀ is the concentration of a tested peptide in a binding assay at which 50% inhibition of binding of the labeled reference peptide is observed. Under the conditions under which the assays are performed ( i.e. , limiting HLA protein and tagged reference peptide concentrations), these values mimic _KD values. Assays for determining binding are known in the art and are described in detail, for example, in PCT publications WO 94/20127 and WO 94/03205, and other publications such as Sidney et al., Current Protocols in Immunology 18,3,1 (1998 ); Sidney, et al., J. Immunol. 154:247 (1995); and Sette, et al., Mol. Immunol. 31:813 (1994). Alternatively, binding may be expressed relative to binding to a reference standard peptide. For example, may be based on their IC ₅₀ compared to the IC ₅₀ of a reference standard peptide. Binding can also be determined using other assay systems, including those using: living cells ( eg , Ceppellini et al., Nature 339:392 (1989); Christnick et al., Nature 352:67 (1991); Busch et al., Nature 352:67 (1991); al., Int. Immunol. 2:443 (1990); Hill et al., J. Immunol. 147:189 (1991); del Guercio et al., J. Immunol. 154:685 (1995)), not containing cell system using wash lysates ( eg , Cerundolo et al., J. Immunol. 21:2069 (1991)) immobilized purified MHC ( eg , Hill et al., J. Immunol. 152, 2890 (1994); Marshall et al., J. Immunol. 152, 2890 (1994); al., J. Immunol. 152:4946 (1994)), ELISA systems ( eg , Reay et al., EMBO J. 11:2829 (1992)), surface plasmon resonance ( eg , Khilko et al., J. Biol Chem. 268:15425 (1993)); high-flux soluble phase assays (Hammer et al., J. Exp. Med. 180:2353 (1994)) and measurements of MHC class I stabilization or assembly ( eg , Ljunggren et al., Nature 346:476 (1990) ; Schumacher et al., Cell 62:563 (1990); Townsend et al., Cell 62:285 (1990); Parker et al., J. Immunol. 149:1896 (1992)). “Cross-reactive binding” means that the peptide is bound by more than one HLA molecule; synonymous with degenerate binding.

The term “derived” and its grammatical equivalents, when used in a discussion of an epitope, is a synonym for “derived” and its grammatical equivalents. The derived epitope can be isolated from a natural source, or it can be synthesized according to standard protocols in the art. Synthetic epitopes may contain artificial amino acid residues “amino acid mimetics”, such as D isomers of naturally occurring L amino acid residues or non-naturally occurring amino acid residues such as cyclohexylalanine. The derived or derived epitope may be an analogue of a naturally occurring epitope.

A “natural” or “wild type” sequence refers to a sequence found in nature. Such a sequence may contain longer sequences in nature.

“Receptor” should be understood to mean a biological molecule or group of molecules capable of binding a ligand. A receptor can serve to transmit information in a cell, cellular formation, or organism. The receptor contains at least one receptor unit, for example, where each receptor unit may consist of a protein molecule. The receptor has a structure that is complementary to the structure of the ligand and can form a complex with the ligand as a binding partner. Information is transmitted, in particular, by conformational changes in the receptor after complexation of the ligand on the cell surface. In some embodiments, receptor is understood to mean, in particular, MHC class I and II proteins capable of forming a receptor/ligand complex with a ligand, particularly a peptide or peptide fragment of suitable length.

“Ligand” is understood to mean a molecule that has a structure complementary to that of a receptor and is capable of forming a complex with that receptor. In some embodiments, a ligand is understood to mean a peptide or peptide fragment that has a suitable length and suitable binding motifs in its amino acid sequence such that the peptide or peptide fragment is capable of forming a complex with MHC class I or MHC class II proteins.

In some embodiments, “receptor/ligand complex” is also understood to mean “receptor/peptide complex” or “receptor/peptide fragment complex,” including a peptide or peptide fragment presenting MHC class I or class II molecule.

“Synthetic peptide” refers to a peptide that is obtained from a non-natural source, such as man-made. Such peptides can be obtained using methods such as chemical synthesis or recombinant DNA technology. “Synthetic peptides” include “fusion proteins.”

The term “motif” refers to a pattern of residues in an amino acid sequence of a certain length, e.g., a peptide less than about 15 amino acid residues long, or less than about 13 amino acid residues long, e.g., from about 8 to about 13 amino acid residues ( e.g. , 8, 9 , 10, 11, 12, or 13) for HLA class I motif and from about 6 to about 25 amino acid residues ( e.g. , 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, or 25) for an HLA class II motif that is recognized by a specific HLA molecule. The motifs are usually different for each HLA protein encoded by a given human HLA allele. These motifs are distinguished by their pattern of primary and secondary anchor residues. In some embodiments, the MHC class I motif defines a peptide of 9, 10, or 11 amino acid residues in length.

The term “existing in nature” and its grammatical equivalents in the present invention refers to the fact that an object can be found in nature. For example, a peptide or nucleic acid that is present in an organism (including viruses) and can be isolated from a source in nature, and that is not intentionally modified by humans, is naturally occurring.

As used herein, the term “vaccine” refers to a pharmaceutical composition or product that, when administered, elicits an immune response, such as a cellular or humoral immune response, that recognizes and attacks a pathogen or disease cell, such as a cancer cell. The vaccine can be used to prevent or treat a disease. The term “individualized cancer vaccine” or “personalized cancer vaccine” refers to a specific cancer patient and means that a cancer vaccine is tailored to the needs or special circumstances of an individual cancer patient.

“Antigenic processing” or “processing” and its grammatical equivalents refers to the decomposition of a polypeptide or antigen into processing products that are fragments of said polypeptide or antigen ( e.g. , decomposition of a polypeptide into peptides) and the association of one or more such fragments ( e.g. , through binding) with MHC molecules for presentation by cells, such as antigen presenting cells, to specific T cells.

“Antigen presenting cells” (APC) are cells that present peptide fragments of protein antigens in association with MHC molecules on their cell surface. Some APCs can activate antigen-specific T cells. Professional antigen presenting cells are very efficient at taking up antigen, either by phagocytosis or receptor-mediated endocytosis, and then displaying a fragment of the antigen bound to an MHC class II molecule on their membrane. The T cell recognizes and interacts with the antigen-MHC class II molecule complex on the membrane of the antigen-presenting cell. An additional co-stimulatory signal is then produced by the antigen-presenting cell, resulting in T cell activation. Expression of costulatory molecules is a defining feature of professional antigen-presenting cells. The major types of professional antigen presenting cells include dendritic cells, which have the widest range of antigen presentation and are probably the most important antigen presenting cells, macrophages, B cells, and certain activated epithelial cells. Dendritic cells (DC) are populations of leukocytes that present antigens taken up from peripheral tissues to T cells via the MHC class I and II antigen-presenting pathways. It is well known that dendritic cells are potent instigators of immune responses, and activation of these cells is a critical step for the induction of antitumor immunity. Dendritic cells are conveniently divided into categories of “immature” and “mature” cells, which can be used as a simple way to distinguish between two well-characterized phenotypes. However, this nomenclature should not be considered as excluding all possible intermediate stages of differentiation. Immature dendritic cells are characterized as antigen-presenting cells with a high capacity for antigen uptake and processing, which correlates with high expression of Fc receptor (FcR) and mannose receptor. The mature phenotype is typically characterized by lower expression of these markers but high expression of cell surface molecules responsible for T cell activation, such as MHC class I and class II, adhesion molecules ( e.g. CD54 and CD11) and co-stimulatory molecules ( e.g. CD40, CD80 , CD86 and 4-1 BB).

The terms “identical” and its grammatical equivalents as used herein, or “sequence identity” in the context of two nucleic acid sequences or polypeptide amino acid sequences, refers to residues in two sequences that are the same when aligned for maximum agreement within a specified comparison window. A “comparison window” in the present invention refers to a segment of at least about 20 contiguous positions, typically from about 50 to about 200, more typically from about 100 to about 150, where the sequence can be compared to a reference sequence with the same number of contiguous positions field optimal alignment of two sequences. Methods for aligning sequences for comparison are well known in the art. Optimal alignment of sequences for comparison can be made using the local homology algorithm from Smith and Waterman, Adv. Appl. Math., 2:482 (1981); alignment algorithm from Needleman and Wunsch, J. Mol. Biol., 48:443 (1970); similarity search from Pearson and Lipman, Proc. Nat. Acad. Sci. USA, 85:2444 (1988); computerized implementations of these algorithms (including, but not limited to, CLUSTAL in the PC/Gene program from Intelligentics, Mountain View Calif., GAP, BESTFIT, BLAST, FASTA and TFASTA in the Wisconsin Genetics Software Package, Genetics Computer Group (GCG), 575 Science Dr., Madison, Wis., USA); the CLUSTAL program is well described in Higgins and Sharp, Gene, 73:237-244 (1988) and Higgins and Sharp, CABIOS, 5:151-153 (1989); Corpet et al., Nucleic Acids Res., 16:10881-10890 (1988); Huang et al., Computer Applications in Biosciences, 8:155-165 (1992); and Pearson et al., Methods in Molecular Biology, 24:307-331 (1994). Alignment is often done through inspection and manual alignment. In one class of embodiments, the polypeptides in the present invention have at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88% 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to a reference polypeptide or fragment thereof, e.g. , as determined by BLASTP (or CLUSTAL, or any other available alignment program), using default parameters. Also, nucleic acids can also be described with reference to the parent nucleic acid, for example they can have 50%, 60%, 70%, 75%, 80%, 85%, 90%, 98%, 99% or 100% identity sequence with a reference nucleic acid or fragment thereof, e.g. as determined by BLASTN (or CLUSTAL, or any other available alignment program) using default parameters. If one molecule is said to have a certain percentage of sequence identity with a larger molecule, it means that when two molecules are optimally aligned, that specified percentage of residues in the smaller molecule are the same as residues in the larger molecule according to the order in which the two molecules are optimally aligned.

The term “substantially identical” and its grammatical equivalents, when applied to nucleic acid or amino acid sequences, means that the nucleic acid or amino acid sequence contains a sequence that has at least 90% sequence identity or more, at least 95%, or at least at least 98% and at least 99%, compared to the reference sequence using the programs described above, for example , BLAST, using standard parameters. For example, the BLASTN program (for nucleotide sequences) uses as default parameters a word length (W) of 11, an expectation (E) of 10, M=5, N=-4, and comparison of both strands. For amino acid sequences, the BLASTP program uses as default parameters a word length (W) of 3, an expectation (E) of 10, and a BLOSUM62 substitution matrix (see Henikoff & Henikoff, Proc. Natl. Acad. Sci. USA 89:10915 (1992 )). The proportion of sequence identity is determined by comparing two optimally aligned sequences in the comparison window, where a portion of the polynucleotide sequence in the comparison window may contain additions or deletions ( i.e. , gaps) compared to the reference sequence (which does not contain additions or deletions) for the optimal alignment of the two sequences. The proportion is calculated by determining the number of positions at which an identical nucleic acid base or amino acid residue exists in both sequences to obtain the number of matching positions, dividing the number of matching positions by the total number of positions in the comparison window, and multiplying the result by 100 to obtain the percentage of sequence identity. In embodiments, substantially identical sequences exist over a region of sequences that is at least about 50 residues in length, over a region of at least about 100 residues, and in embodiments, sequences that are substantially identical over at least about 150 residues . In embodiments, the sequences are substantially identical throughout the entire length of the coding regions.

The term “vector” as used herein means a construct that is capable of delivering and typically expressing one or more genes or sequences of interest in host cells. Examples of vectors include, but are not limited to, viral vectors, naked DNA or RNA expression vectors, plasmid, cosmid or phage vectors, DNA or RNA expression vectors associated with cationic condensing agents, and DNA or RNA expression vectors encapsulated in liposomes.

A polypeptide, antibody, polynucleotide, vector, cell or composition that is “isolated” is a polypeptide, antibody, polynucleotide, vector, cell or composition that is in a form not found in nature. Isolated polypeptides, antibodies, polynucleotides, vectors, cells or compositions include those that have been purified to the extent that they no longer have the form in which they occur naturally. In some embodiments, the polypeptide, antibody, polynucleotide, vector, cell, or composition that is isolated is substantially pure. In some embodiments, “isolated polynucleotide” encompasses a PCR or qPCR reaction comprising the polynucleotide amplified in the PCR or qPCR reaction.

The term “isolated,” “biologically pure,” or their grammatical equivalents refers to a material that is substantially or substantially free of components that would normally accompany the material in its original state. Thus, the isolated peptides described in the present invention do not contain some or all of the materials typically associated with peptides in their in situ environment. An “isolated” epitope refers to an epitope that does not include the entire sequence of the antigen from which the epitope is derived. Typically, an “isolated” epitope does not have additional amino acid residues attached to it that produce a sequence that has 100% identity over the entire length of the original sequence. The starting sequence may be a sequence, such as a tumor-associated antigen, from which the epitope is derived. Thus, the term “isolated” means that the material is removed from its original environment ( eg the natural environment, if it exists in nature). An “isolated” nucleic acid is a nucleic acid that has been removed from its natural environment. For example, a naturally occurring polynucleotide or peptide present in a living animal is not isolated, but the same polynucleotide or peptide separated from some or all of its coexisting materials in a natural system is isolated. Such a polynucleotide may be part of a vector, and/or such a polynucleotide or peptide may be part of a composition and still be “isolated” in the sense that such a vector or composition is not part of its natural environment. Isolated RNA molecules include in vivo or in vitro RNA transcripts of DNA molecules described in the present invention, and additionally include such molecules produced synthetically.

The term “substantially purified” and its grammatical equivalents as used herein refers to a nucleic acid sequence, polypeptide, protein or other compound that is substantially free, i.e. , does not contain more than about 50%, does not contain more than about 70%, does not contain more than about 90% of the polynucleotides, proteins, polypeptides and other molecules with which it is associated in nature.

The term “substantially pure” in the present invention refers to a material that is at least 50% pure ( i.e. , free of impurities), at least 90% pure, at least 95% pure, at least 98% pure, or at least 99% pure.

The terms “polynucleotide”, “nucleotide”, “nucleic acid”, “polynucleic acid” or “oligonucleotide” and their grammatical equivalents are used interchangeably in the present invention and refer to polymers of nucleotides of any length, and includes DNA and RNA, such as mRNA. Thus, these terms include double-stranded and single-stranded DNA, triple-stranded DNA, and double-stranded and single-stranded RNA. They also include modified, for example by methylation and/or capping, and unmodified forms of the polynucleotide. The term also includes molecules that include non-naturally occurring or synthetic nucleotides, as well as nucleotide analogues. Nucleic acid sequences and vectors disclosed or contemplated in the present invention can be introduced into a cell, for example, by transfection, transformation or transduction. Nucleotides can be deoxyribonucleotides, ribonucleotides, modified nucleotides or bases and/or analogs thereof, or any substrate that can be introduced into a polymer by DNA or RNA polymerases. In some embodiments, the polynucleotide and nucleic acid may be in vitro transcribed mRNA. In some embodiments, the polynucleotide that is administered using the methods of the present disclosure is mRNA.

“Transfection,” “transformation,” or “transduction” as used herein refers to the introduction of one or more exogenous polynucleotides into a host cell using physical or chemical means. Many transfection techniques are known in the art and include, for example, co-precipitation of calcium phosphate and DNA (see, for example , Murray EJ (ed.), Methods in Molecular Biology, Vol. 7, Gene Transfer and Expression Protocols, Humana Press ( 1991)); DEAE-dextran; electroporation; cationic liposome-mediated transfection; tungsten-enhanced microparticle bombardment (Johnston, Nature, 346: 776-777 (1990)); and co-precipitation of strontium phosphate and DNA (Brash et al., Mol. Cell Biol., 7: 2031-2034 (1987)). Phage or viral vectors can be introduced into host cells following growth of infectious particles in suitable packaging cells, many of which are commercially available.

Nucleic acids and/or nucleic acid sequences are “homologous” when they are derived, naturally or artificially, from known ancestral nucleic acids or nucleic acid sequences. Proteins and/or protein sequences are “homologous” when the DNA encoding them is derived, naturally or artificially, from known ancestral nucleic acids or nucleic acid sequences. Homologous molecules may be called homologues. For example, any naturally occurring proteins, such as those described in the present invention, can be modified by any available mutagenesis method. When expressed, such mutagenized nucleic acids encode a polypeptide that is homologous to the protein encoded by the original nucleic acid. Homology is usually inferred from sequence identity between two or more nucleic acids or proteins (or sequences thereof). The exact percentage of identity between the sequences that are used to establish homology depends on the nucleic acid and protein in question, but at least 25% sequence identity is typically used to establish homology. Higher levels of sequence identity, e.g. 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95% or 99% or more, can also be used to establish homology. Methods for determining proportions of sequence identity ( eg , BLASTP and BLASTN using default parameters) are described in the present invention and are generally available.

The term "subject" refers to any animal ( e.g. , mammal), including, but not limited to, humans, non-human primates, dogs, cats, rodents, and the like, that are subject to specific treatment. Typically, the terms "subject" and "patient" are used interchangeably herein to refer to a person.

The term "effective amount", "therapeutically effective amount" or "therapeutic effect" refers to an amount of a therapeutic agent effective to "treat" a disease or disorder in a subject or mammal. A therapeutically effective amount of a drug has a therapeutic effect and as such can prevent the development of a disease or disorder; slow the progression of a disease or disorder; slow the progression of a disease or disorder; relieve to some extent one or more symptoms associated with a disease or disorder; reduce morbidity and mortality; improve quality of life; or a combination of such effects.

The term “treating” or “treating” or “treating” or “alleviating” or “alleviating” refers to both (1) therapeutic measures that cure, slow, reduce symptoms and/or stop the progression of a diagnosed pathological condition or disorder; and (2) prophylactic or preventive measures that prevent or slow the development of the target pathological condition or disorder. Thus, those who need treatment include those who already have the disorder; prone to disorder; and those in whom disorder must be prevented.

"Pharmaceutically acceptable" refers to a generally non-toxic, inert and/or physiologically compatible composition or composition component.

A "pharmaceutical excipient" or "excipient" contains material such as an adjuvant, a carrier, pH adjusters and buffering agents, tonicity adjusting agents, wetting agents, preservatives and the like. "Pharmaceutical excipient" is an excipient that is pharmaceutically acceptable.

Neoantigens and their applications

One of the critical barriers to the development of curative and tumor-specific immunotherapies is the identification and selection of highly specific and limited tumor antigens in order to avoid autoimmunity. Tumor neoantigens, which arise from genetic alteration ( eg , insertions, translocations, deletions, missense mutations, splice site mutations, etc.) in malignant T cells, represent the most tumor-specific class of antigens. Neoantigens are rarely used in cancer vaccines or immunogenic compositions due to technical difficulties in identifying them, selecting optimized antigens, and producing neoantigens for use in a vaccine or immunogenic composition. These problems can be addressed by: identifying mutations in neoplasms/tumors that are present at the DNA level in the tumor, but not in matched parent cell samples from a significant proportion of cancer subjects; analyzing identified mutations using one or more peptide-MHC binding prediction algorithms to generate multiple neoantigen T cell epitopes that are expressed in the neoplasm/tumor and that are associated with a significant proportion of the patient's HLA alleles; and synthesizing a plurality of neoantigenic peptides selected from the pluralities of all neoantigenic peptides and predicted binding peptides for use in a cancer vaccine or immunogenic composition suitable for treating a significant proportion of cancer subjects.

For example, translation of peptide sequencing information into a therapeutic vaccine may involve predicting mutated peptides that may be bound by HLA molecules in a significant proportion of individuals. Effective selection of which specific mutations to use as an immunogen requires the ability to predict which mutated peptides will bind effectively to the HLA alleles of a significant proportion of patients. Recently, neural network learning approaches with validated binding and non-binding peptides have improved the accuracy of prediction algorithms for major HLA-A and -B alleles. However, even with the use of advanced neural network-based algorithms to encode HLA peptide binding rules, several factors limit the ability to predict peptides presented on HLA alleles.

Another example of translating peptide sequencing information into a therapeutic vaccine would involve drug formulation as a multi-epitope long peptide vaccine. Targeting as many mutated epitopes as possible maximizes the enormous capabilities of the immune system, prevents the possibility of immune evasion through down-modulation of the immune targeted gene product, and compensates for the known inaccuracy of epitope prediction approaches. Synthetic peptides provide a useful means for efficiently producing multiple immunogens and for rapidly translating the identification of mutant epitopes into an effective vaccine. Peptides can be easily synthesized chemically and easily purified using reagents that do not contain contaminating bacteria or animal substances. The small size allows clear focus on the mutated region of the protein, and also reduces irrelevant antigenic competition from other components (antigens of the non-mutated protein or viral vector).

Another example of translating peptide sequencing information into a therapeutic vaccine could involve combination with a potent vaccine adjuvant. Effective vaccines may require a strong adjuvant to trigger an immune response. For example, poly-ICLC, an agonist of TLR3 and the RNA helicase domains MDA5 and RIG3, has shown some desirable properties for a vaccine adjuvant. These properties include induction of local and systemic activation of immune cells in vivo , production of stimulatory chemokines and cytokines, and promotion of antigen presentation by DCs. Moreover, poly-ICLC can induce robust CD4 ⁺ and CD8 ⁺ responses in humans. Importantly, striking similarities in the activation of transcriptional and signal transduction pathways were observed in subjects vaccinated with poly-ICLC and in volunteers receiving a highly efficacious replication-competent yellow fever vaccine. Moreover, >90% of ovarian carcinoma patients immunized with poly-ICLC in combination with NYESO-1 peptide vaccine (in addition to Montanide) showed induction of CD4 ⁺ and CD8 ⁺ T cells, as well as antibody responses to the peptide in recent phase 1 research. In contrast, poly-ICLC has been extensively tested in over 25 clinical studies to date and has shown a relatively benign toxicity profile.

In some aspects, the invention provides a composition comprising: a first peptide containing a first neo-epitope of a protein and a second peptide containing a second neo-epitope of the same protein, a polynucleotide encoding a first peptide and a second peptide, one or more APCs containing a first peptide and a second peptide, or a first T cell receptor (TCR) specific for the first neoepitope in complex with an HLA protein, and a second TCR specific for the second neoepitope in complex with an HLA protein; where the first peptide is different from the second peptide, and where the first neoepitope contains a mutation and the second neoepitope contains the same mutation.

In some aspects, the invention relates to a composition comprising: a first peptide containing a first neoepitope of a region of a protein, and a second peptide containing a second neoepitope of a region of the same protein, wherein the first neoepitope and the second neoepitope contain at least one amino acid of the region that is the same polynucleotide , encoding a first peptide and a second peptide, or multiple APCs containing a first peptide and a second peptide, or a first T-cell receptor (TCR) specific for a first neoepitope in complex with an HLA protein, and a second TCR specific for a second neoepitope, in complex with HLA protein; where the first peptide is different from the second peptide, and where the first neoepitope contains a first mutation and the second neoepitope contains a second mutation.

In some embodiments, the first mutation and the second mutation are the same. In some embodiments, the first peptide and the second peptide are different molecules. In some embodiments, the first neoepitope comprises a first neoepitope region of the same protein, where the second neoepitope comprises a second neoepitope region of the same protein. In some embodiments, the first neoepitope and the second neoepitope contain at least one amino acid region that is the same. In some embodiments, the protein region comprises at least 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28 , 29, 30, 40, 50, 60,70, 80, 90, 100, 150, 200, 250, 300, 350, 400, 450, 500, 600, 700, 800, 900 or 1000 continuous amino acids of protein. In some embodiments, the protein region contains at most 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 40, 50, 60,70, 80, 90, 100, 150, 200, 250, 300, 350, 400, 450, 500, 600, 700, 800, 900 or 1000 continuous amino acids of protein. In some embodiments, the first neoepitope binds to an HLA class I protein to form an HLA-class I peptide complex. In some embodiments, the second neo-epitope binds to an HLA class II protein to form an HLA-class II peptide complex. In some embodiments, the second neoepitope binds to an HLA class I protein to form an HLA-class I peptide complex. In some embodiments, the first neo-epitope binds to an HLA class II protein to form an HLA-class II peptide complex. In some embodiments, the first neoepitope is a first neoepitope peptide processed from the first peptide, and/or the second neoepitope is a second neoepitope peptide processed from the second peptide. In some embodiments, the first neoepitope is shorter in length than the first peptide and/or the second neoepitope is shorter in length than the second peptide. In some embodiments, the first neo-epitope peptide is processed by an antigen presenting cell (APC) containing the first peptide, and/or the second neo-epitope peptide is processed by an APC containing the second peptide. In some embodiments, the first neoepitope activates CD8 ⁺ T cells. In some embodiments, the second neo-epitope activates CD4 ⁺ T cells. In some embodiments, the second neo-epitope activates CD8 ⁺ T cells. In some embodiments, the first neoepitope activates CD4 ⁺ T cells. In some embodiments, the CD4 ⁺ T cell TCR binds to an HLA class II peptide complex containing a first or second peptide. In some embodiments, the CD8 ⁺ T cell TCR binds to an HLA-class I peptide complex containing a first or second peptide. In some embodiments, the CD4 ⁺ T cell TCR binds to an HLA-class I peptide complex containing a first or second peptide. In some embodiments, the CD8 ⁺ T cell TCR binds to an HLA class II peptide complex containing a first or second peptide. In some embodiments, the one or more APCs comprise a first APC containing a first peptide and a second APC containing a second peptide. In some embodiments, the mutation is selected from the group consisting of a point mutation, a splice site mutation, a frameshift mutation, a read-through mutation, a gene fusion mutation, and any combination thereof. In some embodiments, the first neoepitope and the second neoepitope comprise a sequence encoded by a gene from table 1 or 2. In some embodiments, the protein is encoded by a gene from table 1 or 2. In some embodiments, the mutation is a mutation from column 2 of table 1 or 2 In some embodiments, the protein is GATA3. In some embodiments, the first neoepitope and the second neoepitope comprise a sequence encoded by a gene from Table 34 or Table 36. In some embodiments, the protein is encoded by a gene from Table 34 or Table 36. In some embodiments, the mutation is a mutation from column 2 of Table 34 or Table 36. In some embodiments, the protein is BTK. In some embodiments, the first neoepitope and the second neoepitope comprise a sequence encoded by a gene from Table 40A-40D. In some embodiments, the protein is encoded by a gene from table 3 or 35. In some embodiments, the mutation is a mutation from column 2 of table 3 or 35. In some embodiments, the protein is EGFR. In some embodiments, a single polypeptide comprises a first peptide and a second peptide, or a single polynucleotide encodes a first peptide and a second peptide. In some embodiments, the first peptide and the second peptide are encoded by a sequence transcribed from the same transcription start site. In some embodiments, the first peptide is encoded by a sequence transcribed from a first transcription start site, and the second peptide is encoded by a sequence transcribed from a second transcription start site. In some embodiments, one polypeptide is at least 18 in length; 19; 20; 21; 22; 23; 24; 25; 26; 27; 28; 29; thirty; 40; 50; 60;70; 80; 90; 100; 150; 200; 250; 300; 350; 400; 450; 500; 600; 700; 800; 900; 1000; 1500; 2000; 2500; 3000; 4000; 5000; 7500; or 10,000 amino acids. In some embodiments, the polypeptide contains a first sequence of at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72 %, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to the first corresponding wild-type sequence; and a second sequence with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74 %, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to the corresponding second wild-type sequence. In some embodiments, the polypeptide contains a first sequence of at least 8 or 9 contiguous amino acids with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69 %, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to the first corresponding wild-type sequence; and a second sequence of at least 16 or 17 contiguous amino acids with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71 %, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to the corresponding wild-type second sequence. In some embodiments, the second peptide is longer than the first peptide. In some embodiments, the first peptide is longer than the second peptide. In some embodiments, the first peptide has a length of at least 9; 10; eleven; 12; 13; 14; 15; 16; 17;; 18; 19; 20; 21; 22; 23; 24; 25; 26; 27; 28; 29; thirty; 40; 50; 60;70; 80; 90; 100; 150; 200; 250; 300; 350; 400; 450; 500; 600; 700; 800; 900; 1000; 1500; 2000; 2500; 3000; 4000; 5000; 7500; or 10,000 amino acids. In some embodiments, the second peptide has a length of at least 17; 18; 19; 20; 21; 22; 23; 24; 25; 26; 27; 28; 29; thirty; 40; 50; 60;70; 80; 90; 100; 150; 200; 250; 300; 350; 400; 450; 500; 600; 700; 800; 900; 1000; 1500; 2000; 2500; 3000; 4000; 5000; 7500; or 10,000 amino acids. In some embodiments, the first peptide contains a sequence of at least 9 contiguous amino acids with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86% , 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity to the corresponding wild-type sequence. In some embodiments, the second peptide contains a sequence of at least 17 contiguous amino acids with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86% , 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity to the corresponding wild-type sequence. In some embodiments, the second neo-epitope is longer than the first neo-epitope. In some embodiments, the first neoepitope is at least 8 amino acids in length. In some embodiments, the first neoepitope is 8 to 12 amino acids in length. In some embodiments, the first neo-epitope comprises a sequence of at least 8 contiguous amino acids, wherein at least 2 of the 8 contiguous amino acids differ at corresponding positions in the wild-type sequence. In some embodiments, the second neoepitope is at least 16 amino acids in length. In some embodiments, the second neoepitope is 16 to 25 amino acids in length. In some embodiments, the second neo-epitope comprises a sequence of at least 16 contiguous amino acids, wherein at least 2 of the 16 contiguous amino acids differ at corresponding positions in the wild-type sequence.

In some embodiments, the first peptide contains at least one additional mutation. In some embodiments, one or more of the at least one additional mutation is not a mutation in the first neo-epitope. In some embodiments, one or more of the at least one additional mutation is a mutation in the first neo-epitope. In some embodiments, the second peptide contains at least one additional mutation. In some embodiments, one or more of the at least one additional mutation is not a mutation in the second neo-epitope. In some embodiments, one or more of the at least one additional mutation is a mutation in the second neo-epitope. In some embodiments, the first peptide, the second peptide, or both comprise at least one flanking sequence, wherein the at least one flanking sequence is located upstream or downstream of a neoepitope. In some embodiments, the at least one flanking sequence is at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71% , 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88 %, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the corresponding wild-type sequence. In some embodiments, the at least one flanking sequence comprises a non-wild type sequence. In some embodiments, the at least one flanking sequence is an N-terminal flanking sequence. In some embodiments, the at least one flanking sequence is a C-terminal flanking sequence. In some embodiments, the at least one flanking sequence of the first peptide is at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87% , 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to at least one flanking sequence of a second peptide. In some embodiments, at least one flanking region of the first peptide is different from at least one flanking region of the second peptide. In some embodiments, at least one flanking residue contains a mutation. In some embodiments, the first neoepitope, the second neoepitope, or both contain at least one anchor residue. In some embodiments, at least one anchor residue of the first neoepitope is in a canonical anchor position. In some embodiments, the at least one anchor residue of the first neoepitope is in a non-canonical anchor position. In some embodiments, at least one anchor residue of the second neoepitope is in a canonical anchor position. In some embodiments, the at least one anchor residue of the second neoepitope is not in a canonical anchor position. In some embodiments, the at least one anchor residue of the first neoepitope is different from the at least one anchor residue of the second neoepitope. In some embodiments, the at least one anchor residue is a wild-type residue. In some embodiments, the at least one anchor residue is a substitution. In some embodiments, the first neoepitope and/or the second neoepitope binds to an HLA protein with greater affinity than the corresponding neoepitope without substitution. In some embodiments, the first neoepitope and/or the second neoepitope binds to an HLA protein with greater affinity than the corresponding wild-type sequence without substitution. In some embodiments, the at least one anchor residue does not contain a mutation. In some embodiments, the first neoepitope, the second neoepitope, or both comprise at least one flanking region of an anchor residue. In some embodiments, the neoepitope contains at least one anchor residue. In some embodiments, the at least one anchor residue comprises at least two anchor residues. In some embodiments, the at least two anchor residues are separated by a separation region containing at least 1 amino acid. In some embodiments, the at least one flanking region of the anchor residue is not located within the separation region. In some embodiments, at least one flanking region of the anchor residue is upstream of the N-terminal anchor residue of at least two anchor residues downstream of the C-terminal anchor residue of at least two anchor residues of both (a) and (b).

In some embodiments, the composition contains an adjuvant. In some embodiments, the composition contains one or more additional peptides, where the one or more additional peptides contain a third neo-epitope. In some embodiments, the first and/or second neo-epitope binds to an HLA protein with greater affinity than the corresponding wild-type sequence. In some embodiments, the first and/or second neoepitope binds to an HLA protein with a K _D or IC ₅₀ of less than 1000 nM, 900 nM, 800 nM, 700 nM, 600 nM, 500 nM, 250 nM, 150 nM, 100 nM, 50 nM, 25 nM or 10 nM. In some embodiments, the first and/or second neo-epitope binds to an HLA class I protein with a K _D or IC _{50 of} less than 1000 nM, 900 nM, 800 nM, 700 nM, 600 nM, 500 nM, 250 nM, 150 nM, 100 nM, 50 nM, 25 nM or 10 nM. In some embodiments, the first and/or second neo-epitope binds to an HLA class II protein with a K _D or IC _{50 of} less than 1000 nM, 900 nM, 800 nM, 700 nM, 600 nM, 500 nM, 250 nM, 150 nM, 100 nM, 50 nM, 25 nM or 10 nM. In some embodiments, the first and/or second neo-epitope binds to a protein encoded by an HLA allele expressed by the subject. In some embodiments, the mutation is not present in non-cancerous cells of the subject. In some embodiments, the first and/or second neo-epitope is encoded by a gene or expressed gene of the subject's cancer cells. In some embodiments, the composition contains a first T cell containing a first TCR. In some embodiments, the composition contains a second T cell containing a second TCR. In some embodiments, the first TCR contains a non-native intracellular domain and/or the second TCR contains a non-native intracellular domain. In some embodiments, the first TCR is a soluble TCR and/or the second TCR is a soluble TCR. In some embodiments, the first and/or second T cell is a cytotoxic T cell. In some embodiments, the first and/or second T cell is a gamma delta T cell. In some embodiments, the first and/or second T cell is a helper T cell. In some embodiments, the first T cell is a T cell stimulated, expanded, or induced by the first neoepitope, and/or the second T cell is a T cell stimulated, expanded, or induced by the second neoepitope. In some embodiments, the first and/or second T cell is an autologous T cell. In some embodiments, the first and/or second T cell is an allogeneic T cell. In some embodiments, the first and/or second T cell is an engineered T cell. In some embodiments, the first and/or second T cell is a T cell of a cell line. In some embodiments, the first and/or second TCR binds to the HLA-peptide complex with a K _D or IC ₅₀ of less than 1000 nM, 900 nM, 800 nM, 700 nM, 600 nM, 500 nM, 250 nM, 150 nM, 100 nM, 50 nM, 25 nM or 10 nM. In some aspects, the present invention provides a vector containing a polynucleotide encoding the first and second peptides described in the present invention. In some embodiments, the polynucleotide is operably linked to a promoter. In some embodiments, the vector is a self-amplifying RNA replicon, plasmid, phage, transposon, cosmid, virus, or virion. In some embodiments, the vector is a viral vector. In some embodiments, the vector is derived from a retrovirus, lentivirus, adenovirus, adeno-associated virus, herpes virus, smallpox virus, alpha virus, vaccinia virus, hepatitis B virus, human papillomavirus, or a pseudotype thereof. In some embodiments, the vector is a non-viral vector. In some embodiments, the non-viral vector is a nanoparticle, cationic lipid, cationic polymer, metal nanopolymer, nanorod, liposome, micelle, microbubble, cell penetrating peptide, or liposphere.

In some aspects, the invention relates to a pharmaceutical composition comprising: a composition described in the present invention, or a vector described in the present invention; and a pharmaceutically acceptable excipient.

In some embodiments, the plurality of cells are autologous cells. In some embodiments, the plurality of APC cells are autologous cells. In some embodiments, the plurality of T cells are autologous cells. In some embodiments, the pharmaceutical composition further comprises an immunomodulatory agent or adjuvant. In some embodiments, the immunomodulatory agent is a cytokine. In some embodiments, the adjuvant is polyICLC. In some embodiments, the adjuvant is Hiltonol.

In some aspects, the invention relates to a method of treating cancer, where the method includes administering to a subject in need thereof a pharmaceutical composition described in the present invention.

In some aspects, the invention relates to a method for preventing resistance to anticancer therapy, where the method includes administering to a subject in need thereof a pharmaceutical composition described in the present invention.

In some aspects, the invention relates to a method of inducing an immune response, where the method includes administering to a subject in need thereof a pharmaceutical composition described in the present invention.

In some embodiments, the immune response is a humoral response. In some embodiments, the first peptide and the second peptide are administered simultaneously, separately, or sequentially. In some embodiments, the first peptide is administered sequentially after the second peptide. In some embodiments, the second peptide is administered sequentially after the first peptide. In some embodiments, the first peptide is administered sequentially after a period of time sufficient for T cell activation by the second peptide. In some embodiments, the second peptide is administered sequentially after a period of time sufficient for T cell activation by the first peptide. In some embodiments, the first peptide is administered sequentially after the second peptide to restimulate T cells. In some embodiments, a second peptide is administered sequentially after the first peptide to restimulate T cells. In some embodiments, the first peptide is administered to stimulate T cells and the second peptide is administered after the first peptide to restimulate T cells. In some embodiments, the second peptide is administered to stimulate T cells and the first peptide is administered after the second peptide to restimulate T cells.

In some embodiments, the subject has cancer, where the cancer is selected from the group consisting of melanoma, ovarian cancer, lung cancer, prostate cancer, breast cancer, colorectal cancer, endometrial cancer, and chronic lymphocytic leukemia (CLL). In some embodiments, the cancer is anti-estrogen therapy-resistant breast cancer, MSI breast cancer, metastatic breast cancer, Her2 negative breast cancer, Her2 positive breast cancer, ER negative breast cancer, ER positive breast cancer, PR positive breast cancer, PR negative breast cancer, or any combination of the two. In some embodiments, the breast cancer expresses a mutation in the estrogen receptor. In some embodiments, the subject has breast cancer that is resistant to anti-estrogen therapy. In some embodiments, the breast cancer expresses a mutation in the estrogen receptor. In some embodiments, the subject has CLL that is resistant to ibrutinib therapy. In some embodiments, the CLL expresses a Bruton's tyrosine kinase mutation, such as the C481S mutation. In some embodiments, the subject has lung cancer that is resistant to a tyrosine tyrosine kinase inhibitor. In some embodiments, the lung cancer expresses an epidermal growth factor receptor (EGFR) mutation, such as the T790M mutation. In some embodiments, a plurality of APC cells containing a first peptide and a plurality of APC cells containing a second peptide are administered simultaneously, separately, or sequentially. In some embodiments, a plurality of T cells containing a first TCR and a plurality of T cells containing a second TCR are administered simultaneously, separately, or sequentially. In some embodiments, the method further includes administering at least one additional therapeutic agent or modality. In some embodiments, the at least one additional therapeutic agent or modality is surgery, a checkpoint inhibitor, an antibody or fragment thereof, a chemotherapeutic agent, radiation, a vaccine, a small molecule, a T cell, a vector and APC, a polynucleotide, an oncolytic virus or any combination thereof. In some embodiments, the at least one additional therapeutic agent is an anti-PD-1 agent and an anti-PD-L1 agent, an anti-CTLA-4 agent, or an anti-CD40 agent. In some embodiments, the additional therapeutic agent is administered before, simultaneously with, or after administration of the pharmaceutical composition described in the present invention.

Peptides

In some aspects, the present disclosure relates to isolated peptides that contain a tumor-specific mutation from Table 1 or 2 . In some aspects, the present disclosure relates to isolated peptides that contain a tumor-specific mutation from Table 34 . In some aspects, the present disclosure relates to isolated peptides that contain a tumor-specific mutation from Table 40A-40D . These peptides and polypeptides are referred to herein as “neoantigenic peptides” or “neoantigenic polypeptides”. “Polypeptide”, “peptide” and their grammatical equivalents as used herein refer to a polymer of amino acid residues, typically L-amino acids, linked to each other, typically by peptide bonds between the α-amino and carboxyl groups of adjacent amino acids. Polypeptides and peptides include, but are not limited to, “mutant peptides,” “neoantigen peptides,” and “neoantigen peptides.” Polypeptides or peptides may be of varying lengths, be in their neutral (uncharged) forms or forms that are salts, and either lack or contain modifications such as glycosylation, side chain oxidation, or phosphorylation, provided that the modification does not destroy the biological activity of the polypeptides as described here. The peptide or polypeptide may contain at least one flanking sequence. The term “flanking sequence” as used herein refers to a fragment or region of a peptide that is not part of an epitope.

Table 1. List of GATA3 neoORF peptides

Type Sequences 8mer EPCSMLTG (SEQ ID NO: 305), PCSMLTGP (SEQ ID NO: 306), CSMLTGPP (SEQ ID NO: 307), SMLTGPPA (SEQ ID NO: 308), MLTGPPAR (SEQ ID NO: 309), LTGPPARV (SEQ ID NO : 310), TGPPARVP (SEQ ID NO: 311), GPPARVPA (SEQ ID NO: 312), PPARVPAV (SEQ ID NO: 313), PARVPAVP (SEQ ID NO: 314), ARVPAVPF (SEQ ID NO: 315), RVPAVPFD (SEQ ID NO: 316), VPAVPFDL (SEQ ID NO: 317), PAVPFDLH (SEQ ID NO: 318), AVPFDLHF (SEQ ID NO: 319), VPFDLHFC (SEQ ID NO: 320), PFDLHFCR (SEQ ID NO: 321), FDLHFCRS (SEQ ID NO: 322), DLHFCRSS (SEQ ID NO: 323), LHFCRSSI (SEQ ID NO: 324), HFCRSSIM (SEQ ID NO: 325), FCRSSIMK (SEQ ID NO: 326), CRSSIMKP( SEQ ID NO: 327), RSSIMKPK (SEQ ID NO: 328), SSIMKPKR (SEQ ID NO: 329), SIMKPKRD (SEQ ID NO: 330), IMKPKRDG (SEQ ID NO: 331), MKPKRDGY (SEQ ID NO: 332 ), KPKRDGYM (SEQ ID NO: 333), PKRDGYMF (SEQ ID NO: 334), KRDGYMFL (SEQ ID NO: 335), RDGYMFLK (SEQ ID NO: 336), DGYMFLKA (SEQ ID NO: 337), GYMFLKAE (SEQ ID NO: 338), YMFLKAES (SEQ ID NO: 339), MFLKAESK (SEQ ID NO: 340), FLKAESKI (SEQ ID NO: 341), LKAESKIM (SEQ ID NO: 342), KAESKIMF (SEQ ID NO: 343) , AESKIMFA (SEQ ID NO: 344), ESKIMFAT (SEQ ID NO: 345), SKIMFATL (SEQ ID NO: 346), KIMFATLQ (SEQ ID NO: 347), IMFATLQR (SEQ ID NO: 348), MFATLQRS (SEQ ID NO: 349), FATLQRSS (SEQ ID NO: 350), ATLQRSSL (SEQ ID NO: 351), TLQRSSLW (SEQ ID NO: 352), LQRSSLWC (SEQ ID NO: 353), QRSSLWCL (SEQ ID NO: 354), RSSLWCLC (SEQ ID NO: 355), SSLWCLCS (SEQ ID NO: 356), SLWCLCSN (SEQ ID NO: 357) 9mer EPCSMLTGP (SEQ ID NO: 358), PCSMLTGPP (SEQ ID NO: 359), CSMLTGPPA (SEQ ID NO: 360), SMLTGPPAR (SEQ ID NO: 361), MLTGPPARV (SEQ ID NO: 362), LTGPPARVP (SEQ ID NO : 363), TGPPARVPA (SEQ ID NO: 364), GPPARVPAV (SEQ ID NO: 365), PPARVPAVP (SEQ ID NO: 366), PARVPAVPF (SEQ ID NO: 367), ARVPAVPFD (SEQ ID NO: 368), RVPAVPFDL (SEQ ID NO: 369), VPAVPFDLH (SEQ ID NO: 370), PAVPFDLHF (SEQ ID NO: 371), AVPFDLHFC (SEQ ID NO: 372), VPFDLHFCR (SEQ ID NO: 373), PFDLHFCRS (SEQ ID NO: 374), FDLHFCRSS (SEQ ID NO: 375), DLHFCRSSI (SEQ ID NO: 376), LHFCRSSIM (SEQ ID NO: 377), HFCRSSIMK (SEQ ID NO: 378), FCRSSIMKP (SEQ ID NO: 379), CRSSIMKPK ( SEQ ID NO: 380), RSSIMKPKR (SEQ ID NO: 381), SSIMKPKRD (SEQ ID NO: 382), SIMKPKRDG (SEQ ID NO: 383), IMKPKRDGY (SEQ ID NO: 384), MKPKRDGYM (SEQ ID NO: 385 ), KPKRDGYMF (SEQ ID NO: 386), PKRDGYMFL (SEQ ID NO: 387), KRDGYMFLK (SEQ ID NO: 388), RDGYMFLKA (SEQ ID NO: 389), DGYMFLKAE (SEQ ID NO: 390), GYMFLKAES (SEQ ID NO: 391), YMFLKAESK (SEQ ID NO: 392), MFLKAESKI (SEQ ID NO: 393), FLKAESKIM (SEQ ID NO: 394), LKAESKIMF (SEQ ID NO: 395), KAESKIMFA (SEQ ID NO: 396) , AESKIMFAT (SEQ ID NO: 397), ESKIMFATL (SEQ ID NO: 398), SKIMFATLQ (SEQ ID NO: 399), KIMFATLQR (SEQ ID NO: 400), IMFATLQRS (SEQ ID NO: 401), MFATLQRSS (SEQ ID NO: 402), FATLQRSSL (SEQ ID NO: 403), ATLQRSSLW (SEQ ID NO: 404), TLQRSSLWC (SEQ ID NO: 405), LQRSSLWCL (SEQ ID NO: 406), QRSSLWCLC (SEQ ID NO: 407), RSSLWCLCS (SEQ ID NO: 408), SSLWCLCSN (SEQ ID NO: 409), SLWCLCSNH (SEQ ID NO: 410) 10mer EPCSMLTGPP (SEQ ID NO: 411), PCSMLTGPPA (SEQ ID NO: 412), CSMLTGPPAR (SEQ ID NO: 413), SMLTGPPARV (SEQ ID NO: 414), MLTGPPARVP (SEQ ID NO: 415), LTGPPARVPA (SEQ ID NO : 416), TGPPARVPAV (SEQ ID NO: 417), GPPARVPAVP (SEQ ID NO: 418), PPARVPAVPF (SEQ ID NO: 419), PARVPAVPFD (SEQ ID NO: 420), ARVPAVPFDL (SEQ ID NO: 421), RVPAVPFDLH (SEQ ID NO: 422), VPAVPFDLHF (SEQ ID NO: 423), PAVPFDLHFC (SEQ ID NO: 424), AVPFDLHFCR (SEQ ID NO: 425), VPFDLHFCRS (SEQ ID NO: 426), PFDLHFCRSS (SEQ ID NO: 427), FDLHFCRSSI (SEQ ID NO: 428), DLHFCRSSIM (SEQ ID NO: 429), LHFCRSSIMK (SEQ ID NO: 430), HFCRSSIMKP (SEQ ID NO: 431), FCRSSIMKPK (SEQ ID NO: 432), CRSSIMKPKR ( SEQ ID NO: 433), RSSIMKPKRD (SEQ ID NO: 434), SSIMKPKRDG (SEQ ID NO: 435), SIMKPKRDGY (SEQ ID NO: 436), IMKPKRDGYM (SEQ ID NO: 437), MKPKRDGYMF (SEQ ID NO: 438 ), KPKRDGYMFL (SEQ ID NO: 439), PKRDGYMFLK (SEQ ID NO: 440), KRDGYMFLKA (SEQ ID NO: 441), RDGYMFLKAE (SEQ ID NO: 442), DGYMFLKAES (SEQ ID NO: 443), GYMFLKAESK (SEQ ID NO: 444), YMFLKAESKI (SEQ ID NO: 445), MFLKAESKIM (SEQ ID NO: 446), FLKAESKIMF (SEQ ID NO: 447), LKAESKIMFA (SEQ ID NO: 448), KAESKIMFAT (SEQ ID NO: 449) , AESKIMFATL (SEQ ID NO: 450), ESKIMFATLQ (SEQ ID NO: 451), SKIMFATLQR (SEQ ID NO: 452), KIMFATLQRS (SEQ ID NO: 453), IMFATLQRSS (SEQ ID NO: 454), MFATLQRSSL (SEQ ID NO: 455), FATLQRSSLW (SEQ ID NO: 456), ATLQRSSLWC (SEQ ID NO: 457), TLQRSSLWCL (SEQ ID NO: 458), LQRSSLWCLC (SEQ ID NO: 459), QRSSLWCLCS (SEQ ID NO: 460), RSSLWCLCSN (SEQ ID NO: 461), SSLWCLCSNH (SEQ ID NO: 462), SLWCLCSNH (SEQ ID NO: 463) 11mer EPCSMLTGPPA (SEQ ID NO: 464), PCSMLTGPPAR (SEQ ID NO: 465), CSMLTGPPARV (SEQ ID NO: 466), SMLTGPPARVP (SEQ ID NO: 467), MLTGPPARVPA (SEQ ID NO: 468), LTGPPARVPAV (SEQ ID NO : 469), TGPPARVPAVP (SEQ ID NO: 470), GPPARVPAVPF (SEQ ID NO: 471), PPARVPAVPFD (SEQ ID NO: 472), PARVPAVPFDL (SEQ ID NO: 473), ARVPAVPFDLH (SEQ ID NO: 474), RVPAVPFDLHF (SEQ ID NO: 475), VPAVPFDLHFC (SEQ ID NO: 476), PAVPFDLHFCR (SEQ ID NO: 477), AVPFDLHFCRS (SEQ ID NO: 478), VPFDLHFCRSS (SEQ ID NO: 479), PFDLHFCRSSI (SEQ ID NO: 480), FDLHFCRSSIM (SEQ ID NO: 481), DLHFCRSSIMK (SEQ ID NO: 482), LHFCRSSIMKP (SEQ ID NO: 483), HFCRSSIMKPK (SEQ ID NO: 484), FCRSSIMKPKR (SEQ ID NO: 485), CRSSIMKPKRD ( SEQ ID NO: 486), RSSIMKPKRDG (SEQ ID NO: 487), SSIMKPKRDGY (SEQ ID NO: 488), SIMKPKRDGYM (SEQ ID NO: 489), IMKPKRDGYMF (SEQ ID NO: 490), MKPKRDGYMFL (SEQ ID NO: 491 ), KPKRDGYMFLK (SEQ ID NO: 492), PKRDGYMFLKA (SEQ ID NO: 493), KRDGYMFLKAE (SEQ ID NO: 494), RDGYMFLKAES (SEQ ID NO: 495), DGYMFLKAESK (SEQ ID NO: 496), GYMFLKAESKI (SEQ ID NO: 497), YMFLKAESKIM (SEQ ID NO: 498), MFLKAESKIMF (SEQ ID NO: 499), FLKAESKIMFA (SEQ ID NO: 500), LKAESKIMFAT (SEQ ID NO: 501), KAESKIMFATL (SEQ ID NO: 502) , AESKIMFATLQ (SEQ ID NO: 503), ESKIMFATLQR (SEQ ID NO: 504), SKIMFATLQRS (SEQ ID NO: 505), KIMFATLQRSS (SEQ ID NO: 506), IMFATLQRSSL (SEQ ID NO: 507), MFATLQRSSLW (SEQ ID NO: 508), FATLQRSSLWC (SEQ ID NO: 509), ATLQRSSLWCL (SEQ ID NO: 510), TLQRSSLWCLC (SEQ ID NO: 511), LQRSSLWCLCS (SEQ ID NO: 512), QRSSLWCLCSN (SEQ ID NO: 513), RSSLWCLCSNH (SEQ ID NO: 514) 12mer EPCSMLTGPPAR (SEQ ID NO: 515), PCSMLTGPPARV (SEQ ID NO: 516), CSMLTGPPARVP (SEQ ID NO: 517), SMLTGPPARVPA (SEQ ID NO: 518), MLTGPPARVPAV (SEQ ID NO: 519), LTGPPARVPAVP (SEQ ID NO : 520), TGPPARVPAVPF (SEQ ID NO: 521), GPPARVPAVPFD (SEQ ID NO: 522), PPARVPAVPFDL (SEQ ID NO: 523), PARVPAVPFDLH (SEQ ID NO: 524), ARVPAVPFDLHF (SEQ ID NO: 525), RVPAVPFDLHFC (SEQ ID NO: 526), VPAVPFDLHFCR (SEQ ID NO: 527), PAVPFDLHFCRS (SEQ ID NO: 528), AVPFDLHFCRSS (SEQ ID NO: 529), VPFDLHFCRSSI (SEQ ID NO: 530), PFDLHFCRSSIM (SEQ ID NO: 531), FDLHFCRSSIMK (SEQ ID NO: 532), DLHFCRSSIMKP (SEQ ID NO: 533), LHFCRSSIMKPK (SEQ ID NO: 534), HFCRSSIMKPKR (SEQ ID NO: 535), FCRSSIMKPKRD (SEQ ID NO: 536), CRSSIMKPKRDG ( SEQ ID NO: 537), RSSIMKPKRDGY (SEQ ID NO: 538), SSIMKPKRDGYM (SEQ ID NO: 539), SIMKPKRDGYMF (SEQ ID NO: 540), IMKPKRDGYMFL (SEQ ID NO: 541), MKPKRDGYMFLK (SEQ ID NO: 542 ), KPKRDGYMFLKA (SEQ ID NO: 543), PKRDGYMFLKAE (SEQ ID NO: 544), KRDGYMFLKAES (SEQ ID NO: 545), RDGYMFLKAESK (SEQ ID NO: 546), DGYMFLKAESKI (SEQ ID NO: 547), GYMFLKAESKIM (SEQ ID NO: 548), YMFLKAESKIMF (SEQ ID NO: 549), MFLKAESKIMFA (SEQ ID NO: 550), FLKAESKIMFAT (SEQ ID NO: 551), LKAESKIMFATL (SEQ ID NO: 552), KAESKIMFATLQ (SEQ ID NO: 553) , AESKIMFATLQR (SEQ ID NO: 554), ESKIMFATLQRS (SEQ ID NO: 555), SKIMFATLQRSS (SEQ ID NO: 556), KIMFATLQRSSL (SEQ ID NO: 557), IMFATLQRSSLW (SEQ ID NO: 558), MFATLQRSSLWC (SEQ ID NO: 559), FATLQRSSLWCL (SEQ ID NO: 560), ATLQRSSLWCLC (SEQ ID NO: 561), TLQRSSLWCLCS (SEQ ID NO: 562), LQRSSLWCLCSN (SEQ ID NO: 563), QRSSLWCLCSNH (SEQ ID NO: 564) 13mer EPCSMLTGPPARV (SEQ ID NO: 565), PCSMLTGPPARVP (SEQ ID NO: 566), CSMLTGPPARVPA (SEQ ID NO: 567), SMLTGPPARVPAV (SEQ ID NO: 568), MLTGPPARVPAVP (SEQ ID NO: 569), LTGPPARVPAVPF (SEQ ID NO : 570), TGPPARVPAVPFD (SEQ ID NO: 571), GPPARVPAVPFDL (SEQ ID NO: 572), PPARVPAVPFDLH (SEQ ID NO: 573), PARVPAVPFDLHF (SEQ ID NO: 574), ARVPAVPFDLHFC (SEQ ID NO: 575), RVPAVPFDLHFCR (SEQ ID NO: 576), VPAVPFDLHFCRS (SEQ ID NO: 577), PAVPFDLHFCRSS (SEQ ID NO: 578), AVPFDLHFCRSSI (SEQ ID NO: 579), VPFDLHFCRSSIM (SEQ ID NO: 580), PFDLHFCRSSIMK (SEQ ID NO: 581), FDLHFCRSSIMKP (SEQ ID NO: 582), DLHFCRSSIMKPK (SEQ ID NO: 583), LHFCRSSIMKPKR (SEQ ID NO: 584), HFCRSSIMKPKRD (SEQ ID NO: 585), FCRSSIMKPKRDG (SEQ ID NO: 586), CRSSIMKPKRDGY ( SEQ ID NO: 587), RSSIMKPKRDGYM (SEQ ID NO: 588), SSIMKPKRDGYMF (SEQ ID NO: 589), SIMKPKRDGYMFL (SEQ ID NO: 590), IMKPKRDGYMFLK (SEQ ID NO: 591), MKPKRDGYMFLKA (SEQ ID NO: 592 ), KPKRDGYMFLKAE (SEQ ID NO: 593), PKRDGYMFLKAES (SEQ ID NO: 594), KRDGYMFLKAESK (SEQ ID NO: 595), RDGYMFLKAESKI (SEQ ID NO: 596), DGYMFLKAESKIM (SEQ ID NO: 597), GYMFLKAESKIMF (SEQ ID NO: 598), YMFLKAESKIMFA (SEQ ID NO: 599), MFLKAESKIMFAT (SEQ ID NO: 600), FLKAESKIMFATL (SEQ ID NO: 601), LKAESKIMFATLQ (SEQ ID NO: 602), KAESKIMFATLQR (SEQ ID NO: 603) , AESKIMFATLQRS (SEQ ID NO: 604), ESKIMFATLQRSS (SEQ ID NO: 605), SKIMFATLQRSSL (SEQ ID NO: 606), KIMFATLQRSSLW (SEQ ID NO: 607), IMFATLQRSSLWC (SEQ ID NO: 608), MFATLQRSSLWCL (SEQ ID NO: 609), FATLQRSSLWCLC (SEQ ID NO: 610), ATLQRSSLWCLCS (SEQ ID NO: 611), TLQRSSLWCLCSN (SEQ ID NO: 612), LQRSSLWCLCSNH (SEQ ID NO: 613) 14mer EPCSMLTGPPARVP (SEQ ID NO: 614), PCSMLTGPPARVPA (SEQ ID NO: 615), CSMLTGPPARVPAV (SEQ ID NO: 616), SMLTGPPARVPAVP (SEQ ID NO: 617), MLTGPPARVPAVPF (SEQ ID NO: 618), LTGPPARVPAVPFD (SEQ ID NO : 619), TGPPARVPAVPFDL (SEQ ID NO: 620), GPPARVPAVPFDLH (SEQ ID NO: 621), PPARVPAVPFDLHF (SEQ ID NO: 622), PARVPAVPFDLHFC (SEQ ID NO: 623), ARVPAVPFDLHFCR (SEQ ID NO: 624), RVPAVPFDLHFCRS (SEQ ID NO: 625), VPAVPFDLHFCRSS (SEQ ID NO: 626), PAVPFDLHFCRSSI (SEQ ID NO: 627), AVPFDLHFCRSSIM (SEQ ID NO: 628), VPFDLHFCRSSIMK (SEQ ID NO: 629), PFDLHFCRSSIMKP (SEQ ID NO: 630), FDLHFCRSSIMKPK (SEQ ID NO: 631), DLHFCRSSIMKPKR (SEQ ID NO: 632), LHFCRSSIMKPKRD (SEQ ID NO: 633), HFCRSSIMKPKRDG (SEQ ID NO: 634), FCRSSIMKPKRDGY (SEQ ID NO: 635), CRSSIMKPKRDGYM ( SEQ ID NO: 636), RSSIMKPKRDGYMF (SEQ ID NO: 637), SSIMKPKRDGYMFL (SEQ ID NO: 638), SIMKPKRDGYMFLK (SEQ ID NO: 639), IMKPKRDGYMFLKA (SEQ ID NO: 640), MKPKRDGYMFLKAE (SEQ ID NO: 641 ), KPKRDGYMFLKAES (SEQ ID NO: 642), PKRDGYMFLKAESK (SEQ ID NO: 643), KRDGYMFLKAESKI (SEQ ID NO: 644), RDGYMFLKAESKIM (SEQ ID NO: 645), DGYMFLKAESKIMF (SEQ ID NO: 646), GYMFLKAESKIMFA (SEQ ID NO: 647), YMFLKAESKIMFAT (SEQ ID NO: 648), MFLKAESKIMFATL (SEQ ID NO: 649), FLKAESKIMFATLQ (SEQ ID NO: 650), LKAESKIMFATLQR (SEQ ID NO: 651), KAESKIMFATLQRS (SEQ ID NO: 652) , AESKIMFATLQRSS (SEQ ID NO: 653), ESKIMFATLQRSSL (SEQ ID NO: 654), SKIMFATLQRSSLW (SEQ ID NO: 655), KIMFATLQRSSLWC (SEQ ID NO: 656), IMFATLQRSSLWCL (SEQ ID NO: 657), MFATLQRSSLWCLC (SEQ ID NO: 658), FATLQRSSLWCLCS (SEQ ID NO: 659), ATLQRSSLWCLCSN (SEQ ID NO: 660), TLQRSSLWCLCSNH (SEQ ID NO: 661) 15mer EPCSMLTGPPARVPA (SEQ ID NO: 662), PCSMLTGPPARVPAV (SEQ ID NO: 663), CSMLTGPPARVPAVP (SEQ ID NO: 664), SMLTGPPARVPAVPF (SEQ ID NO: 665), MLTGPPARVPAVPFD (SEQ ID NO: 666), LTGPPARVPAVPFDL (SEQ ID NO : 667), TGPPARVPAVPFDLH (SEQ ID NO: 668), GPPARVPAVPFDLHF (SEQ ID NO: 669), PPARVPAVPFDLHFC (SEQ ID NO: 670), PARVPAVPFDLHFCR (SEQ ID NO: 671), ARVPAVPFDLHFCRS (SEQ ID NO: 672), RVPAVPFDLHFCRSS (SEQ ID NO: 673), VPAVPFDLHFCRSSI (SEQ ID NO: 674), PAVPFDLHFCRSSIM (SEQ ID NO: 675), AVPFDLHFCRSSIMK (SEQ ID NO: 676), VPFDLHFCRSSIMKP (SEQ ID NO: 677), PFDLHFCRSSIMKPK (SEQ ID NO: 678), FDLHFCRSSIMKPKR (SEQ ID NO: 679), DLHFCRSSIMKPKRD (SEQ ID NO: 680), LHFCRSSIMKPKRDG (SEQ ID NO: 681), HFCRSSIMKPKRDGY (SEQ ID NO: 682), FCRSSIMKPKRDGYM (SEQ ID NO: 683), CRSSIMKPKRDGYMF ( SEQ ID NO: 684), RSSIMKPKRDGYMFL (SEQ ID NO: 685), SSIMKPKRDGYMFLK (SEQ ID NO: 686), SIMKPKRDGYMFLKA (SEQ ID NO: 687), IMKPKRDGYMFLKAE (SEQ ID NO: 688), MKPKRDGYMFLKAES (SEQ ID NO: 689 ), KPKRDGYMFLKAESK (SEQ ID NO: 690), PKRDGYMFLKAESKI (SEQ ID NO: 691), KRDGYMFLKAESKIM (SEQ ID NO: 692), RDGYMFLKAESKIMF (SEQ ID NO: 693), DGYMFLKAESKIMFA (SEQ ID NO: 694), GYMFLKAESKIMFAT (SEQ ID NO: 695), YMFLKAESKIMFATL (SEQ ID NO: 696), MFLKAESKIMFATLQ (SEQ ID NO: 697), FLKAESKIMFATLQR (SEQ ID NO: 698), LKAESKIMFATLQRS (SEQ ID NO: 699), KAESKIMFATLQRSS (SEQ ID NO: 700) , AESKIMFATLQRSSL (SEQ ID NO: 701), ESKIMFATLQRSSLW (SEQ ID NO: 702), SKIMFATLQRSSLWC (SEQ ID NO: 703), KIMFATLQRSSLWCL (SEQ ID NO: 704), IMFATLQRSSLWCLC (SEQ ID NO: 705), MFATLQRSSLWCLCS (SEQ ID NO: 706), FATLQRSSLWCLCSN (SEQ ID NO: 707), ATLQRSSLWCLCSNH (SEQ ID NO: 708) 16mer EPCSMLTGPPARVPAV (SEQ ID NO: 709), PCSMLTGPPARVPAVP (SEQ ID NO: 710), CSMLTGPPARVPAVPF (SEQ ID NO: 711), SMLTGPPARVPAVPFD (SEQ ID NO: 712), MLTGPPARVPAVPFDL (SEQ ID NO: 713), LTGPPARVPAVPFDLH (SEQ ID NO : 714), TGPPARVPAVPFDLHF (SEQ ID NO: 715), GPPARVPAVPFDLHFC (SEQ ID NO: 716), PPARVPAVPFDLHFCR (SEQ ID NO: 717), PARVPAVPFDLHFCRS (SEQ ID NO: 718), ARVPAVPFDLHFCRSS (SEQ ID NO: 719), RVPAVPFDLHFCRSSI (SEQ ID NO: 720), VPAVPFDLHFCRSSIM (SEQ ID NO: 721), PAVPFDLHFCRSSIMK (SEQ ID NO: 722), AVPFDLHFCRSSIMKP (SEQ ID NO: 723), VPFDLHFCRSSIMKPK (SEQ ID NO: 724), PFDLHFCRSSIMKPKR (SEQ ID NO: 725), FDLHFCRSSIMKPKRD (SEQ ID NO: 726), DLHFCRSSIMKPKRDG (SEQ ID NO: 727), LHFCRSSIMKPKRDGY (SEQ ID NO: 728), HFCRSSIMKPKRDGYM (SEQ ID NO: 729), FCRSSIMKPKRDGYMF (SEQ ID NO: 730), CRSSIMKPKRDGY MFL ( SEQ ID NO: 731), RSSIMKPKRDGYMFLK (SEQ ID NO: 732), SSIMKPKRDGYMFLKA (SEQ ID NO: 733), SIMKPKRDGYMFLKAE (SEQ ID NO: 734), IMKPKRDGYMFLKAES (SEQ ID NO: 735), MKPKRDGYMFLKAESK (SEQ ID NO: 736 ), KPKRDGYMFLKAESKI (SEQ ID NO: 737), PKRDGYMFLKAESKIM (SEQ ID NO: 738), KRDGYMFLKAESKIMF (SEQ ID NO: 739), RDGYMFLKAESKIMFA (SEQ ID NO: 740), DGYMFLKAESKIMFAT (SEQ ID NO: 741), GYMFLKAESKIMFATL (SE Q ID NO: 742), YMFLKAESKIMFATLQ (SEQ ID NO: 743), MFLKAESKIMFATLQR (SEQ ID NO: 744), FLKAESKIMFATLQRS (SEQ ID NO: 745), LKAESKIMFATLQRSS (SEQ ID NO: 746), KAESKIMFATLQRSSL (SEQ ID NO: 747) , AESKIMFATLQRSSLW (SEQ ID NO: 748), ESKIMFATLQRSSLWC (SEQ ID NO: 749), SKIMFATLQRSSLWCL (SEQ ID NO: 750), KIMFATLQRSSLWCLC (SEQ ID NO: 751), IMFATLQRSSLWCLCS (SEQ ID NO: 752), MFATLQRSSLWCLCSN (SEQ ID NO: 753), FATLQRSSLWCLCSNH (SEQ ID NO: 754) 17mer EPCSMLTGPPARVPAVP (SEQ ID NO: 755), PCSMLTGPPARVPAVPF (SEQ ID NO: 756), CSMLTGPPARVPAVPFD (SEQ ID NO: 757), SMLTGPPARVPAVPFDL (SEQ ID NO: 758), MLTGPPARVPAVPFDLH (SEQ ID NO: 759), LTGPPARVPAVPFDLHF (SEQ ID NO : 760), TGPPARVPAVPFDLHFC (SEQ ID NO: 761), GPPARVPAVPFDLHFCR (SEQ ID NO: 762), PPARVPAVPFDLHFCRS (SEQ ID NO: 763), PARVPAVPFDLHFCRSS (SEQ ID NO: 764), ARVPAVPFDLHFCRSSI (SEQ ID NO: 765), RVPAVPFDLHFCRSSIM (SEQ ID NO: 766), VPAVPFDLHFCRSSIMK (SEQ ID NO: 767), PAVPFDLHFCRSSIMKP (SEQ ID NO: 768), AVPFDLHFCRSSIMKPK (SEQ ID NO: 769), VPFDLHFCRSSIMKPKR (SEQ ID NO: 770), PFDLHFCRSSIMKPKRD (SEQ ID NO: 771), FDLHFCRSSIMKPKRDG (SEQ ID NO: 772), DLHFCRSSIMKPKRDGY (SEQ ID NO: 773), LHFCRSSIMKPKRDGYM (SEQ ID NO: 774), HFCRSSIMKPKRDGYMF (SEQ ID NO: 775), FCRSSIMKPKRDGYMFL (SEQ ID NO: 776), CRSSIMKP KRDGYMFLK ( SEQ ID NO: 777), RSSIMKPKRDGYMFLKA (SEQ ID NO: 778), SSIMKPKRDGYMFLKAE (SEQ ID NO: 779), SIMKPKRDGYMFLKAES (SEQ ID NO: 780), IMKPKRDGYMFLKAESK (SEQ ID NO: 781), MKPKRDGYMFLKAESKI (SEQ ID NO: 7 82 ), KPKRDGYMFLKAESKIM (SEQ ID NO: 783), PKRDGYMFLKAESKIMF (SEQ ID NO: 784), KRDGYMFLKAESKIMFA (SEQ ID NO: 785), RDGYMFLKAESKIMFAT (SEQ ID NO: 786), DGYMFLKAESKIMFATL (SEQ ID NO: 787), GYMFLKAESKIMFATL Q (SEQ ID NO: 788), YMFLKAESKIMFATLQR (SEQ ID NO: 789), MFLKAESKIMFATLQRS (SEQ ID NO: 790), FLKAESKIMFATLQRSS (SEQ ID NO: 791), LKAESKIMFATLQRSSL (SEQ ID NO: 792), KAESKIMFATLQRSSLW (SEQ ID NO: 793) , AESKIMFATLQRSSLWC (SEQ ID NO: 794), ESKIMFATLQRSSLWCL (SEQ ID NO: 795), SKIMFATLQRSSLWCLC (SEQ ID NO: 796), KIMFATLQRSSLWCLCS (SEQ ID NO: 797), IMFATLQRSSLWCLCSN (SEQ ID NO: 798), MFATLQRSSLWCLCSNH (SEQ ID NO: 799) 18mer EPCSMLTGPPARVPAVPF (SEQ ID NO: 800), PCSMLTGPPARVPAVPFD (SEQ ID NO: 801), CSMLTGPPARVPAVPFDL (SEQ ID NO: 802), SMLTGPPARVPAVPFDLH (SEQ ID NO: 803), MLTGPPARVPAVPFDLHF (SEQ ID NO: 804), LTGPPARVPAVPFDLHFC (SEQ ID NO : 805), TGPPARVPAVPFDLHFCR (SEQ ID NO: 806), GPPARVPAVPFDLHFCRS (SEQ ID NO: 807), PPARVPAVPFDLHFCRSS (SEQ ID NO: 808), PARVPAVPFDLHFCRSSI (SEQ ID NO: 809), ARVPAVPFDLHFCRSSIM (SEQ ID NO: 810), RVPAVPFDLHFCRSSIMK (SEQ ID NO: 811), VPAVPFDLHFCRSSIMKP (SEQ ID NO: 812), PAVPFDLHFCRSSIMKPK (SEQ ID NO: 813), AVPFDLHFCRSSIMKPKR (SEQ ID NO: 814), VPFDLHFCRSSIMKPKRD (SEQ ID NO: 815), PFDLHFCRSSIMKPKRDG (SEQ ID NO: 816), FDLHFCRSSIMKPKRDGY (SEQ ID NO: 817), DLHFCRSSIMKPKRDGYM (SEQ ID NO: 818), LHFCRSSIMKPKRDGYMF (SEQ ID NO: 819), HFCRSSIMKPKRDGYMFL (SEQ ID NO: 820), FCRSSIMKPKRDGYMFLK (SEQ ID NO: 821), CR SSIMKPKRDGYMFLKA ( SEQ ID NO: 822), RSSIMKPKRDGYMFLKAE (SEQ ID NO: 823), SSIMKPKRDGYMFLKAES (SEQ ID NO: 824), SIMKPKRDGYMFLKAESK (SEQ ID NO: 825), IMKPKRDGYMFLKAESKI (SEQ ID NO: 826), MKPKRDGYMFLKAESKIM (SEQ ID NO : 827 ), KPKRDGYMFLKAESKIMF (SEQ ID NO: 828), PKRDGYMFLKAESKIMFA (SEQ ID NO: 829), KRDGYMFLKAESKIMFAT (SEQ ID NO: 830), RDGYMFLKAESKIMFATL (SEQ ID NO: 831), DGYMFLKAESKIMFATLQ (SEQ ID NO: 832), GYMFLKAESK IMFATLQR (SEQ ID NO: 833), YMFLKAESKIMFATLQRS (SEQ ID NO: 834), MFLKAESKIMFATLQRSS (SEQ ID NO: 835), FLKAESKIMFATLQRSSL (SEQ ID NO: 836), LKAESKIMFATLQRSSLW (SEQ ID NO: 837), KAESKIMFATLQRSSLWC (SEQ ID NO: 838) , AESKIMFATLQRSSLWCL (SEQ ID NO: 839), ESKIMFATLQRSSLWCLC (SEQ ID NO: 840), SKIMFATLQRSSLWCLCS (SEQ ID NO: 841), KIMFATLQRSSLWCLCSN (SEQ ID NO: 842), IMFATLQRSSLWCLCSNH (SEQ ID NO: 843) 19mer EPCSMLTGPPARVPAVPFD (SEQ ID NO: 844), PCSMLTGPPARVPAVPFDL (SEQ ID NO: 845), CSMLTGPPARVPAVPFDLH (SEQ ID NO: 846), SMLTGPPARVPAVPFDLHF (SEQ ID NO: 847), MLTGPPARVPAVPFDLHFC (SEQ ID NO: 848), LTGPPARVPAVPFDLHFCR (SEQ ID NO : 849), TGPPARVPAVPFDLHFCRS (SEQ ID NO: 850), GPPARVPAVPFDLHFCRSS (SEQ ID NO: 851), PPARVPAVPFDLHFCRSSI (SEQ ID NO: 852), PARVPAVPFDLHFCRSSIM (SEQ ID NO: 853), ARVPAVPFDLHFCRSSIMK (SEQ ID NO: 854), RVPAVPFDLHFCRSSIMKP (SEQ ID NO: 855), VPAVPFDLHFCRSSIMKPK (SEQ ID NO: 856), PAVPFDLHFCRSSIMKPKR (SEQ ID NO: 857), AVPFDLHFCRSSIMKPKRD (SEQ ID NO: 858), VPFDLHFCRSSIMKPKRDG (SEQ ID NO: 859), PFDLHFCRSSIMKPKRDGY (SEQ ID NO: 860), FDLHFCRSSIMKPKRDGYM (SEQ ID NO: 861), DLHFCRSSIMKPKRDGYMF (SEQ ID NO: 862), LHFCRSSIMKPKRDGYMFL (SEQ ID NO: 863), HFCRSSIMKPKRDGYMFLK (SEQ ID NO: 864), FCRSSIMKPKRDGYMFLKA (SEQ ID NO: 86 5), CRSSIMKPKRDGYMFLKAE ( SEQ ID NO: 866), RSSIMKPKRDGYMFLKAES (SEQ ID NO: 867), SSIMKPKRDGYMFLKAESK (SEQ ID NO: 868), SIMKPKRDGYMFLKAESKI (SEQ ID NO: 869), IMKPKRDGYMFLKAESKIM (SEQ ID NO: 870), MKPKRDGYMFLKAESKIMF (SE Q ID NO: 871 ), KPKRDGYMFLKAESKIMFA (SEQ ID NO: 872), PKRDGYMFLKAESKIMFAT (SEQ ID NO: 873), KRDGYMFLKAESKIMFATL (SEQ ID NO: 874), RDGYMFLKAESKIMFATLQ (SEQ ID NO: 875), DGYMFLKAESKIMFATLQR (SEQ ID NO: 876), GYMFL KAESKIMFATLQRS (SEQ ID NO: 877), YMFLKAESKIMFATLQRSS (SEQ ID NO: 878), MFLKAESKIMFATLQRSSL (SEQ ID NO: 879), FLKAESKIMFATLQRSSLW (SEQ ID NO: 880), LKAESKIMFATLQRSSLWC (SEQ ID NO: 881), KAESKIMFATLQRSSLWCL (SEQ ID NO: 882) , AESKIMFATLQRSSLWCLC (SEQ ID NO: 883), ESKIMFATLQRSSLWCLCS (SEQ ID NO: 884), SKIMFATLQRSSLWCLCSN (SEQ ID NO: 885), KIMFATLQRSSLWCLCSNH (SEQ ID NO: 886) 20mer EPCSMLTGPPARVPAVPFDL (SEQ ID NO: 887), PCSMLTGPPARVPAVPFDLH (SEQ ID NO: 888), CSMLTGPPARVPAVPFDLHF (SEQ ID NO: 889), SMLTGPPARVPAVPFDLHFC (SEQ ID NO: 890), MLTGPPARVPAVPFDLHFCR (SEQ ID NO: 891), LTGPPARVPAVPFDLHFCRS (SEQ ID NO : 892), TGPPARVPAVPFDLHFCRSS (SEQ ID NO: 893), GPPARVPAVPFDLHFCRSSI (SEQ ID NO: 894), PPARVPAVPFDLHFCRSSIM (SEQ ID NO: 895), PARVPAVPFDLHFCRSSIMK (SEQ ID NO: 896), ARVPAVPFDLHFCRSSIMKP (SEQ ID NO: 897), RVPAVPFDLHFCRSSIM KPK (SEQ ID NO: 898), VPAVPFDLHFCRSSIMKPKR (SEQ ID NO: 899), PAVPFDLHFCRSSIMKPKRD (SEQ ID NO: 900), AVPFDLHFCRSSIMKPKRDG (SEQ ID NO: 901), VPFDLHFCRSSIMKPKRDGY (SEQ ID NO: 902), PFDLHFCRSSIMKPKRDGYM (SEQ ID NO: 903), FDLHFCRSSIMKPKRDGYMF (SEQ ID NO: 904), DLHFCRSSIMKPKRDGYMFL (SEQ ID NO: 905), LHFCRSSIMKPKRDGYMFLK (SEQ ID NO: 906), HFCRSSIMKPKRDGYMFLKA (SEQ ID NO: 907), FCRSSIMKPKRDGYMFLKAE (SEQ ID NO: 908), CRSSIMKPKRDGYMFLKAES ( SEQ ID NO: 909), RSSIMKPKRDGYMFLKAESK (SEQ ID NO: 910), SSIMKPKRDGYMFLKAESKI (SEQ ID NO: 911), SIMKPKRDGYMFLKAESKIM (SEQ ID NO: 912), IMKPKRDGYMFLKAESKIMF (SEQ ID NO: 913), MKPKRDGYMFLKAESKIM FA (SEQ ID NO: 914 ), KPKRDGYMFLKAESKIMFAT (SEQ ID NO: 915), PKRDGYMFLKAESKIMFATL (SEQ ID NO: 916), KRDGYMFLKAESKIMFATLQ (SEQ ID NO: 917), RDGYMFLKAESKIMFATLQR (SEQ ID NO: 918), DGYMFLKAESKIMFATLQRS (SEQ ID NO: 919), G YMFLKAESKIMFATLQRSS (SEQ ID NO: 920), YMFLKAESKIMFATLQRSSL (SEQ ID NO: 921), MFLKAESKIMFATLQRSSLW (SEQ ID NO: 922), FLKAESKIMFATLQRSSLWC (SEQ ID NO: 923), LKAESKIMFATLQRSSLWCL (SEQ ID NO: 924), KAESKIMFATLQRSSLWCLC (SEQ ID NO: 925) , AESKIMFATLQRSSLWCLCS (SEQ ID NO: 926), ESKIMFATLQRSSLWCLCSN (SEQ ID NO: 927), SKIMFATLQRSSLWCLCSNH (SEQ ID NO: 928) 21mer EPCSMLTGPPARVPAVPFDLH (SEQ ID NO: 929), PCSMLTGPPARVPAVPFDLHF (SEQ ID NO: 930), CSMLTGPPARVPAVPFDLHFC (SEQ ID NO: 931), SMLTGPPARVPAVPFDLHFCR (SEQ ID NO: 932), MLTGPPARVPAVPFDLHFCRS (SEQ ID NO: 933), LTGPPARVPAVPFDLHFCRSS (SEQ ID NO : 934), TGPPARVPAVPFDLHFCRSSI (SEQ ID NO: 935), GPPARVPAVPFDLHFCRSSIM (SEQ ID NO: 936), PPARVPAVPFDLHFCRSSIMK (SEQ ID NO: 937), PARVPAVPFDLHFCRSSIMKP (SEQ ID NO: 938), ARVPAVPFDLHFCRSSIMKPK (SEQ ID NO: 939), RVPAVPFDL HFCRSSIMKPKR (SEQ ID NO: 940), VPAVPFDLHFCRSSIMKPKRD (SEQ ID NO: 941), PAVPFDLHFCRSSIMKPKRDG (SEQ ID NO: 942), AVPFDLHFCRSSIMKPKRDGY (SEQ ID NO: 943), VPFDLHFCRSSIMKPKRDGYM (SEQ ID NO: 944), PFDLHFCRSSIMKPKRDGYMF ( SEQ ID NO: 945), FDLHFCRSSIMKPKRDGYMFL (SEQ ID NO: 946), DLHFCRSSIMKPKRDGYMFLK (SEQ ID NO: 947), LHFCRSSIMKPKRDGYMFLKA (SEQ ID NO: 948), HFCRSSIMKPKRDGYMFLKAE (SEQ ID NO: 949), FCRSSIMKPKRDGYMFLKAES (SEQ ID NO: 950), CRSSIMKPKRDGYMFLKAESK ( SEQ ID NO: 951), RSSIMKPKRDGYMFLKAESKI (SEQ ID NO: 952), SSIMKPKRDGYMFLKAESKIM (SEQ ID NO: 953), SIMKPKRDGYMFLKAESKIMF (SEQ ID NO: 954), IMKPKRDGYMFLKAESKIMFA (SEQ ID NO: 955), MKPKRDGYMFLKAES KIMFAT (SEQ ID NO: 956 ), KPKRDGYMFLKAESKIMFATL (SEQ ID NO: 957), PKRDGYMFLKAESKIMFATLQ (SEQ ID NO: 958), KRDGYMFLKAESKIMFATLQR (SEQ ID NO: 959), RDGYMFLKAESKIMFATLQRS (SEQ ID NO: 960), DGYMFLKAESKIMFATLQRSS (SEQ ID NO: 96 1), GYMFLKAESKIMFATLQRSSL (SEQ ID NO: 962), YMFLKAESKIMFATLQRSSLW (SEQ ID NO: 963), MFLKAESKIMFATLQRSSLWC (SEQ ID NO: 964), FLKAESKIMFATLQRSSLWCL (SEQ ID NO: 965), LKAESKIMFATLQRSSLWCLC (SEQ ID NO: 966), KAESKIMFATLQRSSLWCLCS (SEQ ID NO: 96 7) , AESKIMFATLQRSSLWCLCSN (SEQ ID NO: 968), ESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 969) 22mer EPCSMLTGPPARVPAVPFDLHF (SEQ ID NO: 970), PCSMLTGPPARVPAVPFDLHFC (SEQ ID NO: 971), CSMLTGPPARVPAVPFDLHFCR (SEQ ID NO: 972), SMLTGPPARVPAVPFDLHFCRS (SEQ ID NO: 973), MLTGPPARVPAVPFDLHFCRSS (SEQ ID NO: 974), LTGPPARVPAVPFDLHFCRSSI ( SEQ ID NO R VPAVPFDLHFCRSSIMKPKRD (SEQ ID NO: 981), VPAVPFDLHFCRSSIMKPKRDG (SEQ ID NO: 982), PAVPFDLHFCRSSIMKPKRDGY (SEQ ID NO: 983), AVPFDLHFCRSSIMKPKRDGYM (SEQ ID NO: 984), VPFDLHFCRSSIMKPKRDGYMF (SEQ ID NO: 985), PFDLHFCRSSIMKPKRDG YMFL (SEQ ID NO: 986), FDLHFCRSSIMKPKRDGYMFLK (SEQ ID NO: 987), DLHFCRSSIMKPKRDGYMFLKA (SEQ ID NO: 988), LHFCRSSIMKPKRDGYMFLKAE (SEQ ID NO: 989), HFCRSSIMKPKRDGYMFLKAES (SEQ ID NO: 990), FCRSSIMKPKRDGYMFLKAESK (SEQ ID NO: 991), CRSSIMKPKRDGYMFLKAESKI ( SEQ ID NO: 992), RSSIMKPKRDGYMFLKAESKIM (SEQ ID NO: 993), SSIMKPKRDGYMFLKAESKIMF (SEQ ID NO: 994), SIMKPKRDGYMFLKAESKIMFA (SEQ ID NO: 995), IMKPKRDGYMFLKAESKIMFAT (SEQ ID NO: 996), MKPKRDGYMFL KAESKIMFATL (SEQ ID NO: 997 ), KPKRDGYMFLKAESKIMFATLQ (SEQ ID NO: 998), PKRDGYMFLKAESKIMFATLQR (SEQ ID NO: 999), KRDGYMFLKAESKIMFATLQRS (SEQ ID NO: 1000), RDGYMFLKAESKIMFATLQRSS (SEQ ID NO: 1001), DGYMFLKAESKIMFATLQRSSL (SEQ ID NO: 1002), GYMFLKAESKIMFATLQRSSLW (SEQ ID NO: 1003), YMFLKAESKIMFATLQRSSLWC (SEQ ID NO: 1004), MFLKAESKIMFATLQRSSLWCL (SEQ ID NO: 1005), FLKAESKIMFATLQRSSLWCLC (SEQ ID NO: 1006), LKAESKIMFATLQRSSLWCLCS (SEQ ID NO: 1007), KAESKIMFATLQRSSLWCLCSN (SE Q ID NO: 1008) , AESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 1009) 23mer EPCSMLTGPPARVPAVPFDLHFC (SEQ ID NO: 1010), PCSMLTGPPARVPAVPFDLHFCR (SEQ ID NO: 1011), CSMLTGPPARVPAVPFDLHFCRS (SEQ ID NO: 1012), SMLTGPPARVPAVPFDLHFCRSS (SEQ ID NO: 1013), MLTGPPARVPAVPFDLHFCRSSI (SEQ ID NO: 1014), LTGPPARVP AVPFDLHFCRSSIM (SEQ ID NO : 1015), TGPPARVPAVPFDLHFCRSSIMK (SEQ ID NO: 1016), GPPARVPAVPFDLHFCRSSIMKP (SEQ ID NO: 1017), PPARVPAVPFDLHFCRSSIMKPK (SEQ ID NO: 1018), PARVPAVPFDLHFCRSSIMKPKR (SEQ ID NO: 1019), ARVPAVPFDLHFCRSSIMKPKRD (SEQ ID NO: 1020), RVPAVPFDLHFCRSSIMKPKRDG PFDLHF CRSSIMKPKRDGYMFLK (SEQ ID NO: 1026), FDLHFCRSSIMKPKRDGYMFLKA (SEQ ID NO: 1027), DLHFCRSSIMKPKRDGYMFLKAE (SEQ ID NO: 1028), LHFCRSSIMKPKRDGYMFLKAES (SEQ ID NO: 1029), HFCRSSIMKPKRDGYMFLKAESK (SEQ ID NO: 1030), FCRSSIMKPKRD GYMFLKAESKI (SEQ ID NO: 1031), CRSSIMKPKRDGYMFLKAESKIM ( SEQ ID NO: 1032), RSSIMKPKRDGYMFLKAESKIMF (SEQ ID NO: 1033), SSIMKPKRDGYMFLKAESKIMFA (SEQ ID NO: 1034), SIMKPKRDGYMFLKAESKIMFAT (SEQ ID NO: 1035), IMKPKRDGYMFLKAESKIMFATL (SEQ ID NO: 1036), MK PKRDGYMFLKAESKIMFATLQ (SEQ ID NO: 1037 ), KPKRDGYMFLKAESKIMFATLQR (SEQ ID NO: 1038), PKRDGYMFLKAESKIMFATLQRS (SEQ ID NO: 1039), KRDGYMFLKAESKIMFATLQRSS (SEQ ID NO: 1040), RDGYMFLKAESKIMFATLQRSSL (SEQ ID NO: 1041), DGYMFLKAESKIMFATLQRSSL W (SEQ ID NO: 1042), GYMFLKAESKIMFATLQRSSLWC (SEQ ID NO: 1043), YMFLKAESKIMFATLQRSSLWCL (SEQ ID NO: 1044), MFLKAESKIMFATLQRSSLWCLC (SEQ ID NO: 1045), FLKAESKIMFATLQRSSLWCLCS (SEQ ID NO: 1046), LKAESKIMFATLQRSSLWCLCSN (SEQ ID NO: 1047), KAESKIMFATLQRSSLWCLCSN H (SEQ ID NO: 1048) 24mer EPCSMLTGPPARVPAVPFDLHFCR (SEQ ID NO: 1049), PCSMLTGPPARVPAVPFDLHFCRS (SEQ ID NO: 1050), CSMLTGPPARVPAVPFDLHFCRSS (SEQ ID NO: 1051), SMLTGPPARVPAVPFDLHFCRSSI (SEQ ID NO: 1052), MLTGPPARVPAVPFDLHFCRSSIM (SEQ ID NO: 1053), LTGP PARVPAVPFDLHFCRSSIMK (SEQ ID NO : 1054), TGPPARVPAVPFDLHFCRSSIMKP (SEQ ID NO: 1055), GPPARVPAVPFDLHFCRSSIMKPK (SEQ ID NO: 1056), PPARVPAVPFDLHFCRSSIMKPKR (SEQ ID NO: 1057), PARVPAVPFDLHFCRSSIMKPKRD (SEQ ID NO: 1058), ARVPAVPFDLHFCRSSIMKPKRD G (SEQ ID NO: 1059), RVPAVPFDLHFCRSSIMKPKRDGY (SEQ ID NO: 1060), VPAVPFDLHFCRSSIMKPKRDGYM (SEQ ID NO: 1061), PAVPFDLHFCRSSIMKPKRDGYMF (SEQ ID NO: 1062), AVPFDLHFCRSSIMKPKRDGYMFL (SEQ ID NO: 1063), VPFDLHFCRSSIMKPKRDGYMFLK (SEQ ID NO: 1064), PFDLHFCRSSIMKPKRDGYMFLKA (SEQ ID NO: 1065), FDLHFCRSSIMKPKRDGYMFLKAE (SEQ ID NO: 1066), DLHFCRSSIMKPKRDGYMFLKAES (SEQ ID NO: 1067), LHFCRSSIMKPKRDGYMFLKAESK (SEQ ID NO: 1068), HFCRSSIMKPKRDGYMFLKAESKI (SEQ ID NO: 1069), FCRSSIMK PKRDGYMFLKAESKIM (SEQ ID NO: 1070), CRSSIMKPKRDGYMFLKAESKIMF ( SEQ ID NO: 1071), RSSIMKPKRDGYMFLKAESKIMFA (SEQ ID NO: 1072), SSIMKPKRDGYMFLKAESKIMFAT (SEQ ID NO: 1073), SIMKPKRDGYMFLKAESKIMFATL (SEQ ID NO: 1074), IMKPKRDGYMFLKAESKIMFATLQ (SEQ ID NO: 1075), MKPKRDGYMFLKAESKIMFATLQR (SEQ ID NO: 1076 ), KPKRDGYMFLKAESKIMFATLQRS (SEQ ID NO: 1077), PKRDGYMFLKAESKIMFATLQRSS (SEQ ID NO: 1078), KRDGYMFLKAESKIMFATLQRSSL (SEQ ID NO: 1079), RDGYMFLKAESKIMFATLQRSSLW (SEQ ID NO: 1080), DGYMFLKAESKIMFATLQ RSSLWC (SEQ ID NO: 1081), GYMFLKAESKIMFATLQRSSLWCL (SEQ ID NO: 1082), YMFLKAESKIMFATLQRSSLWCLC (SEQ ID NO: 1083), MFLKAESKIMFATLQRSSLWCLCS (SEQ ID NO: 1084), FLKAESKIMFATLQRSSLWCLCSN (SEQ ID NO: 1085), LKAESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 1086) 25mer EPCSMLTGPPARVPAVPFDLHFCRS (SEQ ID NO: 1087), PCSMLTGPPARVPAVPFDLHFCRSS (SEQ ID NO: 1088), CSMLTGPPARVPAVPFDLHFCRSSI (SEQ ID NO: 1089), SMLTGPPARVPAVPFDLHFCRSSIM (SEQ ID NO: 1090), MLTGPPARVPAVPFDLHFCRSSIMK (SEQ ID NO: 1091), LTGPPARVPAVPFDLHFCRSSIMKP (SEQ ID NO : 1092), TGPPARVPAVPFDLHFCRSSIMKPK (SEQ ID NO: 1093), GPPARVPAVPFDLHFCRSSIMKPKR (SEQ ID NO: 1094), PPARVPAVPFDLHFCRSSIMKPKRD (SEQ ID NO: 1095), PARVPAVPFDLHFCRSSIMKPKRDG (SEQ ID NO: 1096), ARVPAVPFDLHFCRSSIMK PKRDGY (SEQ ID NO: 1097), RVPAVPFDLHFCRSSIMKPKRDGYM (SEQ ID NO: 1098), VPAVPFDLHFCRSSIMKPKRDGYMF (SEQ ID NO: 1099), PAVPFDLHFCRSSIMKPKRDGYMFL (SEQ ID NO: 1100), AVPFDLHFCRSSIMKPKRDGYMFLK (SEQ ID NO: 1101), VPFDLHFCRSSIMKPKRDGYMFLKA (SEQ ID NO: 1102 ), PFDLHFCRSSIMKPKRDGYMFLKAE (SEQ ID NO: FCRSS IMKPKRDGYMFLKAESKIMF (SEQ ID NO: 1108), CRSSIMKPKRDGYMFLKAESKIMFA ( SEQ ID NO: 1109), RSSIMKPKRDGYMFLKAESKIMFAT (SEQ ID NO: 1110), SSIMKPKRDGYMFLKAESKIMFATL (SEQ ID NO: 1111), SIMKPKRDGYMFLKAESKIMFATLQ (SEQ ID NO: 1112), IMKPKRDGYMFLKAESKIMFATLQR (SEQ ID NO: 11 13), MKPKRDGYMFLKAESKIMFATLQRS (SEQ ID NO: 1114 ), KPKRDGYMFLKAESKIMFATLQRSS (SEQ ID NO: 1115), PKRDGYMFLKAESKIMFATLQRSSL (SEQ ID NO: 1116), KRDGYMFLKAESKIMFATLQRSSLW (SEQ ID NO: 1117), RDGYMFLKAESKIMFATLQRSSLWC (SEQ ID NO: 1118), DGYMFLKAESKIMFA TLQRSSLWCL (SEQ ID NO: 1119), GYMFLKAESKIMFATLQRSSLWCLC (SEQ ID NO: 1120), YMFLKAESKIMFATLQRSSLWCLCS (SEQ ID NO: 1121), MFLKAESKIMFATLQRSSLWCLCSN (SEQ ID NO: 1122), FLKAESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 1123) 26mer EPCSMLTGPPARVPAVPFDLHFCRSS (SEQ ID NO: 1124), PCSMLTGPPARVPAVPFDLHFCRSSI (SEQ ID NO: 1125), CSMLTGPPARVPAVPFDLHFCRSSIM (SEQ ID NO: 1126), SMLTGPPARVPAVPFDLHFCRSSIMK (SEQ ID NO: 1127), MLTGPPARVPAVPFDLHFCRSSIMKP (SEQ ID NO: 11) 28), LTGPPARVPAVPFDLHFCRSSIMKPK (SEQ ID NO : 1129), TGPPARVPAVPFDLHFCRSSIMKPKR (SEQ ID NO: 1130), GPPARVPAVPFDLHFCRSSIMKPKRD (SEQ ID NO: 1131), PPARVPAVPFDLHFCRSSIMKPKRDG (SEQ ID NO: 1132), PARVPAVPFDLHFCRSSIMKPKRDGY (SEQ ID NO: 1133), ARVPAVPFDLHFCR SSIMKPKRDGYM (SEQ ID NO: 1134), RVPAVPFDLHFCRSSIMKPKRDGYMF (SEQ ID NO: 1135), VPAVPFDLHFCRSSIMKPKRDGYMFL (SEQ ID NO: 1136), PAVPFDLHFCRSSIMKPKRDGYMFLK (SEQ ID NO: 1137), AVPFDLHFCRSSIMKPKRDGYMFLKA (SEQ ID NO: 1138), VPFDLHFCRSSIMKPKRDGYMFLKAE (SEQ ID NO: 1 139), PFDLHFCRSSIMKPKRDGYMFLKAES (SEQ ID NO: 1140), FDLHFCRSSIMKPKRDGYMFLKAESK (SEQ ID NO: 1141), DLHFCRSSIMKPKRDGYMFLKAESKI (SEQ ID NO: 1142), LHFCRSSIMKPKRDGYMFLKAESKIM (SEQ ID NO: 1143), HFCRSSIMKPKRDGYMFLKAESKIMF (SEQ ID NO: 1144), FCRSSIMKPKRDGYMFLKAESKIMFA (SEQ ID NO: 1145), CRSSIMKPKRDGYMFLKAESKIMFAT ( SEQ ID NO: 1146), RSSIMKPKRDGYMFLKAESKIMFATL (SEQ ID NO: 1147), SSIMKPKRDGYMFLKAESKIMFATLQ (SEQ ID NO: 1148), SIMKPKRDGYMFLKAESKIMFATLQR (SEQ ID NO: 1149), IMKPKRDGYMFLKAESKIMFATLQRS (SEQ ID NO: 1150), MKPKRDGYMFLKAESKIMFATLQRSS (SEQ ID NO: 1151 ), KPKRDGYMFLKAESKIMFATLQRSSL (SEQ ID NO: 1152), PKRDGYMFLKAESKIMFATLQRSSLW (SEQ ID NO: 1153), KRDGYMFLKAESKIMFATLQRSSLWC (SEQ ID NO: 1154), RDGYMFLKAESKIMFATLQRSSLWCL (SEQ ID NO: 1155), DGYMFLKAESK IMFATLQRSSLWCLC (SEQ ID NO: 1156), GYMFLKAESKIMFATLQRSSLWCLCS (SEQ ID NO: 1157), YMFLKAESKIMFATLQRSSLWCLCSN (SEQ ID NO: 1158), MFLKAESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 1159) 27mer EPCSMLTGPPARVPAVPFDLHFCRSSI (SEQ ID NO: 1160), PCSMLTGPPARVPAVPFDLHFCRSSIM (SEQ ID NO: 1161), CSMLTGPPARVPAVPFDLHFCRSSIMK (SEQ ID NO: 1162), SMLTGPPARVPAVPFDLHFCRSSIMKP (SEQ ID NO: 1163), MLTGPPARVPAVPFDLHFCRSSIMKPK (SEQ ID NO : 1164), LTGPPARVPAVPFDLHFCRSSIMKPKR (SEQ ID NO : 1165), TGPPARVPAVPFDLHFCRSSIMKPKRD (SEQ ID NO: 1166), GPPARVPAVPFDLHFCRSSIMKPKRDG (SEQ ID NO: 1167), PPARVPAVPFDLHFCRSSIMKPKRDGY (SEQ ID NO: 1168), PARVPAVPFDLHFCRSSIMKPKRDGYM (SEQ ID NO: 1169), ARVPAVPF DLHFCRSSIMKPKRDGYMF (SEQ ID NO: 1170), RVPAVPFDLHFCRSSIMKPKRDGYMFL (SEQ ID NO: 1171), VPAVPFDLHFCRSSIMKPKRDGYMFLK (SEQ ID NO: 1172), PAVPFDLHFCRSSIMKPKRDGYMFLKA (SEQ ID NO: 1173), AVPFDLHFCRSSIMKPKRDGYMFLKAE (SEQ ID NO: 1174), VPFDLHFCRSSIMKPKRDGYMFLKAES (SEQ ID NO: 1175), PFDLHFCRSSIMKPKRDGYMFLKAESK (SEQ ID NO: 1176), FDLHFCRSSIMKPKRDGYMFLKAESKI (SEQ ID NO: 1177), DLHFCRSSIMKPKRDGYMFLKAESKIM (SEQ ID NO: 1178), LHFCRSSIMKPKRDGYMFLKAESKIMF (SEQ ID NO: 1179), HFCRSSIMKPKRDGYMFLKAESKIMFA (SEQ ID NO: 118 0), FCRSSIMKPKRDGYMFLKAESKIMFAT (SEQ ID NO: 1181), CRSSIMKPKRDGYMFLKAESKIMFATL ( SEQ ID NO: 1182), RSSIMKPKRDGYMFLKAESKIMFATLQ (SEQ ID NO: 1183), SSIMKPKRDGYMFLKAESKIMFATLQR (SEQ ID NO: 1184), SIMKPKRDGYMFLKAESKIMFATLQRS (SEQ ID NO: 1185), IMKPKRDGYMFLKAESKIMFATLQRSS (SEQ ID NO: 1186), MKPKRDGYMFLKAESKIMFATLQRSSL (SEQ ID NO: 1187 ), KPKRDGYMFLKAESKIMFATLQRSSLW (SEQ ID NO: 1188), PKRDGYMFLKAESKIMFATLQRSSLWC (SEQ ID NO: 1189), KRDGYMFLKAESKIMFATLQRSSLWCL (SEQ ID NO: 1190), RDGYMFLKAESKIMFATLQRSSLWCLC (SEQ ID NO: 1191), DGYMFLKA ESKIMFATLQRSSLWCLCS (SEQ ID NO: 1192), GYMFLKAESKIMFATLQRSSLWCLCSN (SEQ ID NO: 1193), YMFLKAESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 1194) 28mer ( SEQ ID NO: 1199), LTGPPARVPAVPFDLHFCRSSIMKPKRD (SEQ ID NO : 1200), TGPPARVPAVPFDLHFCRSSIMKPKRDG (SEQ ID NO: 1201), GPPARVPAVPFDLHFCRSSIMKPKRDGY (SEQ ID NO: 1202), PPARVPAVPFDLHFCRSSIMKPKRDGYM (SEQ ID NO: 1203), PARVPAVPFDLHFCRSSIMKPKRDGYMF (SEQ ID NO: 1204), AR VPAVPFDLHFCRSSIMKPKRDGYMFL (SEQ ID NO: 1205), RVPAVPFDLHFCRSSIMKPKRDGYMFLK (SEQ ID NO: 1206), VPAVPFDLHFCRSSIMKPKRDGYMFLKA (SEQ ID NO: 1207), PAVPFDLHFCRSSIMKPKRDGYMFLKAE (SEQ ID NO: 1208), AVPFDLHFCRSSIMKPKRDGYMFLKAES (SEQ ID NO: 1209), VPFDLHFCRSSIMKPKRDGYMFLKAESK (SEQ ID NO: 1210), PFDLHFCRSSIMKPKRDGYMFLKAESKI (SEQ ID NO: 1211), FDLHFCRSSIMKPKRDGYMFLKAESKIM (SEQ ID NO: 1212), DLHFCRSSIMKPKRDGYMFLKAESKIMF (SEQ ID NO: 1213), LHFCRSSIMKPKRDGYMFLKAESKIMFA (SEQ ID NO: 1214), HFCRSSIMKPKRDGYMFLKAESKIMFAT (SEQ ID NO: 1 215), FCRSSIMKPKRDGYMFLKAESKIMFATL (SEQ ID NO: 1216), CRSSIMKPKRDGYMFLKAESKIMFATLQ ( SEQ ID NO: 1217), RSSIMKPKRDGYMFLKAESKIMFATLQR (SEQ ID NO: 1218), SSIMKPKRDGYMFLKAESKIMFATLQRS (SEQ ID NO: 1219), SIMKPKRDGYMFLKAESKIMFATLQRSS (SEQ ID NO: 1220), IMKPKRDGYMFLKAESKIMFATLQRSSL (SE Q ID NO: 1221), MKPKRDGYMFLKAESKIMFATLQRSSLW (SEQ ID NO: 1222 ), KPKRDGYMFLKAESKIMFATLQRSSLWC (SEQ ID NO: 1223), PKRDGYMFLKAESKIMFATLQRSSLWCL (SEQ ID NO: 1224), KRDGYMFLKAESKIMFATLQRSSLWCLC (SEQ ID NO: 1225), RDGYMFLKAESKIMFATLQRSSLWCLCS (SEQ ID NO: 1226), DGYM FLKAESKIMFATLQRSSLWCLCSN (SEQ ID NO: 1227), GYMFLKAESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 1228) 29mer EPCSMLTGPPARVPAVPFDLHFCRSSIMK (SEQ ID NO: 1229), PCSMLTGPPARVPAVPFDLHFCRSSIMKP (SEQ ID NO: 1230), CSMLTGPPARVPAVPFDLHFCRSSIMKPK (SEQ ID NO: 1231), SMLTGPPARVPAVPFDLHFCRSSIMKPKR (SEQ ID NO: 1232), MLTGPPARVPAVPFDLHFCRSSIMK PKRD (SEQ ID NO: 1233), LTGPPARVPAVPFDLHFCRSSIMKPKRDG (SEQ ID NO : 1234), TGPPARVPAVPFDLHFCRSSIMKPKRDGY (SEQ ID NO: 1235), GPPARVPAVPFDLHFCRSSIMKPKRDGYM (SEQ ID NO: 1236), PPARVPAVPFDLHFCRSSIMKPKRDGYMF (SEQ ID NO: 1237), PARVPAVPFDLHFCRSSIMKPKRDGYMFL (SEQ ID NO: 123) 8), ARVPAVPFDLHFCRSSIMKPKRDGYMFLK (SEQ ID NO: 1239), RVPAVPFDLHFCRSSIMKPKRDGYMFLKA (SEQ ID NO: 1240), VPAVPFDLHFCRSSIMKPKRDGYMFLKAE (SEQ ID NO: 1241), PAVPFDLHFCRSSIMKPKRDGYMFLKAES (SEQ ID NO: 1242), AVPFDLHFCRSSIMKPKRDGYMFLKAESK (SEQ ID NO: 1243), VPFDLHFCRSSIMKPKRDGYMFLKAESKI ( SEQ ID NO: 1244), PFDLHFCRSSIMKPKRDGYMFLKAESKIM (SEQ ID NO: 1245), FDLHFCRSSIMKPKRDGYMFLKAESKIMF (SEQ ID NO: 1246), DLHFCRSSIMKPKRDGYMFLKAESKIMFA (SEQ ID NO: 1247), LHFCRSSIMKPKRDGYMFLKAESKIMFAT (SEQ ID NO: 1248), HFCRSSIMKPKRDGYMFLKAESKIMFATL (SEQ ID NO: 1249), FCRSSIMKPKRDGYMFLKAESKIMFATLQ (SEQ ID NO: 1250), CRSSIMKPKRDGYMFLKAESKIMFATLQR ( SEQ ID NO: 1251), RSSIMKPKRDGYMFLKAESKIMFATLQRS (SEQ ID NO: 1252), SSIMKPKRDGYMFLKAESKIMFATLQRSS (SEQ ID NO: 1253), SIMKPKRDGYMFLKAESKIMFATLQRSSL (SEQ ID NO: 1254), IMKPKRDGYMFLKAESKIMFATLQRSSLW (SEQ ID NO: 1255), MKPKRDGYMFLKAESKIMFATLQRSSLWC (SEQ ID NO: 1256 ), KPKRDGYMFLKAESKIMFATLQRSSLWCL (SEQ ID NO: 1257), PKRDGYMFLKAESKIMFATLQRSSLWCLC (SEQ ID NO: 1258), KRDGYMFLKAESKIMFATLQRSSLWCLCS (SEQ ID NO: 1259), RDGYMFLKAESKIMFATLQRSSLWCLCSN (SEQ ID NO: 1260), DG YMFLKAESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 1261) 30mer EPCSMLTGPPARVPAVPFDLHFCRSSIMKP (SEQ ID NO: 1262), PCSMLTGPPARVPAVPFDLHFCRSSIMKPK (SEQ ID NO: 1263), CSMLTGPPARVPAVPFDLHFCRSSIMKPKR (SEQ ID NO: 1264), SMLTGPPARVPAVPFDLHFCRSSIMKPKRD (SEQ ID NO: 1265), MLTGPPARVPAVPFDLHFCR SSIMKPKRDG (SEQ ID NO: 1266), LTGPPARVPAVPFDLHFCRSSIMKPKRDGY (SEQ ID NO : 1267), TGPPARVPAVPFDLHFCRSSIMKPKRDGYM (SEQ ID NO: 1268), GPPARVPAVPFDLHFCRSSIMKPKRDGYMF (SEQ ID NO: 1269), PPARVPAVPFDLHFCRSSIMKPKRDGYMFL (SEQ ID NO: 1270), PARVPAVPFDLHFCRSSIMKPKRDGYMFLK (SEQ ID NO: 1271), ARVPAVPFDLHFCRSSIMKPKRDGYMFLKA (SEQ ID NO: 1272), RVPAVPFDLHFCRSSIMKPKRDGYMFLKAE (SEQ ID NO: 1273), VPAVPFDLHFCRSSIMKPKRDGYMFLKAES (SEQ ID NO: 1274), PAVPFDLHFCRSSIMKPKRDGYMFLKAESK (SEQ ID NO: 1275), AVPFDLHFCRSSIMKPKRDGYMFLKAESKI (SEQ ID NO: 1276), VPFDLHFCRSSIMKPKRDGYMFLKAESK IM (SEQ ID NO: 1277), PFDLHFCRSSIMKPKRDGYMFLKAESKIMF (SEQ ID NO: 1278), FDLHFCRSSIMKPKRDGYMFLKAESKIMFA (SEQ ID NO: 1279), DLHFCRSSIMKPKRDGYMFLKAESKIMFAT (SEQ ID NO: 1280), LHFCRSSIMKPKRDGYMFLKAESKIMFATL (SEQ ID NO: 1281), HFCRSSIMKPKRDGYMFLKAESKIMFATLQ (SEQ ID NO: 1282), FCRSSIMKPKRDGYMFLKAESKIMFATLQR (SEQ ID NO: 1283), CRSSIMKPKRDGYMFLKAESKIMFATLQRS ( SEQ ID NO: 1284), RSSIMKPKRDGYMFLKAESKIMFATLQRSS (SEQ ID NO: 1285), SSIMKPKRDGYMFLKAESKIMFATLQRSSL (SEQ ID NO: 1286), SIMKPKRDGYMFLKAESKIMFATLQRSSLW (SEQ ID NO: 1287), IMKPKRDGYMFLKAESKIMFATLQRS SLWC (SEQ ID NO: 1288), MKPKRDGYMFLKAESKIMFATLQRSSLWCL (SEQ ID NO: 1289 ), KPKRDGYMFLKAESKIMFATLQRSSLWCLC (SEQ ID NO: 1290), PKRDGYMFLKAESKIMFATLQRASLWCS (SEQ ID NO: 1291), KRDGYMFASKISSSLWCLCSN (Seq ID NO: 129 2), RDGYMFLKAESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 1293) 31mer EPCSMLTGPPARVPAVPFDLHFCRSSIMKPK (SEQ ID NO: 1294), PCSMLTGPPARVPAVPFDLHFCRSSIMKPKR (SEQ ID NO: 1295), CSMLTGPPARVPAVPFDLHFCRSSIMKPKRD (SEQ ID NO: 1296), SMLTGPPARVPAVPFDLHFCRSSIMKPKRDG (SEQ ID NO: 1297), MLTGPPARVPAVPF DLHFCRSSIMKPKRDGY (SEQ ID NO: 1298), LTGPPARVPAVPFDLHFCRSSIMKPKRDGYM (SEQ ID NO : 1299), TGPPARVPAVPFDLHFCRSSIMKPKRDGYMF (SEQ ID NO: 1300), GPPARVPAVPFDLHFCRSSIMKPKRDGYMFL (SEQ ID NO: 1301), PPARVPAVPFDLHFCRSSIMKPKRDGYMFLK (SEQ ID NO: 1302), PARVPAVPFDLHFCRSSIMKPKRDGYMFLKA (SEQ ID NO : 1303), ARVPAVPFDLHFCRSSIMKPKRDGYMFLKAE (SEQ ID NO: 1304), RVPAVPFDLHFCRSSIMKPKRDGYMFLKAES (SEQ ID NO: 1305), VPAVPFDLHFCRSSIMKPKRDGYMFLKAESK (SEQ ID NO: 1306), PAVPFDLHFCRSSIMKPKRDGYMFLKAESKI (SEQ ID NO: 1307), AVPFDLHFCRSSIMKPKRDGYMFLKAESKIM (SEQ ID NO: 1308), VPFDLHFCRSSIMKPKRDGYMFLKA ESKIMF (SEQ ID NO: 1309), PFDLHFCRSSIMKPKRDGYMFLKAESKIMFA (SEQ ID NO: 1310), FDLHFCRSSIMKPKRDGYMFLKAESKIMFAT (SEQ ID NO: 1311), DLHFCRSSIMKPKRDGYMFLKAESKIMFATL (SEQ ID NO: 1312), LHFCRSSIMKPKRDGYMFLKAESKIMFATLQ (SEQ ID NO: 1313), HFCRSSIMKPKRDGYMFLKAESKIMFATLQR ( SEQ ID NO: 1314), FCRSSIMKPKRDGYMFLKAESKIMFATLQRS (SEQ ID NO: 1315), CRSSIMKPKRDGYMFLKAESKIMFATLQRSS ( SEQ ID NO: 1316), RSSIMKPKRDGYMFLKAESKIMFATLQRSSL (SEQ ID NO: 1317), SSIMKPKRDGYMFLKAESKIMFATLQRSSLW (SEQ ID NO: 1318), SIMKPKRDGYMFLKAESKIMFATLQRSSLWC (SEQ ID NO: 1319), IMKPKRDGYMFLKAESKIMFATLQ RSSLWCL (SEQ ID NO: 1320), MKPKRDGYMFLKAESKIMFATLQRSSLWCLC (SEQ ID NO: 1321 ), KPKRDGYMFLKAESKIMFATLQRSSLWCLCS (SEQ ID NO: 1322), PKRDGYMFLKAESKIMFATLQRSSLWCLCSN (SEQ ID NO: 1323), KRDGYMFLKAESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 1324) 32mer EPCSMLTGPPARVPAVPFDLHFCRSSIMKPKR (SEQ ID NO: 1325), PCSMLTGPPARVPAVPFDLHFCRSSIMKPKRD (SEQ ID NO: 1326), CSMLTGPPARVPAVPFDLHFCRSSIMKPKRDG (SEQ ID NO: 1327), SMLTGPPARVPAVPFDLHFCRSSIMKPKRDGY (SEQ ID NO: 1328), MLTGPPAR VPAVPFDLHFCRSSIMKPKRDGYM (SEQ ID NO: 1329), LTGPPARVPAVPFDLHFCRSSIMKPKRDGYMF (SEQ ID NO : 1330), TGPPARVPAVPFDLHFCRSSIMKPKRDGYMFL (SEQ ID NO: 1331), GPPARVPAVPFDLHFCRSSIMKPKRDGYMFLK (SEQ ID NO: 1332), PPARVPAVPFDLHFCRSSIMKPKRDGYMFLKA (SEQ ID NO: 1333), PARVPAVPFDLHFCRSSIMKPKRDGYMFLKAE (SE Q ID NO: 1334), ARVPAVPFDLHFCRSSIMKPKRDGYMFLKAES (SEQ ID NO: 1335), RVPAVPFDLHFCRSSIMKPKRDGYMFLKAESK (SEQ ID NO: 1336), VPAVPFDLHFCRSSIMKPKRDGYMFLKAESKI (SEQ ID NO: 1337), PAVPFDLHFCRSSIMKPKRDGYMFLKAESKIM (SEQ ID NO: 1338), AVPFDLHFCRSSIMKPKRDGYMFLKAESKIMF (SEQ ID NO: 1339), VPFDLHFCRSSIMKPKRDGYM FLKAESKIMFA (SEQ ID NO: 1340), PFDLHFCRSSIMKPKRDGYMFLKAESKIMFAT (SEQ ID NO: 1341), FDLHFCRSSIMKPKRDGYMFLKAESKIMFATL (SEQ ID NO: 1342), DLHFCRSSIMKPKRDGYMFLKAESKIMFATLQ (SEQ ID NO: 1343), LHFCRSSIMKPKRDGYMFLKAESKIMFATLQR (SEQ ID NO: 1344), HFCRSSIMKPKRDGYMFLKAESKIMFATLQ RS (SEQ ID NO: 1345), FCRSSIMKPKRDGYMFLKAESKIMFATLQRSS (SEQ ID NO: 1346), CRSSIMKPKRDGYMFLKAESKIMFATLQRSSL ( SEQ ID NO: 1347), RSSIMKPKRDGYMFLKAESKIMFATLQRSSLW (SEQ ID NO: 1348), SSIMKPKRDGYMFLKAESKIMFATLQRSSLWC (SEQ ID NO: 1349), SIMKPKRDGYMFLKAESKIMFATLQRSSLWCL (SEQ ID NO: 1350), IMKPKRDGYMFLKAESKIMFA TLQRSSLWCLC (SEQ ID NO: 1351), MKPKRDGYMFLKAESKIMFATLQRSSLWCLCS (SEQ ID NO: 1352 ), KPKRDGYMFLKAESKIMFATLQRSSLWCLCSN (SEQ ID NO: 1353), PKRDGYMFLKAESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 1354) 33mer EPCSMLTGPPARVPAVPFDLHFCRSSIMKPKRD (SEQ ID NO: 1355), PCSMLTGPPARVPAVPFDLHFCRSSIMKPKRDG (SEQ ID NO: 1356), CSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGY (SEQ ID NO: 1357), SMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYM (SEQ ID NO: 1358), M LTGPPARVPAVPFDLHFCRSSIMKPKRDGYMF (SEQ ID NO: 1359), LTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFL (SEQ ID NO : 1360), TGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLK (SEQ ID NO: 1361), GPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKA (SEQ ID NO: 1362), PPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAE (SEQ ID NO: 1363), PARVPAVPFDLHFCRSSIMKPKRDGYMFLKAES (SEQ ID NO: 1364), ARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESK (SEQ ID NO: 1365), RVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKI (SEQ ID NO: 1366), VPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIM (SEQ ID NO: 1367), PAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMF (SEQ ID NO: 1368), AVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFA (SEQ ID NO: 1369), VPFDLHFCRSSIMKPKRDGY MFLKAESKIMFAT (SEQ ID NO: 1370), PFDLHFCRSSIMKPKRDGYMFLKAESKIMFATL (SEQ ID NO: 1371), FDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQ (SEQ ID NO: 1372), DLHFCRSSIMKPKRDGYMFLKAESKIMFATLQR (SEQ ID NO: 1373), LHFCRSSIMKPKRDGYMFLKAESKIMFATLQRS (SEQ ID NO: 1374), HFCRSSIMKPKRDGYMFLKAESKIMFA TLQRSS (SEQ ID NO: 1375), FCRSSIMKPKRDGYMFLKAESKIMFATLQRSSL (SEQ ID NO: 1376), CRSSIMKPKRDGYMFLKAESKIMFATLQRSSLW ( SEQ ID NO: 1377), RSSIMKPKRDGYMFLKAESKIMFATLQRSSLWC (SEQ ID NO: 1378), SSIMKPKRDGYMFLKAESKIMFATLQRSSLWCL (SEQ ID NO: 1379), SIMKPKRDGYMFLKAESKIMFATLQRSSLWCLC (SEQ ID NO: 1380), IMKPKRDGYMFLKAESKIM FATLQRSSLWCLCS (SEQ ID NO: 1381), MKPKRDGYMFLKAESKIMFATLQRSSLWCLCSN (SEQ ID NO: 1382 ), KPKRDGYMFLKAESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 1383) 34mer EPCSMLTGPPARVPAVPFDLHFCRSSIMKPKRDG (SEQ ID NO: 1384), PCSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGY (SEQ ID NO: 1385), CSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYM (SEQ ID NO: 1386), SMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMF (SEQ ID NO: 138 7), MLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFL (SEQ ID NO: 1388), LTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLK (SEQ ID NO : 1389), TGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKA (SEQ ID NO: 1390), GPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAE (SEQ ID NO: 1391), PPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAES (SEQ ID NO: 1392), PARVPAVPFDLHFCRSSIMKPKRDGYMFLKA ESK (SEQ ID NO: 1393), ARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKI (SEQ ID NO: 1394), RVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIM (SEQ ID NO: 1395) GYMFLKAESKIMFATL (SEQ ID NO: 1399), PFDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQ (SEQ ID NO: 1400), FDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQR (SEQ ID NO: 1401), DLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRS (SEQ ID NO: 1402), LHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSS (SEQ ID NO: 1403), HFCRSSIMKPKRDGYMFLKAESK IMFATLQRSSL (SEQ ID NO: 1404), FCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLW (SEQ ID NO: 1405), CRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWC ( SEQ ID NO: 1406), RSSIMKPKRDGYMFLKAESKIMFATLQRSSLWCL (SEQ ID NO: 1407), SSIMKPKRDGYMFLKAESKIMFATLQRSSLWCLC (SEQ ID NO: 1408), SIMKPKRDGYMFLKAESKIMFATLQRSSLWCLCS (SEQ ID NO: 1409), IMKPKRDGYMFLKAES KIMFATLQRSSLWCLCSN (SEQ ID NO: 1410), MKPKRDGYMFLKAESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 1411 ) 35mer EPCSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGY (SEQ ID NO: 1412), PCSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYM (SEQ ID NO: 1413), CSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMF (SEQ ID NO: 1414), SMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFL (SEQ ID NO: 1415), MLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLK (SEQ ID NO: 1416), LTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKA (SEQ ID NO : 1417), TGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAE (SEQ ID NO: 1418), GPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAES (SEQ ID NO: 1419), PPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESK (SEQ ID NO: 1420), PARVPAVPFDLHFCRSSIMKPKRDGYM FLKAESKI (SEQ ID NO: 1421), ARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIM (SEQ ID NO: 1422), RVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMF (SEQ ID NO: 1423), VPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFA (SEQ ID NO: 1424), PAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFAT (SEQ ID NO: 1425), AVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFATL (SEQ ID NO: 1426), VPFDLHFCRSSIMKPK RDGYMFLKAESKIMFATLQ (SEQ ID NO: 1427), PFDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQR (SEQ ID NO: 1428), FDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRS (SEQ ID NO: 1429), DLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSS (SEQ ID NO: 1430), LHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSSL (SEQ ID NO: 1431), HFCRSSIMKPKRDGYMFLKAES KIMFATLQRSSLW (SEQ ID NO: 1432), FCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWC (SEQ ID NO: 1433), CRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWCL ( SEQ ID NO: 1434), RSSIMKPKRDGYMFLKAESKIMFATLQRSSLWCLC (SEQ ID NO: 1435), SSIMKPKRDGYMFLKAESKIMFATLQRSSLWCLCS (SEQ ID NO: 1436), SIMKPKRDGYMFLKAESKIMFATLQRSSLWCLCSN (SEQ ID NO: 1437), IMKPKRDGYMFLKA ESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 1438) 36mer EPCSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYM (SEQ ID NO: 1439), PCSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMF (SEQ ID NO: 1440), CSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFL (SEQ ID NO: 1441), SMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLK (SEQ ID NO: 1442), MLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKA (SEQ ID NO: 1443), LTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAE (SEQ ID NO : 1444), TGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAES (SEQ ID NO: 1445), GPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESK (SEQ ID NO: 1446), PPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKI (SEQ ID NO: 1447), PARVPAVPFDLHFCRSSIMKPKRDG YMFLKAESKIM (SEQ ID NO: 1448), ARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMF (SEQ ID NO: 1449), RVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFA (SEQ ID NO: 1450), VPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFAT (SEQ ID NO: 1451), PAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFATL (SEQ ID NO: 1452), AVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQ (SEQ ID NO: 1453), VPFDLHFCRSSIMK PKRDGYMFLKAESKIMFATLQR (SEQ ID NO: 1454), PFDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRS (SEQ ID NO: 1455), FDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSS (SEQ ID NO: 1456), DLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSSL (SEQ ID NO: 1457), LHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLW (SEQ ID NO: 1458), HFCRSSIMKPKRDGYMFL KAESKIMFATLQRSSLWC (SEQ ID NO: 1459), FCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWCL (SEQ ID NO: 1460), CRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWCLC ( SEQ ID NO: 1461), RSSIMKPKRDGYMFLKAESKIMFATLQRSSLWCLCS (SEQ ID NO: 1462), SSIMKPKRDGYMFLKAESKIMFATLQRSSLWCLCSN (SEQ ID NO: 1463), SIMKPKRDGYMFLKAESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 1464) 37mer EPCSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMF (SEQ ID NO: 1465), PCSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFL (SEQ ID NO: 1466), CSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLK (SEQ ID NO: 1467), SMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKA (SE Q ID NO: 1468), MLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAE (SEQ ID NO: 1469), LTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAES (SEQ ID NO : 1470), TGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESK (SEQ ID NO: 1471), GPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKI (SEQ ID NO: 1472), PPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIM (SEQ ID NO: 1473), PARVPAVPFDLHFCRSSIMKPK RDGYMFLKAESKIMF (SEQ ID NO: 1474), ARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFA (SEQ ID NO: 1475), RVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFAT (SEQ ID NO: 1476), VPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFATL (SEQ ID NO: 1477), PAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQ (SEQ ID NO: 1478), AVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQR (SEQ ID NO: 1479), VPFDLHFCRSS IMKPKRDGYMFLKAESKIMFATLQRS (SEQ ID NO: 1480), PFDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSS (SEQ ID NO: 1481), FDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSSL (SEQ ID NO: 1482), DLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLW (SEQ ID NO: 1483), LHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWC (SEQ ID NO: 1484), HFCRSSIMKPKRDGYM FLKAESKIMFATLQRSSLWCL (SEQ ID NO: 1485), FCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWCLC (SEQ ID NO: 1486), CRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWCLCS ( SEQ ID NO: 1487), RSSIMKPKRDGYMFLKAESKIMFATLQRSSLWCLCSN (SEQ ID NO: 1488), SSIMKPKRDGYMFLKAESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 1489) 38mer EPCSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFL (SEQ ID NO: 1490), PCSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLK (SEQ ID NO: 1491), CSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKA (SEQ ID NO: 1492), SMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKA E (SEQ ID NO: 1493), MLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAES (SEQ ID NO: 1494), LTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESK (SEQ ID NO : 1495), TGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKI (SEQ ID NO: 1496), GPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIM (SEQ ID NO: 1497), PPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMF (SEQ ID NO: 1498), PARVPAVPFDLHFCRSSIMK PKRDGYMFLKAESKIMFA (SEQ ID NO: 1499), ARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFAT (SEQ ID NO: 1500), RVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFATL (SEQ ID NO: 1501), VPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQ (SEQ ID NO: 1502), PAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQR (SEQ ID NO: 1503), AVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRS (SEQ ID NO: 1504), VPFDLHF CRSSIMKPKRDGYMFLKAESKIMFATLQRSS (SEQ ID NO: 1505), PFDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSSL (SEQ ID NO: 1506), FDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLW (SEQ ID NO: 1507), DLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWC (SEQ ID NO: 1508), LHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWCL (SEQ ID NO: 1509), HFCRSSIMKPKRDG YMFLKAESKIMFATLQRSSLWCLC (SEQ ID NO: 1510), FCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWCLCS (SEQ ID NO: 1511), CRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWCLCSN ( SEQ ID NO: 1512), RSSIMKPKRDGYMFLKAESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 1513) 39mer EPCSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLK (SEQ ID NO: 1514), PCSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKA (SEQ ID NO: 1515), CSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAE (SEQ ID NO: 1516), SMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYM FLKAES (SEQ ID NO: 1517), MLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESK (SEQ ID NO: 1518), LTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKI (SEQ ID NO : 1519), TGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIM (SEQ ID NO: 1520), GPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMF (SEQ ID NO: 1521), PPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFA (SEQ ID NO: 1522), PARVPAVPFDLHFCRSSIM KPKRDGYMFLKAESKIMFAT (SEQ ID NO: 1523), ARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFATL (SEQ ID NO: 1524), RVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQ (SEQ ID NO: 1525), VPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQR (SEQ ID NO: 1526), PAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRS (SEQ ID NO: 1527), AVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSS (SEQ ID NO: 1528), VPF DLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSSL (SEQ ID NO: 1529), PFDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLW (SEQ ID NO: 1530), FDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWC (SEQ ID NO: 1531), DLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWCL (SEQ ID NO: 1532), LHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWCLC (SEQ ID NO: 1533), HFCRSSIMKPKRD GYMFLKAESKIMFATLQRSSLWCLCS (SEQ ID NO: 1534), FCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWCLCSN (SEQ ID NO: 1535), CRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWCLCSNH ( SEQ ID NO: 1536) 40mer EPCSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKA (SEQ ID NO: 1537), PCSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAE (SEQ ID NO: 1538), CSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAES (SEQ ID NO: 1539), SMLTGPPARVPAVPFDLHFCRSSIMKPKRDGY MFLKAESK (SEQ ID NO: 1540), MLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKI (SEQ ID NO: 1541), LTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIM (SEQ ID NO : 1542), TGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMF (SEQ ID NO: 1543), GPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFA (SEQ ID NO: 1544), PPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFAT (SEQ ID NO: 1545), PARVPAVPFDLHFCR SSIMKPKRDGYMFLKAESKIMFATL (SEQ ID NO: 1546), ARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQ (SEQ ID NO: 1547), RVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQR V PFDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLW (SEQ ID NO: 1552), PFDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWC (SEQ ID NO: 1553), FDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWCL (SEQ ID NO: 1554), DLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWCLC (SEQ ID NO: 1555), LHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWCLCS (SEQ ID NO: 1556), HFCRSSIMKP KRDGYMFLKAESKIMFATLQRSSLWCLCSN (SEQ ID NO: 1557), FCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 1558)

Table 2 below lists typical selected peptides

Gene Typical protein change Sequence Mutation Context Peptides (example(s) of HLA alleles) Typical diseases table 2 FRAME SHIFT ¹ GATA3 L328fs
N334fs AQAKAVCSQESRDVLCELSDHHNHTLEEECQWGPCLQCLWALLQASQY* (SEQ ID NO: 1559) CLQCLWALL (A02.01) (SEQ ID NO: 1561)
CQWGPCLQCL (A02.01) (SEQ ID NO: 1562)
QWGPCLQCL (A24.02) (SEQ ID NO: 1563)
QWGPCLQCLW (A24.02) (SEQ ID NO: 1564) Mammary cancer GATA3 H400fs
S408fs
S408fs
S430fs
H434fs
H435fs PGRPLQTHVLPEPHLALQPLQPHADHAHADAPAIQPVLWTTPPLQHGHRHGLEPCSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWCLCSNH* (SEQ ID NO: 1560) AIQPVLWTT (A02.01) (SEQ ID NO: 1565)
ALQPLQPHA (A02.01) (SEQ ID NO: 1566)
DLHFCRSSIM (B08.01) (SEQ ID NO: 1567)
EPHLALQPL (B07.02, B08.01) (SEQ ID NO: 1568)
ESKIMFATL (B08.01) (SEQ ID NO: 1569)
FATLQRSSL (B07.02, B08.01) (SEQ ID NO: 1570)
FLKAESKIM (B08.01) (SEQ ID NO: 1571)
FLKAESKIMF (B08.01) (SEQ ID NO: 1572)
GPPARVPAV (B07.02) (SEQ ID NO: 1573)
IMKPKRDGYM (B08.01) (SEQ ID NO: 1574)
KIMFATLQR (A03.01) (SEQ ID NO: 1575)
KPKRDGYMF (B07.02) (SEQ ID NO: 1576)
KPKRDGYMFL (B07.02) (SEQ ID NO: 1577)
LHFCRSSIM (B08.01) (SEQ ID NO: 1578)
LQHGHRHGL (B08.01) (SEQ ID NO: 1579)
MFATLQRSSL (B07.02, B08.01) (SEQ ID NO: 1580)
MFLKAESKI (A24.02) (SEQ ID NO: 1581)
MLTGPPARV (A02.01) (SEQ ID NO: 1582)
QPVLWTTPPL (B07.02) (SEQ ID NO: 1583)
SMLTGPPARV (A02.01) (SEQ ID NO: 1584)
TLQRSSLWCL (A02.01) (SEQ ID NO: 1585)
VLPEPHLAL (A02.01) (SEQ ID NO: 1586)
VPAVPFDLHF (B07.02) (SEQ ID NO: 1587)
YMFLKAESK (A03.01) (SEQ ID NO: 1588)
YMFLKAESKI (A02.01, A03.01, A24.02, B08.01) (SEQ ID NO: 1589) Mammary cancer

¹ Underlined AAs represent non-native AAs

Table 3

Gene Change in typical protein Sequence Mutation Context Peptides (example(s) of HLA alleles) Typical diseases table 3A POINT MUTATIONS ¹ AKT1 E17K MSDVAIVKEGWLHKRG K YIKTWRPRYFLLKNDGTFIGYKERPQDVDQREAPLNNFSVAQCQLMKTER (SEQ ID NO: 1590) KYIKTWRPRY (A24.02) (SEQ ID NO: 1632)
WLHKRGKYI (A02.01, B07.02, B08.01) (SEQ ID NO: 1633)
WLHKRGKYIK (A03.01) (SEQ ID NO: 1634) BRCA, CESC, HNSC, LUSC, PRAD, SKCM, THCA ANAPC1 T537A TMLVLEGSGNLVLYTGVVRVGKVFIPGLPAPSLTMSNTMPRPSTPLDGVS A PKPLSKLLGSLDEVVLLSPVPELRDSSKLHDSLYNEDCTFQQLGTYIHSI (SEQ ID NO: 1591) APKPLSKLL (B07.02) (SEQ ID NO: 1635)
GVSAPKPLSK (A03.01) (SEQ ID NO: 1636)
VSAPKPLSK (A03.01) (SEQ ID NO: 1637) GBM, LUSC, PAAD, PRAD, SKCM FGFR3 S249C HRIGGIKLRHQQWSLVMESVVPSDRGNYTCVVENKFGSIRQTYTLDVLER C PHRPILQAGLPANQTAVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKVG (SEQ ID NO: 1592) CPHRPILQA (B07.02) (SEQ ID NO: 1638) BLCA, HNSC, KIRP, LUSC FRG1B I10T MREPIYMHSTMVFLPWELHTKKGPSPPEQFMAVKLSDSR T ALKSGYGKYLGINSDELVGHSDAIGPREQWEPVFQNGKMALLASNSCFIR (SEQ ID NO: 1593) KLSDSRTAL (A02.01, B07.02, B08.01) (SEQ ID NO: 1639)
KLSDSRTALK (A03.01) (SEQ ID NO: 1640)
LSDSRTALK (A01.01, A03.01) (SEQ ID NO: 1641)
RTALKSGYGK (A03.01) (SEQ ID NO: 1642)
TALKSGYGK (A03.01) (SEQ ID NO: 1643) KIRP, PRAD, SKCM FRG1B L52S AVKLSDSRIALKSGYGKYLGINSDELVGHSDAIGPREQWEPVFQNGKMAL S ASNSCFIRCNEAGDIEAKSKTAGEEEMIKIRSCAEKETKKKDDIPEEDKG (SEQ ID NO: 1594) ALSASNSCF (A02.01, A24.02, B07.02) (SEQ ID NO: 1644)
ALSASNSCFI (A02.01) (SEQ ID NO: 1645)
FQNGKMALSA (A02.01, B08.01) (SEQ ID NO: 1646) GBM, KIRP, PRAD, SKCM HER2 L755S
(Resistance) AMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKV S RENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGC (SEQ ID NO: 1595) KVSRENTSPK (A03.01) (SEQ ID NO: 1647) BRCA IDH1 R132G RVEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVSGWVKPIIIG G HAYGDQYRATDFVVPGPGKVEITYTPSDGTQKVTYLVHNFEEGGGVAMGM (SEQ ID NO: 1596) KPIIIGGHAY (B07.02) (SEQ ID NO: 1648) BLCA, BRCA, CRC, GBM, HNSC, LUAD, PAAD, PRAD, UCEC KRAS G12C MTEYKLVVVGA C GVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQE (SEQ ID NO: 1597) KLVVVGACGV (A02.01) (SEQ ID NO: 1649)
LVVVGACGV (A02.01) (SEQ ID NO: 1650)
VVGACGVGK (A03.01, A11.01) (SEQ ID NO: 1651)
VVVGACGVGK (A03.01) (SEQ ID NO: 1652) BRCA, CESC, CRC, HNSC, LUAD, PAAD, UCEC KRAS G12D MTEYKLVVVGA D GVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQE (SEQ ID NO: 1598) VVGADGVGK (A11.01) (SEQ ID NO: 1653)
VVVGADGVGK (A11.01) (SEQ ID NO: 1654)
KLVVVGADGV (A02.01) (SEQ ID NO: 1655)
LVVVGADGV (A02.01) (SEQ ID NO: 1656) BLCA, BRCA, CESC, CRC, GBM, HNSC, KIRP, LIHC, LUAD, PAAD, SKCM, UCEC KRAS G12V MTEYKLVVVGA V GVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQE (SEQ ID NO: 1599) KLVVVGAVGV (A02.01) (SEQ ID NO: 1657)
LVVVGAVGV (A02.01) (SEQ ID NO: 1658)
VVGAVGVGK (A03.01, A11.01) (SEQ ID NO: 1659)
VVVGAVGVGK (A03.01, A11.01) (SEQ ID NO: 1660) BRCA, CESC, CRC, LUAD, PAAD, THCA, UCEC KRAS Q61H AGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAG H EEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPM (SEQ ID NO: 1600) ILDTAGHEEY (A01.01) (SEQ ID NO: 1661) CRC, LUSC, PAAD, SKCM, UCEC KRAS Q61L AGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAG L EEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPM (SEQ ID NO: 1601) ILDTAGLEEY (A01.01) (SEQ ID NO: 1662)
LLDILDTAGL (A02.01) (SEQ ID NO: 1663) CRC, GBM, HNSC, LUAD, SKCM, UCEC NRAS Q61K AGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAG K EEYSAMRDQYMRTGEGFLCVFAINNSKSFADINLYREQIKRVKDSDDVPM (SEQ ID NO: 1602) ILDTAGKEEY (A01.01) (SEQ ID NO: 1664) BLCA, CRC, LIHC, LUAD, LUSC, SKCM, THCA, UCEC NRAS Q61R AGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAG R EEYSAMRDQYMRTGEGFLCVFAINNSKSFADINLYREQIKRVKDSDDVPM (SEQ ID NO: 1603) ILDTAGREEY (A01.01) (SEQ ID NO: 1665) BLCA, CRC, LUSC, PAAD, PRAD, SKCM, THCA, UCEC PIK3CA E542K IEEHANWSVSREAGFSYSHAGLSNRLARDNELRENDKEQLKAISTRDPLS K ITEQEKDFLWSHRHYCVTIPEILPKLLLSVKWNSRDEVAQMYCLVKDWPP (SEQ ID NO: 1604) AISTRDPLSK (A03.01) (SEQ ID NO: 1666) BLCA, BRCA, CESC, CRC, GBM, HNSC, KIRC, KIRP, LIHC, LUAD, LUSC, PRAD, UCEC PTEN R130Q KFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKG Q TGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSY (SEQ ID NO: 1605) QTGVMICAY (A01.01) (SEQ ID NO: 1667) BRCA, CESC, CRC, GBM, KIRC, LUSC, UCEC RAC1 P29S MQAIKCVVVGDGAVGKT
CLLISYTTNAF S GEYIP
TVFDNYSANVMVDGKPV
NLGLWDTAGQEDYDRLR
PLSYPQTVGET
(SEQ ID NO: 1606) FSGEYIPTV (A02.01) (SEQ ID NO: 1668)
TTNAFSGEY (A01.01) (SEQ ID NO: 1669)
YTTNAFSGEY (A01.01) (SEQ ID NO: 1670) Melanoma SF3B1 K700E AVCKSKKSWQARHTGIKIVQQIAILMGCAILPHLRSLVEIIEHGLVDEQQ E VRTISALAIAALAEAATPYGIESFDSVLKPLWKGIRQHRGKGLAAFLKAI (SEQ ID NO: 1607) GLVDEQQEV (A02.01) (SEQ ID NO: 1671) AML associated with MDS; Chronic lymphocytic leukemia – small cell lymphocytic lymphoma; Myelodysplastic syndrome; AML; Luminal NS breast carcinoma; Chronic myeloid leukemia; Pancreatic ductal carcinoma; Chronic myelomonocytic leukemia; Chronic lymphocytic leukemia – small cell lymphocytic lymphoma; Myelofibrosis; Myelodysplastic syndrome; PRAD; Essential thrombocythemia; Medullomyoblastoma SPOP F133L YLSLYLLLVSCPKSEVRAKFKFSILNAKGEETKAMESQRAYRFVQGKDWG L KKFIRRDFLLDEANGLLPDDKLTLFCEVSVVQDSVNISGQNTMNMVKVPE (SEQ ID NO: 1608) FVQGKDWGL (A02.01, B08.01) (SEQ ID NO: 1672) PRAD SPOP F133V YLSLYLLLVSCPKSEVRAKFKFSILNAKGEETKAMESQRAYRFVQGKDWG V KKFIRRDFLLDEANGLLPDDKLTLFCEVSVVQDSVNISGQNTMNMVKVPE (SEQ ID NO: 1609) FVQGKDWGV (A02.01) (SEQ ID NO: 1673) PRAD TP53 G245S IRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMG S MNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEP (SEQ ID NO: 1610) CMGSMNRRPI (A02.01, B08.01) (SEQ ID NO: 1674)
GSMNRRPIL (B08.01) (SEQ ID NO: 1675)
MGSMNRRPI (B08.01) (SEQ ID NO: 1676)
MGSMNRRPIL (B08.01) (SEQ ID NO: 1677)
SMNRRPILTI (A02.01, A24.02, B08.01) (SEQ ID NO: 1678) BLCA, BRCA, CRC, GBM, HNSC, LUSC, PAAD, PRAD TP53 R248Q EGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMN Q RPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHE (SEQ ID NO: 1611) CMGGMNQRPI (A02.01, B08.01) (SEQ ID NO: 1679)
GMNQRPILTI (A02.01, B08.01) (SEQ ID NO: 1680)
NQRPILTII (A02.01, B08.01) (SEQ ID NO: 1681) BLCA, BRCA, CRC, GBM, HNSC, KIRC, LIHC, LUSC, PAAD, PRAD, UCEC TP53 R248W EGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMN W RPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHE (SEQ ID NO: 1612) CMGGMNWRPI (A02.01, A24.02, B08.01) (SEQ ID NO: 1682)
GMNWRPILTI (A02.01, B08.01) (SEQ ID NO: 1683)
MNWRPILTI (A02.01, A24.02, B08.01) (SEQ ID NO: 1684)
MNWRPILTII (A02.01, A24.02) (SEQ ID NO: 1685) BLCA, BRCA, CRC, GBM, HNSC, LIHC, LUSC, PAAD, SKCM, UCEC TP53 R273C PEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEV C VCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPL (SEQ ID NO: 1613) NSFEVCVCA (A02.01) (SEQ ID NO: 1686) BLCA, BRCA, CRC, GBM, HNSC, LUSC, PAAD, UCEC TP53 R273H PEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEV H VCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPL (SEQ ID NO: 1614) NSFEVHVCA (A02.01) (SEQ ID NO: 1687) BRCA, CRC, GBM, HNSC, LIHC, LUSC, PAAD, UCEC TP53 Y220C TEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVP C EPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSF (SEQ ID NO: 1615) VVPCEPPEV (A02.01) (SEQ ID NO: 1688)
VVVPCEPPEV (A02.01) (SEQ ID NO: 1689) BLCA, BRCA, GBM, HNSC, LIHC, LUAD, LUSC, PAAD, SKCM, UCEC table 3B MSI-ASSOCIATED FRAME SHIFT ¹ MSH6 F1088fs; +1 YNFDKNYKDWQSAVECIAVLDVLLCLANYSRGGDGPMCRPVILLPEDTPP LLRA (SEQ ID NO: 1616) ILLPEDTPPL (A02.01) (SEQ ID NO: 1690)
LLPEDTPPL (A02.01) (SEQ ID NO: 1691) MSI+ CRC, MSI+ uterine/endometrial cancer, MSI+ stomach cancer, Lynch syndrome table 3C FRAME SHIFT ¹ APC F1354fs AKFQQCHSTLEPNPADCRVLVYLQNQPGTKLLNFLQERNLPPKVVLRHPKVHLNTMFRRPHSCLADVLLSVHLIVLRVVRLPAPFRVNHAVEW* (SEQ ID NO: 1617) APFRVNHAV (B07.02) (SEQ ID NO: 1692)
CLADVLLSV (A02.01) (SEQ ID NO: 1693)
FLQERNLPPK (A03.01) (SEQ ID NO: 1694)
HLIVLRVVRL (A02.01, B08.01) (SEQ ID NO: 1695)
HPKVHLNTM (B07.02, B08.01) (SEQ ID NO: 1696)
HPKVHLNTMF (B07.02, B08.01) (SEQ ID NO: 1697)
KVHLNTMFR (A03.01) (SEQ ID NO: 1698)
KVHLNTMFRR (A03.01) (SEQ ID NO: 1699)
LPAPFRVNHA (B07.02) (SEQ ID NO: 1700)
MFRRPHSCL (B07.02, B08.01) (SEQ ID NO: 1701)
MFRRPHSCLA (B08.01) (SEQ ID NO: 1702)
NTMFRRPHSC (B08.01) (SEQ ID NO: 1703)
RPHSCLADV (B07.02) (SEQ ID NO: 1704)
RPHSCLADVL (B07.02) (SEQ ID NO: 1705)
RVVRLPAPFR (A03.01) (SEQ ID NO: 1706)
SVHLIVLRV (A02.01) (SEQ ID NO: 1707)
TMFRRPHSC (B08.01) (SEQ ID NO: 1708)
TMFRRPHSCL (A02.01, B08.01) (SEQ ID NO: 1709)
VLLSVHLIV (A02.01) (SEQ ID NO: 1710)
VLLSVHLIVL (A02.01) (SEQ ID NO: 1711)
VLRVVRLPA (B08.01) (SEQ ID NO: 1712)
VVRLPAPFR (A03.01) (SEQ ID NO: 1713) CRC, LUAD, UCEC, STAD ARID1A Y1324fs ALGPHSRISCLPTQTRGCILLAATPRSSSSSSSNDMIPMAISSPPKAPLLAAPSPASRLQCINSNSRITSGQWMAHMALLPSGTKGRCTACHTALGRGSLSSSCPQPSPSLPASNKLPSPLLSKMYTTSMAMPILPLPQLLLSADQQAAPRTNFHSSLAETVSLHPLAPMPSKTCHHK* (SEQ ID NO: 1618) AMPILPLPQL (A02.01) (SEQ ID NO: 1714)
APLLAAPSPA (B07.02) (SEQ ID NO: 1715)
APRTNFHSS (B07.02) (SEQ ID NO: 1716)
APRTNFHSSL (B07.02, B08.01) (SEQ ID NO: 1717)
CPQPSPSLPA (B07.02) (SEQ ID NO: 1718)
GQWMAHMAL (A02.01) (SEQ ID NO: 1719)
GQWMAHMALL (A02.01) (SEQ ID NO: 1720)
HMALLPSGTK (A03.01) (SEQ ID NO: 1721)
HTALGRGSL (B07.02) (SEQ ID NO: 1722)
IPMAISSPP (B07.02) (SEQ ID NO: 1723)
IPMAISSPPK (B07.02) (SEQ ID NO: 1724)
KLPSPLLSK (A03.01) (SEQ ID NO: 1725)
KLPSPLLSKM (A02.01) (SEQ ID NO: 1726)
KMYTTSMAM (A02.01, A03.01) (SEQ ID NO: 1727)
LLAAPSPASR (A03.01) (SEQ ID NO: 1728)
LLLSADQQAA (A02.01) (SEQ ID NO: 1729)
LLSADQQAA (A02.01) (SEQ ID NO: 1730)
LPASNKLPS (B07.02) (SEQ ID NO: 1731)
LPASNKLPSL (B07.02, B08.01) (SEQ ID NO: 1732)
LPLPQLLLSA (B07.02) (SEQ ID NO: 1733)
LPSLPLSKM (B07.02) (SEQ ID NO: 1734)
LSKMYTTSM (B08.01) (SEQ ID NO: 1735)
MALLPSGTK (A03.01) (SEQ ID NO: 1736)
MPILPLPQL (B07.02) (SEQ ID NO: 1737)
MPILPLPQLL (B07.02) (SEQ ID NO: 1738)
MYTTSMAMPI (A24.02) (SEQ ID NO: 1739)
PMAISSPPK (A03.01) (SEQ ID NO: 1740)
QWMAHMALL (A24.02) (SEQ ID NO: 1741)
SKMYTTSMAM (B07.02) (SEQ ID NO: 1742)
SMAMPILPL (A02.01, B07.02, B08.01) (SEQ ID NO: 1743)
SNKLPSLPL (B08.01) (SEQ ID NO: 1744)
SPASRLQCI (B07.02, B08.01) (SEQ ID NO: 1745)
SPPKAPLLAA (B07.02) (SEQ ID NO: 1746)
SPSLPASNKL (B07.02) (SEQ ID NO: 1747)
YTTSMAMPI (A02.01) (SEQ ID NO: 1748)
YTTSMAMPIL (A02.01) (SEQ ID NO: 1749) STAD, UCEC, BLCA, BRCA, LUSC, CESC, KIRC, UCS ARID1A G1848fs RSYRRMIHLWWTAQISLGVCRSLTVACCTGLVGGTPLSISRPTSRARQSCCLPGLTHPAHQPLGSM* (SEQ ID NO: 1619) CLPGLTHPA (A02.01) (SEQ ID NO: 1750)
GLTHPAHQPL (A02.01) (SEQ ID NO: 1751)
HPAHQPLGSM (B07.02) (SEQ ID NO: 1752)
LTHPAHQPL (B07.02) (SEQ ID NO: 1753)
RPTSRARQSC (B07.02) (SEQ ID NO: 1754)
RQSCCLPGL (A02.01) (SEQ ID NO: 1755)
TSRARQSCCL (B08.01) (SEQ ID NO: 1756) STAD, UCEC, BLCA, BRCA, LUSC, CESC, KIRC, UCS β2M L13fs QHSGRDVSLRGLSCARATLSFWPGGYPAYSKDSGLLTSSSREWKVKFPELLCVWVSSIRH* (SEQ ID NO: 1620) ELLCVWVSSI (A02.01) (SEQ ID NO: 1757)
EWKVKFPEL (B08.01) (SEQ ID NO: 1758)
KFPELLCVW (A24.02) (SEQ ID NO: 1759)
LLCVWVSSI (A02.01) (SEQ ID NO: 1760)
LLTSSSREWK (A03.01) (SEQ ID NO: 1761)
LTSSSREWK (A03.01) (SEQ ID NO: 1762)
YPAYSKDSGL (B07.02) (SEQ ID NO: 1763) CRC, STAD, SKCM, HNSC GATA3 L328fs
N334fs AQAKAVCSQESRDVLCELSDHHNHTLEEECQWGPCLQCLWALLQASQY* (SEQ ID NO: 1621) CLQCLWALL (A02.01) (SEQ ID NO: 1764)
CQWGPCLQCL (A02.01) (SEQ ID NO: 1765)
QWGPCLQCL (A24.02) (SEQ ID NO: 1766)
QWGPCLQCLW (A24.02) (SEQ ID NO: 1767) Mammary cancer GATA3 H400fs
S408fs
S408fs
S430fs
H434fs
H435fs PGRPLQTHVLPEPHLALQPLQPHADHAHADAPAIQPVLWTTPPLQHGHRHGLEPCSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWCLCSNH* (SEQ ID NO: 1622) AIQPVLWTT (A02.01) (SEQ ID NO: 1768)
ALQPLQPHA (A02.01) (SEQ ID NO: 1769)
DLHFCRSSIM (B08.01) (SEQ ID NO: 1770)
EPHLALQPL (B07.02, B08.01) (SEQ ID NO: 1771)
ESKIMFATL (B08.01) (SEQ ID NO: 1772)
FATLQRSSL (B07.02, B08.01) (SEQ ID NO: 1773)
FLKAESKIM (B08.01) (SEQ ID NO: 1774)
FLKAESKIMF (B08.01) (SEQ ID NO: 1775)
GPPARVPAV (B07.02) (SEQ ID NO: 1776)
IMKPKRDGYM (B08.01) (SEQ ID NO: 1777)
KIMFATLQR (A03.01) (SEQ ID NO: 1778)
KPKRDGYMF (B07.02) (SEQ ID NO: 1779)
KPKRDGYMFL (B07.02) (SEQ ID NO: 1780)
LHFCRSSIM (B08.01) (SEQ ID NO: 1781)
LQHGHRHGL (B08.01) (SEQ ID NO: 1782)
MFATLQRSSL (B07.02, B08.01) (SEQ ID NO: 1783)
MFLKAESKI (A24.02) (SEQ ID NO: 1784)
MLTGPPARV (A02.01) (SEQ ID NO: 1785)
QPVLWTTPPL (B07.02) (SEQ ID NO: 1786)
SMLTGPPARV (A02.01) (SEQ ID NO: 1787)
TLQRSSLWCL (A02.01) (SEQ ID NO: 1788)
VLPEPHLAL (A02.01) (SEQ ID NO: 1789)
VPAVPFDLHF (B07.02) (SEQ ID NO: 1790)
YMFLKAESK (A03.01) (SEQ ID NO: 1791)
YMFLKAESKI (A02.01, A03.01, A24.02, B08.01) (SEQ ID NO: 1792) Mammary cancer MLL2 P647fs
L656fs TRRCHCCPHLRSHPCPHHLRNHPRPHHLRHHACHHHLRNCPHPHFLRHCTCPGRWRNRPSLRRLRSLLCLPHLNHHLFLHWRSRPCLHRKSHPHLLHLRRLYPHHLKHRPCPHHLKNLLCPRHLRNCPLPRHLKHLACLHHLRSHPCPLHLKSHPCLHHRRHLVCSHHLKSLLCPLHLRSLPFPHHLRHHACPHHLRTRLCPHHLKNHLCPPHLRYRA YPPCLWCHACLHRLRNLPCPHRLRSLPRPLHLRLHASPHHLRTPPHPHHLRTHLLPHHRRTRSCPCRWRSHPCCHYLRSRNSAPGPRGRTCHPGLRSRTCPPGLRSHTYLRRLRSHTCPPSLRSHAYALCLRSHTCPPRLRDHICPLSLRNCTCPPRLRSRTCLLCLRSHACPPNLRNHTCPPSLRSHACPPGLRNRICPLSLRSHPCPLGLKSPLRSQANALHLRSCPCSLPLGNHP YLPCLESQPCLSLGNHLCPLCPRSCRCPHLGSHPCRLS* (SEQ ID NO: 1623) APGPRGRTC (B07.02) (SEQ ID NO: 1793)
CLRSHTCPPR (A03.01) (SEQ ID NO: 1794)
CLWCHACLHR (A03.01) (SEQ ID NO: 1795)
CPHLGSHPC (B07.02) (SEQ ID NO: 1796)
CPLGLKSPL (B07.02) (SEQ ID NO: 1797)
CPRSCRCPH (B07.02) (SEQ ID NO: 1798)
CPRSCRCPHL (B07.02, B08.01) (SEQ ID NO: 1799)
CSLPLGNHPY (A01.01) (SEQ ID NO: 1800)
GLRNRICPL (A02.01, B07.02, B08.01) (SEQ ID NO: 1801)
GLRSHTYLR (A03.01) (SEQ ID NO: 1802)
GLRSHTYLRR (A03.01) (SEQ ID NO: 1803)
GPRGRTCHPG (B07.02) (SEQ ID NO: 1804)
HLGSHPCRL (B08.01) (SEQ ID NO: 1805)
HLRLHASPH (A03.01) (SEQ ID NO: 1806)
HLRSCPCSL (B07.02, B08.01) (SEQ ID NO: 1807)
HLRTHLLPH (A03.01) (SEQ ID NO: 1808)
HLRTHLLPHH (A03.01) (SEQ ID NO: 1809)
HLRYRAYPP (B08.01) (SEQ ID NO: 1810)
HLRYRAYPPC (B08.01) (SEQ ID NO: 1811)
HPHHLRTHL (B07.02) (SEQ ID NO: 1812)
HPHHLRTHLL (B07.02, B08.01) (SEQ ID NO: 1813)
HTYLRRLRSH (A03.01) (SEQ ID NO: 1814)
LPCPHRLRSL (B07.02, B08.01) (SEQ ID NO: 1815)
LPHHRRTRSC (B07.02, B08.01) (SEQ ID NO: 1816)
LPLGNHPYL (B07.02) (SEQ ID NO: 1817)
LPRPLHLRL (B07.02, B08.01) (SEQ ID NO: 1818)
NLRNHTCPP (B08.01) (SEQ ID NO: 1819)
PPRLRSRTCL (B07.02, B08.01) (SEQ ID NO: 1820)
RLHASPHHL (A02.01) (SEQ ID NO: 1821)
RLHASPHHLR (A03.01) (SEQ ID NO: 1822)
RLRDHICPL (A02.01, B07.02, B08.01) (SEQ ID NO: 1823)
RLRNLPCPH (A03.01) (SEQ ID NO: 1824)
RLRNLPCPHR (A03.01) (SEQ ID NO: 1825)
RLRSHTCPP (B08.01) (SEQ ID NO: 1826)
RLRSLPRPL (B07.02, B08.01) (SEQ ID NO: 1827)
RLRSLPRPLH (A03.01) (SEQ ID NO: 1828)
RLRSRTCLL (B07.02, B08.01) (SEQ ID NO: 1829)
RNRICPLSL (B07.02, B08.01) (SEQ ID NO: 1830)
RPLHLRLHA (B07.02) (SEQ ID NO: 1831)
RPLHLRLHAS (B07.02) (SEQ ID NO: 1832)
RSHACPPGLR (A03.01) (SEQ ID NO: 1833)
RSHACPPNLR (A03.01) (SEQ ID NO: 1834)
RSHAYALCLR (A03.01) (SEQ ID NO: 1835)
RSHPCCHYLR (A03.01) (SEQ ID NO: 1836)
RSHPCPLGLK (A03.01) (SEQ ID NO: 1837)
RSHTCPPSLR (A03.01) (SEQ ID NO: 1838)
RSLPRPLHLR (A03.01) (SEQ ID NO: 1839)
RSRTCLLCL (B07.02) (SEQ ID NO: 1840)
RSRTCLLCLR (A03.01) (SEQ ID NO: 1841)
RSRTCPPGL (B07.02) (SEQ ID NO: 1842)
RSRTCPPGLR (A03.01) (SEQ ID NO: 1843)
RTHLLPHHRR (A03.01) (SEQ ID NO: 1844)
RTRSCPCRWR (A03.01) (SEQ ID NO: 1845)
RYRAYPPCL (A24.02) (SEQ ID NO: 1846)
RYRAYPPCLW (A24.02) (SEQ ID NO: 1847)
SLGNHLCPL (A02.01, B07.02, B08.01) (SEQ ID NO: 1848)
SLPLGNHPYL (A02.01) (SEQ ID NO: 1849)
SLPRPLHLRL (A02.01) (SEQ ID NO: 1850)
SLRNCTCPPR (A03.01) (SEQ ID NO: 1851)
SLRSHAYAL (A02.01, B07.02, B08.01) (SEQ ID NO: 1852)
SLRSHPCPL (A02.01, B07.02, B08.01) (SEQ ID NO: 1853)
SPHHLRTPP (B07.02) (SEQ ID NO: 1854)
SPHHLRTPPH (B07.02) (SEQ ID NO: 1855)
SPLRSQANAL (B07.02, B08.01) (SEQ ID NO: 1856)
YLRRLRSHTC (B08.01) (SEQ ID NO: 1857)
YLRSRNSAP (B08.01) (SEQ ID NO: 1858)
YLRSRNSAPG (B08.01) (SEQ ID NO: 1859) STAD, BLCA, CRC, HNSC, BRCA MLL2 P2354fs GPRSHPLPRLWHLLLQVTQTSFALAPTLTHMLSPH* (SEQ ID NO: 1624) ALAPTLTHM (A02.01) (SEQ ID NO: 1860)
ALAPTLTHML (A02.01) (SEQ ID NO: 1861)
LLQVTQTSFA (A02.01) (SEQ ID NO: 1862)
LQVTQTSFAL (A02.01) (SEQ ID NO: 1863)
RLWHLLLQV (A02.01) (SEQ ID NO: 1864)
RLWHLLLQVT (A02.01) (SEQ ID NO: 1865) STAD, BLCA, CRC, HNSC, BRCA RNF43 G659fs PLGLVPWTRWCPQGKPRFPAMSTTTATGTTTTKSGSSGMAGSLAQKPESPSPGLLFLGHSPSQSHLLLISKSPDPTQQPLRGGSLTHSAPGPSLSQPLAQLTPPASAPVPAVCSTCKNPASLPDTHRGKGGGVPPSPPLALGPRMQLCTQLARFFPITPPVWHILGPQRHTP* (SEQ ID NO: 1625) CTQLARFFPI (A24.02) (SEQ ID NO: 1866)
FFPITPPVW (A24.02) (SEQ ID NO: 1867)
FPITPPVWHI (B07.02) (SEQ ID NO: 1868)
GPRMQLCTQL (B07.02, B08.01) (SEQ ID NO: 1869)
ITPPVWHIL (A24.02) (SEQ ID NO: 1870)
LALGPRMQL (B07.02) (SEQ ID NO: 1871)
MQLCTQLARF (A24.02) (SEQ ID NO: 1872)
RFFPITPPV (A02.01, A24.02) (SEQ ID NO: 1873)
RFFPITPPVW (A24.02) (SEQ ID NO: 1874)
RMQLCTQLA (A02.01) (SEQ ID NO: 1875)
RMQLCTQLAR (A03.01) (SEQ ID NO: 1876)
SPPLALGPRM (B07.02) (SEQ ID NO: 1877)
TQLARFFPI (A02.01, A24.02, B08.01) (SEQ ID NO: 1878) STAD SMAP1 E169fs KYEKKKYYDKNAIAITNISSSDAPLQPLVSSPSLQAAVDKNKLEKEKEKK RKRKREKRSQKSRQNHLQLKSCRRKISNWSLKKVPALKKLRSPLWIF (SEQ ID NO: 1626) KSRQNHLQL (B07.02) (SEQ ID NO: 1879)
ALKKLRSPL (B08.01, B07.02) (SEQ ID NO: 1880)
HLQLKSCRRK (A03.01) (SEQ ID NO: 1881)
KISNWSLKK (A03.01, A11.01) (SEQ ID NO: 1882)
KISNWSLKKV (A03.01) (SEQ ID NO: 1883)
KLRSPLWIF (A24.02) (SEQ ID NO: 1884)
KSRQNHLQLK (A03.01) (SEQ ID NO: 1885)
NWSLKKVPAL (B08.01) (SEQ ID NO: 1886)
SLKKVPALK (A03.01, A11.01) (SEQ ID NO: 1887)
SLKKVPALKK (A03.01) (SEQ ID NO: 1888)
SQKSRQNHL (B08.01) (SEQ ID NO: 1889)
WSLKKVPAL (B08.01) (SEQ ID NO: 1890)
WSLKKVPALK (A03.01) (SEQ ID NO: 1891) MSI+ CRC, MSI+ uterine/endometrial cancer, MSI+ stomach cancer TP53 P58fs
P72fs
G108fs
R110fs CCPRTILNNGSLKTQVQMKLPECQRLLPPWPLHQQLLHRRPLHQPPPGPCHLLSLPRKPTRAATVSVWASCILGQPSL* (SEQ ID NO: 1627) KLPECQRLL (A02.01) (SEQ ID NO: 1892)
KPTRAATVSV (B07.02) (SEQ ID NO: 1893)
LPPWPLHQQL (B07.02) (SEQ ID NO: 1894)
LPRKPTRAA (B07.02, B08.01) (SEQ ID NO: 1895)
LPRKPTRAAT (B07.02) (SEQ ID NO: 1896)
QQLLHRRPL (B08.01) (SEQ ID NO: 1897)
RLLPPWPLH (A03.01) (SEQ ID NO: 1898) BRCA, CRC, LUAD, PRAD, HNSC, LUSC, PAAD, STAD, BLCA, OV, LIHC, SKCM, UCEC, LAML, UCS, KICH, GBM, ACC TP53 P152fs LARTPLPSTRCFANWPRPALCSCGLIPHPRPAPASAPWPSTSSHST* (SEQ ID NO: 1628) APASAPWPST (B07.02) (SEQ ID NO: 1899)
APWPSTSSH (B07.02) (SEQ ID NO: 1900)
RPAPASAPW (B07.02) (SEQ ID NO: 1901)
WPSTSSHST (B07.02) (SEQ ID NO: 1902) BRCA, CRC, LUAD, PRAD, HNSC, LUSC, PAAD, STAD, BLCA, OV, LIHC, SKCM, UCEC, LAML, UCS, KICH, GBM, ACC UBR5 K2120fs SQGLYSSSASSGKCLMEVTVDRNCLEVL
PTKMSYAANLKNVMNMQNRQ
KK KGKNSPCCQKKLRVQ
NQGHLLMILLHN* (SEQ ID NO: 1629) RVQNQGHLL (B07.02) (SEQ ID NO: 1903) VHL L116fs
G123fs TRASPPRSSSAIAVRASCCPYGSSTSTASRSPTQRCRLARAAASTATEVTFGSSEMQGHTMGFWLTKLNYLCHLSMLTDSLFLPISHCQCIL* (SEQ ID NO: 1630) FLPISHCQCI (A02.01) (SEQ ID NO: 1904)
FWLTKLNYL (A24.02, B08.01) (SEQ ID NO: 1905)
HLSMLTDSL (A02.01) (SEQ ID NO: 1906)
HTMGFWLTK (A03.01) (SEQ ID NO: 1907)
HTMGFWLTKL (A02.01) (SEQ ID NO: 1908)
KLNYLCHLSM (A02.01) (SEQ ID NO: 1909)
LPISHCQCI (B07.02, B08.01) (SEQ ID NO: 1910)
LPISHCQCIL (B07.02, B08.01) (SEQ ID NO: 1911)
LTDSLFLPI (A01.01, A02.01) (SEQ ID NO: 1912)
LTKLNYLCHL (B08.01) (SEQ ID NO: 1913)
MLTDSLFLPI (A01.01, A02.01, B08.01) (SEQ ID NO: 1914)
MQGHTMGFWL (A02.01) (SEQ ID NO: 1915)
NYLCHLSML (A24.02) (SEQ ID NO: 1916)
SMLTDSLFL (A02.01) (SEQ ID NO: 1917)
TMGFWLTKL (A02.01) (SEQ ID NO: 1918)
YLCHLSMLT (A02.01) (SEQ ID NO: 1919) KIRC, KIRP Table 3D INSERT ¹ HER2 G776insYVMA ("YVMA" disclosed as SEQ ID NO: 3823) LGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMA YVMA GVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNW (SEQ ID NO: 1631) ILDEAYVMAY (A01.01) (SEQ ID NO: 1920)
VMAYVMAGV (A02.01) (SEQ ID NO: 1921)
YVMAYVMAG (A02.01, B07.02, B08.01) (SEQ ID NO: 1922)
YVMAYVMAGV (A02.01, B07.02, B08.01) (SEQ ID NO: 1923) Lungs' cancer

¹ Underlined AAs represent non-native AAs

² AA in bold represent the native AA amino acid sequence encoded by the second of the two fusion genes

³ Bold and underlined AA represent non-native AA of the amino acid sequence encoded by the second of the two frameshift fused genes.

The most common mutation in ibrutinib, a Bruton's tyrosine kinase (BTK)-targeting molecule used for CLL and certain lymphomas, is a cysteine to serine substitution at position 481 (C481S). This change produces a variety of peptides that bind to rank HLA molecules. The mutation is contained in a region having the amino acid sequence: IFIITEYMANG S LLNYLREMRHR (SEQ ID NO: 1924), the mutated serine is underlined.

Typical neoantigenic peptides corresponding to the C481S mutation are presented in Table 34 . The table also provides a list of HLA alleles encoded by protein products that can bind to peptides. In some embodiments, the disclosure provides C481S neo-epitopes for anticancer therapy, such as ANGSLLNY (SEQ ID NO: 1925); ANGSLLNYL (SEQ ID NO: 1926); ANGSLLNYLR (SEQ ID NO: 1927); EYMANGSL (SEQ ID NO: 1928); EYMANGSLLN (SEQ ID NO: 1929); EYMANGSLLNY (SEQ ID NO: 1930); GSLLNYLR (SEQ ID NO: 1931); GSLLNYLREM (SEQ ID NO: 1932); ITEYMANGS (SEQ ID NO: 1933); ITEYMANGSL (SEQ ID NO: 1934); ITEYMANGSLL (SEQ ID NO: 1935); MANGSLLNYL (SEQ ID NO: 1936); MANGSLLNYLR (SEQ ID NO: 1937); NGSLLNYL (SEQ ID NO: 1938); NGSLLNYL (SEQ ID NO: 1939); SLLNYLREMR (SEQ ID NO: 1940); TEYMANGSLL (SEQ ID NO: 1941); TEYMANGSLLNY (SEQ ID NO: 1942); YMANGSLL (SEQ ID NO: 1943); and YMANGSLLN (SEQ ID NO: 1944). Tables 35 and 3 present typical candidate neoantigens corresponding to other tumor-associated gene mutations. Table 36 provides a list of selected HLA-restricted BTK peptides for the purposes of this application and the corresponding protein encoded by the HLA allele to which the BTK peptide binds or is predicted to bind. Table 37 provides a list of selected BTK peptides and the corresponding preferred protein encoded by the HLA allele to which the BTK peptide binds or is predicted to bind, used in the context of this application.

Table 34 below lists typical neoantigenic peptides corresponding to the C481S mutation

BTK Peptides HLA allele ANGSLLNY (SEQ ID NO: 1945) HLA-A36:01 ANGSLLNYL (SEQ ID NO: 1946) HLA-C15:02; HLA-C08:01; HLA-C06:02; HLA-A02:04; HLA-C12:02; HLA-B44:02; HLA-C17:01; HLA-B38:01 ANGSLLNYLR (SEQ ID NO: 1947) HLA-A74:01, HLA-A31:01 EYMANGSL (SEQ ID NO: 1948) HLA-C14:02; HLA-C14:03; HLA-A24:02 EYMANGSLL (SEQ ID NO: 1949) HLA-A24:02; HLA-A23:01; HLA-A68:04; HLA-C14:02, HLA-C14:03, HLA-A33:03, HLA-C04:01, HLA-B15:09, HLA-B38:01, EYMANGSLLN (SEQ ID NO: 1950) HLA-A23:01, HLA-A24:02 EYMANGSLLNY (SEQ ID NO: 1951) HLA-A29:02 GSLLNYLR (SEQ ID NO: 1952) HLA-A74:01, HLA-A31:01 GSLLNYLREM (SEQ ID NO: 1953) HLA-B57:01, HLA-B58:02 ITEYMANGS (SEQ ID NO: 1954) HLA-A01:01 ITEYMANGSL (SEQ ID NO: 1955) HLA-A01:01 ITEYMANGSLL (SEQ ID NO: 1956) HLA-A01:01 MANGSLLNY (SEQ ID NO: 1957) HLA-C02:02, HLA-C03:02, HLA-B53:01, HLA-C12:02, HLA-C12:03, HLA-A36:01, HLA-A26:01, HLA-A25:01, HLA- A03:01, HLA-B46:01, HLA-B15:03, HLA-A33:03, HLA-B35:03, HLA-A11:01, HLA-B15:01, HLA-B35:03, HLA-A29: 02, HLA-B58:01, HLA-A30:02, HLA-B35:01 MANGSLLNYL (SEQ ID NO: 1958) HLA-C17:01, HLA-C02:02, HLA-B35:01, HLA-C03:03, HLA-C08:01, HLA-B35:03, HLA-C12:02, HLA-C01:02, HLA- C03:04, HLA-C08:02 MANGSLLNYLR (SEQ ID NO: 1959) HLA-A33:03, HLA-A74:01 NGSLLNYL (SEQ ID NO: 1960) HLA-B14:02 NGSLLNYLR (SEQ ID NO: 1961) HLA-A68:01, HLA-A33:03, HLA-A31:01, HLA-A74:01 SLLNYLREM (SEQ ID NO: 1962) HLA-A02:04, HLA-A02:03, HLA-C03:02, HLA-A03:01, HLA-A32:01, HLA-A02:07, HLA-C14:03, HLA-C14:02, HLA- A31:01, HLA-A30:02, HLA-A74:01, HLA-C06:02, HLA-B15:03, HLA-B46:01, HLA-B13:02, HLA-A25:01, HLA-A29: 02, HLA-C01:02, HLA-A02:01 SLLNYLREMR (SEQ ID NO: 1963) HLA-A74:01, HLA-A31:01 TEYMANGSL (SEQ ID NO: 1964) HLA-B14:02, HLA-B49:01, HLA-B44:03, HLA-B44:02, HLA-B37:01, HLA-B15:09, HLA-B41:01, HLA-B50:01, HLA- B18:01, HLA-B40:01, HLA-B40:02 TEYMANGSLL (SEQ ID NO: 1965) HLA-B40:02, HLA-B44:03, HLA-B49:01, HLA-B44:02, HLA-B49:01 TEYMANGSLLNY (SEQ ID NO: 1966) HLA-B44:03 YMANGSLL (SEQ ID NO: 1967) HLA-A01:01, HLA-C02:02, HLA-C04:01, HLA-C14:02, HLA-C14:03, HLA-C03:02, HLA-C17:01, HLA-C03:03, HLA- C03:04, HLA-B15:09 YMANGSLLN (SEQ ID NO: 1968) HLA-A01:01, HLA-A29:02 YMANGSLLNY (SEQ ID NO: 1969) HLA-A29:02, HLA-A36:01, HLA-B46:01, HLA-A25:01, HLA-B15:01, HLA-A26:01, HLA-A30:02, HLA-A32:01

Table 35 presents typical candidate neoantigens corresponding to other cancer-associated gene mutations

Gene Change in typical protein Sequence Mutation Context Peptides (example(s) of HLA allele) Typical diseases table 35A POINT MUTATION ¹ ABL1 E255K VADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQYG K VYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVC (SEQ ID NO: 1970) GQYGKVYEG (A02.01) (SEQ ID NO: 2105)
GQYGKVYEGV (A02.01) (SEQ ID NO: 2106)
KLGGGQYGK (A03.01) (SEQ ID NO: 2107)
KLGGGQYGKV (A02.01) (SEQ ID NO: 2108)
KVYEGVWKK (A02.01, A03.01) (SEQ ID NO: 2109)
KVYEGVWKKY (A03.01) (SEQ ID NO: 2110)
QYGKVYEGV (A24.02) (SEQ ID NO: 2111)
QYGKVYEGVW (A24.02) (SEQ ID NO: 2112) Chronic myeloid leukemia (CML), acute lymphocytic leukemia (ALL), gastrointestinal stromal tumors (GIST) ABL1 E255V VADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQYG V VYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVC (SEQ ID NO: 1971) GQYGVVYEG (A02.01) (SEQ ID NO: 2113)
GQYGVVYEGV (A02.01) (SEQ ID NO: 2114)
KLGGGQYGV (A02.01) (SEQ ID NO: 2115)
KLGGGQYGVV (A02.01) (SEQ ID NO: 2116)
QYGVVYEGV (A24.02) (SEQ ID NO: 2117)
QYGVVYEGVW (A24.02) (SEQ ID NO: 2118)
VVYEGVWKK (A02.01, A03.01) (SEQ ID NO: 2119)
VVYEGVWKKY (A03.01) (SEQ ID NO: 2120) Chronic myeloid leukemia (CML), acute lymphocytic leukemia (ALL), gastrointestinal stromal tumors (GIST) ABL1 M351T LLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVNAVVLLYMATQISSA T EYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKF (SEQ ID NO: 1972) ATQISSATEY (A01.01) (SEQ ID NO: 2121)
ISSATEYLEK (A03.01) (SEQ ID NO: 2122)
SSATEYLEK (A03.01) (SEQ ID NO: 2123)
TQISSATEYL (A02.01) (SEQ ID NO: 2124)
YMATQISSAT (A02.01) (SEQ ID NO: 2125) Chronic myeloid leukemia (CML), acute lymphocytic leukemia (ALL), gastrointestinal stromal tumors (GIST) ABL1 T315I SLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYII I EFMTYGNLLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLA (SEQ ID NO: 1973) FYIIIEFMTY (A24.02) (SEQ ID NO: 2126)
IIEFMTYGNL (A02.01) (SEQ ID NO: 2127)
IIIEFMTYG (A02.01) (SEQ ID NO: 2128)
IIIEFMTYGN (A02.01) (SEQ ID NO: 2129)
YIIIEFMTYG (A02.01) (SEQ ID NO: 2130) Chronic myeloid leukemia (CML), acute lymphocytic leukemia (ALL), gastrointestinal stromal tumors (GIST) ABL1 Y253H STVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQ H GEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLG (SEQ ID NO: 1974) GQHGEVYEGV (A02.01) (SEQ ID NO: 2131)
KLGGGQHGEV (A02.01) (SEQ ID NO: 2132) Chronic myeloid leukemia (CML), acute lymphocytic leukemia (ALL), gastrointestinal stromal tumors (GIST) ALK G1269A SSLAMLDLLHVARDIACGCQYLEENHFIHRDIAARNCLLTCPGPGRVAKI A DFGMARDIYRASYYRKGGCAMLPVKWMPPEAFMEGIFTSKTDTWSFGVLL (SEQ ID NO: 1975) KIADFGMAR (A03.01) (SEQ ID NO: 2133)
RVAKIADFGM (A02.01, B07.02) (SEQ ID NO: 2134) NSCLC ALK L1196M QVAVKTLPEVCSEQDELDFLMEALIISKFNHQNIVRCIGVSLQSLPRFIL M ELMAGGDLKSFLRETRPRPSQPSSLAMLDLLHVARDIACGCQYLEENHFI (SEQ ID NO: 1976) FILMELMAGG (A02.01) (SEQ ID NO: 2135)
ILMELMAGG (A02.01) (SEQ ID NO: 2136)
ILMELMAGGD (A02.01) (SEQ ID NO: 2137)
LMELMAGGDL (A02.01) (SEQ ID NO: 2138)
LPRFILMEL (B07.02, B08.01) (SEQ ID NO: 2139)
LPRFILMELM (B07.02) (SEQ ID NO: 2140)
LQSLPRFILM (A02.01, B08.01) (SEQ ID NO: 2141)
SLPRFILMEL (A02.01, A24.02, B07.02, B08.01) (SEQ ID NO: 2142) NSCLC BRAF V600E MIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNNIFLHEDLTVKIGDFGLAT E KSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELM (SEQ ID NO: 1977) LATEKSRWS (A02.01, B08.01) (SEQ ID NO: 2143)
LATEKSRWSG (A02.01, B08.01) (SEQ ID NO: 2144) CRC, GBM, KIRP, LUAD, SKCM, THCA BTK C481S MIKEGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGSLLNYLREMRHRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVND (SEQ ID NO: 1978) EYMANGSLL (A24.02) (SEQ ID NO: 2145) BTK EEF1B2 S43G MGFGDLKSPAGLQVLNDYLADKSYIEGYVPSQADVAVFEAVS G PPPADLCHALRWYNHIKSYEKEKASLPGVKKALGKYGPADVEDTTGSGAT (SEQ ID NO: 1979) GPPPADLCHAL (B07.02) (SEQ ID NO: 2146) BLCA, KIRP, PRAD, SKCM ERBB3 V104M ERCEVVMGNLEIVLTGHNADLSFLQWIREVTGYVLVAMNEFSTLPLPNLR M VRGTQVYDGKFAIFVMLNYNTNSSHALRQLRLTQLTEILSGGVYIEKNDK (SEQ ID NO: 1980) CRC, stomach cancer ESR1 D538G HLMAKAGLTLQQQHQRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPLY G LLLEMLDAHRLHAPTSRGGASVEETDQSHLATAGSTSSHSLQKYYITGEA (SEQ ID NO: 1981) GLLLEMLDA (A02.01) (SEQ ID NO: 2147)
LYGLLLEML (A24.02) (SEQ ID NO: 2148)
NVVPLYGLL (A02.01) (SEQ ID NO: 2149)
PLYGLLLEM (A02.01) (SEQ ID NO: 2150)
PLYGLLLEML (A02.01, A24.02) (SEQ ID NO: 2151)
VPLYGLLLEM (B07.02) (SEQ ID NO: 2152)
VVPLYGLLL (A02.01, A24.02) (SEQ ID NO: 2153) Mammary cancer ESR1 S463P NQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFL P STLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHQRLAQLLLILSH (SEQ ID NO: 1982) FLPSTLKSL (A02.01, A24.02, B08.01) (SEQ ID NO: 2154)
GVYTFLPST (A02.01) (SEQ ID NO: 2155)
GVYTFLPSTL (A02.01, A24.02) (SEQ ID NO: 2156)
TFLPSTLKSL (A24.02) (SEQ ID NO: 2157)
VYTFLPSTL (A24.02) (SEQ ID NO: 2158)
YTFLPSTLK (A03.01) (SEQ ID NO: 2159) Mammary cancer ESR1 Y537C IHLMAKAGLTLQQQHQRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPL C DLLLEMLDAHRLHAPTSRGGASVEETDQSHLATAGSTSSHSLQKYYITGE (SEQ ID NO: 1983) NVVPLCDLL (A02.01) (SEQ ID NO: 2160)
NVVPLCDLLL (A02.01) (SEQ ID NO: 2161)
PLCDLLLEM (A02.01) (SEQ ID NO: 2162)
PLCDLLLEML (A02.01) (SEQ ID NO: 2163)
VPLCDLLLEM (B07.02) (SEQ ID NO: 2164)
VVPLCDLLL (A02.01, A24.02) (SEQ ID NO: 2165) Mammary cancer ESR1 Y537N IHLMAKAGLTLQQQHQRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPL N DLLLEMLDAHRLHAPTSRGGASVEETDQSHLATAGSTSSHSLQKYYITGE (SEQ ID NO: 1984) NVVPLNDLL (A02.01) (SEQ ID NO: 2166)
NVVPLNDLLL (A02.01) (SEQ ID NO: 2167)
PLNDLLLEM (A02.01) (SEQ ID NO: 2168)
PLNDLLLEML (A02.01) (SEQ ID NO: 2169)
VPLNDLLLEM (B07.02) (SEQ ID NO: 2170) Mammary cancer ESR1 Y537S IHLMAKAGLTLQQQHQRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPL S DLLLEMLDAHRLHAPTSRGGASVEETDQSHLATAGSTSSHSLQKYYITGE (SEQ ID NO: 1985) NVVPLSDLL (A02.01) (SEQ ID NO: 2171)
NVVPLSDLLL (A02.01) (SEQ ID NO: 2172)
PLSDLLLEM (A02.01) (SEQ ID NO: 2173)
PLSDLLLEML (A02.01) (SEQ ID NO: 2174)
VPLSDLLLEM (B07.02) (SEQ ID NO: 2175)
VVPLSDLLL (A02.01, A24.02) (SEQ ID NO: 2176) Mammary cancer FGFR3 S249C HRIGGIKLRHQQWSLVMESVVPSDRGNYTCVVENKFGSIRQTYTLDVLER C PHRPILQAGLPANQTAVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKVG (SEQ ID NO: 1986) VLERCPHRPI (A02.01, B08.01) (SEQ ID NO: 2177)
YTLDVLERC (A02.01) (SEQ ID NO: 2178) BLCA, HNSC, KIRP, LUSC FRG1B L52S AVKLSDSRIALKSGYGKYLGINSDELVGHSDAIGPREQWEPVFQNGKMAL S ASNSCFIRCNEAGDIEAKSKTAGEEEMIKIRSCAEKETKKKDDIPEEDKG (SEQ ID NO: 1987) FQNGKMALS (A02.01) (SEQ ID NO: 2179) GBM, KIRP, PRAD, SKCM HER2 V777L
(Resistance) GSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAG L GSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCM (SEQ ID NO: 1988) VMAGLGSPYV (A02.01, A03.01) (SEQ ID NO: 2180) BRCA IDH1 R132H RVEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVSGWVKPIIIG H HAYGDQYRATDFVVPGPGKVEITYTPSDGTQKVTYLVHNFEEGGGVAMGM (SEQ ID NO: 1989) KPIIIGHHA (B07.02) (SEQ ID NO: 2181) BLCA, GBM, PRAD IDH1 R132C RVEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVSGWVKPIIIG C HAYGDQYRATDFVVPGPGKVEITYTPSDGTQKVTYLVHNFEEGGGVAMGM (SEQ ID NO: 1990) KPIIIGCHA (B07.02) (SEQ ID NO: 2182) BLCA, GBM, PRAD IDH1 R132G RVEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVSGWVKPIIIG G HAYGDQYRATDFVVPGPGKVEITYTPSDGTQKVTYLVHNFEEGGGVAMGM (SEQ ID NO: 1991) KPIIIGGHA (B07.02) (SEQ ID NO: 2183) BLCA, BRCA, CRC, GBM, HNSC, LUAD, PAAD, PRAD, UCEC IDH1 R132S RVEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVSGWVKPIIIG S HAYGDQYRATDFVVPGPGKVEITYTPSDGTQKVTYLVHNFEEGGGVAMGM (SEQ ID NO: 1992) KPIIIGSHA (B07.02) (SEQ ID NO: 2184) BLCA, BRCA, GBM, HNSC, LIHC, LUAD, LUSC, PAAD, SKCM, UCEC KIT T670I VAVKMLKPSAHLTEREALMSELKVLSYLGNHMNIVNLLGACTIGGPTLVI I EYCCYGDLLNFLRRKRDSFICSKQEDHAEAALYKNLLHSKESSCSDSTNE (SEQ ID NO: 1993) IIEYCCYGDL (A02.01) (SEQ ID NO: 2185)
TIGGPTLVII (A02.01) (SEQ ID NO: 2186)
VIIEYCCYG (A02.01) (SEQ ID NO: 2187) Gastrointestinal stromal tumors (GIST) KIT V654A VEATAYGLIKSDAAMTVAVKMLKPSAHLTEREALMSELKVLSYLGNHMNI A NLLGACTIGGPTLVITEYCCYGDLLNFLRRKRDSFICSKQEDHAEAALYK (SEQ ID NO: 1994) HMNIANLLGA (A02.01) (SEQ ID NO: 2188)
IANLLGACTI (A02.01) (SEQ ID NO: 2189)
MNIANLLGA (A02.01) (SEQ ID NO: 2190)
YLGNHMNIA (A02.01, B08.01) (SEQ ID NO: 2191)
YLGNHMNIAN (A02.01) (SEQ ID NO: 2192) Gastrointestinal stromal tumors (GIST) MEK C121S ISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQVLHE S NSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKKAGRIPEQILGKVSI (SEQ ID NO: 1995) VLHESNSPY (A03.01) (SEQ ID NO: 2193)
VLHESNSPYI (A02.01) (SEQ ID NO: 2194) Melanoma MEK P124L LGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQVLHECNS L YIVGFYGAFYSDGEISICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVI (SEQ ID NO: 1996) LQVLHECNSL (A02.01, B08.01) (SEQ ID NO: 2195)
LYIVGFYGAF (A24.02) (SEQ ID NO: 2196)
NSLYIVGFY (A01.01) (SEQ ID NO: 2197)
QVLHECNSL (A02.01, B08.01) (SEQ ID NO: 2198)
SLYIVGFYG (A02.01) (SEQ ID NO: 2199)
SLYIVGFYGA (A02.01) (SEQ ID NO: 2200)
VLHECNSLY (A03.01) (SEQ ID NO: 2201)
VLHECNSLYI (A02.01, A03.01) (SEQ ID NO: 2202) Melanoma MYC E39D MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQS D LQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGG (SEQ ID NO: 1997) FYQQQQQSDL (A24.02) (SEQ ID NO: 2203)
QQQSDLQPPA (A02.01) (SEQ ID NO: 2204)
QQSDLQPPA (A02.01) (SEQ ID NO: 2205)
YQQQQQSDL (A02.01, B08.01) (SEQ ID NO: 2206) Cancer of the lymphatic system; Burkitt's lymphoma MYC P57S FTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELL S TPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLG (SEQ ID NO: 1998) FELLSTPPL (A02.01, B08.01) (SEQ ID NO: 2207)
LLSTPPLSPS (A02.01) (SEQ ID NO: 2208) Lymphatic system cancer MYC T58I TNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLP I PPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGG (SEQ ID NO: 1999) FELLPIPPL (A02.01) (SEQ ID NO: 2209)
IWKKFELLPI (A24.02) (SEQ ID NO: 2210)
LLPIPPLSPS (A02.01, B07.02) (SEQ ID NO: 2211)
LPIPPLSPS (B07.02) (SEQ ID NO: 2212) Neuroblastoma PDGFRa T674I VAVKMLKPTARSSEKQALMSELKIMTHLGPHLNIVNLLGACTKSGPIYII I EYCFYGDLVNYLHKNRDSFLSHHPEKPKKELDIFGLNPADESTRSYVILS (SEQ ID NO: 2000) IIEYCFYGDL (A02.01) (SEQ ID NO: 2213)
IIIEYCFYG (A02.01) (SEQ ID NO: 2214)
IYIIIEYCF (A24.02) (SEQ ID NO: 2215)
IYIIIEYCFY (A24.02) (SEQ ID NO: 2216)
YIIIEYCFYG (A02.01) (SEQ ID NO: 2217) Chronic eosinophilic leukemia PIK3CA E542K IEEHANWSVSREAGFSYSHAGLSNRLARDNELRENDKEQLKAISTRDPLS K ITEQEKDFLWSHRHYCVTIPEILPKLLLSVKWNSRDEVAQMYCLVKDWPP (SEQ ID NO: 2001) KITEQEKDFL (A02.01) (SEQ ID NO: 2218) BLCA, BRCA, CESC, CRC, GBM, HNSC, KIRC, KIRP, LIHC, LUAD, LUSC, PRAD, UCEC PIK3CA E545K HANWSVSREAGFSYSHAGLSNRLARDNELRENDKEQLKAISTRDPLSEIT K QEKDFLWSHRHYCVTIPEILPKLLLSVKWNSRDEVAQMYCLVKDWPPIKP (SEQ ID NO: 2002) STRDPLSEITK (A03.01) (SEQ ID NO: 2219)
DPLSEITK (A03.01) (SEQ ID NO: 2220) BLCA, BRCA, CESC, CRC, GBM, HNSC, KIRC, KIRP, LIHC, LUAD, LUSC, PRAD, SKCM, UCEC PIK3CA H1047R LFINLFSMMLGSGMPELQSFDDIAYIRKTLALDKTEQEALEYFMKQMNDA R HGGWTTKMDWIFHTIKQHALN (SEQ ID NO: 2003) BRCA, CESC, CRC, GBM, HNSC, LIHC, LUAD, LUSC, PRAD, UCEC POLE P286R QRGGVITDEEETSKKIADQLDNIVDMREYDVPYHIRLSIDIETTKLPLKF R DAETDQIMMISYMIDGQGYLITNREIVSEDIEDFEFTPKPEYEGPFCVFN (SEQ ID NO: 2004) LPLKFRDAET (B07.02) (SEQ ID NO: 2221) Colorectal adenocarcinoma; adenocarcinoma of the uterus/endometrium; Colorectal adenocarcinoma, MSI+; uterine/endometrial adenocarcinoma, MSI+; Endometrioid adenocarcinoma; Serous endometrial carcinoma; Endometrial carcinosarcoma is a malignant mesodermal mixed tumor; Glioma; Astrocytoma; G.B.M. PTEN R130Q KFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKG Q TGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSY (SEQ ID NO: 2005) QTGVMICAYL (A02.01) (SEQ ID NO: 2222) BRCA, CESC, CRC, GBM, KIRC, LUSC, UCEC RAC1 P29S MQAIKCVVVGDGAVG
KTCLLISYTTNAF S G
EYIPTVFDNYSANVM
VDGKPVNLGLWDTAG
QEDYDRLRPLSYPQT
VGET (SEQ ID NO: 2006) AFSGEYIPTV (A02.01, A24.02) (SEQ ID NO: 2223) Melanoma TP53 G245S IRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMG S MNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEP (SEQ ID NO: 2007) SMNRRPILT (A02.01, B08.01) (SEQ ID NO: 2224)
YMCNSSCMGS (A02.01) (SEQ ID NO: 2225) BLCA, BRCA, CRC, GBM, HNSC, LUSC, PAAD, PRAD TP53 R175H TYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVR H CPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEV (SEQ ID NO: 2008) BLCA, BRCA, CRC, GBM, HNSC, LUAD, PAAD, PRAD, UCEC TP53 R248Q EGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMN Q RPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHE (SEQ ID NO: 2009) GMNQRPILT (A02.01) (SEQ ID NO: 2226) BLCA, BRCA, CRC, GBM, HNSC, KIRC, LIHC, LUSC, PAAD, PRAD, UCEC TP53 R248W EGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMN W RPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHE (SEQ ID NO: 2010) GMNWRPILT (A02.01) (SEQ ID NO: 2227) BLCA, BRCA, CRC, GBM, HNSC, LIHC, LUSC, PAAD, SKCM, UCEC TP53 R273C PEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEV C VCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPL (SEQ ID NO: 2011) LLGRNSFEVC (A02.01) (SEQ ID NO: 2228) BLCA, BRCA, CRC, GBM, HNSC, LUSC, PAAD, UCEC table 35B MSI-ASSOCIATED FRAME SHIFT ¹ ACVR2A D96fs; +1 GVEPCYGDKDKRRHCFATWKNISGSIEIVKQGCWLDDINCYDRTDCVEKK RQP* (SEQ ID NO: 2012) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome ACVR2A D96fs; -1 GVEPCYGDKDKRRHCFATWKNISGSIEIVKQGCWLDDINCYDRTDCVEKK TALKYIFVAVRAICVMKSFLIFRRWKSHSPLQIQLHLSHPITTSCSIPWCHLC* (SEQ ID NO: 2013) ALKYIFVAV (A02.01, B08.01) (SEQ ID NO: 2229)
ALKYIFVAVR (A03.01) (SEQ ID NO: 2230)
AVRAICVMK (A03.01) (SEQ ID NO: 2231)
AVRAICVMKS (A03.01) (SEQ ID NO: 2232)
CVEKKTALK (A03.01) (SEQ ID NO: 2233)
CVEKKTALKY (A01.01) (SEQ ID NO: 2234)
CVMKSFLIF (A24.02, B08.01) (SEQ ID NO: 2235)
CVMKSFLIFR (A03.01) (SEQ ID NO: 2236)
FLIFRRWKS (A02.01, B08.01) (SEQ ID NO: 2237)
FRRWKSHSPL (B08.01) (SEQ ID NO: 2238)
FVAVRAICV (A02.01, B08.01) (SEQ ID NO: 2239)
FVAVRAICVM (B08.01) (SEQ ID NO: 2240)
IQLHLSHPI (A02.01) (SEQ ID NO: 2241)
KSFLIFRRWK (A03.01) (SEQ ID NO: 2242)
KTALKYIFV (A02.01) (SEQ ID NO: 2243)
KYIFVAVRAI (A24.02) (SEQ ID NO: 2244)
RWKSHSPLQI (A24.02) (SEQ ID NO: 2245)
TALKYIFVAV (A02.01, B08.01) (SEQ ID NO: 2246)
VAVRAICVMK (A03.01) (SEQ ID NO: 2247)
VMKSFLIFR (A03.01) (SEQ ID NO: 2248)
VMKSFLIFRR (A03.01) (SEQ ID NO: 2249)
YIFVAVRAI (A02.01) (SEQ ID NO: 2250) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome C15ORF40 L132fs; +1 TAEAVNVAIAAPPSEGEANAELCRYLSKVLELRKSDVVLDKVGLALFFFF FETKSCSVAQAGVQWRSLGSLQPPPPGFKLFSCLSFLSSWDYRRMPPCLANFCIFNRDGVSPCWSGWS* (SEQ ID NO: 2014) ALFFFFFET (A02.01) (SEQ ID NO: 2251)
ALFFFFFETK (A03.01) (SEQ ID NO: 2252)
AQAGVQWRSL (A02.01) (SEQ ID NO: 2253)
CLANFCIFNR (A03.01) (SEQ ID NO: 2254)
CLSFLSSWDY (A01.01, A03.01) (SEQ ID NO: 2255)
FFETKSCSV (B08.01) (SEQ ID NO: 2256)
FFFETKSCSV (A02.01) (SEQ ID NO: 2257)
FKLFSCLSFL (A02.01) (SEQ ID NO: 2258)
FLSSWDYRRM (A02.01) (SEQ ID NO: 2259)
GFKLFSCLSF (A24.02) (SEQ ID NO: 2260)
KLFSCLSFL (A02.01, A03.01) (SEQ ID NO: 2261)
KLFSCLSFLS (A02.01, A03.01) (SEQ ID NO: 2262)
LALFFFFFET (A02.01) (SEQ ID NO: 2263)
LFFFFFETK (A03.01) (SEQ ID NO: 2264)
LSFLSSWDY (A01.01) (SEQ ID NO: 2265)
LSFLSSWDYR (A03.01) (SEQ ID NO: 2266)
RMPPCLANF (A24.02) (SEQ ID NO: 2267)
RRMPPCLANF (A24.02) (SEQ ID NO: 2268)
SLQPPPPGFK (A03.01) (SEQ ID NO: 2269)
VQWRSLGSL (A02.01) (SEQ ID NO: 2270) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome CNOT1 L1544fs; +1 LSVIIFFFVYIWHWALPLILNNHHICLMSSIILDCNSVRQSIMSVCFFFF SVIFSTRCLTDSRYPNICWFK* (SEQ ID NO: 2015) FFFSVIFST (A02.01) (SEQ ID NO: 2271)
MSVCFFFFSV (A02.01) (SEQ ID NO: 2272)
SVCFFFFSV (A02.01, B08.01) (SEQ ID NO: 2273)
SVCFFFFSVI (A02.01) (SEQ ID NO: 2274) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome CNOT1 L1544fs; -1 LSVIIFFFVYIWHWALPLILNNHHICLMSSIILDCNSVRQSIMSVCFFFF CYILNTMFDR* (SEQ ID NO: 2016) FFCYILNTMF (A24.02) (SEQ ID NO: 2275)
MSVCFFFFCY (A01.01) (SEQ ID NO: 2276)
SVCFFFFCYI (A02.01) (SEQ ID NO: 2277) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome EIF2B3 A151fs; -1 VLVLSCDLITTDVALHEVVDLFRAYDASLAMLMRKGQDSIEPVPGQKGKKK QWSSVTSLEWTAQERGCSSWLMKQTWMKSWSLRDPSYRSILEYVSTRVLWMPTSTV* (SEQ ID NO: 2017) KQWSSVTSL (A02.01) (SEQ ID NO: 2278)
VLWMPTSTV (A02.01) (SEQ ID NO: 2279) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome EPHB2 K1020fs; -1 SIQVMRAQMNQIQSVEGQPLARRPRATGRTKRCQPRDVTKKTCNSNDGKK REWEKRKQILGGGGKYKEYFLKRILIRKAMTVLAGDKKGLGRFMRCVQSETKAVSLQLPLGR* (SEQ ID NO: 2018) ILIRKAMTV (A02.01) (SEQ ID NO: 2280) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome ESRP1 N512fs; +1 LDFLGEFATDIRTHGVHMVLNHQGRPSGDAFIQMKSADRAFMAAQKCHKK KHEGQIC* (SEQ ID NO: 2019) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome ESRP1 N512fs; -1 LDFLGEFATDIRTHGVHMVLNHQGRPSGDAFIQMKSADRAFMAAQKCHKK T* (SEQ ID NO: 2020) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome FAM111B A273fs; -1 GALCKDGRRFRSDIGE
FEWKLKEGHKKIYGK
QSMVDEVSGKVLEMD
ISKKK HYNRKISIKK
LNRMKVPLMKLITRV*
(SEQ ID NO: 2021) RMKVPLMK (A03.01) (SEQ ID NO: 2281) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome GBP3 T585fs; -1 RERAQLLEEQEKTLTSKLQEQARVLKERCQGESTQLQNEIQKLQKTLKKK PRDICRIS* (SEQ ID NO: 2022) TLKKKPRDI (B08.01) (SEQ ID NO: 2282) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome JAK1 P861fs; +1 VNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK TSN* (SEQ ID NO: 2023) LIEGFEALLK (A03.01) (SEQ ID NO: 2283) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome JAK1 K860fs; -1 CRPVTPSCKELADLMTRCMNYDPNQRPFFRAIMRDINKLEEQNPDIVSEK NQQLKWTPHILKSAS* (SEQ ID NO: 2024) QQLKWTPHI (A02.01) (SEQ ID NO: 2284)
QLKWTPHILK (A03.01) (SEQ ID NO: 2285)
IVSEKNQQLK (A03.01) (SEQ ID NO: 2286)
QLKWTPHILK (A03.01) (SEQ ID NO: 2287)
QQLKWTPHI (A24.02) (SEQ ID NO: 2288)
NQQLKWTPHIL (B08.01) (SEQ ID NO: 2289)
NQQLKWTPHI (B08.01) (SEQ ID NO: 2290)
QLKWTPHIL (B08.01) (SEQ ID NO: 2291) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome LMAN1 E305fs; +1 DDHDVLSFLTFQLTEPGKEPPTPDKEISEKEKEKYQEEFEHFQQELDKKK RGIPEGPPRPPRAACGGNI* (SEQ ID NO: 2025) GPPRPPRAAC (B07.02) (SEQ ID NO: 2292)
PPRPPRAAC (B07.02) (SEQ ID NO: 2293) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome LMAN1 E305fs; -1 DDHDVLSFLTFQLTEPGKEPPTPDKEISEKEKEKYQEEFEHFQQELDKKK RNSRRATPTSKGSLRRKYLRV* (SEQ ID NO: 2026) SLRRKYLRV (B08.01) (SEQ ID NO: 2294) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome MSH3 N385fs; +1 TKSTLIGEDVNPLIKLDDAVNVDEIMTDTSYLLCISENKENVRDKKKG QHFYWHCGSAACHRRGCV* (SEQ ID NO: 2027) SAACHRRGCV (B08.01) (SEQ ID NO: 2295) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome MSH3 K383fs; -1 LYTKSTLIGEDVNPLIKLDDAVNVDEIMTDTSTSYLLCISENKENVRDKK RATFLLALWECSLPQARLCLIVSRTLLLVQS* (SEQ ID NO: 2028) ALWECSLPQA (A02.01) (SEQ ID NO: 2296)
CLIVSRTLL (B08.01) (SEQ ID NO: 2297)
CLIVSRTLLL (A02.01, B08.01) (SEQ ID NO: 2298)
FLLALWECS (A02.01) (SEQ ID NO: 2299)
FLLALWECSL (A02.01, B08.01) (SEQ ID NO: 2300)
IVSRTLLLV (A02.01) (SEQ ID NO: 2301)
LIVSRTLLL (A02.01, B08.01) (SEQ ID NO: 2302)
LIVSRTLLLV (A02.01) (SEQ ID NO: 2303)
LLALWECSL (A02.01, B08.01) (SEQ ID NO: 2304)
LPQARLCLI (B08.01, B07.02) (SEQ ID NO: 2305)
LPQARLCLIV (B08.01) (SEQ ID NO: 2306)
NVRDKKRATF (B08.01) (SEQ ID NO: 2307)
SLPQARLCLI (A02.01, B08.01) (SEQ ID NO: 2308) MSI+CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome NDUFC2 A70fs; +1 LPPPKLTDPRLLYIGFLGYCSGLIDNLIRRRPIATAGLHRQLLYITAFFF CWILSCKT* (SEQ ID NO: 2029) FFCWILSCK (A03.01) (SEQ ID NO: 2309)
FFFCWILSCK (A03.01) (SEQ ID NO: 2310)
ITAFFFCWI (A02.01) (SEQ ID NO: 2311)
LYITAFFFCW (A24.02) (SEQ ID NO: 2312)
YITAFFFCWI (A02.01) (SEQ ID NO: 2313) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome NDUFC2 F69fs; -1 SLPPPKLTDPRLLYIGFLGYCSGLIDNLIRRRPIATAGLHRQLLYITAFF LLDIIL* (SEQ ID NO: 2030) ITAFFLLDI (A02.01) (SEQ ID NO: 2314)
LLYITAFFL (A02.01, B08.01) (SEQ ID NO: 2315)
LLYITAFFLL (A02.01, A24.02) (SEQ ID NO: 2316)
LYITAFFLL (A24.02) (SEQ ID NO: 2317)
LYITAFFLLD (A24.02) (SEQ ID NO: 2318)
YITAFFLLDI (A02.01) (SEQ ID NO: 2319) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome RBM27 Q817; +1 NQSGGAGEDCQIFSTPGHPKMIYSSSNLKTPSKLCSGSKSHDVQEVLKKK TGSNEVTTRYEEKKTGSVRKANRMPKDVNIQVRKKQKHETRRKSKYNEDFERAWREDLTIKR* (SEQ ID NO: 2031) GSNEVTTRY (A01.01) (SEQ ID NO: 2320)
MPKDVNIQV (B07.02) (SEQ ID NO: 2321)
TGSNEVTTRY (A01.01) (SEQ ID NO: 2322) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome RPL22 K16fs; +1 MAPVKKLVVKGGKKK EASSEVHS* (SEQ ID NO: 2032) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome RPL22 K15fs; -1 MAPVKKLVVKGGKK RSKF* (SEQ ID NO: 2033) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome SEC31A I462fs; +1 MPSHQGAEQQQQQHHVFISQVVTEKEFLSRSDQLQQAVQSQGFINYCQKK N* (SEQ ID NO: 2034) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome SEC31A I462fs; -1 MPSHQGAEQQQQQHHVFISQVVTEKEFLSRSDQLQQAVQSQGFINYCQKK LMLLRLNLRKMCGPF* (SEQ ID NO: 2035) KKLMLLRLNL (A02.01) (SEQ ID NO: 2323)
KLMLLRLNL (A02.01, A03.01, B07.02, B08.01) (SEQ ID NO: 2324)
KLMLLRLNLR (A03.01) (SEQ ID NO: 2325)
LLRLNLRKM (B08.01) (SEQ ID NO: 2326)
LMLLRLNL (B08.01) (SEQ ID NO: 2327)
LMLLRLNLRK (A03.01) (SEQ ID NO: 2328)
LNLRKMCGPF (B08.01) (SEQ ID NO: 2329)
MLLRLNLRK (A03.01) (SEQ ID NO: 2330)
MLLRLNLRKM (A02.01, A03.01, B08.01) (SEQ ID NO: 2331)
NLRKMCGPF (B08.01) (SEQ ID NO: 2332)
NYCQKKLMLL (A24.02) (SEQ ID NO: 2333)
YCQKKLMLL (B08.01) (SEQ ID NO: 2334) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome SEC63 K530fs; +1 AEVFEKEQSICAAEE
QPAEDGQGETNKNRT
KGGWQQKSKGPKKTA
KSKKK ETFKKKTYTC
AITTVKATETKAGKW
SRWE* (SEQ ID NO: 2036) FKKKTYTCAI (B08.01) (SEQ ID NO: 2335)
ITTVKATETK (A03.01) (SEQ ID NO: 2336)
KSKKKETFK (A03.01) (SEQ ID NO: 2337)
KSKKKETFKK (A03.01) (SEQ ID NO: 2338)
KTYTCAITTV (A02.01, A24.02) (SEQ ID NO: 2339)
TFKKKTYTC (B08.01) (SEQ ID NO: 2340)
TYTCAITTV (A24.02) (SEQ ID NO: 2341)
TYTCAITTVK (A03.01) (SEQ ID NO: 2342)
YTCAITTVK (A03.01) (SEQ ID NO: 2343) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome SEC63 K529fs; -1 MAEVFEKEQSICAAEEQPAEDGQGETNKNRTKGGWQQKSKGPKKTAKSKK RNL* (SEQ ID NO: 2037) TAKSKKRNL (B08.01) (SEQ ID NO: 2344) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome SLC35F5 C248fs; -1 NIMEIRQLPSSHALEAKLSRMSYPVKEQESILKTVGKLTATQVAKISFFF ALCGFWQICHIKKHFQTHKLL* (SEQ ID NO: 2038) FALCGFWQI (A02.01) (SEQ ID NO: 2345) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome SMAP1 K172fs; +1 YEKKKYYDKNAIAITNISSSDAPLQPLVSSPSLQAAVDKNKLEKEKEKKK GREKERKGARKAGKTTYS* (SEQ ID NO: 2039) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome SMAP1 K171fs; -1 KYEKKKYYDKNAIAITNISSSDAPLQPLVSSPSLQAAVDKNKLEKEKEKK RKRKREKRSQKSRQNHLQLKSCRRKISNWSLKKVPALKKLRSPLWIF* (SEQ ID NO: 2040) LKKLRSPL (B08.01) (SEQ ID NO: 2346)
SLKKVPAL (B08.01) (SEQ ID NO: 2347)
RKISNWSLKK (A03.01) (SEQ ID NO: 2348)
VPALKKLRSPL (B07.02) (SEQ ID NO: 2349) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome TFAM E148fs; +1 IYQDAYRAEWQVYKEEISRFKEQLTPSQIMSLEKEIMDKHLKRKAMTKKK RVNTAWKTKKTSFSL* (SEQ ID NO: 2041) KRVNTAWKTK (A03.01) (SEQ ID NO: 2350)
MTKKKRVNTA (B08.01) (SEQ ID NO: 2351)
RVNTAWKTK (A03.01) (SEQ ID NO: 2352)
RVNTAWKTKK (A03.01) (SEQ ID NO: 2353)
TKKKRVNTA (B08.01) (SEQ ID NO: 2354)
WKTKKTSFSL (B08.01) (SEQ ID NO: 2355) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome TFAM E148fs; -1 IYQDAYRAEWQVYKEEISRFKEQLTPSQIMSLEKEIMDKHLKRKAMTKKK S* (SEQ ID NO: 2042) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome TGFBR2 P129fs; +1 KPQEVCVAVWRKNDENITLETVCHDPKLPYHDFILEDAASPKCIMKEKKK AW* (SEQ ID NO: 2043) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome TGFBR2 K128fs: -1 EKPQEVCVAVWRKNDENITLETVCHDPKLPYHDFILEDAASPKCIMKEKK SLVRLSSCVPVALMSAMTTSSSQKNITPAILTCC* (SEQ ID NO: 2044) ALMSAMTTS (A02.01) (SEQ ID NO: 2356)
AMTTSSSQK (A03.01, A11.01) (SEQ ID NO: 2357)
AMTTSSSQKN (A03.01) (SEQ ID NO: 2358)
CIMKEKKSL (B08.01) (SEQ ID NO: 2359)
CIMKEKKSLV (B08.01) (SEQ ID NO: 2360)
IMKEKKSL (B08.01) (SEQ ID NO: 2361)
IMKEKKSLV (B08.01) (SEQ ID NO: 2362)
KSLVRLSSCV (A02.01) (SEQ ID NO: 2363)
LVRLSSCVPV (A02.01) (SEQ ID NO: 2364)
RLSSCVPVA (A02.01, A03.01) (SEQ ID NO: 2365)
RLSSCVPVAL (A02.01) (SEQ ID NO: 2366)
SAMTTSSSQK (A03.01, A11.01) (SEQ ID NO: 2367)
SLVRLSSCV (A02.01) (SEQ ID NO: 2368)
VPVALMSAM (B07.02) (SEQ ID NO: 2369)
VRLSSCVPVA (A02.01) (SEQ ID NO: 2370) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome THAP5 K99fs; -1 VPSKYQFLCSDHFTTP
DSLDIRWGIRYLKQT
AVPTIFSLPEDNQGK
DPSKK NPRRKTWKMR
KKYAQKPSQKNHLY*
(SEQ ID NO: 2045) KMRKKYAQK (A03.01) (SEQ ID NO: 2371) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome TTK R854fs; -1 GTTEEMKYVLGQLVGLNSPNSILKAAKTLYEHYSGGESHNSSSSKTFEKK GEKNDLQLFVMSDTTYKIYWTVILLNPCGNLHLKTTSL* (SEQ ID NO: 2046) FVMSDTTYK (A03.01) (SEQ ID NO: 2372)
FVMSDTTYKI (A02.01) (SEQ ID NO: 2373)
KTFEKKGEK (A03.01) (SEQ ID NO: 2374)
LFVMSDTTYK (A03.01) (SEQ ID NO: 2375)
MSDTTYKIY (A01.01) (SEQ ID NO: 2376)
VMSDTTYKI (A02.01) (SEQ ID NO: 2377)
VMSDTTYKIY (A01.01) (SEQ ID NO: 2378) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome XPOT F126fs; -1 QQLIRETLISWLQAQMLNPQPEKTFIRNKAAQVFALLFVTEYLTKWPKFF LTFSQ* (SEQ ID NO: 2047) YLTKWPKFFL (A02.01) (SEQ ID NO: 2379) MSI+ CRC, MSI+ Uterine/endometrial cancer, MSI+ Stomach cancer, Lynch syndrome table 35C FRAME SHIFT ¹ APC V1352fs
F1354fs
Q1378fs
S1398fs AKFQQCHSTLEPNPADCRVLVYLQNQPGTKLLNFLQERNLPPKVVLRHPKVHLNTMFRRPHSCLADVLLSVHLIVLRVVRLPAPFRVNHAVEW* (SEQ ID NO: 2048) FLQERNLPP (A02.01) (SEQ ID NO: 2380)
FRRPHSCLA (B08.01) (SEQ ID NO: 2381)
LIVLRVVRL (B08.01) (SEQ ID NO: 2382)
LLSVHLIVL (A02.01, B08.01) (SEQ ID NO: 2383) CRC, LUAD, UCEC, STAD APC S1421fs
R1435fs
T1438fs
P1442fs
P1443fs
V1452fs
P1453fs
K1462fs
E1464fs APVIFQIALDKPCHQAEVKHLHHLLKQLKPSEKYLKIKHLLLKRERVDLSKLQ* (SEQ ID NO: 2049) EVKHLHHLL (B08.01) (SEQ ID NO: 2384)
HLHHLLKQLK (A03.01) (SEQ ID NO: 2385)
HLLLKRERV (B08.01) (SEQ ID NO: 2386)
KIKHLLLKR (A03.01) (SEQ ID NO: 2387)
KPSEKYLKI (B07.02) (SEQ ID NO: 2388)
KYLKIKHLL (A24.02) (SEQ ID NO: 2389)
KYLKIKHLLL (A24.02) (SEQ ID NO: 2390)
LLKQLKPSEK (A03.01) (SEQ ID NO: 2391)
LLKRERVDL (B08.01) (SEQ ID NO: 2392)
LLLKRERVDL (B08.01) (SEQ ID NO: 2393)
QLKPSEKYLK (A03.01) (SEQ ID NO: 2394)
YLKIKHLLL (A02.01, B08.01) (SEQ ID NO: 2395)
YLKIKHLLLK (A03.01) (SEQ ID NO: 2396) CRC, LUAD, UCEC, STAD APC T1487fs
H1490fs
L1488fs MLQFRGSRFFQMLILYYILPRKVLQMDFLVHPA* (SEQ ID NO: 2050) ILPRKVLQM (B08.01) (SEQ ID NO: 2397)
KVLQMDFLV (A02.01, A24.02) (SEQ ID NO: 2398)
LPRKVLQMDF (B07.02, B08.01) (SEQ ID NO: 2399)
LQMDFLVHPA (A02.01) (SEQ ID NO: 2400)
QMDFLVHPA (A02.01) (SEQ ID NO: 2401)
YILPRKVLQM (A02.01, B08.01) (SEQ ID NO: 2402) CRC, LUAD, UCEC, STAD ARID1A Q1306fs
S1316fs
Y1324fs
T1348fs
G1351fs
G1378fs
P1467fs ALGPHSRISCLPTQTRGCILLAATPRSSSSSSSNDMIPMAISSPPKAPLLAAPSPASRLQCINSNSRITSGQWMAHMALLPSGTKGRCTACHTALGRGSLSSSSSCPQPSPSLPASNKLPSPLLSKMYTTSMAMPILPLPQLLLSADQQAAPRTNFHSSLAETVSLHPLAPMPSKTCHHK* (SEQ ID NO: 2051) APSPASRLQC (B07.02) (SEQ ID NO: 2403)
HPLAPMPSKT (B07.02) (SEQ ID NO: 2404)
ILPLPQLLL (A02.01) (SEQ ID NO: 2405)
LLLSADQQA (A02.01) (SEQ ID NO: 2406)
LPTQTRGCI (B07.02) (SEQ ID NO: 2407)
LPTQTRGCIL (B07.02) (SEQ ID NO: 2408)
RISCLPTQTR (A03.01) (SEQ ID NO: 2409)
SLAETVSLH (A03.01) (SEQ ID NO: 2410)
TPRSSSSSS (B07.02) (SEQ ID NO: 2411)
TPRSSSSSSS (B07.02) (SEQ ID NO: 2412) STAD, UCEC, BLCA, BRCA, LUSC, CESC, KIRC, UCS ARID1A S674fs
P725fs
R727fs
I736fs AHQGFPAAKESRVIQLSLLSLLIPPLTCLASEALPRPLLALPPVLLSLAQDHSRLLQCQATRCHLGHPVASRTASCILP* (SEQ ID NO: 2052) ALPPVLLSL (A02.01) (SEQ ID NO: 2413)
ALPPVLLSLA (A02.01) (SEQ ID NO: 2414)
ALPRPLLAL (A02.01) (SEQ ID NO: 2415)
ASRTASCIL (B07.02) (SEQ ID NO: 2416)
EALPRPLLAL (B08.01) (SEQ ID NO: 2417)
HLGHPVASR (A03.01) (SEQ ID NO: 2418)
HPVASRTAS (B07.02) (SEQ ID NO: 2419)
HPVASRTASC (B07.02) (SEQ ID NO: 2420)
IIQLSLLLSLL (A02.01) (SEQ ID NO: 2421)
IQLSLLLSLL (A02.01) (SEQ ID NO: 2422)
IQLSLLSLLI (A02.01, A24.02) (SEQ ID NO: 2423)
LLALPPVLL (A02.01) (SEQ ID NO: 2424)
LLIPPLTCL (A02.01) (SEQ ID NO: 2425)
LLIPPLTCLA (A02.01) (SEQ ID NO: 2426)
LLSLLIPPL (A02.01) (SEQ ID NO: 2427)
LLSLLIPPLT (A02.01) (SEQ ID NO: 2428)
LPRPLLALPP (B07.02) (SEQ ID NO: 2429)
QLSLLSLLI (A02.01) (SEQ ID NO: 2430)
RLLQCQATR (A03.01) (SEQ ID NO: 2431)
RPLLALPPV (B07.02) (SEQ ID NO: 2432)
RPLLALPPVL (B07.02) (SEQ ID NO: 2433)
SLAQDHSRL (A02.01) (SEQ ID NO: 2434)
SLAQDHSRLL (A02.01) (SEQ ID NO: 2435)
SLLIPPLTCL (A02.01) (SEQ ID NO: 2436)
SLLSLLIPP (A02.01) (SEQ ID NO: 2437)
SLLSLLIPPL (A02.01, B08.01) (SEQ ID NO: 2438) STAD, UCEC, BLCA, BRCA, LUSC, CESC, KIRC, UCS ARID1A G414fs
Q473fs
H477fs
S499fs
P504fs
Q548fs
P549fs PILAATGTSVRTAARTWVPRAAIRVPDPAAVPDDHAGPGAECHGRPLLYTADSSLWTTRPQRVWSTGPDSILQPAKSSPSAAAATLLPATTVPDPSCPTFVSAAATVSTTTTAPVLSASILPAAIPASTSAVPGSIPLPAVDDTAAPPEPAPLLTATGSVSLPAAATSAASTLDALPAGCVSSAPVSAVPANCLFPAALPSTAGAISRFIWVSGILSPLNDLQ* (SEQ ID NO: 2053) AAATSAASTL (B07.02) (SEQ ID NO: 2439)
AAIPASTSAV (B07.02) (SEQ ID NO: 2440)
AIPASTSAV (A02.01) (SEQ ID NO: 2441)
ALPAGCVSSA (A02.01) (SEQ ID NO: 2442)
APLLTATGSV (B07.02) (SEQ ID NO: 2443)
APVLSASIL (B07.02) (SEQ ID NO: 2444)
ATLLPATTV (A02.01) (SEQ ID NO: 2445)
ATVSTTTAPV (A02.01) (SEQ ID NO: 2446)
AVPANCLFPA (A02.01) (SEQ ID NO: 2447)
CLFPAALPST (A02.01) (SEQ ID NO: 2448)
CPTFVSAAA (B07.02) (SEQ ID NO: 2449)
FPAALPSTA (B07.02) (SEQ ID NO: 2450)
FPAALPSTAG (B07.02) (SEQ ID NO: 2451)
GAECHGRPL (B07.02) (SEQ ID NO: 2452)
GAISRFIWV (A02.01) (SEQ ID NO: 2453)
ILPAAIPAST (A02.01) (SEQ ID NO: 2454)
IWVSGILSPL (A24.02) (SEQ ID NO: 2455)
LLTATGSVSL (A02.01) (SEQ ID NO: 2456)
LLYTADSSL (A02.01) (SEQ ID NO: 2457)
LPAAATSAA (B07.02) (SEQ ID NO: 2458)
LPAAATSAAS (B07.02) (SEQ ID NO: 2459)
LPAAIPAST (B07.02) (SEQ ID NO: 2460)
LPAGCVSSA (B07.02) (SEQ ID NO: 2461)
LPAGCVSSAP (B07.02) (SEQ ID NO: 2462)
LYTADSSLW (A24.02) (SEQ ID NO: 2463)
QPAKSSPSA (B07.02) (SEQ ID NO: 2464)
QPAKSSPSAA (B07.02) (SEQ ID NO: 2465)
RFIWVSGIL (A24.02) (SEQ ID NO: 2466)
RPQRVWSTG (B07.02) (SEQ ID NO: 2467)
RVWSTGPDSI (A02.01) (SEQ ID NO: 2468)
SAVPGSIPL (B07.02) (SEQ ID NO: 2469)
SILPAAIPA (A02.01) (SEQ ID NO: 2470)
SLPAAATSA (A02.01) (SEQ ID NO: 2471)
SLPAAATSAA (A02.01) (SEQ ID NO: 2472)
SLWTTRPQR (A03.01) (SEQ ID NO: 2473)
SLWTTRPQRV (A02.01) (SEQ ID NO: 2474)
SPSAAAATL (B07.02) (SEQ ID NO: 2475)
SPSAAAATLL (B07.02) (SEQ ID NO: 2476)
TLDALPAGCV (A02.01) (SEQ ID NO: 2477)
TVSTTTAPV (A02.01) (SEQ ID NO: 2478)
VLSASILPA (A02.01) (SEQ ID NO: 2479)
VLSASILPAA (A02.01) (SEQ ID NO: 2480)
VPANCLFPA (B07.02) (SEQ ID NO: 2481)
VPANCLFPAA (B07.02) (SEQ ID NO: 2482)
VPDPSCPTF (B07.02) (SEQ ID NO: 2483)
VPGSIPLPA (B07.02) (SEQ ID NO: 2484)
VPGSIPLPAV (B07.02) (SEQ ID NO: 2485)
WVSGILSPL (A02.01) (SEQ ID NO: 2486)
YTADSSLWTT (A02.01) (SEQ ID NO: 2487) STAD, UCEC, BLCA, BRCA, LUSC, CESC, KIRC, UCS ARID1A T433fs
A441fs
Y447fs
P483fs
P484fs
P504fs
S519fs
H544fs
P549fs
P554fs
Q563fs PCRAGRRVPWAASLIHSRFLLMDNKAPAGMVNRARLHITTSKVLTLSSSSHPTPSNHRPRPLMPNLRISSSHSLNHHSSSPLSLHTPSSHPSLHISSPRLHTPPSSRRHSSTPRASPPTHSHRLSLLTSSSNLSSQHPRRSPSRLRILSPSLSSPSKLPIPSSASLHRRSYLKIHLGLRHPQPPQ* (SEQ ID NO: 2054) APAGMVNRA (B07.02) (SEQ ID NO: 2488)
ASLHRRSYL (B08.01) (SEQ ID NO: 2489)
ASLHRRSYLK (A03.01) (SEQ ID NO: 2490)
FLLMDNKAPA (A02.01) (SEQ ID NO: 2491)
HPRRSPSRL (B07.02, B08.01) (SEQ ID NO: 2492)
HPSLHISSP (B07.02) (SEQ ID NO: 2493)
HRRSYLKIHL (B08.01) (SEQ ID NO: 2494)
HSRFLLMDNK (A03.01) (SEQ ID NO: 2495)
KLPIPSSASL (A02.01) (SEQ ID NO: 2496)
KVLTLSSSSH (A03.01) (SEQ ID NO: 2497)
LIHSRFLLM (B08.01) (SEQ ID NO: 2498)
LLMDNKAPA (A02.01) (SEQ ID NO: 2499)
LMDNKAPAGM (A02.01) (SEQ ID NO: 2500)
LPIPSSASL (B07.02) (SEQ ID NO: 2501)
MPNLRISSS (B07.02, B08.01) (SEQ ID NO: 2502)
MPNLRISSSH (B07.02) (SEQ ID NO: 2503)
NLRISSSHSL (B07.02, B08.01) (SEQ ID NO: 2504)
PPTHSHRLSL (B07.02) (SEQ ID NO: 2505)
RAGRRVPWAA (B08.01) (SEQ ID NO: 2506)
RARLHITTSK (A03.01) (SEQ ID NO: 2507)
RISSSHSLNH (A03.01) (SEQ ID NO: 2508)
RLHTPPSSR (A03.01) (SEQ ID NO: 2509)
RLHTPPSSRR (A03.01) (SEQ ID NO: 2510)
RLRILSPSL (A02.01, B07.02, B08.01) (SEQ ID NO: 2511)
RPLMPNLRI (B07.02) (SEQ ID NO: 2512)
RPRPLMPNL (B07.02) (SEQ ID NO: 2513)
SASLHRRSYL (B07.02, B08.01) (SEQ ID NO: 2514)
SLHISSPRL (A02.01) (SEQ ID NO: 2515)
SLHRRSYLK (A03.01) (SEQ ID NO: 2516)
SLHRRSYLKI (B08.01) (SEQ ID NO: 2517)
SLIHSRFLL (A02.01) (SEQ ID NO: 2518)
SLIHSRFLLM (A02.01, B08.01) (SEQ ID NO: 2519)
SLLTSSSNL (A02.01) (SEQ ID NO: 2520)
SLNHHSSSPL (A02.01, B07.02, B08.01) (SEQ ID NO: 2521)
SLSSPSKLPI (A02.01) (SEQ ID NO: 2522)
SPLSLHTPS (B07.02) (SEQ ID NO: 2523)
SPLSLHTPSS (B07.02) (SEQ ID NO: 2524)
SPPTHSHRL (B07.02) (SEQ ID NO: 2525)
SPRLHTPPS (B07.02) (SEQ ID NO: 2526)
SPRLHTPPSS (B07.02) (SEQ ID NO: 2527)
SPSLSSPSKL (B07.02) (SEQ ID NO: 2528)
SYLKIHLGL (A24.02) (SEQ ID NO: 2529)
TPSNHRPRPL (B07.02, B08.01) (SEQ ID NO: 2530)
TPSSHPSLHI (B07.02) (SEQ ID NO: 2531) STAD, UCEC, BLCA, BRCA, LUSC, CESC, KIRC, UCS ARID1A A2137fs
P2139fs
L1970fs
V1994fs RTNPTVRMRPHCVPFWTGRILLPSAASVCPIPFEACHLQAMTLRCPNTQGCCSSWAS* (SEQ ID NO: 2055) CVPFWTGRIL (B07.02) (SEQ ID NO: 2532)
HCVPFWTGRIL (B07.02) (SEQ ID NO: 2533)
ILLPSAASV (A02.01) (SEQ ID NO: 2534)
ILLPSAASVC (A02.01) (SEQ ID NO: 2535)
LLPSAASVCPI (A02.01) (SEQ ID NO: 2536)
LPSAASVCPI (B07.02) (SEQ ID NO: 2537)
MRPHCVPF (B08.01) (SEQ ID NO: 2538)
RILLPSAASV (A02.01) (SEQ ID NO: 2539)
RMRPHCVPF (A24.02, B07.02, B08.01) (SEQ ID NO: 2540)
RMRPHCVPFW (A24.02) (SEQ ID NO: 2541)
RTNPTVRMR (A03.01) (SEQ ID NO: 2542)
SVCPIPFEA (A02.01) (SEQ ID NO: 2543)
TVRMRPHCV (B08.01) (SEQ ID NO: 2544)
TVRMRPHCVPF (B08.01) (SEQ ID NO: 2545)
VPFWTGRIL (B07.02) (SEQ ID NO: 2546)
VPFWTGRILL (B07.02) (SEQ ID NO: 2547)
VRMRPHCVPF (B08.01) (SEQ ID NO: 2548) STAD, UCEC, BLCA, BRCA, LUSC, CESC, KIRC, UCS ARID1A N756fs
S764fs
T783fs
Q799fs
A817fs TNQALPKIEVICRGTPRCPSTVPPSPAQPYLRVSLPEDRYTQAWAPTSRTPWGAMVPRGVSMAHKVATPGSQTIMPCPMPTTPVQAWLEA* (SEQ ID NO: 2056) AMVPRGVSM (B07.02, B08.01) (SEQ ID NO: 2549)
AMVPRGVSMA (A02.01) (SEQ ID NO: 2550)
AWAPTSRTPW (A24.02) (SEQ ID NO: 2551)
CPMPTTPVQA (B07.02) (SEQ ID NO: 2552)
CPSTVPPSPA (B07.02) (SEQ ID NO: 2553)
GAMVPRGVSM (B07.02, B08.01) (SEQ ID NO: 2554)
MPCPMPTTPV (B07.02) (SEQ ID NO: 2555)
MPTTPVQAW (B07.02) (SEQ ID NO: 2556)
MPTTPVQAWL (B07.02) (SEQ ID NO: 2557)
SLPEDRYTQA (A02.01) (SEQ ID NO: 2558)
SPAQPYLRV (B07.02) (SEQ ID NO: 2559)
SPAQPYLRVS (B07.02) (SEQ ID NO: 2560)
TIMPCPMPT (A02.01) (SEQ ID NO: 2561)
TPVQAWLEA (B07.02) (SEQ ID NO: 2562)
TSRTPWGAM (B07.02) (SEQ ID NO: 2563)
VPPSPAQPYL (B07.02) (SEQ ID NO: 2564)
VPRGVSMAH (B07.02) (SEQ ID NO: 2565) STAD, UCEC, BLCA, BRCA, LUSC, CESC, KIRC, UCS β2M N62fs
E67fs
L74fs
F82fs
T91fs
E94fs RMERELKKWSIQTCLSARTGLSISCTTLNSPPLKKMSMPAV* (SEQ ID NO: 2057) CLSARTGLSI (B08.01) (SEQ ID NO: 2566)
CTTLNSPPLK (A03.01) (SEQ ID NO: 2567)
GLSISCTTL (A02.01) (SEQ ID NO: 2568)
SPPLKKMSM (B07.02, B08.01) (SEQ ID NO: 2569)
TLNSPPLKK (A03.01) (SEQ ID NO: 2570)
TTLNSPPLK (A03.01) (SEQ ID NO: 2571)
TTLNSPPLKK (A03.01) (SEQ ID NO: 2572) CRC, STAD, SKCM, HNSC β2M L13fs
S14fs LCSRYSLFLAWRLLSSVLQRFRFTHVIQQRMESQIS* (SEQ ID NO: 2058) LQRFRFTHV (B08.01) (SEQ ID NO: 2573)
LQRFRFTHVI (B08.01) (SEQ ID NO: 2574)
RLSSVLQRF (A24.02) (SEQ ID NO: 2575)
RLSSVLQRFR (A03.01) (SEQ ID NO: 2576)
VLQRFRFTHV (A02.01, B08.01) (SEQ ID NO: 2577) CRC, STAD, SKCM, HNSC CDH1 A691fs
P708fs
L711fs RSACVTVKGPLASVGRHSLSKQDCKFLPFWGFLEEFLLC* (SEQ ID NO: 2059) ASVGRHSLSK (A03.01) (SEQ ID NO: 2578)
KFLPFWGFL (A24.02) (SEQ ID NO: 2579)
LASVGRHSL (B07.02) (SEQ ID NO: 2580)
LPFWGFLEEF (B07.02) (SEQ ID NO: 2581)
PFWGFLEEF (A24.02) (SEQ ID NO: 2582)
SVGRHSLSK (A03.01) (SEQ ID NO: 2583) ILC LumA Breast cancer CDH1 H121fs
P126fs
H128fs
N144fs
V157fs
P159fs
N166fs
N181fs
F189fs
P201fs
F205fs IQWGTTTAPRPIRPPFLESKQNCSHFPTPLLASEDRRETGLFLPSAAQKMKKAHFLKTWFRSNPTKTKKARFSTASLAKELTHPLLVSLLLKEKQDG* (SEQ ID NO: 2060) APRPIRPPF (B07.02) (SEQ ID NO: 2584)
APRPIRPPFL (B07.02) (SEQ ID NO: 2585)
AQKMKKAHFL (B08.01) (SEQ ID NO: 2586)
FLPSAAQKM (A02.01) (SEQ ID NO: 2587)
GLFLPSAAQK (A03.01) (SEQ ID NO: 2588)
HPLLVSLLL (B07.02) (SEQ ID NO: 2589)
KAHFLKTWFR (A03.01) (SEQ ID NO: 2590)
KARFSTASL (B07.02) (SEQ ID NO: 2591)
KMKKAHFLK (A03.01) (SEQ ID NO: 2592)
KTWFRSNPTK (A03.01) (SEQ ID NO: 2593)
LAKELTHPL (B07.02, B08.01) (SEQ ID NO: 2594)
LAKELTHPLL (B08.01) (SEQ ID NO: 2595)
NPTKTKKARF (B07.02) (SEQ ID NO: 2596)
QKMKKAHFL (B08.01) (SEQ ID NO: 2597)
RFSTASLAK (A03.01) (SEQ ID NO: 2598)
RPIRPPFLES (B07.02) (SEQ ID NO: 2599)
RSNPTKTKK (A03.01) (SEQ ID NO: 2600)
SLAKELTHPL (A02.01, B08.01) (SEQ ID NO: 2601)
TKKARFSTA (B08.01) (SEQ ID NO: 2602) ILC LumA Breast cancer CDH1 V114fs
P127fs
V132fs
P160fs PTDPFLGLRLGLHLQKVFHQSHAEYSGAPPPPPAPSGLRFWNPSRIAHISQLLSWPQKTEERLGYSSHQLPRK* (SEQ ID NO: 2061) GLRFWNPSR (A03.01) (SEQ ID NO: 2603)
ISQLLSWPQK (A03.01) (SEQ ID NO: 2604)
RIAHISQLL (A02.01) (SEQ ID NO: 2605)
RLGYSSHQL (A02.01) (SEQ ID NO: 2606)
SQLLSWPQK (A03.01) (SEQ ID NO: 2607)
SRIAHISQL (B08.01) (SEQ ID NO: 2608)
WPQKTEERL (B07.02) (SEQ ID NO: 2609)
YSSHQLPRK (A03.01) (SEQ ID NO: 2610) ILC LumA Breast cancer CDH1 L731fs
R749fs
E757fs
G759fs FCCSCCFFGGERWSKSPYCPQRMTPGTTFITMMKKEAEKRTRTLT* (SEQ ID NO: 2062) CPQRMTPGTT (B07.02) (SEQ ID NO: 2611)
EAEKRTRTL (B08.01) (SEQ ID NO: 2612)
GTTFITMMK (A03.01) (SEQ ID NO: 2613)
GTTFITMMKK (A03.01) (SEQ ID NO: 2614)
ITMMKKEAEK (A03.01) (SEQ ID NO: 2615)
RMTPGTTFI (A02.01) (SEQ ID NO: 2616)
SPYCPQRMT (B07.02) (SEQ ID NO: 2617)
TMMKKEAEK (A03.01) (SEQ ID NO: 2618)
TPGTTFITM (B07.02) (SEQ ID NO: 2619)
TPGTTFITMM (B07.02) (SEQ ID NO: 2620)
TTFITMMKK (A03.01) (SEQ ID NO: 2621) ILC LumA Breast cancer CDH1 S19fs
E24fs
S36fs WRRNCKAPVSLRKSVQTPARSSPARPDRTRRLPSLGVPGQPWALGAAASRRCCCCCRSPLGSARSRSPATLALTPRATRSRCPGATWREAASWAE* (SEQ ID NO: 2063) CPGATWREA (B07.02) (SEQ ID NO: 2622)
CPGATWREAA (B07.02) (SEQ ID NO: 2623)
RSRCPGATWR (A03.01) (SEQ ID NO: 2624)
TPRATRSRC (B07.02) (SEQ ID NO: 2625) ILC LumA Breast cancer GATA3 P394fs
P387fs
S398fs
H400fs
M401fs
S408fs
P409fs
S408fs
P409fs
T419fs
H424fs
P425fs
S427fs
F431fs
S430fs
H434fs
H435fs
S438fs
M443fs
G444fs
*445fs PGRPLQTHVLPEPHLALQPLQPHADHAHADAPAIQPVLWTTPPLQHGHRHGLEPCSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWCLCSNH* (SEQ ID NO: 2064) HVLPEPHLAL (B07.02) (SEQ ID NO: 2626)
RPLQTHVLPE (B07.02) (SEQ ID NO: 2627)
VLWTTPPLQH (A03.01) (SEQ ID NO: 2628) Mammary cancer GATA3 P426fs
H434fs
P433fs
T441fs PRPRRCTRHPACPLDHTTPPAWSPPWVRALLDAHRAPESPCSPFRLAFLQEQYHEA* (SEQ ID NO: 2065) APSESPCSPF (B07.02) (SEQ ID NO: 2629)
CPLDHTTPPA (B07.02) (SEQ ID NO: 2630)
FLQEQYHEA (A02.01, B08.01) (SEQ ID NO: 2631)
RLAFLQEQYH (A03.01) (SEQ ID NO: 2632)
SPCSPFRLAF (B07.02) (SEQ ID NO: 2633)
SPPWVRALL (B07.02) (SEQ ID NO: 2634)
YPACPLDHTT (B07.02) (SEQ ID NO: 2635) Mammary cancer MLL2 P519fs
E524fs
P647fs
S654fs
L656fs
R755fs
L761fs
Q773fs TRRCHCCPHLRSHPCPHHLRNHPRPHHLRHHACHHHLRNCPHPHFLRHCTCPGRWRNRPSLRRLRSLLCLPHLNHHLFLHWRSRPCLHRKSHPHLLHLRRLYPHHLKHRPCPHHLKNLLCPRHLRNCPLPRHLKHLACLHHLRSHPCPLHLKSHPCLHHRRHLVCSHHLKSLLCPLHLRSLPFPHHLRHHACPHHLRTRLCPHHLKNHLCPPHLRYRA YPPCLWCHACLHRLRNLPCPHRLRSLPRPLHLRLHASPHHLRTPPHPHHLRTHLLPHHRRTRSCPCRWRSHPCCHYLRSRNSAPGPRGRTCHPGLRSRTCPPGLRSHTYLRRLRSHTCPPSLRSHAYALCLRSHTCPPRLRDHICPLSLRNCTCPPRLRSRTCLLCLRSHACPPNLRNHTCPPSLRSHACPPGLRNRICPLSLRSHPCPLGLKSPLRSQANALHLRSCPCSLPLGNHP YLPCLESQPCLSLGNHLCPLCPRSCRCPHLGSHPCRLS* (SEQ ID NO: 2066) ALHLRSCPC (B08.01) (SEQ ID NO: 2636)
CLHHRRHLV (B08.01) (SEQ ID NO: 2637)
CLHHRRHLVC (B08.01) (SEQ ID NO: 2638)
CLHRKSHPHL (B08.01) (SEQ ID NO: 2639)
CLRSHACPP (B08.01) (SEQ ID NO: 2640)
CLRSHTCPP (B08.01) (SEQ ID NO: 2641)
CLWCHACLH (A03.01) (SEQ ID NO: 2642)
CPHHLKNHL (B07.02) (SEQ ID NO: 2643)
CPHHLKNLL (B07.02) (SEQ ID NO: 2644)
CPHHLRTRL (B07.02, B08.01) (SEQ ID NO: 2645)
CPLHLRSLPF (B07.02, B08.01) (SEQ ID NO: 2646)
CPLPRHLKHL (B07.02, B08.01) (SEQ ID NO: 2647)
CPLSLRSHPC (B07.02) (SEQ ID NO: 2648)
CPRHLRNCPL (B07.02, B08.01) (SEQ ID NO: 2649)
FPHHLRHHA (B07.02, B08.01) (SEQ ID NO: 2650)
FPHHLRHHAC (B07.02, B08.01) (SEQ ID NO: 2651)
GLRSRTCPP (B08.01) (SEQ ID NO: 2652)
HACLHRLRNL (B08.01) (SEQ ID NO: 2653)
HLACLHHLR (A03.01) (SEQ ID NO: 2654)
HLCPPHLRY (A03.01) (SEQ ID NO: 2655)
HLCPPHLRYR (A03.01) (SEQ ID NO: 2656)
HLKHLACLH (A03.01) (SEQ ID NO: 2657)
HLKHRPCPH (B08.01) (SEQ ID NO: 2658)
HLKNHLCPP (B08.01) (SEQ ID NO: 2659)
HLKSHPCLH (A03.01) (SEQ ID NO: 2660)
HLKSLLCPL (A02.01, B08.01) (SEQ ID NO: 2661)
HLLHLRRLY (A03.01) (SEQ ID NO: 2662)
HLRNCPLPR (A03.01) (SEQ ID NO: 2663)
HLRNCPLPRH (A03.01) (SEQ ID NO: 2664)
HLRRLYPHHL (B08.01) (SEQ ID NO: 2665)
HLRSHPCPL (B07.02, B08.01) (SEQ ID NO: 2666)
HLRSHPCPLH (A03.01) (SEQ ID NO: 2667)
HLRSLPFPH (A03.01) (SEQ ID NO: 2668)
HLRTRLCPH (A03.01, B08.01) (SEQ ID NO: 2669)
HLVCSHHLK (A03.01) (SEQ ID NO: 2670)
HPCLHHRRHL (B07.02, B08.01) (SEQ ID NO: 2671)
HPGLRSRTC (B07.02) (SEQ ID NO: 2672)
HPHLLHLRRRL (B07.02, B08.01) (SEQ ID NO: 2673)
HRKSHPHLL (B08.01) (SEQ ID NO: 2674)
HRRTRSCPC (B08.01) (SEQ ID NO: 2675)
KSHPHLLHLR (A03.01) (SEQ ID NO: 2676)
KSLLCPLHLR (A03.01) (SEQ ID NO: 2677)
LLCPLHLRSL (A02.01, B08.01) (SEQ ID NO: 2678)
LLHLRRLYPH (B08.01) (SEQ ID NO: 2679)
LPRHLKHLA (B07.02) (SEQ ID NO: 2680)
LPRHLKHLAC (B07.02, B08.01) (SEQ ID NO: 2681)
LRRLRSHTC (B08.01) (SEQ ID NO: 2682)
LRRLYPHHL (B08.01) (SEQ ID NO: 2683)
LVCSHHLKSL (B08.01) (SEQ ID NO: 2684)
NLRNHTCPPS (B08.01) (SEQ ID NO: 2685)
PLHLRSLPF (B08.01) (SEQ ID NO: 2686)
RLCPHHLKNH (A03.01) (SEQ ID NO: 2687)
RLYPHHLKH (A03.01) (SEQ ID NO: 2688)
RLYPHHLKHR (A03.01) (SEQ ID NO: 2689)
RPCPHHLKNL (B07.02) (SEQ ID NO: 2690)
RSHPCPLHLK (A03.01) (SEQ ID NO: 2691)
RSLPFPHHLR (A03.01) (SEQ ID NO: 2692)
RTRLCPHHL (B07.02) (SEQ ID NO: 2693)
RTRLCPHHLK (A03.01) (SEQ ID NO: 2694)
SLLCPLHLR (A03.01) (SEQ ID NO: 2695)
SLRSHACPP (B08.01) (SEQ ID NO: 2696)
SPLRSQANA (B07.02) (SEQ ID NO: 2697)
YLRRLRSHT (B08.01) (SEQ ID NO: 2698)
YPHHLKHRPC (B07.02, B08.01) (SEQ ID NO: 2699) STAD, BLCA, CRC, HNSC, BRCA PTEN I122fs
I135fs
A148fs
L152fs
D162fs
I168fs SWKGTNWCNDMCIFITSGQIFKGTRGPRFLWGSKDQRQKGSNYSQSEALCVLL* (SEQ ID NO: 2067) FITSGQIFK (A03.01) (SEQ ID NO: 2700)
IFITSGQIF (A24.02) (SEQ ID NO: 2701)
SQSEALCVL (A02.01) (SEQ ID NO: 2702)
SQSEALCVLL (A02.01) (SEQ ID NO: 2703) UCEC, PRAD, SKCM, STAD, BRCA, LUSC, KIRC, LIHC, KIRP, GBM PTEN L265fs
K266fs KRTKCFTFG* (SEQ ID NO: 2068) UCEC, PRAD, SKCM, STAD, BRCA, LUSC, KIRC, LIHC, KIRP, GBM PTEN A39fs
E40fs
V45fs
R47fs
N48fs PIFIQTLLLWDFLQK
DLKAYTGTILMM*
(SEQ ID NO: 2069) AYTGTILMM (A24.02) (SEQ ID NO: 2704)
DLKAYTGTIL (B08.01) (SEQ ID NO: 2705) UCEC, PRAD, SKCM, STAD, BRCA, LUSC, KIRC, LIHC, KIRP, GBM PTEN T319fs
T321fs
K327fs
A328fs
A333fs QKMILTKQIKTKPTDTFLQILR* (SEQ ID NO: 2070) ILTKQIKTK (A03.01) (SEQ ID NO: 2706)
KMILTKQIK (A03.01) (SEQ ID NO: 2707)
KPTDTFLQI (B07.02) (SEQ ID NO: 2708)
KPTDTFLQIL (B07.02) (SEQ ID NO: 2709)
MILTKQIKTK (A03.01) (SEQ ID NO: 2710) UCEC, PRAD, SKCM, STAD, BRCA, LUSC, KIRC, LIHC, KIRP, GBM PTEN N63fs
E73fs
A86fs
N94fs GFWIQSIKTITRYTIFVLKDIMTPPNLIAELHNILLKTITHHS* (SEQ ID NO: 2071) ITRYTIFVLK (A03.01) (SEQ ID NO: 2711)
LIAELHNIL (A02.01) (SEQ ID NO: 2712)
LIAELHNILL (A02.01) (SEQ ID NO: 2713)
MTPPNLIAEL (A02.01) (SEQ ID NO: 2714)
NLIAELHNI (A02.01) (SEQ ID NO: 2715)
NLIAELHNIL (A02.01) (SEQ ID NO: 2716)
RYTIFVLKDI (A24.02) (SEQ ID NO: 2717)
TITRYTIFVL (A02.01) (SEQ ID NO: 2718)
TPPNLIAEL (B07.02) (SEQ ID NO: 2719) UCEC, PRAD, SKCM, STAD, BRCA, LUSC, KIRC, LIHC, KIRP, GBM PTEN T202fs
G209fs
C211fs
I224fs
G230fs
P231fs
R233fs
D236fs NYSNVQWRNLQSSVCGLPAKGEDIFLQFRTHTTGRQVHVL* (SEQ ID NO: 2072) FLQFRTHTT (A02.01, B08.01) (SEQ ID NO: 2720)
LPAKGEDIFL (B07.02) (SEQ ID NO: 2721)
LQFRTHTTGR (A03.01) (SEQ ID NO: 2722)
NLQSSVCGL (A02.01) (SEQ ID NO: 2723)
SSVCGLPAK (A03.01) (SEQ ID NO: 2724)
VQWRNLQSSV (A02.01) (SEQ ID NO: 2725) UCEC, PRAD, SKCM, STAD, BRCA, LUSC, KIRC, LIHC, KIRP, GBM PTEN G251fs
E256fs
K260fs
Q261fs
L265fs
M270fs
H272fs
T286fs
E288fs YQSRVLPQTEQDAKKGQNVSLLGKYILHTRTRGNLRKSRKWKSM* (SEQ ID NO: 2073) GQNVSLLGK (A03.01) (SEQ ID NO: 2726)
HTRTRGNLRK (A03.01) (SEQ ID NO: 2727)
ILHTRTRGNL (B08.01) (SEQ ID NO: 2728)
KGQNVSLLGK (A03.01) (SEQ ID NO: 2729)
LLGKYILHT (A02.01) (SEQ ID NO: 2730)
LRKSRKWKSM (B08.01) (SEQ ID NO: 2731)
SLLGKYILH (A03.01) (SEQ ID NO: 2732)
SLLGKYILHT (A02.01) (SEQ ID NO: 2733) UCEC, PRAD, SKCM, STAD, BRCA, LUSC, KIRC, LIHC, KIRP, GBM TP53 A70fs
P72fs
A76fs
A79fs
P89fs
W91fs
S96fs
V97fs
V97fs
G108fs
G117fs
S121fs
V122fs
C124fs
K139fs
V143fs SSQNARGCSPRGPCTSSSYTGGPCTSPLLAPVIFCPFPENLPGQLRFPSGLLAFWDSQVCDLHVLPCPQQDVLPTGQDLPCAAVG* (SEQ ID NO: 2074) CTSPLLAPV (A02.01) (SEQ ID NO: 2734)
FPENLPGQL (B07.02) (SEQ ID NO: 2735)
GLLAFWDSQV (A02.01) (SEQ ID NO: 2736)
IFCPFPENL (A24.02) (SEQ ID NO: 2737)
LLAFWDSQV (A02.01) (SEQ ID NO: 2738)
LLAPVIFCP (A02.01) (SEQ ID NO: 2739)
LLAPVIFCPF (A02.01, A24.02) (SEQ ID NO: 2740)
LPCPQQDVL (B07.02) (SEQ ID NO: 2741)
RFPSGLLAF (A24.02) (SEQ ID NO: 2742)
RFPSGLLAFW (A24.02) (SEQ ID NO: 2743)
SPLLAPVIF (B07.02) (SEQ ID NO: 2744)
SPRGPCTSS (B07.02) (SEQ ID NO: 2745)
SPRGPCTSSS (B07.02) (SEQ ID NO: 2746)
SQVCDLHVL (A02.01) (SEQ ID NO: 2747)
VIFCPFPENL (A02.01) (SEQ ID NO: 2748) BRCA, CRC, LUAD, PRAD, HNSC, LUSC, PAAD, STAD, BLCA, OV, LIHC, SKCM, UCEC, LAML, UCS, KICH, GBM, ACC TP53 V173fs
H178fs
D186fs
H193fs
L194fs
E198fs
V203fs
E204fs
L206fs
D207fs
N210fs
T211fs
F212fs
V225fs
S241fs GAAPTMSAAQIAMVWPLLSILSEWKEICVWSIWMTETLFDIVWWCPMSRLRLALTVPPSTTTTCVTVPAWAA* (SEQ ID NO: 2075) AMVWPLLSI (A02.01) (SEQ ID NO: 2749)
AMVWPLLSIL (A02.01) (SEQ ID NO: 2750)
AQIAMVWPL (A02.01, A24.02) (SEQ ID NO: 2751)
AQIAMVWPLL (A02.01) (SEQ ID NO: 2752)
CPMSRLRLA (B07.02, B08.01) (SEQ ID NO: 2753)
CPMSRLRLAL (B07.02, B08.01) (SEQ ID NO: 2754)
IAMVWPLLSI (A02.01, A24.02, B08.01) (SEQ ID NO: 2755)
ILSEWKEICV (A02.01) (SEQ ID NO: 2756)
IVWWCPMSR (A03.01) (SEQ ID NO: 2757)
IVWWCPMSRL (A02.01) (SEQ ID NO: 2758)
IWMTETLFDI (A24.02) (SEQ ID NO: 2759)
LLSILSEWK (A03.01) (SEQ ID NO: 2760)
MSAAQIAMV (A02.01) (SEQ ID NO: 2761)
MSRLRLALT (B08.01) (SEQ ID NO: 2762)
MSRLRLALTV (B08.01) (SEQ ID NO: 2763)
MVWPLLSIL (A02.01) (SEQ ID NO: 2764)
RLALTVPPST (A02.01) (SEQ ID NO: 2765)
TLFDIVWWC (A02.01) (SEQ ID NO: 2766)
TLFDIVWWCP (A02.01) (SEQ ID NO: 2767)
TMSAAQIAMV (A02.01) (SEQ ID NO: 2768)
VWSIWMTETL (A24.02) (SEQ ID NO: 2769)
WMTETLFDI (A02.01, A24.02) (SEQ ID NO: 2770)
WMTETLFDIV (A01.01, A02.01) (SEQ ID NO: 2771) BRCA, CRC, LUAD, PRAD, HNSC, LUSC, PAAD, STAD, BLCA, OV, LIHC, SKCM, UCEC, LAML, UCS, KICH, GBM, ACC TP53 R248fs
P250fs
S260fs
N263fs
G266fs
N268fs
V272fs
V274fs
P278fs
D281fs
R282fs
T284fs
E285fs
L289fs
K292fs
P301fs
S303fs
T312fs
S314fs
K319fs
K320fs
P322fs
Y327fs
F328fs
L330fs
R333fs
R335fs
R337fs
E339fs TGGPSSPSSHWKTPVVIYWDGTALRCVFVPVLGETGAQRKRISARKGSLTTSCPQGALSEHCPTTPAPLPSQRRNHWMENISPFRSVGVSASRCSES* (SEQ ID NO: 2076) ALRCVFVPV (A02.01, B08.01) (SEQ ID NO: 2772)
ALRCVFVPVL (A02.01, B08.01) (SEQ ID NO: 2773)
ALSEHCPTT (A02.01) (SEQ ID NO: 2774)
AQRKRISARK (A03.01) (SEQ ID NO: 2775)
GAQRKRISA (B08.01) (SEQ ID NO: 2776)
HWMENISPF (A24.02) (SEQ ID NO: 2777)
LPSQRRNHW (B07.02) (SEQ ID NO: 2778)
LPSQRRNHWM (B07.02, B08.01) (SEQ ID NO: 2779)
NISPFRSVGV (A02.01) (SEQ ID NO: 2780)
RISARKGSL (B07.02, B08.01) (SEQ ID NO: 2781)
SPFRSVGVSA (B07.02) (SEQ ID NO: 2782)
SPSSHWKTPV (B07.02, B08.01) (SEQ ID NO: 2783)
TALRCVFVPV (A02.01) (SEQ ID NO: 2784)
VIYWDGTAL (A02.01) (SEQ ID NO: 2785)
VIYWDGTALR (A03.01) (SEQ ID NO: 2786)
VLGETGAQRK (A03.01) (SEQ ID NO: 2787) BRCA, CRC, LUAD, PRAD, HNSC, LUSC, PAAD, STAD, BLCA, OV, LIHC, SKCM, UCEC, LAML, UCS, KICH, GBM, ACC TP53 S149fs
P151fs
P152fs
V157fs
Q165fs
S166fs
H168fs
V173fs FHTPARHPRPRHGHLQAVTAHDGGCEALPPP* (SEQ ID NO: 2077) HPRPRHGHL (B07.02, B08.01) (SEQ ID NO: 2788)
HPRPRHGHLQ (B07.02) (SEQ ID NO: 2789)
RPRHGHLQA (B07.02) (SEQ ID NO: 2790)
RPRHGHLQAV (B07.02, B08.01) (SEQ ID NO: 2791) BRCA, CRC, LUAD, PRAD, HNSC, LUSC, PAAD, STAD, BLCA, OV, LIHC, SKCM, UCEC, LAML, UCS, KICH, GBM, ACC TP53 P47fs
D48fs
D49fs
Q52fs
F54fs
E56fs
P58fs
P60fs
E62fs
M66fs
P72fs
V73fs
P75fs
A78fs
P82fs
P85fs
S96fs
P98fs
T102fs
Y103fs
G108fs
F109fs
R110fs
G117fs CCPRTILNNGSLKTQVQMKLPECQRLLPPWPLHQQLLHRRPLHQPPPGPCHLLSLPRKPTRAATVSVWASCILGQPSL* (SEQ ID NO: 2078) GSLKTQVQMK (A03.01) (SEQ ID NO: 2792)
PPGPCHLLSL (B07.02) (SEQ ID NO: 2793)
RTILNNGSLK (A03.01) (SEQ ID NO: 2794)
SLKTQVQMK (A03.01) (SEQ ID NO: 2795)
SLKTQVQMKL (B08.01) (SEQ ID NO: 2796)
TILNNNGSLK (A03.01) (SEQ ID NO: 2797) BRCA, CRC, LUAD, PRAD, HNSC, LUSC, PAAD, STAD, BLCA, OV, LIHC, SKCM, UCEC, LAML, UCS, KICH, GBM, ACC TP53 L26fs
P27fs
P34fs
P36fs
A39fs
Q38fs VRKHFQTYGNYFLKT
TFCPPCRPKQWMI*
(SEQ ID NO: 2079) CPPCRPKQWM (B07.02) (SEQ ID NO: 2798)
TTFCPPCRPK (A03.01) (SEQ ID NO: 2799) BRCA, CRC, LUAD, PRAD, HNSC, LUSC, PAAD, STAD, BLCA, OV, LIHC, SKCM, UCEC, LAML, UCS, KICH, GBM, ACC TP53 C124fs
L130fs
N131fs
C135fs
K139fs
A138fs
T140fs
V143fs
Q144fs
V147fs
T150fs
P151fs
P152fs
G154fs
R156fs
R158fs
A161fs LARTPLPSTRCFANWPRPALCSCGLIPHPRPAPASAPWPSTSSHST* (SEQ ID NO: 2080) CFANWPRPAL (A24.02) (SEQ ID NO: 2800)
FANWPRPAL (B07.02, B08.01) (SEQ ID NO: 2801)
GLIPHPRPA (A02.01) (SEQ ID NO: 2802)
HPRPAPASA (B07.02, B08.01) (SEQ ID NO: 2803)
HPRPAPASAP (B07.02) (SEQ ID NO: 2804)
IPHPRPAPA (B07.02, B08.01) (SEQ ID NO: 2805)
IPHPRPAPAS (B07.02) (SEQ ID NO: 2806)
RPALCSCGL (B07.02) (SEQ ID NO: 2807)
RPALCSCGLI (B07.02) (SEQ ID NO: 2808)
TPLPSTRCF (B07.02) (SEQ ID NO: 2809)
WPRPALCSC (B07.02) (SEQ ID NO: 2810)
WPRPALCSCG (B07.02) (SEQ ID NO: 2811) BRCA, CRC, LUAD, PRAD, HNSC, LUSC, PAAD, STAD, BLCA, OV, LIHC, SKCM, UCEC, LAML, UCS, KICH, GBM, ACC VHL L178fs
D179fs
L184fs
T202fs
R205fs
D213fs
G212fs ELQETGHRQVALRRSGRPPKCAERPGAADTGAHCTSTDGRLKISVETYTVSSQLLMVLMSLDLDTGLVPSLVSKCLILRVK* (SEQ ID NO: 2081) ALRRSGRPPK (A03.01) (SEQ ID NO: 2812)
GLVPSLVSK (A03.01) (SEQ ID NO: 2813)
KISVETYTV (A02.01) (SEQ ID NO: 2814)
LLMVLMSLDL (A02.01, B08.01) (SEQ ID NO: 2815)
LMSLLDTGL (A02.01) (SEQ ID NO: 2816)
LMVLMSLDL (A02.01) (SEQ ID NO: 2817)
LVSKCLILRV (A02.01) (SEQ ID NO: 2818)
QLLMVLMSL (A02.01, B08.01) (SEQ ID NO: 2819)
RPGAADTGA (B07.02) (SEQ ID NO: 2820)
RPGAADTGAH (B07.02) (SEQ ID NO: 2821)
SLDLDTGLV (A02.01) (SEQ ID NO: 2822)
SLVSKCLIL (A02.01, B08.01) (SEQ ID NO: 2823)
SQLLMVLMSL (A02.01) (SEQ ID NO: 2824)
TVSSQLLMV (A02.01) (SEQ ID NO: 2825)
TYTVSSQLL (A24.02) (SEQ ID NO: 2826)
TYTVSSQLLM (A24.02) (SEQ ID NO: 2827)
VLMSLDLDT (A02.01) (SEQ ID NO: 2828)
VPSLVSKCL (B07.02) (SEQ ID NO: 2829)
VSKCLILRVK (A03.01) (SEQ ID NO: 2830)
YTVSSQLLM (A01.01) (SEQ ID NO: 2831)
YTVSSQLLMV (A02.01) (SEQ ID NO: 2832) KIRC, KIRP VHL L158fs
K159fs
R161fs
Q164fs KSDASRLSGA* (SEQ ID NO: 2082) KIRC, KIRP VHL P146fs
I147fs
F148fs
L158fs RTAYFCQYHTASVYS
ERAMPPGCPEPSQA*
(SEQ ID NO: 2083) FCQYHTASV (B08.01) (SEQ ID NO: 2833) KIRC, KIRP VHL S68fs
S72fs
I75fs
S80fs
P86fs
P97fs
I109fs
H115fs
L116fs
G123fs
T124fs
N131fs
L135fs
V137fs
G144fs
D143fs
I147fs TRASPPRSSSAIAVRASCCPYGSSTSTASRSPTQRCRLARAAASTATEVTFGSSEMQGHTMGFWLTKLNYLCHLSMLTDSLFLPISHCQCIL* (SEQ ID NO: 2084) CPYGSTSTA (B07.02) (SEQ ID NO: 2834)
CPYGSTSTAS (B07.02) (SEQ ID NO: 2835)
LARAAASTAT (B07.02) (SEQ ID NO: 2836)
MLTDSLFLP (A02.01) (SEQ ID NO: 2837)
PPRSSSAIAV (B07.02) (SEQ ID NO: 2838)
RAAASTATEV (B07.02) (SEQ ID NO: 2839)
SPPRSSSAI (B07.02) (SEQ ID NO: 2840)
SPPRSSSAIA (B07.02) (SEQ ID NO: 2841)
SPTQRCRLA (B07.02) (SEQ ID NO: 2842)
TQRCRLARA (B08.01) (SEQ ID NO: 2843)
TQRCRLARAA (B08.01) (SEQ ID NO: 2844) KIRC, KIRP VHL K171fs
P172fs
N174fs
L178fs
D179fs
L188fs SSLRITGDWTSSGRSTKIWKTTQMCRKTWSG* (SEQ ID NO: 2085) KIWKTTQMCR (A03.01) (SEQ ID NO: 2845)
WTSSGRSTK (A03.01) (SEQ ID NO: 2846) KIRC, KIRP VHL V62fs
V66fs
Q73fs
V84fs
F91fs
T100fs
P103fs
S111fs
L116fs
H115fs
D126fs RRRRGGVGRRGVRPGGRVRPGGTGRRGGDGGRAAAARAALGELARALPGHLLQSQSARRAARMAQLRRRAALPNAAAAWHGPPHPQLPRSPLALQRCRDTRWASG* (SEQ ID NO: 2086) ALGELARAL (A02.01) (SEQ ID NO: 2847)
AQLRRRAAA (B08.01) (SEQ ID NO: 2848)
AQLRRRAAAL (B08.01) (SEQ ID NO: 2849)
ARRAARMAQL (B08.01) (SEQ ID NO: 2850)
HPQLPRSPL (B07.02, B08.01) (SEQ ID NO: 2851)
HPQLPRSPLA (B07.02) (SEQ ID NO: 2852)
LARALPGHL (B07.02) (SEQ ID NO: 2853)
LARALPGHLL (B07.02) (SEQ ID NO: 2854)
MAQLRRRAA (B07.02, B08.01) (SEQ ID NO: 2855)
MAQLRRRAAA (B07.02, B08.01) (SEQ ID NO: 2856)
QLRRRAAAL (B07.02, B08.01) (SEQ ID NO: 2857)
RAALPNAAAA (B07.02) (SEQ ID NO: 2858)
RMAQLRRRAA (B07.02, B08.01) (SEQ ID NO: 2859)
SQSARRAARM (B08.01) (SEQ ID NO: 2860) KIRC, KIRP table 35D CRYPTIC EXON ¹ AR-v7 cryptic terminal exon SCKVFFKRAAEGKQKYLCASRNDCTIDKFRRKNCPSCRLRKCYEAGMTLG EKFRVGNCKHLKMTRP* (SEQ ID NO: 2087) GMTLGEKFRV (A02:01) (SEQ ID NO: 2861)
RVGNCKHLK (A03.01) (SEQ ID NO: 2862) Prostate cancer, Castration-resistant prostate cancer table 35E OUT OF FRAME FUSIONS ^1.3 AC011997,1:LRRC69 AC011997,1:LRRC69
*out of reading frame MAGAPPPASLPPCSLISDCCASNQRDSVGVGPSEP: G : NNIKICNESASRK* (SEQ ID NO: 2088) GPSEPGNNI (B07.02) (SEQ ID NO: 2863)
KICNESASRK (A03.01) (SEQ ID NO: 2864) LUSC, Breast Cancer, Head and Neck Cancer, LUAD EEF1DP3 EEF1DP3:FRY *out of reading frame HGWRPFLPVRARSRW
NRRLDVTVANGR: S :
WKYGWSLLRVPQVNG
IQVLNVSLKSSSNVI
SYE* (SEQ ID NO: 2089) GIQVLNVSLK (A03.01) (SEQ ID NO: 2865)
IQVLNVSLK (A03.01) (SEQ ID NO: 2866)
KSSSNVISY (A01.01, A03.01) (SEQ ID NO: 2867)
KYGWSLLRV (A24.02) (SEQ ID NO: 2868)
RSWKYGWSL (A02.01) (SEQ ID NO: 2869)
SLKSSSNVI (B08.01) (SEQ ID NO: 2870)
SWKYGWSLL (A24.02) (SEQ ID NO: 2871)
TVANGRSWK (A03.01) (SEQ ID NO: 2872)
VPQVNGIQV (B07.02) (SEQ ID NO: 2873)
VPQVNGIQVL (B07.02) (SEQ ID NO: 2874)
VTVANGRSWK (A03.01) (SEQ ID NO: 2875)
WSLLRVPQV (B08.01) (SEQ ID NO: 2876) Mammary cancer MAD1L1:MAFK MAD1L1:MAFK RLKEVFQTKIQEFRKACYTLTGYQIDITTENQYRLTSLYAEHPGDCLIFK:: LRVPGSSVLVTVPGL* (SEQ ID NO: 2090) HPGDCLIFKL (B07.02) (SEQ ID NO: 2877)
KLRVPGSSV (B07.02) (SEQ ID NO: 2878)
KLRVPGSSVL (B07.02) (SEQ ID NO: 2879)
RVPGSSVLV (A02.01) (SEQ ID NO: 2880)
SVLVTVPGL (A02.01) (SEQ ID NO: 2881)
VPGSSVLVTV (B07.02) (SEQ ID NO: 2882) CLL PPP1R1B:STARD3 PPP1R1B:STARD3 AEVLKVIRQSAGQKTTCGQGLEGPWERPPPLDESERDGGSEDQVEDPALS: A : LLLRPRPPRPEVGAHQDEQAAQGADPRLGAQPACRGLPGLLTVPQPEPLLAPPSAA* (SEQ ID NO: 2091) ALLLRPRPPR (A03.01) (SEQ ID NO: 2883)
ALSALLLRPR (A03.01) (SEQ ID NO: 2884) Mammary cancer tables 35F IN FRAME DELETIONS and FUSIONS ^1.2 BCR:ABL BCR:ABL ERAEWRENIREQQKKCFRSFSLTSVELQMLTNSCVKLQTVHSIPLTINKE:: EALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASG (SEQ ID NO: 2092) LTINKEEAL (A02.01, B08.01) (SEQ ID NO: 2885) CML, AML BCR:ABL BCR:ABL ELQMLTNSCVKLQTVHSIPLTINKEDDESPGLYGFLNVIVHSATGFKQSS: K : ALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGD (SEQ ID NO: 2093) IVHSATGFK (A03.01) (SEQ ID NO: 2886)
ATGFKQSSK (A03.01) (SEQ ID NO: 2887) CML, AML C11orf95:RELA C11orf95:RELA ISNSWDAHLGLGACGEAEGLGVQGAEEEEEEEEEEEEEGAGVPACPPKGP: E : LFPLIFPAEPAQASGPYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTD (SEQ ID NO: 2094) ELFPLIFPA (A02.01, B08.01) (SEQ ID NO: 2888)
KGPELFPLI (A02.01, A24.02) (SEQ ID NO: 2889)
KGPELFPLIF (A24.02) (SEQ ID NO: 2890) Supratentorial ependymomas CBFB:MYH11 (option “type a”) LQRLDGMGCLEFDEERAQQEDALAQQAFEEARRRRTREFEDRDRSHREEME:: VHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQF (SEQ ID NO: 2095) AML CD74:ROS1 (exon6:exon32) ( SEQ ID NO: 2096) KPTDAPPKAGV (B07.02) (SEQ ID NO: 2891) NSCLC, Crizotinib-resistant EML4:ALK EML4:ALK SWENSDDSRNKLSKIPSTPKLIPKVTKTADKHKDVIINQAKMSTREKNSQ: V : YRRKHQELQAMQMELQSPEYKLSKLRTSTIMTDYNPNYCFAGKTSSISDL (SEQ ID NO: 2097) QVYRRKHQEL (B08.01) (SEQ ID NO: 2892)
STREKNSQV (B08.01) (SEQ ID NO: 2893)
VYRRKHQEL (A24.02, B08.01) (SEQ ID NO: 2894) NSCLC FGFR3:TACC3 FGFR3:TACC3 EGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLTVTSTD:: VKATQEENRELRSRCEELHGKNLELGKIMDRFEEVVYQAMEEVQKQKELS (SEQ ID NO: 2098) VLTVTSTDV (A02.01) (SEQ ID NO: 2895)
VLTVTSTDVK (A03.01) (SEQ ID NO: 2896) Bladder Cancer, LUSC NAB:STAT6 NAB:STAT6 “” RDNTLLLRRVELFSLSRQVARESTYLSSLKGSRLHPEELGGPPLKKLKQE:: ATSKSQI MSLWGLVSKMPPEKVQRLYVDFPQHLRHLLGDWLESQPWEFLVGSDAFCC (SEQ ID NO: 2099) IMSLWGLVS (A02.01) (SEQ ID NO: 2897)
IMSLWGLVSK (A03.01) (SEQ ID NO: 2898)
KLKQEATSK (A03.01) (SEQ ID NO: 2899)
QIMSLWGLV (A02.01) (SEQ ID NO: 2900)
SQIMSLWGL (A02.01, A24.02, B08.01) (SEQ ID NO: 2901)
SQIMSLWGLV (A02.01) (SEQ ID NO: 2902)
TSKSQIMSL (B08.01) (SEQ ID NO: 2903) Benign mesotheliomas NDRG1:ERG NDRG1:ERG MSREMQDVDLAEVKPLVEKGETITGLLQEFDVQ:: EALSVVSEDQSLFECAYGTPHLAKTEMTASSSSDYGQTSKMSPRVPQQDW (SEQ ID NO: 2100) LLQEFDVQEA (A02.01) (SEQ ID NO: 2904)
LQEFDVQEAL (A02.01) (SEQ ID NO: 2905) Prostate cancer PML:RARA PML:RARA (exon3:exon3) VLDMHGFLRQALCRLRQEEPQSLQAAVRTDGFDEFKVRLQDLSSCITQGK: A : IETQSSSSEEIVPSPPSPPPLPRIYKPCFVCQDKSSGYHYGVSACEGCKG (SEQ ID NO: 2101) Acute promyelocytic leukemia PML:RARA PML:RARA (exon6:exon3) RSSPEQPRPSTSKAVSPPHLDGPPSPRSPVIGSEVFLPNSNHVASGAGEA: A : IETQSSSSEEIVPSPPSPPPLPRIYKPCFVCQDKSSGYHYGVSACEGCKG (SEQ ID NO: 2102) Acute promyelocytic leukemia RUNX1 RUNX1 (ex5)-RUNX1T1 (ex2) VARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKITVDGPREPR: N : RTEKHSTMPDSPVDVKTQSRLTPPTMPPPPTTQGAPRTSSFTPTTLTNGT (SEQ ID NO: 2103) GPREPRNRT (B07.02) (SEQ ID NO: 2906)
RNRTEKHSTM (B08.01) (SEQ ID NO: 2907) AML TMPRSS2:ERG TMPRSS2:ERG MALNS::EALSVVSEDQSLFECAYGTPHLAKTEMTASSSSDYGQTSKMSPRVPQQDW (SEQ ID NO: 2104) ALNSEALSV (A02.01) (SEQ ID NO: 2908)
ALNSEALSVV (A02.01) (SEQ ID NO: 2909)
MALNSEALSV (A02.01, B08.01) (SEQ ID NO: 2910) Prostate cancer

¹ Underlined AAs represent non-native AAs

² AA in bold represent the native AA amino acid sequence encoded by the second of the two fusion genes

³ Bold and underlined AA represent non-native AA of the amino acid sequence encoded by the second of the two frameshift fused genes.

Table 36 below provides a list of selected HLA-restricted BTK peptides for the purpose of this application, and the corresponding protein encoded by the HLA allele to which the mutant BTK peptide binds or is predicted to bind.

Table 36

BTK PEPTIDE HLA allele SLLNYLREM (SEQ ID NO: 2911) HLA-A02:04 HLA-A02:03 HLA-C03:02 HLA-A03:01 HLA-A32:01 HLA-A02:07 HLA-C14:03 HLA-C14:02 HLA-A31:01 HLA-A30:02 HLA-A74:01 HLA-C06:02 HLA-B15:03 HLA-B46:01 HLA-B13:02 HLA-A25:01 HLA-A29:02 HLA-C01:02 EYMANGSLL (SEQ ID NO: 2912) HLA-C14:02 HLA-C14:03 HLA-A33:03 HLA-C04:01 HLA-B15:09 HLA-B38:01 TEYMANGSL (SEQ ID NO: 2913) HLA-B14:02 HLA-B49:01 HLA-B44:03 HLA-B44:02 HLA-B37:01 HLA-B15:09 HLA-B41:01 HLA-B50:01 MANGSLLNY (SEQ ID NO: 2914) HLA-C02:02 HLA-C03:02 HLA-B53:01 HLA-C12:02 HLA-C12:03 HLA-A36:01 HLA-A26:01 HLA-A25:01 HLA-B57:01 HLA-A03:01 HLA-B46:01 HLA-B15:03 HLA-A33:03 HLA-B35:03 HLA-A11:01 YMANGSLLNY (SEQ ID NO: 2915) HLA-A29:02 HLA-A36:01 HLA-B46:01 HLA-A25:01 HLA-B15:01 HLA-A26:01 HLA-A30:02 HLA-A32:01

Table 37 provides a list of selected BTK peptides and the corresponding preferred protein encoded by the HLA allele to which the peptide binds or is predicted to bind, as applicable in the context of this application.

Table 37

PEPTIDE ALLELE ANGSLLNY (SEQ ID NO: 2916) HLA-A36:01 ANGSLLNYL (SEQ ID NO: 2917) HLA-C15:02 HLA-C08:01 HLA-C06:02 HLA-A02:04 HLA-C12:02 HLA-B44:02 HLA-C17:01 HLA-B38:01 ANGSLLNYLR (SEQ ID NO: 2918) HLA-A74:01 HLA-A31:01 EYMANGSL (SEQ ID NO: 2919) HLA-C14:02 HLA-C14:03 HLA-A24:02 EYMANGSLL (SEQ ID NO: 2920) HLA-C14:02 HLA-C14:03 HLA-A33:03 HLA-C04:01 HLA-B15:09 HLA-B38:01 EYMANGSLLN (SEQ ID NO: 2921) HLA-A24:02 HLA-A23:01 EYMANGSLLNY (SEQ ID NO: 2922) HLA-A29:02 GSLLNYLR (SEQ ID NO: 2923) HLA-A31:01 HLA-A74:01 GSLLNYLREM (SEQ ID NO: 2924) HLA-B58:02 HLA-B57:01 ITEYMANGS (SEQ ID NO: 2925) HLA-A01:01 ITEYMANGSL (SEQ ID NO: 2926) HLA-A01:01 ITEYMANGSLL (SEQ ID NO: 2927) HLA-A01:01 MANGSLLNY (SEQ ID NO: 2928) HLA-C02:02 HLA-C03:02 HLA-B53:01 HLA-C12:02 HLA-C12:03 HLA-A36:01 HLA-A26:01 HLA-A25:01 HLA-B57:01 HLA-A03:01 HLA-B46:01 HLA-B15:03 HLA-A33:03 HLA-B35:03 HLA-A11:01 MANGSLLNYL (SEQ ID NO: 2929) HLA-C17:01 HLA-C02:02 HLA-B35:01 HLA-C03:03 HLA-C08:01 HLA-B35:03 HLA-C12:02 HLA-C01:02 HLA-C03:04 HLA-C08:02 MANGSLLNYLR (SEQ ID NO: 2930) HLA-A33:03 HLA-A74:01 NGSLLNYL (SEQ ID NO: 2931) HLA-B14:02 NGSLLNYLR (SEQ ID NO: 2932) HLA-A68:01 HLA-A33:03 HLA-A31:01 HLA-A74:01 SLLNYLREM (SEQ ID NO: 2933) HLA-A02:04 HLA-A02:03 HLA-C03:02 HLA-A03:01 HLA-A32:01 HLA-A02:07 HLA-C14:03 HLA-C14:02 HLA-A31:01 HLA-A30:02 HLA-A74:01 HLA-C06:02 HLA-B15:03 HLA-B46:01 HLA-B13:02 HLA-A25:01 HLA-A29:02 HLA-C01:02 SLLNYLREMR (SEQ ID NO: 2934) HLA-A74:01 HLA-A31:01 TEYMANGSL (SEQ ID NO: 2935) HLA-B14:02 HLA-B49:01 HLA-B44:03 HLA-B44:02 HLA-B37:01 HLA-B15:09 HLA-B41:01 HLA-B50:01 TEYMANGSLL (SEQ ID NO: 2936) HLA-B40:01 HLA-B44:03 HLA-B49:01 HLA-B44:02 HLA-B40:02 TEYMANGSLLNY (SEQ ID NO: 2937) HLA-B44:03 YMANGSLL (SEQ ID NO: 2938) HLA-B15:09 HLA-C03:04 HLA-C03:03 HLA-C17:01 HLA-C03:02 HLA-C14:03 HLA-C14:02 HLA-C04:01 HLA-C02:02 HLA-A01:01 YMANGSLLN (SEQ ID NO: 2939) HLA-A29:02 HLA-A01:01 YMANGSLLNY (SEQ ID NO: 2940) HLA-A29:02 HLA-A36:01 HLA-B46:01 HLA-A25:01 HLA-B15:01 HLA-A26:01 HLA-A30:02 HLA-A32:01

Typical EGFR gene mutations that are prevalent in different types of cancer are presented in Table 40A-40D . The table also shows EGFR neoantigenic peptides. Mutations involving individual amino acid substitutions that are prevalent in cancer are listed in Tables 40A-40C . Typical deletion and insertion mutations are presented in Table 40D .

Table 40A. Typical EGFR point mutations in cancer and mutant peptides

Gene Nucleotide Mutation (amino acid) Sequence Mutation Context Neopeptides Cancer EGFR c,1786C>T p.P596S CTGRGPDNCIQCAHYIDGPRCVRTC[p.P596S]SAGVMGENNTLVWKYADAGHVCHLCH (SEQ ID NO: 2941) CVKTCSAGV (SEQ ID NO: 2959), VKTCSAGVM (SEQ ID NO: 2960), CVKTCSAGVM (SEQ ID NO: 2961) G.B.M. EGFR c,1787C>T p.P596L CTGRCPDNCIQCAHYIDGPHCVKTC[p.S596L]LAGVMGENNTLVWKYADAGHVCHLCH (SEQ ID NO: 2942) CVKTCLAGV (SEQ ID NO: 2962),GPHCVKTCL (SEQ ID NO: 2963),VKTCLAGVM (SEQ ID NO: 2964) G.B.M. EGFR c,1793G>C p.G598A GRGPDNCIQCAHYIDGPHCVKTCPA[p.G598A]AVMGENNTLVWKYADAGHVCHLCHPN (SEQ ID NO: 2943) CVKTCPAAV (SEQ ID NO: 2965),VKTCPAAVM (SEQ ID NO: 2966),AVMGENNTL (SEQ ID NO: 2967),AVMGENNTLV (SEQ ID NO: 2968),CVKTCPAAVM (SEQ ID NO: 2969),AAVMGENNTL (SEQ ID NO : 2970) G.B.M. EGFR c,1793G>T p.G598V GRGPDNCIQCAHYIDGPHCVKTCPA[p.G598V]VVMGENNTLVWKYADAGHVCHLCHPN (SEQ ID NO: 2944) CVKCPAVV (SEQ ID NO: 2971),VKTCPAVVM (SEQ ID NO: 2972),VVMGENNTLV (SEQ ID NO: 2973),CVKTCPAVVM (SEQ ID NO: 2974) G.B.M. EGFR c,185T>G p.162R KLTQLGTFEDHFLSLQRMFNNCLVV[p.L62R]RGNLEITYVQRNYDLSFLKTQEVAG (SEQ ID NO: 2945) MFNNCEVVR (SEQ ID NO: 2975),EVVRGNLEI (SEQ ID NO: 2976),VRGNLETTY (SEQ ID NO: 2977),RMFNNCEVVR (SEQ ID NO: 2978),VVRGNLEITY (SEQ ID NO: 2979),CEVVRGNIE (SEQ ID NO : 2980) G.B.M. EGFR c,2125G>A p.E709K QERELVEPLTPSGEAPNQALLRILK[p.E709K]KTEFKKIKVLGSGAFGTVYKGLWIP (SEQ ID NO: 2946) RILKKTEFK (SEQ ID NO: 2981),ILKKTEFKK (SEQ ID NO: 2982),QALLRILKK (SEQ ID NO: 2983),LRILKTEF (SEQ ID NO: 2984),RILKKTEFKK (SEQ ID NO: 2985),NQALLRILKK (SEQ ID NO : 2986),LLRLKKTEF (SEQ ID NO: 2987) G.B.M. EGFR c,2156G>C p.G719A PSGEAPNQALLRILKETEFKKIKVL[p.G719A]ASGAFGTVYKGLWIPEGEKVKIPVAI (SEQ ID NO: 2947) ASGAFGTVY (SEQ ID NO: 2988),VLASGAFGT (SEQ ID NO: 2989),LASAFGTY (SEQ ID NO: 2990),KIKVLASGA (SEQ ID NO: 2991),KVLASGAFG (SEQ ID NO: 2992),IKVLASGAF (SEQ ID NO : 2993),KKIKVLASG (SEQ ID NO: 2994),VLASG (SEQ ID NO: 2995),VLASGAFGTV (SEQ ID NO: 2996),ASGAFGTVYK (SEQ ID NO: 2997),KIKVLASGAF (SEQ ID NO: 2998),LASGAFGTVY (SEQ ID NO: 2999),KKIKVLASGA (SEQ ID NO: 3000),TEFKKIKVIA (SEQ ID NO: 3001) LUAD EGFR c,2235, 2249> | GGAATTAA
GAGAAGC
(SEQ ID NO: 3820) p.ELREA746deI("ELREA" disclosed as SEQ ID NO: 3821) GAFGTVYKGLWIPEGEKVKIPVAIK[p.ELREA745del]
TSPKANKEILDEAYVMAS
VDNPHVCRLLGICLTSTV
QLIT
(SEQ ID NO: 2948)
("ELREA" disclosed as SEQ ID NO: 3822) AIKTSPKANK (SEQ ID NO: 3002),KVKIPVAIKT (SEQ ID NO: 3003),KTSPKANKEI (SEQ ID NO: 3004) LUAD EGFR c,2303G>T p.S768I AIKELREQATSPKANKEILDEAYVMA[p.S768I]IVDNPHVCRLLGICLTSTVQLITQLM (SEQ ID NO: 2949) MAIVDNPHV (SEQ ID NO: 3005),VMAIVDNPH (SEQ ID NO: 3006),DEAYVMAIV (SEQ ID NO: 3007),LDEAYYMAI (SEQ ID NO: 3008),RDEAYVMAI (SEQ ID NO: 3009),VMAIVDNPHV (SEQ ID NO : 3010),AIVDNPHVCR (SEQ ID NO: 3011),YVMAIVDNPH (SEQ ID NO: 3012),DEAYVMAIVD (SEQ ID NO: 3013) LUAD EGFR c,2512C>A p.L838M YLLNVVCVQLAKGMNYLEDRRLVHRD[p.L838M]MAARNVLVKTPQHVKITDFGLAKLLG (SEQ ID NO: 2950) RLVHRDMAA (SEQ ID NO: 3014),DMAARNVLV (SEQ ID NO: 3015),MAARNVLVK (SEQ ID NO: 3016),LVHRDMARR (SEQ ID NO: 3017),RDMAARNVL (SEQ ID NO: 3018),RLVHRDMAAR (SEQ ID NO : 3019),DMAARNVLVK (SEQ ID NO: 3020),HRDMAARNVL (SEQ ID NO: 3021),RDMAARNVLV (SEQ ID NO: 3022) KIRC EGFR c,2573T>G p.L858R LVHRDLAARNVLVKTPQHIVKITDEG[p.L858R]RAKLGAEEKEYHAFGGRVPIKWMAL (SEQ ID NO: 2951) KITDGRAK (SEQ ID NO: 3023),HVKITDFGR (SEQ ID NO: 3024),FGRAKLLGA (SEQ ID NO: 3025),HVKITDFGRA (SEQ ID NO: 3026),RAKLIGAEEK (SEQ ID NO: 3027) LUAD EGFR c,2582T>A p.L861Q RDLAARNVLVKTPQHVRITDFGLAK[p.L861Q]QLGAEEKEYHAEGGKVPIKWMALES (SEQ ID NO: 2952) LAKQLGAEEK (SEQ ID NO: 3028),KQLGAEEKEY (SEQ ID NO: 3029) LUSC EGFR c,323G>A p.R108K QEVAGYVLIALNTVERIPLENLQAIE[p.R108K]KGNMYYENSYALVLSNYDANKTGLK (SEQ ID NO: 2953) QHKGNMYY (SEQ ID NO: 3030),LQHKGNMY (SEQ ID NO: 3031),LQHKGNMYY (SEQ ID NO: 3032),KGNMYYENSY (SEQ ID NO: 3033) G.B.M. EGFR c.754C>T p.R252C SPSDECLMNQCAAGEIGPNESDLVC[p.R252C]CKFRDEATCKDTCPPLMLYNPTTYQM (SEQ ID NO: 2954) RESDCLVCC (SEQ ID NO: 3034) G.B.M. EGFR c.865G>A p.A289T CPPLMLYNPTTYQMDVNPEGKYSFG[p.A289T]TTCVKKCPRNYVVTDHGSCVRACGAD (SEQ ID NO: 2955) YSFGTTCVK (SEQ ID NO: 3035),TTCVKKCPR (SEQ ID NO: 3036),GKYSFGTTC (SEQ ID NO: 3037),YSFGTTCVKK (SEQ ID NO: 3038),KYSFGTTCVK (SEQ ID NO: 3039),GTTCVKKCPR (SEQ ID NO : 3040),GKYSFGTTCV (SEQ ID NO: 3041) G.B.M. EGFR c.866C>A p.A289D CPPLMLYNPTTYQMDVNPEGKYSFG[p.A289D]DTCVKKCPRNYVVTDHGSCVRACGAD (SEQ ID NO: 2956) YSFGDTCVK (SEQ ID NO: 3042),DTCVKKCPR (SEQ ID NO: 3043),GKYSFGDTC (SEQ ID NO: 3044),YSFGDTCVKK (SEQ ID NO: 3045),KYSFGTCVK (SEQ ID NO: 3046),GKYSFGDTCV (SEQ ID NO : 3047) G.B.M. EGFR c.866C>T p.A289V CPPLMLYNPTTYQMDVNPEGKYSFG[p.A289V]VTCVKKCPRNYVVTDHGSCVRACGAD (SEQ ID NO: 2957) YSFGVTCVK (SEQ ID NO: 3048),KYSFGVTCV (SEQ ID NO: 3049),VTCVKKCPR (SEQ ID NO: 3050),GKYSFGVTC (SEQ ID NO: 3051),YSFGVTCVKK (SEQ ID NO: 3052),KYSFGVTCVK (SEQ ID NO : 3053),GVTCVKKCPR (SEQ ID NO: 3054),GKYSFGVTCV (SEQ ID NO: 3055) G.B.M. EGFR c,910C>T p.H304Y VNPEGKYSFGATCVKKICPRNYVVTD[p.H304Y]YGSCVRACGADSYEMEEDGVRKCKKC (SEQ ID NO: 2958) VVTDYGSCV (SEQ ID NO: 3056),YVVTDYGSCV (SEQ ID NO: 3057),VVTDYGSCVR (SEQ ID NO: 3058),CPRNYVVTDY (SEQ ID NO: 3059) G.B.M.

Table 40B. Typical EGFR point mutations in cancer and mutant peptides

Amino acid (nucleotide) mutation Neopeptides Cancer Allele EGFRp.L858R (uc003tqk,2) FGRAKLLGA (SEQ ID NO: 3060) Lung adenocarcinoma HLA.B08.01 EGFRp.L858R (uc003tqk,2) KITDFGRAK (SEQ ID NO: 3061) Lung adenocarcinoma HLA.A03.01
HLA.A11.01
HLA.A30.01

Table 40C. Typical EGFR point mutations in cancer and mutant peptides

EGFR mutation Sequence Mutation Context Neopeptides Disease EGFR, T790M GICLTSTVQLI M QLMPFGCLLDY (SEQ ID NO: 3062) VQLI M QLMPF (SEQ ID NO: 3064), STVQLI M QLM (SEQ ID NO: 3065), QLI M QLMPF (SEQ ID NO: 3066), M QLMPFGCLL (SEQ ID NO: 3067), LI M QLMPF (SEQ ID NO : 3068), LTSTVQLI M (SEQ ID NO: 3069), STVQLI M QL (SEQ ID NO: 3070), TSTVQLI M QL (SEQ ID NO: 3071), TVQLI M QL (SEQ ID NO: 3072), TVQLI M QLM (SEQ ID NO: 3073), VQLI M QLM (SEQ ID NO: 3074), CLTSTVQLI M (SEQ ID NO: 3075), I M QLMPFGC (SEQ ID NO: 3076), I M QLMPFGCL (SEQ ID NO: 3077) , LI M QLMPFG (SEQ ID NO: 3078), LI M QLMPFGC (SEQ ID NO: 3079), QLI M QLMPFG (SEQ ID NO: 3080) CRC EGFR, S492R SLNITSSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKII R NRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLL (SEQ ID NO: 3063) II R NRGENSCK (SEQ ID NO: 3081) NSCLC, PRAD

Table 40D. Typical EGFR deletion mutations, fusion mutations in cancer

EGFR mutation Sequence Mutation Context Neopeptides Disease EGFRvIII (internal deletion) MRPSGTAGAALLALLAALCPASRALEEKK: G :NYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKD (SEQ ID NO: 3082) ALEEKK G NYV (SEQ ID NO: 3084) G.B.M. EGFR:SEPT14 LPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQ:: LQDKFEHLKMIQQEEIRKLEEEKKQLEGEIIDFYKMKAASEALQTQLSTD (SEQ ID NO: 3083) IQ LQDKFEHL (SEQ ID NO: 3085) GBM, Glioma, head and neck cancer Q LQDKFEHL (SEQ ID NO: 3086) Q LQDKFEHLK (SEQ ID NO: 3087) YLVIQ LQDKF (SEQ ID NO: 3088)

In the tables above, for one or more typical fusions, the sequence listed before the first “:” belongs to the exon of the polypeptide sequence encoded by the first gene, the sequence listed after the second “:” belongs to the exon of the polypeptide sequence encoded by the second gene, and the amino acid that appears between the characters “:” is encoded by a codon that is divided between an exon of the polypeptide sequence encoded by the first gene and an exon of the polypeptide sequence encoded by the second gene.

However, in some embodiments, such as NAB:STAT6, the NAB exon is linked to the STAT6 5' UTR, and the first amino acid that appears after the junction point is the normal STAT6 start codon (no frame is present at this site (since it is not translated Fine).

AR-V7 in the tables above can also be considered, in some embodiments, to be a splice variant of the AR gene that encodes a protein that does not have the ligand binding domain found in full-length AR.

In some embodiments, sequencing methods are used to identify tumor-specific mutations. Any suitable sequencing method can be used in accordance with the present description, for example, next generation sequencing (NGS) technology. Third generation sequencing methods may be a replacement for NGS technology in the future to speed up the sequencing stage of the method. For the purpose of clarification, the terms “next generation sequencing” or “NGS” as used herein refers to all new high-throughput sequencing technologies that, unlike “conventional” sequencing techniques known as Sanger chemistry, read nucleic acid patterns randomly in parallel. entire genome by breaking the entire genome into small parts (also known as massively parallel sequencing technologies) and are capable of delivering nucleic acid sequence information of the entire genome, exome, transcriptome (all transcribed sequences of the genome) or methylome (all methylated sequences of the genome) in very short periods time, for example within 1-2 weeks, for example within 1-7 days or within less than 24 hours, and allow, in principle, single cell sequencing approaches. A variety of NGS platforms that are commercially available or that are mentioned in the literature can be used in the context of the present disclosure, for example those described in detail in WO 2012/159643.

In some embodiments, a peptide described herein may contain, but is not limited to, about 5, about 6, about 7, about 8, about 9, about 10, about 11, about 12, about 13, about 14, about 15, approximately 16, approximately 17, approximately 18, approximately 19, approximately 20, approximately 21, approximately 22, approximately 23, approximately 24, approximately 25, approximately 26, approximately 27, approximately 28, approximately 29, approximately 30, approximately 31, approximately 32, approximately 33, approximately 34, approximately 35, approximately 36, approximately 37, approximately 38, approximately 39, approximately 40, approximately 41, approximately 42, approximately 43, approximately 44, approximately 45, approximately 46, approximately 47, approximately 48 , approximately 49, approximately 50, approximately 60, approximately 70, approximately 80, approximately 90, approximately 100, approximately 110, approximately 120, approximately 150, approximately 200, approximately 300, approximately 350, approximately 400, approximately 450, approximately 500, approximately 600, about 700, about 800, about 900, about 1000, about 1500, about 2000, about 2500, about 3000, about 4000, about 5000, about 7500, about 10,000 amino acids or more amino acid residue, and any range derived therefrom . In specific embodiments, the neoantigenic peptide molecule is equal to or less than 100 amino acids.

In some embodiments, the peptides may be from about 8 to about 50 amino acid residues in length, or from about 8 to about 30, from about 8 to about 20, from about 8 to about 18, from about 8 to about 15 , or from about 8 to about 12 amino acid residues in length. In some embodiments, the peptides can be from about 8 to about 500 amino acid residues in length, or from about 8 to about 450, from about 8 to about 400, from about 8 to about 350, from about 8 to about 400 about 300, from about 8 to about 250, from about 8 to about 200, from about 8 to about 150, from about 8 to about 100, from about 8 to about 50, or from about 8 to about 50 30 amino acid residues in length.

In some embodiments, the peptides may be at least 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27 , 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50 or more amino acid residues in length. In some embodiments, the peptides may be at least 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27 , 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 55, 60 , 70, 80, 90, 100, 150, 200, 250, 300, 350, 400, 450, 500 or more amino acid residues in length. In some embodiments, the peptides may be at most 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50 or fewer amino acid residues in length. In some embodiments, the peptides may be at most 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 55, 60, 70, 80, 90, 100, 150, 200, 250, 300, 350, 400, 450, 500 or less amino acid residues in length.

In some embodiments, the peptides have a total length of at least 8, at least 9, at least 10, at least 11, at least 12, at least 13, at least 14, at least 15, at least 16, at least 17, at least 18, at least 19, at least 20, at least 21, at least 22, at least 23, at least 24, at least 25, according to at least 26, at least 27, at least 28, at least 29, at least 30, at least 40, at least 50, at least 60, at least 70, at least 80, according to at least 90, at least 100, at least 150, at least 200, at least 250, at least 300, at least 350, at least 400, at least 450, or at least 500 amino acids.

In some embodiments, the peptides have a total length of at most 8, at most 9, at most 10, at most 11, at most 12, at most 13, at most 14, at most 15, at most 16, at most 17, at most at most 18, at most 19, at most 20, at most 21, at most 22, at most 23, at most 24, at most 25, at most 26, at most 27, at most 28, at most 29, at most 30 , at most 40, at most 50, at most 60, at most 70, at most 80, at most 90, at most 100, at most 150, at most 200, at most 250, at most 300, at most 350, at most at most 400, at most 450, or at most 500 amino acids.

A longer peptide can be designed in several ways. In some embodiments, when HLA binding peptides are predicted or known, the longer peptide comprises (1) individual binding peptides with 2-5 amino acid extensions towards the N- and C-terminus of each respective gene product; or (2) concatenation of some or all of the binding peptides with extended sequences for each. In other embodiments, when sequencing reveals a long (>10 residues) neo-epitope sequence present in the tumor ( eg , due to a frameshift, pass-through, or intron insertion that yields a new peptide sequence), the longer peptide may consist of entire stretches new tumor-specific amino acids in the form of either a single longer peptide or multiple overlapping longer peptides. In some embodiments, use of a longer peptide is believed to allow endogenous processing by the patient's cells, and may result in more efficient antigen presentation and elicitation of T cell responses. In some embodiments, two or more peptides may be used, where the peptides overlap and are surrounded by long neoantigenic peptides.

In some embodiments, the peptides may have a pI value of from about 0.5 to about 12, from about 2 to about 10, or from about 4 to about 8. In some embodiments, the peptides may have a pI value of at least 4. 5, 5, 5.5, 6, 6.5, 7, 7.5 or more. In some embodiments, the peptides may have a pI value of at most 4.5, 5, 5.5, 6, 6.5, 7, 7.5 or less.

In some embodiments, the peptide described in the present invention may be in solution, lyophilized, or may be in crystalline form. In some embodiments, a peptide described in the present invention may be produced synthetically, by recombinant DNA or chemical synthesis, or may be isolated from natural sources such as native tumors or pathogenic organisms. Neoepitopes can be synthesized individually or combined directly or indirectly into a peptide. Although the peptide described in the present invention may be substantially free of other naturally occurring host cell proteins and fragments thereof, in some embodiments, the peptide can be synthetically conjugated to combine with native fragments or particles.

In some embodiments, the peptide described in the present invention can be obtained in a variety of ways. In some embodiments, peptides can be synthesized in solution or on a solid support according to conventional techniques. Various automatic synthesizers are commercially available and can be used according to known protocols. See, for example, Stewart & Young, Solid Phase Peptide Synthesis, 2d. Ed., Pierce Chemical Co., 1984. In addition, individual peptides can be combined using chemical ligation to produce larger peptides, which are still within the scope of the present disclosure.

Alternatively, recombinant DNA technology can be used where the nucleotide sequence that encodes the peptide inserted into the expression vector is transformed or transfected into suitable host cells and cultured under conditions suitable for expression. These techniques are generally known in the art, as described generally in Sambrook et al., Molecular Cloning, Laboratory Manual, Cold Spring Harbor Press, Cold Spring Harbor, N.Y. (1989). Thus, recombinant peptides that contain one or more neoantigenic peptides described in the present invention can be used to present a suitable T cell epitope.

In some embodiments, the peptide is encoded by a gene with a point mutation resulting from an amino acid substitution of the native peptide. In some embodiments, the peptide is encoded by a gene with a point mutation resulting from a frameshift mutation. A frameshift occurs when a mutation disrupts the normal codon periodicity phase of a gene (also known as the “reading frame”), causing translation of a non-native protein sequence. Different mutations in a gene can achieve the same altered reading frames. In some embodiments, the peptide is encoded by a gene with a mutation resulting in a fusion polypeptide, an in-frame deletion, an insertion, expression of endogenous retroviral polypeptides, and tumor-specific overexpression of polypeptides. In some embodiments, the peptide is encoded by fusion of a first gene with a second gene. In some embodiments, the peptide is encoded by an in-frame fusion of a first gene with a second gene. In some embodiments, the peptide is encoded by a fusion of the first gene to an exon of a splice variant of the first gene. In some embodiments, the peptide is encoded by fusion of the first gene to a cryptic exon of the first gene. In some embodiments, the peptide is encoded by fusion of a first gene with a second gene, where the peptide contains an amino acid sequence encoded by the out-of-frame sequence resulting from the fusion.

In some aspects, the present description relates to a composition containing at least two or more than two peptides. In some embodiments, the composition described in the present invention contains at least two separate peptides. In some embodiments, the composition described in the present invention contains a first peptide containing a first neoepitope and a second peptide containing a second neoepitope. In some embodiments, the first and second peptides are derived from the same protein. The at least two individual peptides may vary in length, amino acid sequence, or both. Peptides can be obtained from any protein in which a tumor-specific mutation is known or found. In some embodiments, the composition described in the present invention contains a first peptide containing a first neo-epitope of a protein, and a second peptide containing a second neo-epitope of the same protein, wherein the first peptide is different from the second peptide, and where the first neo-epitope contains a mutation and the second neo-epitope contains the same mutation. In some embodiments, the composition described in the present invention contains a first peptide containing a first neo-epitope of a first region of a protein, and a second peptide containing a second neo-epitope of a second region of the same protein, wherein the first region contains at least one amino acid of the second region, wherein the first the peptide is different from the second peptide and wherein the first neoepitope contains a first mutation and the second neoepitope contains a second mutation. In some embodiments, the first mutation and the second mutation are the same. In some embodiments, the mutation is selected from the group consisting of a point mutation, a splice site mutation, a frameshift mutation, a read-through mutation, a gene fusion mutation, and any combination thereof.

In some embodiments, the peptide may be derived from a protein by a notice mutation, for example , a KRAS G12C, G12D, G12V, Q61H, or Q61L mutation, or an NRAS Q61K or Q61R mutation, or a BTK C481S mutation, or an EGFR S492R or EGFR T490M mutation. The substitution can be located anywhere along the length of the peptide. For example, it may be located in the N-terminal third of the peptide, the central third of the peptide, or the C-terminal third of the peptide. In another embodiment, the substituted residue is located 2-5 residues from the N-terminus or 2-5 residues from the C-terminus. Peptides can also be derived from tumor-specific insertional mutations, where the peptide contains one or more or all of the inserted residues.

In some embodiments, the first peptide contains at least one additional mutation. In some embodiments, one or more of the at least one additional mutation is not a mutation in the first neo-epitope. In some embodiments, one or more of the at least one additional mutation is a mutation in the first neo-epitope. In some embodiments, the second peptide contains at least one additional mutation. In some embodiments, one or more of the at least one additional mutation is not a mutation in the second neo-epitope. In some embodiments, one or more of the at least one additional mutation is a mutation in the second neo-epitope.

In some aspects, the present disclosure relates to a composition comprising a single polypeptide comprising a first peptide and a second peptide, or a single polynucleotide encoding a first peptide and a second peptide. In some embodiments, the composition provided herein comprises one or more additional peptides, wherein the one or more additional peptides comprise a third neo-epitope. In some embodiments, the first peptide and the second peptide are encoded by a sequence transcribed from the same transcription start site. In some embodiments, the first peptide is encoded by a sequence transcribed from a first transcription start site, and the second peptide is encoded by a sequence transcribed from a second transcription start site. In some embodiments, the polypeptide is at least 26 in length; 27; 28; 29; thirty; 40; 50; 60; 70; 80; 90; 100; 150; 200; 250; 300; 350; 400; 450; 500; 600; 700; 800; 900; 1000; 1500; 2000; 2500; 3000; 4000; 5000; 7500; or 10,000 amino acids. In some embodiments, the polypeptide contains a first sequence of at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72 %, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to the corresponding wild-type sequence; and a second sequence with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74 %, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to the corresponding wild-type sequence. In some embodiments, the polypeptide contains a first sequence of at least 8 or 9 contiguous amino acids with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69 %, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to the corresponding wild-type sequence; and a second sequence of at least 16 or 17 contiguous amino acids with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71 %, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to the corresponding wild-type sequence.

In some embodiments, the second peptide is longer than the first peptide. In some embodiments, the first peptide is longer than the second peptide. In some embodiments, the first peptide has a length of at least 9; 10; eleven; 12; 13; 14; 15; 16; 17; 18; 19; 20; 21; 22; 23; 24; 25; 26; 27; 28; 29; thirty; 40; 50; 60; 70; 80; 90; 100; 150; 200; 250; 300; 350; 400; 450; 500; 600; 700; 800; 900; 1000; 1500; 2000; 2500; 3000; 4000; 5000; 7500; or 10,000 amino acids. In some embodiments, the second peptide has a length of at least 17; 18; 19; 20; 21; 22; 23; 24; 25; 26; 27; 28; 29; thirty; 40; 50; 60; 70; 80; 90; 100; 150; 200; 250; 300; 350; 400; 450; 500; 600; 700; 800; 900; 1000; 1500; 2000; 2500; 3000; 4000; 5000; 7500; or 10,000 amino acids. In some embodiments, the first peptide contains a sequence of at least 9 contiguous amino acids with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86% , 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity to the corresponding wild-type sequence. In some embodiments, the second peptide contains a sequence of at least 17 contiguous amino acids with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86% , 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to the corresponding wild-type sequence.

In some embodiments, the first peptide, the second peptide, or both comprise at least one flanking sequence, wherein the at least one flanking sequence is located upstream or downstream of a neoepitope. In some embodiments, the at least one flanking sequence is at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71% , 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88 %, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the corresponding wild-type sequence. In some embodiments, the at least one flanking sequence comprises a non-wild type sequence. In some embodiments, at least one flanking sequence is an N-terminal flanking sequence. In some embodiments, the at least one flanking sequence is a C-terminal flanking sequence. In some embodiments, the at least one flanking sequence of the first peptide is at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87% , 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to at least one flanking sequence of the second peptide . In some embodiments, at least one flanking region of the first peptide is different from at least one flanking region of the second peptide. In some embodiments, at least one flanking residue contains a mutation.

In some embodiments, the neoantigenic peptide with flanking sequences comprises a polypeptide that can be represented by the formula (N-terminus Xaa) _N -(Xaa _BTK ) _P- (Xaa-C-terminus) _C , wherein (Xaa _BTK ) _P is a mutant BTK a peptide sequence containing at least 8 contiguous amino acids of the mutant BTK protein, P is an integer greater than 7; N is equal to (i) 0 or (ii) an integer greater than 2; (N-terminus of Xaa) _N is any amino acid sequence heterologous to the mutant protein; C is equal to (i) 0 or (ii) an integer greater than 2; (Xaa-C-terminus) _C is any amino acid sequence heterologous to the mutant BTK protein; and both N and C are not equal to 0.

In some embodiments, the neoantigenic peptide with flanking sequences comprises a polypeptide that can be represented by the formula (N-terminus Xaa) _N -(Xaa _EGFR ) _P- (Xaa-C-terminus) _C , wherein ( _XaaEGFR ) _P is a mutant EGFR a peptide sequence containing at least 8 contiguous amino acids of the mutant EGFR protein, P is an integer greater than 7; N is equal to (i) 0 or (ii) an integer greater than 2; (N-terminus Xaa) _N is any amino acid sequence heterologous to the mutant EGFR protein; C is equal to (i) 0 or (ii) an integer greater than 2; (Xaa-C-terminus) _C is any amino acid sequence heterologous to the mutant EGFR protein; and both N and C are not equal to 0.

In some embodiments, the peptide contains a neo-epitope sequence containing at least one mutant amino acid. In some embodiments, the peptide contains a neo-epitope sequence comprising at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more mutant amino acids. In some embodiments, the peptide contains a neo-epitope sequence derived from a protein containing at least one mutant amino acid and at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more non-mutant amino acids. In some embodiments, the peptide contains a neo-epitope sequence derived from a protein comprising at least one mutant amino acid and at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13 , 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more non-mutant amino acids above at least one mutant amino acid. In some embodiments, the peptide contains a neo-epitope sequence derived from a protein comprising at least one mutant amino acid and at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13 , 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more non-mutant amino acids downstream of at least one mutant amino acid. In some embodiments, the peptide comprises a neo-epitope sequence derived from a protein containing at least one mutant amino acid; at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24 25, 26, 27, 28, 29, 30 or more non-mutant amino acids above at least one mutant amino acid; and at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more non-mutant amino acids below at least one mutant amino acid.

In some embodiments, the peptide comprises a neoantigenic peptide sequence depicted in Tables 1 or 2 . In some embodiments, the peptide contains a neo-epitope sequence depicted in Tables 1 or 2 . In some embodiments, the peptide contains a neo-epitope sequence comprising at least one mutant amino acid (underlined amino acids) shown in Tables 1 or 2 . In some embodiments, the peptide contains a neo-epitope sequence comprising at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more mutant amino acids (underlined amino acids) shown in Tables 1 or 2 . In some embodiments, the peptide comprises a neoantigenic peptide sequence depicted in Tables 34 or 36 . In some embodiments, the peptide contains a neo-epitope BTK sequence depicted in tables 34 or 36 . In some embodiments, the peptide contains a neo-epitope sequence containing at least one mutant amino acid shown in tables 34 or 36 . In some embodiments, the peptide contains a neo-epitope sequence comprising at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more amino mutants. In some embodiments, the peptide comprises a neo-epitope sequence comprising at least one mutant amino acid (underlined amino acid) and at least one bold amino acid depicted in Tables 1 or 2 . In some embodiments, the peptide contains a neo-epitope sequence derived from a protein comprising at least one mutant amino acid (underlined amino acid) and at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more non-mutant amino acids shown in Tables 1 or 2 . In some embodiments, the peptide contains a neo-epitope sequence derived from a protein comprising at least one mutant amino acid (underlined amino acid) and at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more non-mutant amino acids above at least one mutant amino acid shown in tables 1 or 2 . In some embodiments, the peptide contains a neo-epitope sequence derived from a protein comprising at least one mutant amino acid (underlined amino acid) and at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more non-mutant amino acids, below at least one mutant amino acid shown in tables 1 or 2 . In some embodiments, the peptide contains a neo-epitope sequence derived from a protein containing at least one mutant amino acid (underlined amino acid), at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more non-mutant amino acids above at least one mutant amino acid, and at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22 23, 24, 25, 26, 27, 28, 29, 30 or more non-mutant amino acids below at least one mutant amino acid shown in Tables 1 or 2 .

In some embodiments, the peptide contains a neo-epitope sequence derived from a protein comprising at least one mutant amino acid and at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more non-mutant amino acids downstream of at least one mutant amino acid shown in tables 34 or 36 . In some embodiments, the peptide contains a neo-epitope sequence derived from a protein containing at least one mutant amino acid of at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more non-mutant amino acids upstream of at least one mutant amino acid, and at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24 , 25, 26, 27, 28, 29, 30 or more non-mutant amino acids below at least one mutant amino acid shown in tables 34 or 36 .

In some embodiments, the peptide comprises a neoantigenic peptide sequence depicted in Tables 40A-40D, 32, or 3A-3D . In some embodiments, the peptide contains a neo-epitope EGFR sequence depicted in Tables 40A-40D . In some embodiments, the peptide contains a neo-epitope sequence containing at least one mutant amino acid shown in tables 40A-40D . In some embodiments, the peptide contains a neo-epitope sequence comprising at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more mutant amino acids (for example, the underlined amino acids in any of Tables 40A-40D ). In some embodiments, the EGFR peptide comprises a neo-epitope sequence comprising at least one mutant amino acid shown in bold in Table 40D . In some embodiments, the peptide contains a neo-epitope sequence derived from a protein comprising at least one mutant amino acid (underlined amino acid) and at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more non-mutant amino acids shown in Tables 40A- 40D . In some embodiments, the peptide comprises a neo-epitope sequence derived from a protein comprising at least one mutant amino acid (e.g., the underlined amino acid in Table 40C ) and at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more non-mutant amino acids above , at least one mutant amino acid shown in tables 40A-40D . In some embodiments, the peptide contains a neo-epitope sequence derived from a protein comprising at least one mutant amino acid (underlined amino acid) and at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more non-mutant amino acids downstream of at least one mutant amino acid shown in tables 40A-40D . In some embodiments, the peptide contains a neo-epitope sequence derived from a protein containing at least one mutant amino acid (underlined amino acid), at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more non-mutant amino acids above at least one mutant amino acid, and at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22 23, 24, 25, 26, 27, 28, 29, 30 or more non-mutant amino acids below at least one mutant amino acid shown in Tables 40A-40D .

In some embodiments, the peptide contains a neo-epitope sequence derived from a protein containing at least one mutant amino acid and the sequence upstream of at least one mutant amino acid with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81% , 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98 %, 99% or 100% sequence identity to the corresponding wild-type sequence. In some embodiments, the peptide contains a neo-epitope sequence derived from a protein containing at least one mutant amino acid and the sequence downstream of at least one mutant amino acid with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81% , 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98 %, 99% or 100% sequence identity to the corresponding wild-type sequence. In some embodiments, the peptide contains a neo-epitope sequence derived from a protein containing at least one mutant amino acid, sequence upstream of at least one mutant amino acid with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81% , 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98 %, 99% or 100% sequence identity to the corresponding wild-type sequence, and the sequence below at least one mutant amino acid with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83% , 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100 % sequence identity to the corresponding wild-type sequence.

In some embodiments, the peptide contains a neoepitope sequence derived from a protein containing at least one mutant amino acid and a sequence upstream of at least one mutant amino acid containing at least 1, 2, 3, 4, 5, 6, 7, 8 , 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more continuous amino acids from to at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92% , 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the corresponding wild-type sequence. In some embodiments, the peptide contains a neo-epitope sequence derived from a protein containing at least one mutant amino acid and a sequence downstream of at least one mutant amino acid containing at least 1, 2, 3, 4, 5, 6, 7, 8 , 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more continuous amino acids from to at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92% , 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the corresponding wild-type sequence. In some embodiments, the peptide contains a neo-epitope sequence derived from a protein containing at least one mutant amino acid, a sequence higher than at least one mutant amino acid containing at least 1, 2, 3, 4, 5, 6, 7, 8 , 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more continuous amino acids from to at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92% , 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the corresponding wild-type sequence, and the sequence below, of at least one mutant amino acid containing at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more continuous amino acids with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72 %, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the corresponding wild-type sequence.

In some embodiments, the peptide contains a neo-epitope sequence derived from a protein containing at least one mutant amino acid (underlined amino acid) depicted in Tables 1 or 2 and the sequence above of at least one mutant amino acid with at least 60%, 61% , 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78 %, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the corresponding wild-type sequence. In some embodiments, the peptide contains a neo-epitope sequence derived from a protein containing at least one mutant amino acid (underlined amino acid) depicted in Tables 1 or 2 and the sequence below of at least one mutant amino acid with at least 60%, 61% , 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78 %, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the corresponding wild-type sequence. In some embodiments, the peptide contains a neo-epitope sequence derived from a protein containing at least one mutant amino acid (underlined amino acid) depicted in Tables 1 or 2 , sequence above, of at least one mutant amino acid with at least 60%, 61 %, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94% 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the corresponding wild-type sequence, and sequence downstream of at least one mutant amino acid with at least 60%, 61%, 62%, 63 %, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96% , 97%, 98%, 99%, or 100% sequence identity to the corresponding wild-type sequence.

In some embodiments, the peptide contains a neo-epitope sequence derived from a protein containing at least one mutant amino acid (the underlined amino acid) shown in Tables 1 or 2 and the sequence above of at least one mutant amino acid containing at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more continuous amino acids with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72 %, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the corresponding wild-type sequence. In some embodiments, the peptide contains a neo-epitope sequence derived from a protein containing at least one mutant amino acid (the underlined amino acid) shown in Tables 1 or 2 and the sequence below of at least one mutant amino acid containing at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more continuous amino acids with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72 %, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the corresponding wild-type sequence. In some embodiments, the peptide contains a neo-epitope sequence derived from a protein containing at least one mutant amino acid (the underlined amino acid) shown in Tables 1 or 2 , sequence above, of at least one mutant amino acid containing at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more continuous amino acids with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72 %, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the corresponding wild-type sequence, and the sequence below is at least one mutant amino acid containing at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22 , 23, 24, 25, 26, 27, 28, 29, 30 or more continuous amino acids with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68% , 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85 %, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the corresponding wild type sequences.

In some embodiments, the BTK peptide contains a neoepitope sequence derived from a protein containing at least one mutant amino acid (the underlined amino acid) shown in Tables 34 or 36 and the sequence above of at least one mutant amino acid with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77% , 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94 %, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the corresponding wild-type sequence. In some embodiments, the peptide contains a neo-epitope sequence derived from a protein containing at least one mutant amino acid shown in Tables 34 or 36, and a sequence downstream of at least one mutant amino acid with at least 60%, 61%, 62 %, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95% , 96%, 97%, 98%, 99%, or 100% sequence identity to the corresponding wild-type sequence. In some embodiments, the peptide contains a neo-epitope sequence derived from a protein containing at least one mutant amino acid shown in Tables 34 or 36 , the sequence above the at least one mutant amino acid with at least 60%, 61%, 62% , 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79 %, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the corresponding wild-type sequence, and the sequence below at least one mutant amino acid with at least 60%, 61%, 62%, 63%, 64% , 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81 %, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the corresponding wild-type sequence.

In some embodiments, the peptide contains a neo-epitope sequence derived from a protein containing at least one mutant amino acid (the underlined amino acid) shown in Tables 34 or 36, and the sequence above of at least one mutant amino acid containing at least 1, 2 , 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27 , 28, 29, 30 or more continuous amino acids with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88% 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the corresponding wild-type sequence. In some embodiments, the peptide contains a neo-epitope sequence derived from a protein containing at least one mutant amino acid shown in Tables 34 or 36 and the sequence below of at least one mutant amino acid containing at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more continuous amino acids with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73% , 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90 %, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the corresponding wild-type sequence. In some embodiments, the peptide contains a neo-epitope sequence derived from a protein containing at least one mutant amino acid (the underlined amino acid) shown in Tables 34 or 36 , sequence above, of at least one mutant amino acid containing at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more continuous amino acids with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72 %, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the corresponding wild-type sequence, and the sequence below is at least one mutant amino acid containing at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22 , 23, 24, 25, 26, 27, 28, 29, 30 or more continuous amino acids with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68% , 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85 %, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the corresponding wild type sequences.

Typical neoantigenic peptides corresponding to the C481S mutation are presented in Table 34 . The table also provides a list of HLA alleles encoded by proteins whose products can bind to peptides. In some embodiments, the peptide containing the C481S mutation is: MIKEGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANG S LLNYLREMRHRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVND (SEQ ID NO: 3089). In some embodiments, the peptide containing the BTK mutation contains the neo-epitope sequence ANGSLLNY (SEQ ID NO: 3090). In some embodiments, the peptide containing the C481S BTK mutation contains the neo-epitope sequence ANGSLLNYL (SEQ ID NO: 3091). In some embodiments, the peptide containing the C481S BTK mutation contains the neo-epitope sequence ANGSLLNYLR (SEQ ID NO: 3092). In some embodiments, the peptide containing the C481S BTK mutation contains the neo-epitope sequence EYMANGSL (SEQ ID NO: 3093). In some embodiments, the peptide containing the C481S BTK mutation contains the neo-epitope sequence EYMANGSLLN (SEQ ID NO: 3094). In some embodiments, the peptide containing the C481S BTK mutation contains the neo-epitope sequence EYMANGSLLNY (SEQ ID NO: 3095). In some embodiments, the peptide containing the C481S BTK mutation contains the neo-epitope sequence GSLLNYLR (SEQ ID NO: 3096). In some embodiments, the peptide containing the C481S BTK mutation contains the neo-epitope sequence GSLLNYLREM (SEQ ID NO: 3097). In some embodiments, the peptide containing the C481S BTK mutation contains the neo-epitope sequence ITEYMANGS (SEQ ID NO: 3098). In some embodiments, the peptide containing the C481S BTK mutation contains the neo-epitope sequence ITEYMANGSL (SEQ ID NO: 3099). In some embodiments, the peptide containing the C481S BTK mutation contains the neo-epitope sequence ITEYMANGSLL (SEQ ID NO: 3100). MANGSLLNYL (SEQ ID NO: 3101). In some embodiments, the peptide containing the C481S BTK mutation contains the neo-epitope sequence MANGSLLNYLR (SEQ ID NO: 3102). In some embodiments, the peptide containing the C481S BTK mutation contains the neo-epitope sequence NGSLLNYL (SEQ ID NO: 3103). In some embodiments, the peptide containing the C481S BTK mutation contains the neo-epitope sequence NGSLLNYL (SEQ ID NO: 3104). In some embodiments, the peptide containing the C481S BTK mutation contains the neo-epitope sequence SLLNYLREMR (SEQ ID NO: 3105). In some embodiments, the peptide containing the C481S BTK mutation contains the neo-epitope sequence TEYMANGSLL (SEQ ID NO: 3106); TEYMANGSLLNY (SEQ ID NO: 3107). In some embodiments, the peptide containing the C481S BTK mutation contains the neo-epitope sequence YMANGSLL (SEQ ID NO: 3108).

In some embodiments, the EGFR peptide contains a neo-epitope sequence derived from a protein containing at least one mutant amino acid (underlined amino acid) depicted in Tables 40A-40D and the sequence above of at least one mutant amino acid with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77% , 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94 %, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the corresponding wild-type sequence. In some embodiments, the peptide contains a neo-epitope sequence derived from a protein containing at least one mutant amino acid (underlined amino acid) shown in Tables 40A - 40D and the sequence below of at least one mutant amino acid with at least 60%, 61 %, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94% , 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the corresponding wild-type sequence. In some embodiments, the peptide contains a neo-epitope sequence derived from a protein containing at least one mutant amino acid shown in Tables 40A-40D , a sequence higher than at least one mutant amino acid with at least 60%, 61%, 62% , 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79 %, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the corresponding wild-type sequence, and the sequence below at least one mutant amino acid with at least 60%, 61%, 62%, 63%, 64% , 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81 %, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the corresponding wild-type sequence.

In some embodiments, the peptide contains a neo-epitope sequence derived from a protein containing at least one mutant amino acid (the underlined amino acid) shown in Tables 40A-40D and the sequence above of at least one mutant amino acid containing at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more continuous amino acids with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72 %, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the corresponding wild-type sequence. In some embodiments, the peptide contains a neo-epitope sequence derived from a protein containing at least one mutant amino acid (the underlined amino acid) shown in Tables 40A-40D and the sequence below of at least one mutant amino acid containing at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more continuous amino acids with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72 %, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the corresponding wild-type sequence. In some embodiments, the peptide contains a neo-epitope sequence derived from a protein containing at least one mutant amino acid (underlined amino acid) shown in Tables 40A-40D , sequence above, at least one mutant amino acid containing at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more continuous amino acids with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72 %, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the corresponding wild-type sequence, and a sequence lower than at least one a mutant amino acid containing at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more continuous amino acids with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85% , 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the corresponding sequence wild type.

In some embodiments, the peptide containing the EGFR T790M mutation contains the sequence GICLTSTVQLI M QLMPFGCLLDY (SEQ ID NO: 3109). In some embodiments, the peptide containing the EGFR T790M mutation contains the neo-epitope sequence VQLI M QLMPF (SEQ ID NO: 3110). In some embodiments, the peptide containing the EGFR T790M mutation contains the neo-epitope sequence STVQLI M QLM (SEQ ID NO: 3111). In some embodiments, the mutant EGFR peptide containing the EGFR T790M mutation contains the neo-epitope sequence QLI M QLMPF (SEQ ID NO: 3112). In some embodiments, the peptide containing the EGFR T790M mutation contains the neo-epitope sequence M QLMPFGCLL (SEQ ID NO: 3113). In some embodiments, the peptide containing the EGFR T790M mutation contains the neo-epitope sequence LI M QLMPF (SEQ ID NO: 3114). In some embodiments, the peptide containing the EGFR T790M mutation contains the neo-epitope sequence LTSTVQLI M (SEQ ID NO: 3115). In some embodiments, the peptide containing the EGFR T790M mutation contains the neo-epitope sequence STVQLI M QL (SEQ ID NO: 3116). In some embodiments, the peptide containing the EGFR T790M mutation contains the neo-epitope sequence TSTVQLI M QL (SEQ ID NO: 3117). In some embodiments, the peptide containing the EGFR T790M mutation contains the neo-epitope sequence TVQLI M QL (SEQ ID NO: 3118). In some embodiments, the peptide containing the EGFR T790M mutation contains the neo-epitope sequence TVQLI M QLM (SEQ ID NO: 3119). In some embodiments, the peptide containing the EGFR T790M mutation contains the neo-epitope sequence VQLI M QLM (SEQ ID NO: 3120). In some embodiments, the peptide containing the EGFR T790M mutation contains the neo-epitope sequence CLTSTVQLI M (SEQ ID NO: 3121). In some embodiments, the peptide containing the EGFR T790M mutation contains the neo-epitope sequence I M QLMPFGC (SEQ ID NO: 3122). In some embodiments, the peptide containing the EGFR T790M mutation contains the neo-epitope sequence I M QLMPFGC (SEQ ID NO: 3123). In some embodiments, the peptide containing the EGFR T790M mutation contains the neo-epitope sequence I M QLMPFGCL (SEQ ID NO: 3124). In some embodiments, the peptide containing the EGFR T790M mutation contains the neo-epitope sequence LI M QLMPFG (SEQ ID NO: 3125). In some embodiments, the peptide containing the EGFR T790M mutation contains the neo-epitope sequence LI M QLMPFGC (SEQ ID NO: 3126). In some embodiments, the peptide containing the EGFR T790M mutation contains the neo-epitope sequence QLI M QLMPFG (SEQ ID NO: 3127).

In some embodiments, the peptide containing the EGFR S492R mutation contains the sequence SLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKII R NRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLL (SEQ ID NO: 3128). In some embodiments, the peptide containing the EGFR S492R mutation contains the neo-epitope sequence II R NRGENSCK (SEQ ID NO: 3129).

In some embodiments, the EGFR neopeptide is selected from Tables 40A-40D .

In some embodiments, a peptide containing a deletion mutation in EGFR, such as a G deletion in EGFRvIII (internal deletion), MRPSGTAGAALLALLAALCPASRALEEKK: G :NYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKD (SEQ ID NO: 3130), contains the neo-epitope sequence ALEEKK G NYV (SEQ ID NO: 313 1) .

In some embodiments, the peptide containing the mutation depicted in the sequence: LPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQ:: LQDKFEHLKMIQQEEIRKLEEEKKQLEGEIIDFYKMKAASEALQTQLSTD (SEQ ID NO: 3132) contains the neo-epitope sequence IQ LQDKFEHL (SEQ ID NO: 3 133 ) In some embodiments, the peptide containing the mutation depicted in the sequence: LPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQ:: LQDKFEHLKMIQQEEIRKLEEEKKQLEGEIIDFYKMKAASEALQTQLSTD (SEQ ID NO: 3134) contains the neo-epitope sequence Q LQDKFEHL (SEQ ID NO: 31 35). In some embodiments, the peptide containing the mutation depicted in the sequence: LPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQ:: LQDKFEHLKMIQQEEIRKLEEEKKQLEGEIIDFYKMKAASEALQTQLSTD (SEQ ID NO: 3136), contains the neo-epitope sequence Q LQDKFEHLK (SEQ ID NO: 31 37). In some embodiments, the peptide containing the mutation depicted in the sequence: LPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQ:: LQDKFEHLKMIQQEEIRKLEEEKKQLEGEIIDFYKMKAASEALQTQLSTD (SEQ ID NO: 3138), contains a neo-epitope sequence

Peptide modification

In some embodiments, the present disclosure includes modified peptides. The modification may include a covalent chemical modification that does not change the primary amino acid sequence of the antigenic peptide itself. Modifications may produce peptides with desired properties, such as extended in vivo half-life, increased stability, decreased clearance, altered immunogenicity or allergenicity, ability to induce certain antibodies, cellular targeting, antigen uptake, antigen processing, HLA affinity, HLA stability, or antigen presentation. In some embodiments, the peptide may contain one or more sequences that enhance the processing and presentation of APC epitopes, for example, to generate an immune response.

In some embodiments, the peptide may be modified to obtain the desired parameters. For example, the ability of peptides to induce CTL activity can be improved by binding to a sequence that contains at least one epitope that is capable of inducing a T helper cell response. In some embodiments, the immunogenic peptides/T helper conjugates are linked by a spacer molecule. In some embodiments, the spacer contains relatively small neutral molecules, such as amino acids or amino acid mimetics, that are substantially uncharged under physiological conditions. Spacers may be selected from, for example , Ala, Gly or other neutral non-polar amino acid spacers or neutral polar amino acids. It should be understood that the optionally present spacer does not necessarily consist of identical residues and, therefore, may be a hetero- or homo-oligomer. The neoantigen peptide can be linked to the T helper peptide directly or through a spacer, either at the amino or carboxy terminus of the peptide. The amino terminus of either the neoantigen peptide or the T helper peptide may be acylated. Examples of T helper peptides include tetanus toxin residues 830-843, influenza residues 307-319, and malaria circumsporozoite residues 382-398 and residues 378-389.

The peptide sequences of the present disclosure may optionally be altered through changes at the DNA level, in particular by mutation of the DNA encoding the peptide at preselected bases, so that codons are created that will translate into the desired amino acids.

In some embodiments, a peptide described in the present invention may be subject to substitutions to modify the physical property ( eg , stability or solubility) of the resulting peptide. For example, peptides can be modified by replacing cysteine (C) with α-aminobutyric acid (“B”). Due to its chemical nature, cysteine has a tendency to form disulfide bridges and sufficiently alter the structure of the peptide to reduce binding capacity. Substituting α-aminoaminobutyric acid for C not only alleviates this problem, but actually improves binding and cross-linking ability in certain cases. Substitution of α-aminobutyric acid for cysteine can occur at any residue of the neoantigenic peptide, for example at any anchoring or non-anchoring position of an epitope or analog in the peptide, or at other positions in the peptide.

The peptide can also be modified by increasing or decreasing the amino acid sequence of the compound, such as by adding or deleting amino acids. Peptides or analogs can also be modified by changing the order or composition of certain residues. It will be appreciated by one skilled in the art that certain amino acid residues vital for biological activity, such as those located at critical contact sites, or conserved residues, generally cannot be changed without adversely affecting the biological activity. Non-critical amino acids are not necessarily limited to naturally occurring residues in proteins such as L-α-amino acids, but may also include non-naturally occurring amino acids such as the D-isomer, β-γ-δ-amino acids, as well as many L derivatives -α-amino acids.

In some embodiments, the peptide may be modified using a number of peptides with individual amino acid substitutions to determine electrostatic charge effects, hydrophobicity, etc. for HLA binding. For example, a range of positively charged ( eg Lys or Arg) or negatively charged ( eg Glu) amino acid substitutions can be made along the length of the peptide, revealing different sensitivity patterns towards different HLA molecules and T cell receptors. In addition, multiple substitutions using small, relatively neutral groups such as Ala, Gly, Pro, or similar residues can be used. Substitutions may be homo-oligomers or hetero-oligomers. The number and types of residues that are substituted or added depend on the distance required between the significant points of contact and the particular functional attributes sought ( eg , hydrophobicity and hydrophilicity). Increased binding affinity for HLA molecules or T cell receptor can also be achieved by such substitutions, compared to the affinity of the original peptide. In any case, such substitutions should employ amino acid residues or other molecular moieties selected to avoid, for example, steric and charge interference that could break the bond. Amino acid substitutions are usually single residues. Substitutions, deletions, insertions, or any combination thereof may be combined to produce the final peptide.

In some embodiments, the peptide described in the present invention may contain amino acid mimetics or non-naturally occurring amino acid residues, such as D- or L-naphthylalanine; D- or L-phenylglycine; D- or L-2-thieneylalanine; D- or L-1, -2, 3-, or 4-pyrenylalanine; D- or L-3 thienylalanine; D- or L-(2-pyridinyl)alanine; D- or L-(3-pyridinyl)alanine; D- or L-(2-pyrazinyl)alanine; D- or L-(4-isopropyl)phenylglycine; D-(trifluoromethyl)phenylglycine; D-(trifluoromethyl)phenylalanine; D-ρ-fluorophenylalanine; D- or L-ρ-biphenylphenylalanine; D- or L-ρ-methoxyphenylphenylalanine; D- or L-2-indole(allyl)alanines; and, D- or L-alkylalanines, wherein the alkyl group may be substituted or unsubstituted with methyl, ethyl, propyl, hexyl, butyl, pentyl, isopropyl, isobutyl, sec-isoyl, isopentyl; or non-acidic amino acid residues. Aromatic rings of non-naturally occurring amino acids include, for example, thiazolyl, thiophenyl, pyrazolyl, benzimidazolyl, naphthyl, furanyl, pyrrolyl, pyridyl aromatic rings. Modified peptides that contain various amino acid mimetics or non-naturally occurring amino acid residues may have increased in vivo stability. Such peptides may also have improved shelf life or manufacturing properties.

In some embodiments, the peptide described in the present invention may be modified by NH ₂ -terminal acylation, e.g. , alkanoyl (C ₁ -C ₂₀ ), or thioglycolyl cetylation, carboxyl-terminal amidation, e.g. , ammonia, methylamine, etc. . In some embodiments, these modifications may provide sites for binding to a support or other molecule. In some embodiments, the peptide described in the present invention may contain modifications such as, but not limited to, glycosylation, side chain oxidation, biotinylation, phosphorylation, addition of a surfactant such as fat, or may be chemically modified, for example , acetylation, etc. Moreover, the bonds in a peptide may be different from peptide bonds, such as covalent bonds, ester bonds, disulfide bonds, hydrogen bonds, ionic bonds, etc.

In some embodiments, the peptide described in the present invention may contain carriers that are well known in the art, for example , thyroglobulin, albumins such as human serum albumin, tetanus toxoid, polyamino acid residues such as poly L-lysine and poly L-glutamic acid, influenza virus proteins, hepatitis B virus core protein and the like.

Peptides can be further modified to contain additional chemical groups not typically found as part of the protein. Such derivative groups may improve solubility, biological half-life, protein absorption, or binding affinity. The groups can also reduce or eliminate any desired side effects of peptides and the like. A review of such groups can be found in Remington's Pharmaceutical Sciences, 20th ed., Mack Publishing Co., Easton, PA (2000). For example, neoantigenic peptides having desired activity can be modified as needed to provide certain desired attributes, such as improved pharmacological properties, while increasing or at least maintaining substantially all of the biological activity of the unmodified peptide for binding the desired HLA molecule and activating the corresponding T- cells. For example, a peptide may be subject to various changes, such as substitutions, conservative or non-conservative, where such changes may provide certain advantages in their use, such as improved HLA binding. Such conservative substitutions may involve replacing an amino acid residue with another amino acid residue that is biologically and/or chemically similar, for example , one hydrophobic residue for another, or one polar residue for another. The effect of individual amino acid substitutions can also be tested using D-amino acids. Such modifications can be carried out using well known peptide synthesis methods, as described in, for example , Merrifield, Science 232:341-347 (1986), Barany & Merrifield, Peptides, Gross & Meienhofer, eds. (NY, Academic Press), pp. 1-284 (1979); and Stewart & Young, Solid Phase Peptide Synthesis, (Rockford, III., Pierce), 2d Ed. (1984).

In some embodiments, a peptide described in the present invention may be conjugated to large, slowly metabolized macromolecules such as proteins; polysaccharides such as sepharose, agarose, cellulose, cellulose spheres; polymeric amino acids such as polyglutamic acid, polylysine; amino acid copolymer; inactivated virus particles; inactivated bacterial toxins, such as toxoid preparations of diphtheria, tetanus, cholera, leukotoxin molecules; inactivated bacteria; and dendritic cells.

Peptide modifications may include, but are not limited to, carrier protein conjugation, ligand conjugation, antibody conjugation, PEGylation, polysialylation, HESylation, recombinant PEG mimetics, Fc fusion, albumin fusion, nanoparticle attachment, nanoparticle encapsulation, cholesterol fusion , iron fusion, acylation, amidation, side chain oxidation, phosphorylation, biotinylation, surfactant addition, addition of amino acid mimetics, or addition of non-naturally occurring amino acids.

Glycosylation can affect the physical properties of proteins and may also be important for protein stability, secretion, and subcellular localization. Proper glycosylation may be important for biological activity. In fact, some genes from eukaryotic organisms, when expressed in a bacterium ( eg E. coli) that does not have the cellular processes for protein glycosylation, produce proteins that are regenerated with little or no activity due to their lack of glycosylation. The addition of glycosylation sites may be accompanied by a change in the amino acid sequence. Modification of the peptide or protein can be accomplished, for example, by the addition or substitution of one or more serine or threonine residues (for O -linked glycosylation sites) or aspartic residues (for N -linked glycosylation sites). The structure of N -linked and O -linked oligosaccharides and sugar residues found in each type may differ. One type of sugar that is commonly found on both is N -acetylneuraminic acid (hereinafter called sialic acid). Sialic acid is usually the terminal residue of both N -linked and O -linked oligosaccharides and, due to its negative charge, can impart acidic properties to the glycoprotein. Embodiments of the present disclosure include the creation and use of N -glycosylated variants. Removal of carbohydrates can be accomplished chemically or enzymatically, or by substitution of codons encoding amino acid residues that are glycosylated. Chemical deglycosylation techniques are known, and enzymatic cleavage of carbohydrate groups on polypeptides can be achieved using a variety of endo- and exoglycosidases.

Additional suitable components and molecules for conjugation include, for example, molecules for targeting the lymphatic system, thyroglobulin; albumins such as human serum albumin (HAS); tetanus toxoid preparation; diphtheria toxoid drug; polyamino acids such as poly(D-lysine:D-glutamic acid); VP6 polypeptides of rotaviruses; influenza virus hemagglutinin, influenza virus nucleoprotein; snail limpet hemocyanin (KLH); and hepatitis B virus core protein and surface antigen; or any combination of the above.

Another type of modification is the conjugation ( eg , binding) of one or more additional components or molecules at the N- and/or C-termini of a polypeptide sequence, such as another protein ( eg , a protein having an amino acid sequence heterologous to the subject protein) or a carrier molecule. Thus, exemplary polypeptide sequences may be presented as conjugates with another component or molecule. In some embodiments, fusion of albumin to a peptide or protein of the present disclosure may, for example, be achieved by genetic manipulation, such as DNA coding for HSA, or a fragment thereof, coupled to DNA coding for one or more polypeptide sequences. A suitable host can then be transformed or transfected with the fusion nucleotide sequences in the form of, for example, a suitable plasmid so as to express the polypeptide. Expression can be carried out in vitro from, for example, prokaryotic or eukaryotic cells, or in vivo from, for example, a transgenic organism. In some embodiments of the present disclosure, expression of the fusion protein is carried out in a mammalian cell line, CHO cell lines. Moreover, albumin itself can be modified to extend its half-life in the bloodstream. Fusion of the modified albumin with one or more polypeptides can be achieved by genetic manipulation methods described above or by chemical conjugation; the resulting fusion molecules have a half-life greater than that of unmodified albumin fusions (see e.g. WO2011/051489). Several albumin binding strategies have been developed as alternatives to direct fusion, including binding albumin via a conjugated fatty acid chain (acylation). Since serum albumin is a transport protein for fatty acids, these natural ligands with albumin binding activity are used to prolong the half-life of small protein therapeutic agents.

Additional candidate components and molecules for conjugation include those suitable for isolation or purification. Non-limiting examples include binding molecules such as biotin (biotin-avidin specific binding pairs), antibody, receptor, ligand, lectin or molecules that contain a solid support including, for example, plastic or polystyrene spheres, plates or beads, magnetic beads, test strips and membranes. Purification methods such as cation exchange chromatography can be used to separate conjugates through a charge difference that effectively separates the conjugates into their different molecular weights. The contents of fractions obtained by cation exchange chromatography can be identified by molecular weight using conventional methods, for example, mass spectroscopy, SDS-PAGE or other known methods for separating molecular substances by molecular weight.

In some embodiments, the amino or carboxyl terminus of a peptide or protein sequence of the present disclosure can be fused to the Fc region of an immunoglobulin ( eg , human Fc) to produce a fusion conjugate (or fusion molecule). Fc fusion conjugates have been shown to increase the systemic half-life of biopharmaceutical agents and therefore the biopharmaceutical agent may require less frequent administration. Fc binds to the neonatal Fc receptor (FcRn) on endothelial cells that line blood vessels and, when bound, the Fc fusion molecules are protected from destruction and re-released into the bloodstream, keeping the molecule in the bloodstream longer. This Fc binding is believed to be the mechanism by which endogenous IgG maintains its long half-life in plasma. More recent Fc fusion technology links one copy of a biopharmaceutical agent to the Fc region of an antibody to optimize the pharmacokinetic and pharmacodynamic properties of the biopharmaceutical agent compared to traditional Fc fusion conjugates.

Disclosed herein is the use of other modifications, currently known or to be developed in the future, of peptides to improve one or more properties. One such method of prolonging the circulating half-life, increasing stability, decreasing clearance, or altering the immunogenicity of a peptide of the present disclosure involves modifying peptide sequences by hesylation, which uses hydroxyethyl starch derivatives linked to other molecules to modify the characteristics of the molecule. Various aspects of hesylation are described in, for example, US patent applications No. 2007/0134197 and 2006/0258607.

Peptide stability can be assessed in a variety of ways. For example, peptidases and various biological media such as human plasma and serum are used for stability testing. See, for example , Verhoef, et al., Eur. J. Drug Metab. Pharmacokinetics 11:291 (1986). The half-life of the peptides described in the present invention is conveniently determined using a 25% human serum (v/v) assay. The protocol is as follows: Pooled human serum (type AB, not heat inactivated) is destroyed by centrifugation prior to use. The serum is then diluted to 25% with RPMI-1640 or other suitable tissue culture medium. At predetermined time intervals, a small amount of the reaction solution is removed and added to either 6% aqueous trichloroacetic acid (TCA) or ethanol. The turbid reaction sample is cooled (4°C) for 15 minutes and then centrifuged to obtain a cake of precipitated whey proteins. The presence of peptides is then determined by reverse phase HPLC using stability-specific chromatographic conditions.

Problems associated with short plasma half-life or susceptibility to protease degradation can be overcome by various modifications, including conjugating or linking the peptide or protein sequence to any of a variety of non-protein polymers, e.g. polyethylene glycol (PEG), polypropylene glycol, or polyoxyalkylenes (see, for example, usually through the binding of a group covalently bound to both proteins and a non-protein polymer, e.g. PEG). Such PEG-conjugated biomolecules have been shown to have clinically useful properties, including better physical and thermal stability, protection against susceptibility to enzymatic degradation, increased solubility, longer in vivo circulating half-life and reduced clearance, reduced immunogenicity and antigenicity, and reduced toxicity. .

PEGs suitable for conjugation to a polypeptide or protein sequence are generally soluble in water at room temperature, and have the general formula R-(O-CH ₂ -CH ₂ ) _n -OR, where R is hydrogen or a protecting group such as an alkyl or an alkanoyl group, and where n is an integer from 1 to 1000. If R is a protecting group, it typically has from 1 to 8 carbon atoms. The PEG conjugated to the polypeptide sequence may be linear or branched. Branched PEG derivatives, star-PEGs and multi-armed PEGs are contemplated herein. The present disclosure also contemplates conjugate compositions where the PEG has different n values and such different PEGs are present in certain proportions. For example, some compositions include a mixture of conjugates where n=1, 2, 3 and 4. In some compositions, the proportion of conjugates where n=1 is 18-25%, the proportion of conjugates where n=2 is 50-66% , the proportion of conjugates where n=3 is 12-16%, and the proportion of conjugates where n=4 is up to 5%. Such compositions can be prepared under reaction conditions and purification methods known in the art. For example, cation exchange chromatography can be used to separate conjugates, and then the fraction that contains the conjugate having, for example, the desired number of PEGs attached, is identified, purified from unmodified protein sequences, and from conjugates having a different number of PEGs attached.

PEG may be linked to a peptide or protein of the present disclosure via a terminal reactive group (“spacer”). A spacer is, for example, a terminal reactive group that mediates the connection between the free amino or carboxyl groups of one or more polypeptide sequences and a PEG. PEG having a spacer that can be linked to a free amino group includes PEG N-hydroxysuccinyl imide, which can be prepared by activating the succinic acid ester of PEG with N-hydroxysuccinyl imide. Another activated PEG that can be linked to a free amino group is 2,4-bis(O-methoxypolyethylene glycol)-6-chloro-s-triazine, which can be prepared by reacting PEG monomethyl ether with cyanuric chloride. Activated PEG, which is linked to a free carboxyl group, includes polyoxyethylenediamine.

Conjugation of one or more peptide or protein sequences of the present disclosure to a PEG having a spacer can be accomplished by a variety of conventional methods. For example, the conjugation reaction can be carried out in solution at a pH of 5 to 10, at a temperature of 4°C to room temperature, for 30 minutes to 20 hours, using a reagent to peptide/protein ratio of 4:1 to 30: 1. Reaction conditions can be selected to direct the reaction to produce predominantly the desired degree of substitution. In general, low temperature, low pH ( e.g. pH=5) and short reaction times tend to reduce the amount of attached PEG, while high temperature, neutral to high pH ( e.g. pH>7) and longer times reactions tend to increase the amount of PEG attached. Various means known in the art can be used to stop the reaction. In some embodiments, the reaction is stopped by acidifying the reaction mixture and freezing it at, for example , -20°C.

The present disclosure also addresses the use of PEG mimetics. Recombinant PEG mimetics have been developed that retain the features of PEG ( e.g. , improved serum half-life) while gaining some additional beneficial properties. As an example, simple polypeptide chains (containing, for example, Ala, Glu, Gly, Pro, Ser and Thr) capable of forming an extended conformation similar to PEG can be produced recombinantly already fused to the peptide or protein drug of interest ( eg , AmunixXTEN technology; Mountain View, CA). This eliminates the need for an additional conjugation step during the manufacturing process. Moreover, established molecular biology techniques allow control of the side chain composition of polypeptide chains, allowing optimization of immunogenicity and manufacturing properties.

Neoepitopes

The neoepitope contains the neoantigenic defining portion of a neoantigenic peptide or neoantigenic polypeptide that is recognized by the immune system. A neoepitope refers to an epitope that is not present in a reference, such as a non-diseased cell, e.g. a non-cancer cell or parent cell, but is found in a diseased cell, e.g. a cancer cell. This includes situations where the corresponding epitope is found in a normal non-diseased cell or parent cell, but, due to one or more mutations in a diseased cell, for example a cancer cell, the sequence of the epitope is changed so as to produce a neo-epitope. The term “neoepitope” is used interchangeably with “tumor-specific neoepitope” as used herein to refer to a series of residues, typically L-amino acids, linked to each other, typically through peptide bonds between the α-amino and carboxyl groups of adjacent amino acids. A neo-epitope can be of varying lengths, be in either neutral (unmodified) forms or in forms that are salts, and either have no modifications such as glycosylation, side chain oxidation or phosphorylation, or contain these modifications, provided the modifications are not destructive biological activity of the polypeptides as described in the present invention. Presented herein are isolated neoepitopes that contain tumor-specific mutations from Tables 1 or 2 . The present description also presents exemplary isolated neoepitopes that contain tumor-specific mutations from Table 34 . This description also presents exemplary isolated neoepitopes that contain tumor-specific mutations from Tables 40A-40D and Tables 3A-3D .

In some embodiments, the neoepitopes described herein for HLA class I are 13 residues or less in length and typically consist of from about 8 to about 12 residues, particularly 9 or 10 residues. In some embodiments, the neoepitopes described herein for HLA class II are 25 residues or less in length and typically consist of from about 16 to about 25 residues.

In some embodiments, the composition described in the present invention contains a first peptide containing a first neo-epitope of a protein, and a second peptide containing a second neo-epitope of the same protein, wherein the first peptide is different from the second peptide, and where the first neo-epitope contains a mutation and the second neo-epitope contains the same mutation. In some embodiments, the composition described in the present invention contains a first peptide containing a first neo-epitope of a first region of a protein, and a second peptide containing a second neo-epitope of a second region of the same protein, wherein the first region contains at least one amino acid of the second region, wherein the first the peptide is different from the second peptide, and wherein the first neoepitope contains a first mutation and the second neoepitope contains a second mutation. In some embodiments, the first mutation and the second mutation are the same. In some embodiments, the mutation is selected from the group consisting of a point mutation, a splice site mutation, a frameshift mutation, a read-through mutation, a gene fusion mutation, and any combination thereof.

In some embodiments, the first neoepitope binds to an HLA class I protein to form an HLA-class I peptide complex. In some embodiments, the second neo-epitope binds to an HLA class II protein to form an HLA-class II peptide complex. In some embodiments, the second neoepitope binds to an HLA class I protein to form an HLA-class I peptide complex. In some embodiments, the first neo-epitope binds to an HLA class II protein to form an HLA-class II peptide complex. In some embodiments, the first neoepitope activates CD8 ⁺ T cells. In some embodiments, the first neoepitope activates CD4 ⁺ T cells. In some embodiments, the second neo-epitope activates CD4 ⁺ T cells. In some embodiments, the second neo-epitope activates CD8 ⁺ T cells. In some embodiments, the TCR of the CD4 ⁺ T cell binds to the HLA-class II peptide complex. In some embodiments, the CD8 ⁺ T cell TCR binds to the HLA class II peptide complex. In some embodiments, the TCR of the CD8 ⁺ T cell binds to the HLA-class I peptide complex. In some embodiments, the TCR of the CD4 ⁺ T cell binds to the HLA-class I peptide complex. In some embodiments, a composition comprising neoantigenic C481S BTK peptides contains a first BTK neoepitope and a second BTK neoepitope. In some embodiments, the first BTK neo-epitope comprises a neo-epitope selected from Table 34 . In some embodiments, the second BTK neo-epitope comprises a neo-epitope selected from Table 34 .

In some embodiments, the first mutant BTK peptide sequence, which is selected from Table 34, binds or is predicted to bind to a protein encoded by the HLA allele listed in Table 34 corresponding to the corresponding peptide (left column and right column).

In some embodiments, a composition comprising neoantigenic EGFR peptides contains a first EGFR neoepitope and a second EGFR neoepitope. In some embodiments, the first EGFR neo-epitope comprises a neo-epitope selected from Tables 40A-40D . In some embodiments, the second EGFR neo-epitope comprises a neo-epitope selected from Tables 40A-40D .

In some embodiments, the first mutant EGFR neoepitope is selected from the group consisting of STVQLIMQL (SEQ ID NO: 3139), LIMQLMPF (SEQ ID NO: 3140), LTSTVQLIM (SEQ ID NO: 3141), TVQLIMQL (SEQ ID NO: 3142) , TSTVQLIMQL (SEQ ID NO: 3143), TVQLIMQLM (SEQ ID NO: 3144) and VQLIMQLM (SEQ ID NO: 3145).

In some embodiments, a first mutant EGFR peptide sequence that is selected from the group consisting of STVQLIMQL (SEQ ID NO: 3146), LIMQLMPF (SEQ ID NO: 3147), LTSTVQLIM (SEQ ID NO: 3148), TVQLIMQL (SEQ ID NO: : 3149), TSTVQLIMQL (SEQ ID NO: 3150), TVQLIMQLM (SEQ ID NO: 3151) and VQLIMQLM (SEQ ID NO: 3152), binds to or is predicted to bind to the protein encoded by the HLA-A68:01 allele, HLA-B15 :02 allele, HLA-A25:01 allele, HLA-B57:03 allele, HLA-C12:02 allele, HLA-C03:02 allele and HLA-A26:01 allele, HLA-C12:03 allele, HLA-C06: 02 allele, HLA-C03:03, HLA-B52:01 allele, HLA-A30:01 allele, HLA-C02:02 allele, HLA-C12:03 allele, HLA-A11:01 allele, HLA-A32:01 allele , HLA-A02:04 allele, HLA-B15:09 allele, HLA-C17:01 allele, HLA-C03:04 allele, HLA-B08:01 allele, HLA-A01:01 allele, HLA-B42:01 allele, HLA-B57:01 allele, HLA-B14:02 allele, HLA-B37:01 allele, HLA-B36:01 allele, HLA-B38:01 allele, HLA-C03:03 allele, HLA-B14:02 allele, HLA -B37:01 allele, HLA-A02:03 allele, HLA-B58:02 allele, HLA-C08:01 allele, HLA-B35:01 allele, HLA-B40:01 allele and/or HLA-B35:03 allele.

Table 41 provides a list of typical HLA alleles encoding an HLA protein that may bind or is predicted to bind to the EGFR neoantigen peptide.

HLA-A23:01 HLA-A25:01 HLA-A26:01 HLA-A32:01 HLA-B15:01 HLA-B15:02 HLA-B38.01 HLA-B39:01 HLA-B39:06 HLA-B40:02 HLA-C03:02 HLA-C12:03 HLA-A01:01 HLA-C15:02 HLA-B57:01 HLA-B57:03 HLA-A36:01 HLA-C12:02 HLA-C03:03 HLA-B58:02 HLA-B15:01 HLA-A26:01 HLA-A68:02 HLA-C15:02 HLA-A25:01 HLA-B57:03 HLA-C12:02 HLA-A26:01 HLA-C12:03 HLA-C06:02 HLA-C03:03 HLA-A30:01 HLA-C02:02 HLA-A11:01 HLA-A32:01 HLA-A02:04 HLA-A68:01 HLA-B15:09 HLA-C03:04 HLA-B38:01 HLA-B57:01 HLA-A02:03 HLA-C08:01 HLA-B35:01 HLA-B40:01 HLA-A26:01 HLA-B57:01 HLA-C15:02 HLA-C17:01 HLA-B08:01 HLA-B42:01 HLA-B14:02 HLA-B37:01 HLA-B15:09 HLA-B35:03 HLA-B52:01 HLA-B14:02 HLA-B37:01

Tables 42Ai, 42Aii and 42B show EGFR neo-epitopes with predicted HLA subtype specificity.

Tables 5Ai, 5Aii and 5B show EGFR neo-epitopes with predicted HLA subtype specificity.

Table 42Ai

EGFR mutation Sequence Mutation Context Peptides HLA allele S492R SLNITSSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKII R NRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLL (SEQ ID NO: 3153) IIRNRGENSCK (SEQ ID NO: 3154) A03.01

Table 42Aii

EGFR mutation Sequence Mutation Context Peptides HLA allele T790M IPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLI M QLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAA (SEQ ID NO: 3155) CLTSTVQLIM (SEQ ID NO: 3156) A01.01, A02.01 IMQLMPFGC (SEQ ID NO: 3157) A02.01 IMQLMPFGCL (SEQ ID NO: 3158) A02.01, A24.02, B08.01 LIMQLMPFG (SEQ ID NO: 3159) A02.01 LIMQLMPFGC (SEQ ID NO: 3160) A02.01 LTSTVQLIM (SEQ ID NO: 3161) A01.01 MQLMPFGCL (SEQ ID NO: 3162) A02.01, B07.02, B08.01 MQLMPFGCLL (SEQ ID NO: 3163) A02.01, A24.02, B08.01 VQLIMQLMPF (SEQ ID NO: 3164) A02.01, A24.02, B08.01 LIMQLMPF (SEQ ID NO: 3165) HLA-C03:02 LTSTVQLIM (SEQ ID NO: 3166) HLA-C12:03, HLA-A01:01, HLA-C15:02, HLA-B57:01, HLA-B57:03, HLA-A36:01, HLA-C12:02, HLA-C03:03, HLA- B58:02, QLIMQLMPF (SEQ ID NO: 3167) HLA-A26:01 STVQLIMQL (SEQ ID NO: 3168) HLA-A68:02, HLA-C15:02, HLA-A25:01, HLA-B57:03, HLA-C12:02, HLA-A26:01, HLA-C12:03, HLA-C06:02, HLA- C03:03, HLA-A30:01, HLA-C02:02, HLA-A11:01, HLA-A32:01, HLA-A02:04, HLA-A68:01, HLA-B15:09, HLA-C03: 04, HLA-B38:01, HLA-B57:01, HLA-A02:03, HLA-C08:01, HLA-B35:01, HLA-B40:01 STVQLIMQLM (SEQ ID NO: 3169) HLA-B57:01 TSTVQLIMQL (SEQ ID NO: 3170) HLA-C15:02 TVQLIMQL (SEQ ID NO: 3171) HLA-C17:01, HLA-B08:01, HLA-B42:01, HLA-B14:02, HLA-B37:01, HLA-B15:09 TVQLIMQLM (SEQ ID NO: 3172) HLA-B35:03 VQLIMQLM (SEQ ID NO: 3173) HLA-B52:01, HLA-B14:02, HLA-B37:01

Table 42B

EGFR mutation Sequence Mutation Context Peptides HLA allele EGFRvIII (internal deletion) MRPSGTAGAALLALLAALCPASRALEEKK: G :NYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKD (SEQ ID NO: 3174) ALEEKKGNYV (SEQ ID NO: 3176) A02.01 EGFR:SEPT14 LPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQ:: LQDKFEHLKMIQQEEIRKLEEEKKQLEGEIIDFYKMKAASEALQTQLSTD (SEQ ID NO: 3175) IQLQDKFEHL (SEQ ID NO: 3177) A02.01, B08.01 QLQDKFEHL (SEQ ID NO: 3178) A02.01, B08.01 QLQDKFEHLK (SEQ ID NO: 3179) A03.01 YLVIQLQDKF (SEQ ID NO: 3180) A02.01, A24.02

In some embodiments, the first and second neo-epitopes are different epitopes. In some embodiments, the second neo-epitope is longer than the first neo-epitope. In some embodiments, the first neoepitope is at least 8 amino acids in length. In some embodiments, the first neoepitope is 8 to 12 amino acids in length. In some embodiments, the first neoepitope comprises a sequence of at least 8 contiguous amino acids, wherein at least 1 of the 8 contiguous amino acids differs at appropriate positions from the wild type sequence. In some embodiments, the first neoepitope comprises a sequence of at least 8 contiguous amino acids, wherein at least 2 of the 8 contiguous amino acids differ at appropriate positions from the wild type sequence. In some embodiments, the second neoepitope is at least 16 amino acids in length. In some embodiments, the second neoepitope is 16 to 25 amino acids in length. In some embodiments, the second neo-epitope comprises a sequence of at least 16 contiguous amino acids, wherein at least 1 of the 16 contiguous amino acids differs at appropriate positions from the wild-type sequence. In some embodiments, the second neoepitope comprises a sequence of at least 16 contiguous amino acids, wherein at least 2 of the 16 contiguous amino acids differ at appropriate positions from the wild type sequence.

In some embodiments, the neoepitope contains at least one anchor residue. In some embodiments, the first neoepitope, the second neoepitope, or both contains at least one anchor residue. In one embodiment, the at least one anchor residue of the first neoepitope is in a canonical anchor position or a non-canonical anchor position. In another embodiment, the at least one anchor residue of the second neoepitope is in a canonical anchor position or a non-canonical anchor position. In yet another embodiment, the at least one anchor residue of the first neoepitope is different from the at least one anchor residue of the second neoepitope.

In some embodiments, the at least one anchor residue is a wild-type residue. In some embodiments, the at least one anchor residue is a substitution. In some embodiments, the at least one anchor residue does not contain a mutation.

In some embodiments, the first or second neo-epitope, or both, comprise at least one flanking region of an anchor residue. In some embodiments, the neoepitope contains at least one anchor residue. In some embodiments, the at least one anchor residue comprises at least two anchor residues. In some embodiments, the at least two anchor residues are separated by a separation region containing at least 1 amino acid. In some embodiments, the at least one flanking region of the anchor residue is not within the separation region. In some embodiments, the at least one flanking region of the anchor residue is (a) upstream of the N-terminus of the anchor residue of at least two anchor residues; (b) below the C-terminus of an anchor residue of at least two anchor residues; or both (a) and (b). In some embodiments, the second neopeptide is selected from Table 34.

In some embodiments, the second neo-epitope contains the T790M mutation. In some embodiments, the second neo-epitope containing the EGFR T790M mutation contains the sequence VQLI M QLMPF (SEQ ID NO: 3181). In some embodiments, the second neo-epitope containing the EGFR T790M mutation contains the sequence STVQLI M QLM (SEQ ID NO: 3182). In some embodiments, the second neo-epitope containing the EGFR T790M mutation contains the sequence QLI M QLMPF (SEQ ID NO: 3183). In some embodiments, the second neo-epitope containing the EGFR T790M mutation contains the sequence M QLMPFGCLL (SEQ ID NO: 3184). In some embodiments, the second neo-epitope containing the EGFR T790M mutation contains the sequence LI M QLMPF (SEQ ID NO: 3185). In some embodiments, the second neo-epitope containing the EGFR T790M mutation contains the neo-epitope sequence LTSTVQLI M (SEQ ID NO: 3186). In some embodiments, the second neopeptide containing the EGFR T790M mutation contains the sequence STVQLI M QL (SEQ ID NO: 3187). In some embodiments, the second neo-epitope containing the EGFR T790M mutation contains the sequence TSTVQLI M QL (SEQ ID NO: 3188). In some embodiments, the second neo-epitope containing the EGFR T790M mutation contains the sequence TVQLI M QL (SEQ ID NO: 3189). In some embodiments, the second neo-epitope containing the EGFR T790M mutation contains the sequence TVQLI M QLM (SEQ ID NO: 3190). In some embodiments, the second neo-epitope containing the EGFR T790M mutation contains the sequence VQLI M QLM (SEQ ID NO: 3191). In some embodiments, the second neo-epitope containing the EGFR T790M mutation contains the sequence CLTSTVQLI M (SEQ ID NO: 3192). In some embodiments, the second neo-epitope containing the EGFR T790M mutation contains the sequence I M QLMPFGC (SEQ ID NO: 3193). In some embodiments, the second neoepitope containing the EGFR T790M mutation contains the sequence I M QLMPFGC (SEQ ID NO: 3194). In some embodiments, the second neo-epitope containing the EGFR T790M mutation contains the sequence I M QLMPFGCL (SEQ ID NO: 3195). In some embodiments, the second neo-epitope containing the EGFR T790M mutation contains the neo-epitope sequence LI M QLMPFG (SEQ ID NO: 3196). In some embodiments, the second neo-epitope containing the EGFR T790M mutation contains the sequence LI M QLMPFGC (SEQ ID NO: 3197). In some embodiments, the second neo-epitope containing the EGFR T790M mutation contains the sequence QLI M QLMPFG (SEQ ID NO: 3198).

In some embodiments, the second neo-epitope comprises the EGFR S492R mutation. In some embodiments, the peptide containing the EGFR S492R mutation contains the neo-epitope sequence II R NRGENSCK (SEQ ID NO: 3199).

In some embodiments, the second EGFR neoepitope comprises a deletion mutation in EGFR, such as a G deletion in EGFRvIII (internal deletion), wherein the neoepitope sequence is NYV ALEEKK G (SEQ ID NO: 3200).

In some embodiments, the second neo-epitope contains the mutation depicted in the sequence: LPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQ:: LQDKFEHLKMIQQEEIRKLEEEKKQLEGEIIDFYKMKAASEALQTQLSTD (SEQ ID NO: 3201), where the neo-epitope sequence is IQ LQDKFEHL (SEQ ID NO: 3202) . In some embodiments, the second neo-epitope sequence is Q LQDKFEHL (SEQ ID NO: 3203). In some embodiments, the second neo-epitope sequence is Q LQDKFEHLK (SEQ ID NO: 3204). In some embodiments, the second neo-epitope sequence is YLVIQ LQDKF (SEQ ID NO: 3205) .

In some embodiments, the second neopeptide is selected from Table 35 or Table 3A to Table 3D .

In some embodiments, neoepitopes bind an HLA protein ( eg , HLA class I or HLA class II). In some embodiments, neoepitopes bind HLA protein with greater affinity than the corresponding wild-type peptide. In some embodiments, the neoepitope has an IC ₅₀ of less than 5000 nM, less than 1000 nM, less than 500 nM, less than 100 nM, less than 50 nM, or less.

In some embodiments, the neoepitope may have an HLA binding affinity of from about 1 pM to about 1 mM, from about 100 pM to about 500 μM, from about 500 pM to about 10 μM, from about 1 nM to about 1 μM , or up to about 10 nM and up to about 1 µM. In some embodiments, the neoepitope may have an HLA binding affinity of at least 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55 , 60, 65, 70, 75, 80, 85, 90, 95, 100, 150, 200, 250, 300, 350, 400, 450, 500, 550, 600, 700, 800, 900 or 1000 nM or more. In some embodiments, the neoepitope may have an HLA binding affinity of at most 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60 , 65, 70, 75, 80, 85, 90, 95, 100, 150, 200, 250, 300, 350, 400, 450, 500, 550, 600, 700, 800, 900 or 1000 nM.

In some embodiments, the first and/or second neo-epitope binds to an HLA protein with greater affinity than the corresponding wild-type neo-epitope. In some embodiments, the first and/or second neo-epitope binds to an HLA protein with a K _D or IC ₅₀ of less than 1000 nM, 900 nM, 800 nM, 700 nM, 600 nM, 500 nM, 250 nM, 150 nM, 100 nM, 50 nM, 25 nM or 10 nM. In some embodiments, the first and/or second neo-epitope binds to an HLA class I protein with a K _D or IC _{50 of} less than 1000 nM, 900 nM, 800 nM, 700 nM, 600 nM, 500 nM, 250 nM, 150 nM, 100 nM, 50 nM, 25 nM or 10 nM. In some embodiments, the first and/or second neo-epitope binds to an HLA class II protein with a K _D or IC _{50 of} less than 2000 nM, 1500 nM, 1000 nM, 900 nM, 800 nM, 700 nM, 600 nM, 500 nM, 250 nM, 150 nM, 100 nM, 50 nM, 25 nM or 10 nM.

In one aspect, the first and/or second neo-epitope binds to a protein encoded by an HLA allele expressed by the subject. In another aspect, the mutation is not present in non-cancerous cells of the subject. In yet another aspect, the first and/or second neo-epitope is encoded by a gene or expressed gene of the subject's cancer cells.

In some embodiments, the first neo-epitope contains the mutation shown in column 2 of table 1 or 2 . In some embodiments, the second neo-epitope contains the mutation shown in column 2 of table 1 or 2 . In some embodiments, certain antigenic peptides are paired with certain alleles.

The substitution can be located at any position along this length of the neoepitope. For example, it may be located in the N-terminal third of the peptide, the central third of the peptide, or the C-terminal third of the peptide. In another embodiment, the substituted residue is located 2-5 residues from the N-terminus or 2-5 residues from the C-terminus. Peptides can similarly be derived from tumor-specific insertion mutations, where the peptide contains one or more or all of the inserted residues.

In some embodiments, the peptide described in the present invention can be readily synthesized chemically using reagents that do not contain bacterial or animal contaminants (Merrifield RB: Solid phase peptide synthesis. I. synthesis of tetrapeptide. J. Am. Chem. Soc.85:2149-54, 1963). In some embodiments, peptides are produced by (1) parallel solid-phase synthesis of multichannel tools using uniform synthesis and digestion conditions; (2) purification on a RP-HPLC column with a desorption column; and repeated washing, but not substitution, between peptides; followed by (3) analysis with a limited set of the most informative analyses. The GMP footprint may be defined around a peptide series for an individual patient, thereby requiring series change techniques only between peptide synthesis for different patients.

Polynucleotides

Alternatively, a nucleic acid ( eg , polynucleotide) encoding a peptide as described herein can be used to produce a neoantigenic peptide in vitro . The polynucleotide may be, for example , DNA, cDNA, PNA, CNA, RNA, single- and/or double-stranded, or native or stabilized forms of polynucleotides, such as polynucleotides with a phosphorothiate backbone, or combinations, and may or may not contain introns as long as they code for a peptide. In some embodiments , in vitro translation is used to produce the peptide.

The present invention relates to neoantigenic polynucleotides encoding each neoantigenic peptide described herein. The term “polynucleotide”, “nucleotides” or “nucleic acid” is used interchangeably with “mutant polynucleotide”, “mutant nucleotide”, “mutant nucleic acid”, “neoantigenic polynucleotide”, “neoantigenic nucleotide” or “neoantigenic mutant nucleic acid” herein description. Different nucleic acid sequences can code for the same peptide due to redundancy in the genetic code. Each of these nucleic acids falls within the scope of the present description. The nucleic acids encoding the peptides may be DNA or RNA, such as mRNA, or a combination of DNA and RNA. In some embodiments, the nucleic acid sequence encoding the peptide is a self-amplifying mRNA (Brito et al., Adv. Genet. 2015; 89:179-233). Any suitable polynucleotide that encodes a peptide described in the present invention falls within the scope of the present description.

The term “RNA” includes, and in some embodiments, refers to “mRNA.” The term “mRNA” stands for “messenger RNA” and refers to a “transcript” that is created using a DNA template and encodes a peptide or polypeptide. Typically, mRNA contains a 5'UTR, a protein coding region, and a 3'UTR. mRNA has only a limited half-life in cells and in vitro . In some embodiments, the mRNA is a self-amplifying mRNA. As used herein, mRNA can be constructed by in vitro transcription from a DNA template. In vitro transcription techniques are known to those skilled in the art. For example, there are many commercially available in vitro transcription kits.

The stability and efficiency of RNA translation can be modified as required. For example, the RNA may be stabilized and its translation enhanced by one or more modifications that have a stabilizing effect and/or increase the translation efficiency of the RNA. Such modifications are described, for example, in PCT/EP2006/009448, incorporated herein by reference. To increase the expression of the RNA used according to this description, it can be modified in the coding region, i.e. the sequence encoding the expressed peptide or protein, without changing the sequence of the expressed peptide or protein, so as to increase the GC content to improve the stability of the mRNA and to perform codon optimization and therefore improve translation in cells.

The term “modification” in the context of RNA as used herein includes any modification of RNA that is not naturally present in said RNA. In some embodiments, the RNA does not have uncapped 5'-triphosphates. Removal of such uncapped 5'-triphosphates can be achieved by treatment with RNA phosphatase. In other embodiments, the RNA may have modified ribonucleotides to increase its stability and/or reduce cytotoxicity. In some embodiments, 5-methylcytidine may be partially or completely substituted in the RNA, such as cytidine. Alternatively, pseudouridine is partially or completely substituted, for example, uridine.

In some embodiments, the term “modification” refers to producing RNA with a 5' cap or 5' cap analog. The term “5' cap” refers to the cap structure found at the 5' end of an mRNA molecule and typically consists of a guanosine nucleotide linked to the mRNA through an unusual 5' to 5' triphosphate bond. In some embodiments, the guanosine is methylated at position 7. The term “conventional 5' cap” refers to the naturally occurring 5' cap of RNA, the 7-methylguanosine cap (mG). As used herein, the term “5' cap” includes a 5' cap analogue that is similar to the structure of an RNA cap and is modified to impart the ability to stabilize RNA and/or improve translation of RNA attached thereto in vivo and/or in a cell.

In some embodiments, mRNA encoding a neoantigenic peptide as described herein is administered to a subject in need thereof. In some embodiments, the present disclosure relates to RNA, oligoribonucleotide, and polyribonucleotide molecules containing the modified nucleoside, gene therapy vectors containing them, gene therapy methods, and methods for turning off the transcription of genes containing them. In some embodiments, the administered mRNA contains at least one modified nucleoside.

Polynucleotides encoding the peptides described in the present invention can be synthesized by chemical methods, for example, by the phosphotriester method from Matteucci, et al., J. Am. Chem. Soc. 103:3185 (1981). Polynucleotides encoding peptides containing or constituting an analogue can be obtained simply by substituting suitable and desired nucleic acid bases for those encoding the native epitope.

The polynucleotides described in the present invention may contain one or more synthetic or naturally occurring introns in the transcribed region. Incorporation of mRNA stabilization sequences and sequences for replication in mammalian cells may also be considered to enhance polynucleotide expression. In addition, the polynucleotide described in the present invention may contain immunostimulatory sequences (ISS or CpG). These sequences may be included in the vector outside of the polynucleotide encoding the sequence to improve immunogenicity.

In some embodiments, the polynucleotides may contain a coding sequence for a peptide or protein fused in frame to a polynucleotide that assists, for example, in the expression and/or secretion of the peptide or protein from a host cell ( e.g. , a leader sequence , which acts as a secretory sequence to regulate the transport of the polypeptide out of the cell). A polypeptide having a leader sequence is a pre-protein and may have the leader sequence cleaved by a host cell to form the mature form of the polypeptide.

In some embodiments, the polynucleotides may contain a coding sequence for a peptide or protein fused in frame to a marker sequence that allows, for example, purification of the encoded peptide, which can then be inserted into a personalized disease vaccine or immunogenic composition . For example, the marker sequence may be a hexahistidine tag (SEQ ID NO: 3206) supplied by the pQE-9 vector to effect purification of the mature polypeptide condensed with the marker in the case of a bacterial host, or the marker sequence may be a hemagglutinin (HA) tag derived from the hemagglutinin protein influenza in a mammalian host ( eg COS-7 cells). Additional tags include, but are not limited to, calmodulin tags, FLAG tags, Myc tags, S tags, SBP tags, Softag 1, Softag 3, V5 tag, Xpress tag, Isopeptag, SpyTag, biotin carboxyl carrier protein (BCCP) tags, GST tags, fluorescent protein tags ( eg green fluorescent protein tags), maltose binding protein tags, Nus tags, Strep tag, thioredoxin tag, TC tag, Ty tag, and the like.

In some embodiments, the polynucleotides may contain a coding sequence for one or more peptides or proteins described herein fused in the same reading frame to create a single concatamerized neoantigenic peptide construct capable of producing multiple neoantigenic peptides.

In some embodiments, the DNA sequence is constructed using recombinant technology through the isolation or synthesis of a DNA sequence encoding a wild-type protein of interest. Optionally, the sequence can be mutagenized by site-directed mutagenesis to produce functional analogues thereof. See, for example, Zoeller et al., Proc. Nat'l. Acad. Sci. USA 81:5662-5066 (1984) and US Patent No. 4,588,585. In another embodiment, the DNA sequence encoding the peptide or protein of interest can be constructed by chemical synthesis using an oligonucleotide synthesizer. Such oligonucleotides can be designed based on the amino acid sequence of the desired peptide and the selection of those codons that favor the host cell in which the recombinant polypeptide of interest is produced. Standard methods can be used to synthesize an isolated polynucleotide sequence encoding an isolated polypeptide of interest. For example, the complete amino acid sequence can be used to construct a gene with a possible sequence reconstructed from the polypeptide. A DNA oligomer containing the nucleotide sequence encoding the particular isolated polypeptide can then be synthesized. For example, several small oligonucleotides encoding parts of the desired polypeptide can be synthesized and then ligated. Individual oligonucleotides typically contain 5' or 3' overhangs for complementary assembly.

Once assembled ( eg , by synthesis, site-directed mutagenesis, or other means), polynucleotide sequences encoding the particular isolated polypeptide of interest are inserted into an expression vector and optionally operably linked to an expression control sequence for expression of the protein in the desired host. A suitable assembly can be confirmed by nucleotide sequencing, restriction mapping and expression of the biologically active polypeptide in a suitable host. As is well known in the art, to obtain high levels of expression of a transfected gene in a host, the gene can be operably linked to transcriptional and translational expression control sequences that are functional in the host selected for expression.

Thus, the present disclosure is also directed to vectors and expression vectors used for the production and administration of neoantigenic peptides and neoepitopes described in the present invention, and to host cells containing such vectors.

Vectors

In some embodiments, an expression vector capable of expressing a peptide or protein described in the present invention can also be obtained. Expression vectors for different cell types are well known in the art and can be selected without undue experimentation. Typically, the DNA is inserted into an expression vector, such as a plasmid, in a suitable orientation and the correct reading frame for expression. If desired, the DNA can be linked to suitable transcriptional and translational regulatory nucleotide sequences recognized by the desired host ( eg , a bacterium), although such controls are typically found in the expression vector. The vector is then introduced into the host bacterium for cloning using standard techniques (see, for example , Sambrook et al. (1989) Molecular Cloning, Laboratory Manual, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY).

A large number of vectors and host systems suitable for the production and administration of the neoantigen peptide described in the present invention are known to one skilled in the art and are commercially available. The following vectors are provided as an example. Bacterial: pQE70, pQE60, pQE-9 (Qiagen), pBS, pD10, phagescript, psiX174, pBluescript SK, pbsks, pNH8A, pNH16a, pNH18A, pNH46A (Stratagene); ptrc99a, pKK223-3, pKK233-3, pDR540, pRIT5 (Pharmacia); pCR (Invitrogen). Eukaryotic: pWLNEO, pSV2CAT, pOG44, pXT1, pSG (Stratagene) pSVK3, pBPV, pMSG, pSVL (Pharmacia); p75.6 (Valentis); pCEP (Invitrogen); pCEI (Epimmune). However, any other plasmid or vector can be used as long as it is replicable and viable in the host.

For expression of the neoantigenic peptides described in the present invention, the coding sequence must be provided with operably linked start and stop codons, promoter and terminator regions, and in some embodiments, a replication system to provide an expression vector for expression in the desired cellular host. For example, promoter sequences compatible with bacterial hosts are provided in plasmids containing convenient restriction sites for insertion of the desired coding sequences. The resulting expression vectors are transformed into suitable bacterial hosts.

Mammalian expression vectors will contain an origin of replication, a suitable promoter and enhancer, as well as any necessary ribosome binding sites, a polyadenylation site, splice donor and acceptor sites, transcriptional stop codons and 5' flanking untranscribed sequences. Such promoters can also be obtained from viral sources, such as, for example , human cytomegalovirus (CMV-IE promoter) or herpes simplex virus type-1 (HSV TK promoter). Nucleic acid sequences derived from SV40 splicing and polyadenylation sites can be used to obtain the desired non-transcribed genetic elements.

Recombinant expression vectors can be used to amplify and express DNA encoding a peptide or protein described in the present invention. Recombinant expression vectors are DNA replicable constructs that have synthetic or cDNA-derived DNA fragments encoding a peptide or bioequivalent analog linked to suitable transcriptional or translational regulatory elements derived from mammalian, microbial, viral or insect genes. A transcription unit typically contains an assembly of (1) a genetic element or elements having a regulatory role in gene expression, such as transcriptional promoters or enhancers, (2) a structural or coding sequence that is transcribed into mRNA and translated into protein, and (3) suitable transcription and translation initiation and termination sequences described in detail in the present invention. Such regulatory elements may include a transcription control operator sequence. The ability to replicate in the host, typically provided by the origin of replication, and a selection gene to enhance recognition of transformants may be additionally included. Regions of DNA are functionally related when they are functionally related to each other. For example, DNA for a signal peptide (secretory leader) is operably linked to DNA for a polypeptide if it is expressed as a precursor that participates in the secretion of the polypeptide; a promoter is operably linked to a coding sequence if it controls transcription of the sequence; or the ribosome binding site is operably linked to the coding sequence if it is located to allow translation. In general, functionally related means contiguous, and in the case of secretory leaders, means contiguous and within reading frame. Structural elements intended for use in yeast expression systems include a leader sequence allowing extracellular secretion of the translated protein by the host cell. Alternatively, if the recombinant protein is expressed without a leader or transport sequence, it may include an N-terminal methionine residue. This residue may optionally be further cleaved from the expressed recombinant protein to obtain the final product.

Typically, recombinant expression vectors will include origins of replication and selectable markers allowing transformation of the host cell, for example the E. coli ampicillin resistance gene and the S. cerevisiae TRP1 gene, and a promoter derived from the highly expressed gene to direct transcription downstream of the structural sequence. Such promoters can be derived from operons encoding glycolytic enzymes such as 3-phosphoglycerate kinase (PGK), acid phosphatase, or heat shock proteins, among others. The heterologous structural sequence is assembled in suitable phase with translation start and termination sequences, and in some embodiments, a leader sequence capable of directing secretion of the translated protein into the periplasmic space or extracellular environment. Optionally, the heterologous sequence may encode a fusion protein comprising an N-terminal identification peptide conferring desired characteristics, such as stabilization or simplified purification, of the expressed recombinant product.

The polynucleotides encoding the neoantigenic peptides described in the present invention may also contain a ubiquitination signal sequence and/or a targeting sequence, such as an endoplasmic reticulum (ER) signal sequence to facilitate movement of the resulting peptide into the endoplasmic reticulum.

In some embodiments, a neoantigenic peptide described in the present invention can also be administered and/or expressed by viral or bacterial vectors. Examples of expression vectors include attenuated viral hosts such as vaccinia or fowlpox. As an example of this approach, vaccinia virus is used as a vector for the expression of nucleotide sequences that encode the neoantigenic peptides described in the present invention. Vaccine vectors and methods used in immunization protocols are described in, for example , US Patent No. 4,722,848. Another vector is BCG (Bacillus Calmette-Guerin). BCG vectors are described in Stover et al., Nature 351:456-460 (1991).

A wide range of other vectors useful for therapeutic administration or immunization of neoantigenic polypeptides described in the present invention, for example, adeno- and adeno-associated virus vectors, retrovirus vectors, Salmonella Typhimurium vectors, detoxified anthrax toxin vectors, Sendai virus vectors, poxvirus vectors, canarypox vectors and fowlpox vectors, and the like, will be apparent to those skilled in the art from the description herein. In some embodiments, the vector is a modified vaccinia Ankara (VA) virus (eg, Bavarian Noridic (MVA-BN)).

Among the vectors that may be used in the practice of the present disclosure, integration into the host cell genome is possible using retroviral gene transfer techniques, often resulting in long-term expression of the inserted transgene. In some embodiments, the retrovirus is a lentivirus. Additionally, high transduction efficiency was observed in many different cell types and target tissues. Retrovirus tropism can be altered by the introduction of foreign envelope proteins, expanding the potential target population of target cells. Also, the retrovirus can be engineered to allow conditional expression of the inserted transgene so that only certain cell types will be infected by the lentivirus. Cell type-specific promoters can be used to target expression to specific cell types. Lentiviral vectors are retroviral vectors (and therefore both lentiviral and retroviral vectors can be used in the practice of the present disclosure). Moreover, lentiviral vectors are capable of transducing or infecting non-dividing cells and typically produce high viral titers. The choice of retroviral gene transfer system may therefore depend on the target tissue. Retroviral vectors consist of cis -acting long terminal repeats with packaging capacity up to 6-10 kb. foreign sequence. A minimum of cis -acting LTRs is sufficient for replication and packaging of vectors, which are then used to integrate the desired nucleic acid into the target cell to obtain persistent expression. Commonly used retroviral vectors that may be used in the practice of the present disclosure include those based on murine leukemia virus (MuLV), gibbon leukemia virus (GaLV), simian immunodeficiency virus (SIV), human immunodeficiency virus (HIV), and combinations thereof ( see eg Buchscher et al. (1992) J Virol 66:2731-2739; Johann et al. (1992) J Virol 66:1635-1640; Sommnerfelt et al. (1990) Virol ,176:58-59; Wilson et al., (1998) J. Virol,63:2374-2378; Miller et al., (1991) J. Virol,65:2220-2224; PCT/US94/05700).

a minimal non-primate lentiviral vector, such as an equine infectious anemia virus (EIAV) lentiviral vector, may also be used in the practice of the present disclosure. Vectors may have a cytomegalovirus (CMV) promoter that drives expression of the target gene. Accordingly, the present disclosure includes among the vector(s) useful in the practice of the present disclosure: viral vectors, including retroviral vectors and lentiviral vectors.

an adenoviral vector may also be used in the practice of the present disclosure. One advantage is the ability of recombinant adenoviruses to efficiently transfer and express recombinant genes in a variety of mammalian cells and tissues in vitro and in vivo , resulting in high expression of the transferred nucleic acids. Also, the ability to productively infect resting cells expands the applicability of recombinant adenoviral vectors. In addition, high expression levels ensure that the nucleic acid products will be expressed to sufficient levels to generate an immune response (see, for example , US Pat. No. 7,029,848, incorporated herein by reference).

With respect to adenoviral vectors that may be used in the practice of the present disclosure, reference may be made to US Patent No. 6,955,808. The adenoviral vector used may be selected from the group consisting of Ad5, Ad35, Ad11, C6, and C7 vectors. The genome sequence of Adenovirus 5 (“Ad5”) has been published. (Chroboczek, J., Bieber, F., and Jacrot, B. (1992) Sequence Genome of Adenovirus Type 5 and Its Comparison with Genome of Adenovirus Type 2, Virology 186, 280-285; the contents of which are incorporated herein by reference) . Ad35 vectors are described in US Patent Nos. 6,974,695, 6,913,922 and 6,869,794. Ad11 vectors are described in US Patent No. 6,913,922. C6 adenoviral vectors are described in US Pat. Nos. 6,780,407; 6,537,594; 6,309,647; 6,265,189; 6,156,567; 6,090,393; 5,942,235 and 5,833,975. C7 vectors are described in US Patent No. 6,277,558. Adenoviral vectors that are E1 defective or deleted, E3 defective or deleted, and/or E4 defective or deleted can also be used. Certain adenoviruses having mutations in the E1 region have an improved safety margin, since E1-defective adenovirus mutants are replication-defective in non-permissive cells, or at least are severely attenuated. Adenoviruses having mutations in the E3 region may have improved immunogenicity through the cleavage mechanism by which the adenovirus suppresses MHC class I molecules. Adenoviruses with E4 mutations may have reduced immunogenicity of the adenoviral vector due to suppression of late gene expression. Such vectors may be particularly useful when booster vaccination using the same vector is desired. Adenoviral vectors that are deleted or mutated in E1, E3, E4; E1 and E3; and E1 and E4, can be used in accordance with the present description.

Moreover, “gutted” adenoviral vectors, in which all viral vectors have been removed, can also be used in accordance with the present description. Such vectors require a helper virus for their replication and require a special colony of 293 human cells expressing both E1a and Cre, a condition that does not exist in nature. Such “gutted” vectors are non-immunogenic, and therefore vectors can be inoculated multiple times for revaccination. Gutted adenoviral vectors can be used to insert heterologous inserts/genes, such as the transgenes of the present disclosure, and can even be used to deliver large numbers of heterologous inserts/genes together.

In some embodiments, delivery occurs via an adenovirus, which may be in a single booster dose. In some embodiments, the adenovirus is delivered in multiple doses. With regard to in vivo delivery, AAV has an advantage over other viral vectors due to its low toxicity and low likelihood of causing insertional mutagenesis since it does not integrate into the host genome. AAV has a packaging limit of 4.5 or 4.75 kn. Constructs over 4.5 or 4.75 kn. gives a significant reduction in virus production. There are a variety of promoters that can be used to drive the expression of nucleic acid molecules. The AAV ITR can serve as a promoter and is preferred to eliminate the need for an additional promoter element.

The following promoters can be used for widespread expression: CMV, CAG, CBh, PGK, SV40, Ferritin heavy and light chains, etc. The following promoters can be used for expression in the brain: SynapsinI for all neurons, CaMKIIalpha for excitatory neurons, GAD67 or GAD65 or VGAT for GABAergic neurons, etc. Promoters used to drive RNA synthesis may include: Pol III promoters such as U6 or H1. The use of a Pol II promoter and intronic cassettes can be used for guide RNA (gRNA) expression. With regard to the AAV vectors used in the practice of the present disclosure, mention may be made of US Patent Nos. 5658785, 7115391, 7172893, 6953690, 6936466, 6924128, 6893865, 6793926, 6537540, 6475769 and 6258595, and op. documents contained there. As for AAV, AAV can be AAV1, AAV2, AAV5 or any combination thereof. AAVs can be selected taking into account the target cells; for example , one can select AAV serotypes 1, 2, 5 or hybrid capsid AAV1, AAV2, AAV5 or any combination thereof to target the brain or neurons; and AAV4 can be selected to target cardiac tissue. AAV8 is used for delivery to the liver. In some embodiments, delivery occurs via AAV. The dose may be adjusted to balance therapeutic benefit and any side effects.

In some embodiments, a poxvirus is used in the composition described herein. These include orthopoxvirus, avipoxvirus, vaccinia, MVA, NYVAC, canaripox, ALVAC, fowlpox virus, TROVAC, etc. (See, for example , Verardiet al., Hum. Vaccin. Immunother. 2012 Jul;8(7):961-70; and Moss, Vaccine. 2013; 31(39): 4220–4222). Poxviral expression vectors were described in 1982 and quickly became widely used for vaccine development as well as research in a variety of fields. Advantages of vectors include simple construction, the ability to accommodate large amounts of foreign DNA, and high expression levels. Information regarding poxviruses that may be used in the practice of this disclosure, such as poxviruses of the subfamily Chordopoxvirinae (vertebrate poxviruses), e.g., orthopoxviruses and avipoxviruses, e.g. , vaccinia virus ( e.g. , Wyeth Strain, WR Strain ( e.g. , ATCC® VR-1354), Copenhagen Strain, NYVAC, NYVAC,1, NYVAC,2, MVA, MVA-BN), canaripoxvirus ( eg Wheatley C93 Strain, ALVAC), fowlpox virus ( eg FP9 Strain, Webster Strain, TROVAC), pigeonpox virus, pigeon pox virus, quail pox virus, raccoon pox virus, among others, their synthetic and non-naturally occurring recombinants, their uses and methods for producing and using such recombinants can be found in the scientific and patent literature.

In some embodiments, the vaccinia virus is used in a disease vaccine or immunogenic composition to express an antigen. (Rolph et al., Recombinant viruses as vaccines and immunological tools. Curr. Opin. Immunol. 9:517-524, 1997). Recombinant vaccinia virus is capable of replicating in the cytoplasm of an infected host cell and, therefore, the polypeptide of interest can induce an immune response. Moreover, poxviruses are widely used as vaccine vectors or immunogenic compositions due to their ability to target encoded antigens for MHC class I processing through direct infection of immune cells, particularly antigen presenting cells, and also due to their ability to -adjuvant.

In some embodiments, ALVAC is used as a vector in a disease vaccine or immunogenic composition. ALVAC is a canarypoxvirus that can be modified to express foreign transgenes and is used as a method of vaccination against both prokaryotic and eukaryotic antigens (Horig H, Lee DS, Conkright W, et al. Phase I clinical trial of recombinant canarypoxvirus (ALVAC) vaccine expressing human carcinoembryonic antigen and B7.1 co-stimulatory molecule. Cancer Immunol. Immunother, 2000;49:504–14; von Mehren M, Arlen P, Tsang KY, et al. Pilot study of dual gene recombinant avipox vaccine containing both carcinoembryonic antigen ( CEA) and B7.1 transgenes in patients with recurrent CEA-expressing adenocarcinomas. Clin. Cancer. Res. 2000;6:2219–28; Musey L, Ding Y, Elizaga M, et al. HIV-1 vaccination administered intramuscularly can induce both systemic and mucosal T-cell immunity in HIV-1-uninfected individuals. J. Immunol. 2003;171:1094–101; Paoletti E. Applications of pox virus vectors to vaccination: update. Proc. Natl. Acad. Sci. U S 1996;93:11349–53; US Patent No. 7,255,862). In a phase I clinical trial, ALVAC virus expressing the CEA tumor antigen showed an excellent safety profile and induced an increase in CEA-specific T cell responses in selected patients; objective clinical responses, however, were not observed (Marshall JL, Hawkins MJ, Tsang KY, et al. Phase I study in cancer patients of replication-defective avipox recombinant vaccine that expresses human carcinoembryonic antigen. J. Clin. Oncol. 1999;17: 332–7).

In some embodiments, a modified vaccinia virus Ankara (MVA) can be used as a viral vector for an antigenic vaccine or immunogenic composition. MVA is a member of the Orthopoxvirus family and was generated through approximately 570 serial passages on chicken embryo fibroblasts of the Ankara strain of vaccinia virus (CVA) (see, e.g. , Mayr, A., et al., Infection 3, 6-14, 1975). As a result of these passages, the resulting MVA virus contains 31 thousand nucleotides less genomic information compared to CVA, and is limited to the host cell (Meyer, H. et al., J. Gen. Virol. 72, 1031-1038, 1991 ). MVA is characterized by extreme attenuation, namely reduced virulence or ability to infect, but still has excellent immunogenicity. When tested in a variety of animal models, MVA has been shown to be avirulent even in immunosuppressed individuals. Moreover, MVA-BN®-HER2 is an immunotherapy candidate developed for the treatment of HER-2-positive breast cancer and is currently in clinical trials. (Mandl et al., Cancer Immunol. Immunother. Jan 2012; 61(1): 19–29). Methods for the preparation and use of recombinant MVA have been described ( for example , see US Patent Nos. 8,309,098 and 5,185,146 incorporated herein by reference in their entirety).

Suitable host cells for expression of the polypeptide include prokaryotes, yeast, eukaryotic insect or higher animal cells, under the control of suitable promoters. Prokaryotes include gram-negative or gram-positive microorganisms, such as E. coli , or bacilli. Higher eukaryotic cells include stable cell lines of mammalian origin. Cell-free translation systems can also be used. Suitable cloning and expression vectors for use with bacterial, fungal, yeast and mammalian host cells are well known in the art (see Pouwels et al., Cloning Vectors: Laboratory Manual, Elsevier, NY, 1985).

Various mammalian or insect cell culture systems are also advantageously used for recombinant protein expression. Expression of recombinant proteins in mammalian cells can be accomplished since such proteins are typically correctly folded, suitably modified, and fully functional. Examples of suitable mammalian host cell colonies include COS-7 monkey kidney cell colonies described by Gluzman (Cell 23:175, 1981), and other cell colonies capable of expressing a suitable vector, including, for example, L cells, C127, 3T3 cells Chinese hamster ovary (CHO), 293, HeLa and BHK cell colonies. Mammalian expression vectors contain non-transcribed elements, such as an origin of replication, a suitable promoter and enhancer associated with the gene to be expressed, and other 5' or 3' flanking non-transcribed sequences, and 5' or 3' non-translated sequences, such as necessary ribosome binding sites, polyadenylation site, splice donor and acceptor sites, and transcription termination sequences. Baculovirus systems for producing heterologous proteins in insect cells are described in Luckow and Summer, Bio/Technology 6:47 (1988).

The host cells are genetically engineered (transduced or transformed or transfected) with vectors, which may be, for example, a cloning vector or an expression vector. The vector may, for example, be in the form of a plasmid, viral particle, phage, etc. The engineered host cells can be cultured in conventional culture media, suitably modified for promoter activation, transformant selection, or polynucleotide amplification. Culture conditions, such as temperature, pH and the like, are the same as those previously used for the host cells selected for expression and will be apparent to one skilled in the art.

Typical examples of suitable hosts may include: bacterial cells such as E. coli , Bacillus subtilis, Salmonella typhimurium and various species of the genera Pseudomonas, Streptomyces and Staphylococcus; fungal cells such as yeast; insect cells such as Drosophila and Sf9; animal cells, such as COS-7 monkey kidney fibroblast colonies described in Gluzman, Cell 23:175 (1981), and other cell colonies capable of expressing a compatible vector, such as C127, 3T3, CHO, HeLa and BHK cell colonies or melanomas Bowes; plant cells, etc. The selection of a suitable host is considered to be within the competence of one skilled in the art based on the ideas set forth herein.

Yeast, insect or mammalian host cells can also be used using suitable vectors and regulatory sequences. Examples of mammalian expression systems include monkey kidney fibroblast COS-7 colonies described in Gluzman, Cell 23:175 (1981), and other cell colonies capable of expressing a compatible vector, such as C127, 3T3, CHO, HeLa and BHK cell colonies.

The polynucleotides described in the present invention can be introduced into and expressed in human cells ( eg , immune cells, including dendritic cells). The Human Codon Usage Chart can be used as a guide to select a codon for each amino acid. Such polynucleotides contain a spacer amino acid residue between epitopes and/or analogs such as those described above, or may contain naturally occurring flanking sequences adjacent to the epitopes and/or analogs (and/or CTL ( eg CD8 ⁺ ), Th ( eg CD4 ⁺ ) and B-cell epitopes).

Standard regulatory sequences well known to those skilled in the art can be included in the vector to promote expression in human target cells. Several vector elements are desirable: a promoter with an underlying cloning site for a polynucleotide, such as a minigene insert; polyadenylation signal for efficient transcription termination; E. coli origin of replication; and a selectable marker for E. coli ( eg, ampicillin or kanamycin resistance). A variety of promoters can be used for this purpose, for example the human cytomegalovirus (hCMV) promoter. See, for example , US Patent Nos. 5,580,859 and 5,589,466 for other suitable promoter sequences. In some embodiments, the promoter is a CMV-IE promoter.

Useful expression vectors for eukaryotic hosts, especially mammals or humans, include, for example, vectors containing expression control sequences from SV40, bovine papillomavirus, adenovirus and cytomegalovirus. Useful expression vectors for bacterial hosts include known bacterial plasmids, such as those from Escherichia coli, including pCR1, pBR322, pMB9 and derivatives thereof, wider host range plasmids such as M13 and ssDNA phages.

Vectors can be introduced into animal tissue in a variety of different ways. The two most popular approaches include injection of DNA in saline using a standard hypodermal needle, or gene gun delivery. A schematic representation of the vaccine DNA plasmid construction and its subsequent delivery to the host by these two routes is illustrated in Scientific American (Weiner et al., (1999) Scientific American 281 (1): 34–41). Saline injection is usually given intramuscularly (IM) into skeletal muscle, or intradermal (IC) where DNA is delivered into extracellular spaces. This may be facilitated by electroporation through temporary damage to muscle fibers by myotoxins such as bupivacaine; or using hypertonic saline or sucrose solutions (Alarcon et al., (1999). Adv. Parasitol. Advances in Parasitology 42: 343–410). Immune responses to this delivery method can be influenced by many factors, including needle type, needle location, speed of injection, volume of injection, type of muscle, and the age, condition and physiological state of the animal being injected (Alarcon et al., (1999). Adv) Parasitol Advances in Parasitology 42: 343–410).

Gene gun delivery, another widely used delivery method, ballistically enhances plasmid DNA (pDNA) that is adsorbed onto gold or tungsten microparticles in target cells using pressurized helium as an enhancer (Alarcon et al., (1999). Adv. Parasitol Advances in Parasitology 42: 343–410 Lewis et al., (1999) Advances in Virus Research (Academic Press) 54: 129–88.

Alternative delivery methods may include aerosol instillation of naked DNA onto mucosal surfaces such as the nasal and pulmonary mucosa (Lewis et al., (1999). Advances in Virus Research (Academic Press) 54: 129–88) and topical administration of pDNA to the eye and to the vaginal mucosa (Lewis et al., (1999) Advances in Virus Research (Academic Press) 54: 129–88). Mucosal delivery has also been achieved using cationic liposome-DNA formulations, biodegradable microspheres, attenuated Shigella or Listeria vectors for oral administration to the intestinal mucosa, and recombinant adenoviral vectors. DNA or RNA can also be delivered into cells after mild mechanical disruption of the cell membrane, temporarily permeabilizing the cells. This mild mechanical disruption of the membrane can be accomplished by gently pushing cells through small holes (Sharei et al., Ex Vivo Cytosolic Delivery of Functional Macromolecules to Immune Cells, PLOS ONE (2015)).

Chemical means of introducing a polynucleotide into a host cell include colloidal dispersion systems such as macromolecular complexes, nanoparticles, spheres and lipid-based systems, including oil-in-water emulsions, micelles, mixed micelles and liposomes. A typical colloidal system for use as a delivery vehicle in vitro and in vivo is a liposome ( eg , an artificial membrane vesicle). When using a non-viral delivery system, a typical delivery vehicle is a liposome. “Liposome” is a general term covering a variety of single- and multilayer lipid carriers formed through the creation of closed fat bilayers or aggregates. Liposomes can be characterized as having vesicular structures with a phospholipid bilayer membrane and an internal aqueous environment. A multilayer liposome has multiple fat layers separated by an aqueous medium. They form spontaneously when phospholipids are suspended in excess aqueous solution. The fatty components undergo self-rearrangement to form closed structures and trap water and solutes between the fatty bilayers (Ghosh et al., Glycobiology 5: 505-10 (1991)). However, compositions that have structures in solution other than the normal bubble structure are also covered. For example, fats can take on a micellar structure or simply exist as heterogeneous aggregates of fat molecules. Lipofectamine-nucleic acid complexes are also considered.

The use of lipid formulations is being considered for the introduction of nucleic acids into host cells ( in vitro , ex vivo or in vivo ). In another aspect, the nucleic acid may be associated with fat. The fat-bound nucleic acid can be encapsulated in the aqueous interior of the liposome, dispersed in the fat bilayer of the liposome, attached to the liposome through a linking molecule that is associated with both the liposome and the oligonucleotide, entrapped in the liposome, complexed with the liposome, dispersed in solution containing fat, mixed with fat, combined with fat, suspended in fat, contained in or complexed with a micelle, or otherwise associated with fat. Compositions associated with fat, fat/DNA or fat/expression vector are not limited to any particular structure in solution. For example, they can be present in a two-layer structure, in the form of micelles and with a “destroyed” structure. They may also be simply dispersed in solution, possibly forming aggregates that are not uniform in size or shape. Fats are fatty substances that may exist in nature or synthetic fats. For example, fats include fatty droplets that naturally exist in the cytoplasm, as well as a class of compounds that contains long-chain aliphatic hydrocarbons and their derivatives such as fatty acids, alcohols, amines, amino alcohols, and aldehydes.

Fats suitable for use can be obtained from commercial sources. For example, dimyristylphosphatidylcholine (“DMPC”) can be obtained from Sigma, St. Louis, Mo.; Dicetyl phosphate (“DCP”) can be obtained from K & K Laboratories (Plainview, N.Y.); cholesterol (“Choi”) can be obtained from Calbiochem-Behring; Dimyristylphosphatidylglycerol (“DMPG”) and other fats can be obtained from Avanti Polar Lipids, Inc. (Birmingham, Ala.). Fat stock solutions in chloroform or chloroform/methanol can be stored at approximately -20°C. Chloroform is used as the only solvent because it evaporates more easily than methanol.

In some embodiments, the vector contains a polynucleotide encoding a first peptide containing a first neoepitope and a second peptide containing a second neoepitope. In some embodiments, the first and second peptides are derived from the same protein. The at least two individual peptides may vary in length, amino acid sequence, or both. Peptides are derived from any protein that is known or has been found to contain a tumor-specific mutation. In some embodiments, the vector contains a first peptide containing a first neoepitope of a protein, and a second peptide containing a second neoepitope of the same protein, wherein the first peptide is different from the second peptide, and wherein the first neoepitope contains a mutation and the second neoepitope contains the same mutation. In some embodiments, the vector contains a first peptide containing a first neo-epitope of a first region of a protein, and a second peptide containing a second neo-epitope of a second region of the same protein, wherein the first region contains at least one amino acid of the second region, wherein the first peptide is different from the second peptide, and where the first neo-epitope contains the first mutation and the second neo-epitope contains the second mutation. In some embodiments, the first mutation and the second mutation are the same. In some embodiments, the mutation is selected from the group consisting of a point mutation, a splice site mutation, a frameshift mutation, a read-through mutation, a gene fusion mutation, and any combination thereof.

In some embodiments, the vector contains a polynucleotide operably linked to a promoter. In some embodiments, the vector is a self-amplifying RNA replicon, plasmid, phage, transposon, cosmid, virus, or virion. In some embodiments, the vector is derived from a retrovirus, lentivirus, adenovirus, adeno-associated virus, herpesvirus, poxvirus, alphavirus, vaccinia virus, hepatitis B virus, human papillomavirus, or a pseudotype thereof. In some embodiments, the vector is a non-viral vector. In some embodiments, the non-viral vector is a nanoparticle, cationic fat, cationic polymer, metal nanopolymer, nonrod, liposome, micelle, microbubble, cell entry peptide, or liposphere.

T cell receptors

In one aspect, the present disclosure relates to cells expressing a neoantigen recognition receptor that activates an immunoresponsive cell ( e.g. , T cell receptor (TCR) or chimeric antigen receptor (CAR)), and methods of using such cells to treat a disease that requires improved immune response. Such cells include genetically modified immunoreactive cells ( eg T cells, natural killer (NK) cells, cytotoxic T lymphocytes (CTL ( eg CD8 ⁺ )), helper T lymphocytes (Th ( eg CD4 ⁺ ))) expressing antigen- recognition receptor ( eg , TCR or CAR) that binds one of the neoantigen peptides described in the present invention, and methods of using them for the treatment of neoplasms and other pathologies in which enhancement of an antigen-specific immune response is desired. T cell activation is mediated by a TCR or CAR targeting an antigen.

The present disclosure relates to cells expressing a combination of an antigen recognition receptor that activates an immunoresponsive cell ( eg , TCR, CAR) and a chimeric costimulatory receptor (CCR), and methods of using such cells to treat a disease that requires an enhanced immune response. In some embodiments, tumor antigen-specific T cells, NK cells, CTL cells, or other immunoreactive cells are used as shuttles to selectively enrich one or more costimulatory ligands for the treatment or prevention of neoplasms. Such cells are administered to a person in need to treat or prevent a specific cancer.

In some embodiments, human tumor antigen-specific lymphocytes that can be used in the methods herein include, but are not limited to, peripheral donor lymphocytes genetically modified to express chimeric antigen receptors (CARs) (Sadelain, M., et al. 2003 Nat Rev Cancer 3:35-45), peripheral donor lymphocytes genetically modified to express a full-length tumor antigen-recognizing T-cell receptor complex containing an a and p heterodimer (Morgan, RA, et al. 2006 Science 314:126-129) , lymphocyte cultures derived from tumor infiltrating lymphocytes (TILs) in tumor biopsies (Panell, MC, et al. 2000 J Immunol 164:495-504; Panelli, MC, et al. 2000 J Immunol 164:4382-4392) and selectively in vitro -expanded antigen-specific peripheral blood leukocytes using artificial antigen-presenting cells (AAPC) or activated dendritic cells (Dupont, J., et al. 2005 Cancer Res 65:5417-5427; Papanicolaou, G. A., et al. 2003 Blood 102:2498-2505). T cells can be autologous, allogeneic, or derived in vitro from an engineered precursor or stem cells.

In some embodiments, the immunotherapeutic agent is an engineered receptor. In some embodiments, the engineered receptor is a chimeric antigen receptor (CAR), T cell receptor (TCR), or B cell receptor (BCR), adoptive T cell therapy (ACT), or a derivative thereof. In other aspects, the engineered receptor is a chimeric antigen receptor (CAR). In some aspects, the CAR is a first generation CAR. In other aspects, the CAR is a second generation CAR. In additional other aspects, the CAR is a third generation CAR. In some aspects, the CAR comprises an extracellular portion, a transmembrane portion, and an intracellular portion. In some aspects, the intracellular portion comprises at least one T cell costimulatory domain. In some aspects, the T cell costimulatory domain is selected from the group consisting of CD27, CD28, TNFRS9 (4-1BB), TNFRSF4 (OX40), TNFRSF8 (CD30), CD40LG (CD40L), ICOS, ITGB2 (LFA-1), CD2, CD7, KLRC2 (NKG2C), TNFRS18 (GITR), TNFRSF14 (HVEM) or any combination thereof.

In some aspects, the engineered receptor binds a target. In some aspects, the binding is specific to a peptide specific to one or more subjects suffering from a disease or condition.

In some aspects, the immunotherapeutic agent is a cell, as described in detail herein. In some aspects, the immunotherapeutic agent is a cell containing a receptor that specifically binds a peptide or neo-epitope described in the present invention. In some aspects, the immunotherapeutic agent is a cell used in combination with the peptides/nucleic acids of the present disclosure. In some embodiments, the cell is a patient cell. In some embodiments, the cell is a T cell. In some embodiments, the cell is a lymphocyte infiltrating the cell.

In some aspects, a subject with a condition or disease is treated based on the subject's T cell receptor repertoire. In some embodiments, the peptide or neoepitope is selected based on the T cell receptor repertoire of the subject. In some embodiments, the subject is treated with T cells expressing a TCR specific for a peptide or neo-epitope described in the present invention. In some embodiments, the subject is treated with a TCR-specific peptide or neo-epitope, e.g. , subject-specific TCR. In some embodiments, the subject is treated with a peptide or neoepitope specific to T cells expressing a TCR, e.g. , subject-specific TCRs. In some embodiments, the subject is treated with a peptide or neoepitope specific to subject-specific TCRs.

In some embodiments, the compositions described in the present invention are selected based on TCRs identified in one or more subjects. In some embodiments, identification of the T cell repertoire and testing in functional assays is used to determine a composition for administration to one or more subjects with a condition or disease. In some embodiments, the composition is an antigen vaccine containing one or more peptides or proteins as described in the present invention. In some embodiments, the vaccine contains subject-specific neoantigen peptides. In some embodiments, the peptides included in the vaccine are selected based on quantification of subject-specific TCRs that bind to neo-epitopes. In some embodiments, peptides are selected based on the binding affinity of the peptide to the TCR. In some embodiments, the selection is based on a combination of both amount and binding affinity. For example, a TCR that binds strongly to a neoepitope in a functional assay, but that is not highly abundant in the TCR repertoire, may be a good candidate for an antigen vaccine, since T cells expressing the TCR will be preferentially amplified.

In some embodiments, the peptide or protein is selected for administration to one or more subjects based on binding to the TCR. In some embodiments, T cells, such as T cells from a subject with a disease or condition, can be expanded. Expanded T cells that express a TCR specific for the neoantigen peptide or neoepitope can be reintroduced to the subject. In some embodiments, suitable cells, e.g. , PBMC, are transduced or transfected with polynucleotides to express a TCR specific for a neoantigen peptide or neoepitope and administered to a subject. T cells expressing a TCR specific for the neoantigen peptide or neoepitope can be expanded and reintroduced to the subject. In some embodiments, T cells expressing a TCR specific for a neoantigen peptide or neoepitope that induces cytolytic activity when incubated with autologous disease tissues can be expanded and administered to a subject. In some embodiments, T cells used in functional assays resulting in binding to a neoantigen peptide or neoepitope can be expanded and administered to a subject. In some embodiments, TCRs that are determined to bind to specific neoantigenic peptides or neoepitopes of a subject can be expressed in T cells and administered to the subject.

In an embodiment, the present disclosure relates to a composition comprising a first peptide containing a first neo-epitope and a second peptide containing a second neo-epitope, wherein the first peptide is different from the second peptide, and where the first neo-epitope contains a mutation and the second neo-epitope contains the same mutation. In some embodiments, the composition provided herein comprises a first T cell comprising a first T cell receptor (TCR) specific for a first neoepitope and a second T cell comprising a second TCR specific for a second neoepitope. In some embodiments, the first and second peptides are derived from the same protein.

In another embodiment, the present disclosure relates to a composition comprising a first peptide containing a first neo-epitope of a first region of a protein, and a second peptide containing a second neo-epitope of a second region of the same protein, wherein the first region contains at least one amino acid of the second region wherein the first peptide different from the second peptide, and wherein the first neoepitope contains the first mutation and the second neoepitope contains the second mutation. In some embodiments, the composition provided herein comprises a first T cell comprising a first T cell receptor (TCR) specific for a first neo-epitope and a second T cell comprising a second TCR specific for a second neo-epitope. In some embodiments, the first mutation and the second mutation are the same.

In some embodiments, the first neoepitope binds to an HLA class I protein to form an HLA-class I peptide complex. In some embodiments, the first neo-epitope binds to an HLA class II protein to form an HLA-class II peptide complex. In some embodiments, the second neo-epitope binds to an HLA class II protein to form an HLA-class II peptide complex. In some embodiments, the second neoepitope binds to an HLA class I protein to form an HLA-class I peptide complex. In some embodiments, the first neoepitope activates CD8 ⁺ T cells. In some embodiments, the first neoepitope activates CD4 ⁺ T cells. In some embodiments, the second neo-epitope activates CD4 ⁺ T cells. In some embodiments, the second neo-epitope activates CD8 ⁺ T cells. In some embodiments, the TCR of the CD4 ⁺ T cell binds to the HLA-class II peptide complex. In some embodiments, the CD8 ⁺ T cell TCR binds to the HLA class II peptide complex. In some embodiments, the TCR of the CD8 ⁺ T cell is bound by the HLA-class I peptide complex. In some embodiments, the TCR of CD4 ⁺ T cells is bound by the HLA-class I peptide complex.

In some embodiments, the first TCR is a first chimeric antigen receptor specific for a first neoepitope, and the second TCR is a second chimeric antigen receptor specific for a second neoepitope. In some embodiments, the first T cell is a cytotoxic T cell. In some embodiments, the first T cell is a gamma delta T cell. In some embodiments, the second T cell is a helper T cell. In some embodiments, the first and/or second TCR binds to the HLA-peptide complex with a K _D or IC ₅₀ of less than 1000 nM, 900 nM, 800 nM, 700 nM, 600 nM, 500 nM, 250 nM, 150 nM, 100 nM, 50 nM, 25 nM or 10 nM. In some embodiments, the first and/or second TCR binds to the HLA class I-peptide complex with a K _D or IC _{50 of} less than 1000 nM, 900 nM, 800 nM, 700 nM, 600 nM, 500 nM, 250 nM, 150 nM , 100 nM, 50 nM, 25 nM or 10 nM. In some embodiments, the first and/or second TCR binds to an HLA class II-peptide complex with a K _D or IC ₅₀ of less than 2000, 1500, 1000 nM, 900 nM, 800 nM, 700 nM, 600 nM, 500 nM, 250 nM, 150 nM, 100 nM, 50 nM, 25 nM or 10 nM.

Antigen presenting cells

The neoantigenic peptide or protein may be present in the form of antigen presenting cells ( eg , dendritic cells) containing such peptides, proteins or polynucleotides as described in the present invention. In other embodiments, such antigen presenting cells are used to stimulate T cells for use in patients. Thus, one embodiment of the present disclosure is a composition comprising at least one antigen presenting cell ( eg , a dendritic cell) that is activated or loaded with one or more neoantigen peptides or polynucleotides described in the present invention. In some embodiments, such APCs are autologous ( eg , autologous dendritic cells). Alternatively, peripheral blood mononuclear cells (PBMCs) isolated from a patient can be loaded with neoantigenic peptides or polynucleotides ex vivo . In related embodiments, such APCs or PBMCs are injected back into the patient. In some embodiments, the antigen presenting cells are dendritic cells. In related embodiments, dendritic cells are autologous dendritic cells that are activated by a neoantigenic peptide or nucleic acid. The neoantigenic peptide can be any suitable peptide that induces a suitable T cell response. T cell therapy using autologous dendritic cells activated with peptides from tumor-associated antigen is described by Murphy et al. (1996) Prostate 29, 371-380 and Tjua et al. (1997) Prostate 32, 272-278. In some embodiments, the T cell is a CTL ( eg , CD8 ⁺ ). In some embodiments, the T cell is a helper T lymphocyte (Th ( eg , CD4 ⁺ )).

In some embodiments, the present disclosure relates to a composition comprising an immunogenic cell-based pharmaceutical composition that may also be administered to a subject. For example, an antigen presenting cell (APC) immunogenic pharmaceutical composition can be formulated using any well known methods, carriers and excipients, as appropriate and understood in the art. APCs include monocytes, monocyte-derived cells, macrophages, and dendritic cells. Sometimes, the APC-based immunogenic pharmaceutical composition may be a dendritic cell-based immunogenic pharmaceutical composition.

The dendritic cell-based immunogenic pharmaceutical composition can be prepared by any methods known in the art. In some cases, dendritic cell-based immunogenic pharmaceutical compositions can be prepared by an ex vivo or in vivo method. An ex vivo method may include the use of autologous DCs activated ex vivo with polypeptides described in the present invention to activate or load DCs prior to administration to a patient. An in vivo method may involve targeting specific DC receptors using antibodies coupled to the polypeptides described in the present invention. The DC-based immunogenic pharmaceutical composition may further contain DC activators such as TLR3, TLR-7-8 and CD40 agonists. The DC-based immunogenic pharmaceutical composition may further contain adjuvants and a pharmaceutically acceptable carrier.

Antigen presenting cells (APCs) can be obtained from a variety of sources, including humans and non-human primates, other mammals and vertebrates. In some embodiments, APCs may be derived from the blood of a human or non-human vertebrate. APCs can also be isolated from an enriched leukocyte population. Leukocyte populations can be obtained by methods known to those skilled in the art. Such methods typically include heparinized blood collection, apheresis or leukapheresis, buffy coat preparation, rosette formation, centrifugation, density gradient centrifugation ( eg , Ficoll, colloidal silica particles, and sucrose), differential lysis of non-leukocyte cells, and filtration. The leukocyte population can also be obtained by collecting blood from the subject, defibrillating to remove platelets, and lysing red blood cells. The leukocyte population may not necessarily be enriched in monocytic dendritic cell precursors.

The blood cell populations can be obtained from a variety of subjects, according to the desired use of the enriched leukocyte population. The subject may be a healthy subject. Alternatively, the blood cells may be obtained from a subject in need of immunostimulation, such as, for example, a cancer patient or other patient who would benefit from immunostimulation. Also, blood cells can be obtained from a subject in need of immune suppression, such as, for example, a patient having an autoimmune disorder ( eg , rheumatoid arthritis, diabetes, lupus, multiple sclerosis, and the like). The leukocyte population can also be obtained from an HLA-matched healthy individual.

When blood is used as a source of APC, blood leukocytes can be obtained using conventional methods that maintain their viability. According to one aspect of the present disclosure, the blood may be diluted in a medium that may or may not contain heparin or other suitable anticoagulant. The volume of blood to medium can be approximately 1 to 1. Cells can be concentrated by centrifuging blood in medium at approximately 1000 rpm. (150 g) at 4°C. Platelets and red blood cells can be depleted by resuspending the cells in any number of solutions known in the art that will lyse red blood cells, such as ammonium chloride. For example, the mixture may be medium and ammonium chloride in a ratio of approximately 1:1 by volume. The cells can be concentrated by centrifugation and washed in the desired solution to obtain a leukocyte population substantially free of platelets and red blood cells. Any isotonic solution commonly used in tissue culture can be used as a medium to separate white blood cells from platelets and red blood cells. Examples of such isotonic solutions include phosphate buffered saline, Hank's balanced salt solution, and complete growth medium. APC and/or precursors can also be purified by elutriation.

In one embodiment, the APCs may be non-nominal APCs under inflammatory or otherwise activated conditions. For example, non-nominal APCs may include epithelial cells stimulated by interferon-gamma, T cells, B cells and/or monocytes activated by factors or conditions that induce APC activity. Such non-nominal APCs can be prepared by methods known in the art.

The APCs can be cultured, propagated, differentiated and/or matured, if desired, according to the APC type. APCs can be cultured in any suitable culture vessel, such as, for example, culture plates, flasks, culture bags and bioreactors.

In some embodiments, APCs may be cultured in a suitable culture or growth medium to maintain and/or increase the amount of APCs in the formulation. The culture medium can be selected according to the type of APC isolated. For example, mature APCs, such as mature dendritic cells, can be cultured in a growth medium suitable for their preservation and propagation. Amino acids, vitamins, antibiotics, divalent cations and the like can be added to the culture medium. In addition, cytokines, growth factors and/or hormones may be included in the growth medium. For example, cytokines such as granulocyte/macrophage colony-stimulating factor (GM-CSF) and/or interleukin 4 (IL-4) may be added to maintain and/or propagate mature dendritic cells. In other embodiments, immature APCs can be cultured and/or propagated. Immature dendritic cells may retain the ability to take up target mRNA and process new antigen. In some embodiments, immature dendritic cells can be cultured in a medium suitable for their preservation and culture. Amino acids, vitamins, antibiotics, divalent cations and the like can be added to the culture medium. In addition, cytokines, growth factors and/or hormones may be included in the growth medium.

Other immature APCs can also be cultured or propagated. Preparations of immature APCs can be left to mature to produce mature APCs. APC maturation can occur during or after treatment with neoantigenic peptides. In some embodiments, immature dendritic cell preparations may be allowed to mature. Suitable maturation factors include, for example, the cytokines TNF-α, bacterial products ( eg BCG) and the like. In another aspect, isolated APC precursors can be used to prepare immature APC preparations. APC precursors can be cultured, differentiated and/or allowed to mature. In some embodiments, monocytic dendritic cell precursors can be cultured in the presence of a suitable culture medium supplemented with amino acids, vitamins, cytokines, and/or divalent cations to promote differentiation of the monocytic dendritic cell precursors into immature dendritic cells. In some embodiments, APC precursors are isolated from PBMC. PBMCs can be obtained from a donor, such as a human donor, and can be used fresh or frozen for future use. In some embodiments, APC is derived from one or more APC preparations. In some embodiments, the APC comprises an APC loaded with first and second neoantigenic peptides containing the first and second neoepitopes, or polynucleotides encoding first and second neoantigenic peptides containing the first and second neoepitopes. In some embodiments, the APC is autologous APC, allogeneic APC, or artificial APC.

In an embodiment, the present disclosure relates to a composition comprising an APC comprising a first peptide containing a first neoepitope and a second peptide containing a second neoepitope, wherein the first peptide is different from the second peptide, and wherein the first neoepitope contains a mutation and the second neoepitope contains the same mutation . In some embodiments, the first and second peptides are derived from the same protein. In another embodiment, the present disclosure relates to a composition comprising an APC comprising a first peptide containing a first neo-epitope of a first region of a protein, and a second peptide containing a second neo-epitope of a second region of the same protein, wherein the first region contains at least one amino acid of the second region, where the first peptide is different from the second peptide, and where the first neoepitope contains a first mutation and the second neoepitope contains a second mutation. In some embodiments, the first mutation and the second mutation are the same.

Adjuvants

An adjuvant can be used to improve the immune response (humoral and/or cellular) induced in a patient receiving the composition provided herein. Sometimes adjuvants can induce a Th1-type response. At other times, adjuvants may induce a Th2-type response. A Th1-type response can be characterized by the production of cytokines such as IFN-γ, as opposed to a Th2-type response, which can be characterized by the production of cytokines such as IL-4, IL-5 and IL-10.

In some aspects, fat-based adjuvants, such as MPLA and MDP, can be used with the immunogenic pharmaceutical compositions described in the present invention. Monophosphoryl lipid (MPLA), for example, is an adjuvant that causes increased presentation of liposomal antigen to specific T lymphocytes. In addition, muramyl dipeptide (MDP) can also be used as a suitable adjuvant in combination with the immunogenic pharmaceutical compositions described in the present invention.

Suitable adjuvants are known in the art (see, WO 2015/095811) and include, but are not limited to, poly(I:C), poly-ICLC, Hiotonol, STING agonist, 1018 ISS, aluminum salts, Amplivax, AS15, BCG, CP-870,893, CpG7909, CyaA, dSLIM, GM-CSF, IC30, IC31, Imiquimod, ImuFact IMP321, IS Patch, ISS, ISCOMATRIX, JuvImmune, LipoVac, MF59, monophosphoryl lipid A, Montanide IMS 1312, Montanide ISA 206 , Montanid ISA 50V, Montanid ISA-51, OK-432, OM-174, OM-197-MP-EC, ONTAK, PepTel®, vector systems, PLG microparticles, resiquimod, SRL172, virosomes and other virus-like particles, YF-17D , VEGF trap, R848, beta-glucan, Pam3Cys, Pam3CSK4, Aquila's QS21 stimone (Aquila Biotech, Worcester, Mass., USA), which is derived from saponin, mycobacterial extracts and synthetic bacterial cell wall mimetics, and other suitable adjuvants such as Ribi's Detox, Quil or Superfos. Adjuvants also include Freund's incomplete adjuvant or GM-CSF. Several immunological adjuvants ( eg MF59) specific to dendritic cells and their preparation have been described previously (Dupuis M, et al., Cell Immunol. 1998; 186(1):18-27; Allison C; Dev. Biol. Stand . 1998; 92:3-11) (Mosca et al. Frontiers in Bioscience, 2007; 12:4050-4060) (Gamvrellis et al. Immunol & Cell Biol. 2004; 82: 506-516). Cytokines may also be used. Several cytokines have been directly linked to influence the migration of dendritic cells into lymphoid tissues ( eg TNF-alpha), enhancing the maturation of dendritic cells into effective antigen presenting cells for T lymphocytes ( eg GM-CSF, PGE1, PGE2, IL-1, IL -1b, IL-4, IL-6 and CD40L) (US Patent No. 5,849,589, incorporated herein by reference in its entirety) and acting as immunoadjuvants ( eg , IL-12) (Gabrilovich DI, et al., J. Immunother. Emphasis Tumor Immunol 1996(6):414-418).

The adjuvant may also contain stimulating molecules such as cytokines. Non-limiting examples of cytokines include: CCL20, interferon a (IFN-a), interferon beta (IFN-β), interferon γ, platelet-derived growth factor (PDGF), TNFα, TNFβ (lymphotoxin alpha (LTα)), GM- CSF, epidermal growth factor (EGF), cutaneous T cell recruiting chemokine (CTACK), thymus expressed epithelial chemokine (TECK), mucosal associated epithelial chemokine (MEC), IL-12, IL-15, IL-28 , MHC, CD80, CD86, IL-1, IL-2, IL-4, IL-5, IL-6, IL-10, IL-18, MCP-1, MIP-la, MIP-1-, IL- 8, L-selectin, P-selectin, E-selectin, CD34, GlyCAM-1, MadCAM-1, LFA-1, VLA-1, Mac-1, pl50.95, PECAM, ICAM-1, ICAM-2, ICAM-3, CD2, LFA-3, M-CSF, G-CSF, mutant forms of IL-18, CD40, CD40L, vascular growth factor, fibroblast growth factor, IL-7, nerve growth factor, vascular endothelial growth factor, Fas , TNF receptor, Fit, Apo-1, p55, WSL-1, DR3, TRAMP, Apo-3, AIR, LARD, NGRF, DR4, DRS, KILLER, TRAIL-R2, TRICK2, DR6, Caspase ICE, Fos, c -jun, Sp-1, Ap-1, Ap-2, p38, p65Rel, MyD88, IRAK, TRAF6, IκB, inactive NIK, SAP K, SAP-I, JNK, interferon response genes, NFκB, Bax, TRAIL, TRAILrec , TRAILrecDRC5, TRAIL-R3, TRAIL-R4, RANK, RANK LIGAND, Ox40, Ox40 LIGAND, NKG2D, MICA, MICB, NKG2A, NKG2B, NKG2C, NKG2E, NKG2F, TAPI, and TAP2.

Additional adjuvants include: MCP-1, MIP-la, MIP-lp, IL-8, RANTES, L-selectin, P-selectin, E-selectin, CD34, GlyCAM-1, MadCAM-1, LFA-1, VLA- 1, Mac-1, pl50.95, PECAM, ICAM-1, ICAM-2, ICAM-3, CD2, LFA-3, M-CSF, G-CSF, IL-4, mutant forms of IL-18, CD40, CD40L, vascular growth factor, fibroblast growth factor, IL-7, IL-22, nerve growth factor, vascular endothelial growth factor, Fas, TNF receptor, Fit, Apo-1, p55, WSL-1, DR3, TRAMP, Apo- 3, AIR, LARD, NGRF, DR4, DR5, KILLER, TRAIL-R2, TRICK2, DR6, Caspase ICE, Fos, c-jun, Sp-1, Ap-1, Ap-2, p38, p65Rel, MyD88, IRAK , TRAF6, IκB, inactive NIK, SAP K, SAP-1, JNK, interferon response genes, NFκB, Bax, TRAIL, TRAILrec, TRAILrecDRC5, TRAIL-R3, TRAIL-R4, RANK, RANK LIGAND, Ox40, Ox40 LIGAND, NKG2D , MICA, MICB, NKG2A, NKG2B, NKG2C, NKG2E, NKG2F, TAP1, TAP2 and their functional fragments.

In some aspects, the adjuvant may be a toll-like receptor modulator. Examples of toll-like receptor modulators include TLR-9 agonists and are not limited to small molecule toll-like receptor modulators such as imiquimod. Other examples of adjuvants that are used in combination with the immunogenic pharmaceutical compositions described in the present invention may include, but are not limited to, saponin, CpG ODN and the like. Sometimes the adjuvant is selected from bacterial toxoids, polyoxypropylene-polyoxyethylene block polymer, aluminum salts, liposomes, CpG polymer, oil-in-water emulsions, or a combination thereof. Sometimes the adjuvant is an oil-in-water emulsion. The oil-in-water emulsion may include at least one oil and at least one surfactant, where the oil(s) and surfactant(s) are biodegradable (metabolizable) and biocompatible. Oil droplets in an emulsion can be less than 5 μm in diameter, and can even have a submicron diameter, where such small sizes are achieved using a microfluidizer to produce stable emulsions. Droplets smaller than 220 nm can be sterilized by filtration.

Methods of treatment and pharmaceutical compositions

Neoantigen therapeutic agents ( eg , peptides, polynucleotides, TCR, CAR, cells containing TCR or CAR, APC or dendritic cells containing polypeptide, dendritic cells containing polynucleotide, antibody, etc.) described in the present invention are used in a variety of fields, including, but not limited to, therapeutic treatments such as cancer treatment. In some embodiments, the therapeutic treatments include immunotherapy. In some embodiments, the neoantigenic peptide is used to activate, stimulate, enhance and/or enhance an immune response, redirect an existing immune response to a new target, increase tumor immunogenicity, inhibit tumor growth, reduce tumor volume, increase tumor cell apoptosis and/or reduce tumorigenicity tumors. Methods of application may be in vitro , ex vivo or in vivo methods.

In some aspects, the present description relates to methods of activating an immune response in a subject using a neoantigen peptide or protein described in the present invention. In some embodiments, the present disclosure relates to methods of stimulating an immune response in a subject using a neoantigen peptide described in the present invention. In some embodiments, the present disclosure relates to methods of enhancing an immune response in a subject using a neoantigen peptide described herein. In some embodiments, the present disclosure relates to methods of enhancing an immune response using a neoantigen peptide. In some embodiments, activating, stimulating, enhancing and/or improving the immune response includes enhancing cell-mediated immunity. In some embodiments, activating, stimulating, enhancing and/or improving the immune response includes increasing T cell activity or humoral immunity. In some embodiments, activating, stimulating, enhancing and/or improving the immune response includes increasing CTL or Th activity. In some embodiments, activating, stimulating, enhancing and/or improving the immune response includes increasing NK cell activity. In some embodiments, activating, stimulating, enhancing and/or improving the immune response includes increasing T cell activity and increasing NK cell activity. In some embodiments, activating, stimulating, enhancing and/or improving the immune response includes increasing CTL activity and increasing NK cell activity. In some embodiments, activating, stimulating, enhancing, and/or improving the immune response involves inhibiting or reducing the suppressive activity of T regulatory (Treg) cells. In some embodiments, the immune response is the result of antigenic stimulation. In some embodiments, the antigen stimulation is a tumor cell. In some embodiments, the antigen stimulation is cancer.

In some embodiments, the present description relates to methods of activating, stimulating, enhancing and/or improving an immune response using a neoantigen peptide described in the present invention. In some embodiments, the method includes administering to a subject in need thereof a therapeutically effective amount of a neoantigenic peptide that delivers the neoantigenic peptide or polynucleotide to a tumor cell. In some embodiments, the method comprises administering to a subject in need thereof a therapeutically effective amount of a neoantigenic peptide taken up by a tumor cell. In some embodiments, the method comprises administering to a subject in need thereof a therapeutically effective amount of a neoantigenic peptide that is taken up by a tumor cell, and the neoantigenic peptide is processed by the cell. In some embodiments, the method comprises administering to a subject in need thereof a therapeutically effective amount of a neoantigenic polypeptide that is taken up by a tumor cell and the neoepitope is present on the surface of the tumor cell. In some embodiments, the method comprises administering to a subject in need thereof a therapeutically effective amount of a neoantigenic polypeptide that is taken up by a tumor cell, processed by the cell, and the antigenic peptide is present on the surface of the tumor cell.

In some embodiments, the method comprises administering to a subject in need thereof a therapeutically effective amount of a neoantigenic peptide or polynucleotide described herein that delivers an exogenous polypeptide comprising at least one neoantigenic peptide to a tumor cell, wherein at least one a neoepitope derived from a neoantigen peptide present on the surface of the tumor cell. In some embodiments, the antigenic peptide is present on the surface of the tumor cell in complex with an MHC class I molecule. In some embodiments, the neoepitope is present on the surface of the tumor cell in complex with an MHC class II molecule.

In some embodiments, the method includes contacting a tumor cell with a neoantigenic polypeptide or polynucleotide described in the present invention that delivers an exogenous polypeptide containing at least one neoantigenic peptide to the tumor cell, wherein at least one neoepitope derived from at least one at least one neoantigenic peptide is present on the surface of the tumor cell. In some embodiments, the neoepitope is present on the surface of the tumor cell in complex with an MHC class I molecule. In some embodiments, the neoepitope is present on the surface of the tumor cell in complex with an MHC class II molecule.

In some embodiments, the method comprises administering to a subject in need thereof a therapeutically effective amount of a neoantigenic polypeptide or polynucleotide described herein that delivers an exogenous polypeptide comprising at least one antigenic peptide to a tumor cell where the neoepitope is present on the surface of the tumor cell. cells and triggers an immune response against the tumor cell. In some embodiments, the immune response against the tumor cell is enhanced. In some embodiments, the neoantigenic polypeptide or polynucleotide delivers an exogenous polypeptide containing at least one neoantigenic peptide to a tumor cell, where the neoepitope is present on the surface of the tumor cell and inhibits tumor growth.

In some embodiments, the method comprises administering to a subject in need thereof a therapeutically effective amount of a neoantigenic polypeptide or polynucleotide described herein that delivers an exogenous polypeptide comprising at least one neoantigenic peptide to a tumor cell, wherein the neoepitope derived from at least one neoantigenic peptide is present on the surface of the tumor cell and causes cytolysis of the T cell directed against the tumor cell. In some embodiments, T cell cytolysis directed against a tumor cell is enhanced. In some embodiments, T cell cytolysis directed against a tumor cell is increased.

In some embodiments, a method of enhancing an immune response in a subject comprises administering to the subject a therapeutically effective amount of a neoantigen therapeutic agent described herein, wherein the agent is an antibody that specifically binds a neoantigen described herein. In some embodiments, a method of enhancing an immune response in a subject comprises administering to the subject a therapeutically effective amount of an antibody.

The present description relates to methods of redirecting an existing immune response to a tumor. In some embodiments, a method of redirecting an existing immune response to a tumor includes administering to a subject a therapeutically effective amount of a neoantigen therapeutic agent described in the present invention. In some embodiments, the existing immune response is directed against the virus. In some embodiments, the virus is selected from the group consisting of: measles virus, varicella-zoster virus (VZV; varicella zoster virus), influenza virus, mumps virus, poliovirus, rubella virus, rotavirus, hepatitis virus (HAV), hepatitis B virus (HBV), Epstein-Barr virus (EBV) and cytomegalovirus (CMV). In some embodiments, the virus is varicella-zoster virus. In some embodiments, the virus is a cytomegalovirus. In some embodiments, the virus is a measles virus. In some embodiments, the existing immune response was acquired following a natural viral infection. In some embodiments, the existing immune response was acquired following vaccination against the virus. In some embodiments, the existing immune response is a cell-mediated response. In some embodiments, the existing immune response comprises cytotoxic T cells (CTLs) or Th cells.

In some embodiments, a method of redirecting an existing immune response to a tumor includes administering a fusion protein comprising (i) an antibody that specifically binds a neoantigen, and (ii) at least one neoantigen peptide described in the present invention, wherein (a) the fusion protein taken up by a tumor cell after binding to a tumor-associated antigen or neoepitope; (b) the neoantigenic peptide is processed and presented on the surface of the tumor cell bound by an MHC class I molecule; and (c) the neoantigen peptide/MHC class I complex is recognized by the cytotoxic T cell. In some embodiments, the cytotoxic T cells are memory T cells. In some embodiments, memory T cells are the result of vaccination with a neoantigen peptide.

The present description relates to methods for increasing the immunogenicity of a tumor. In some embodiments, a method of enhancing the immunogenicity of a tumor includes contacting the tumor or tumor cells with an effective amount of a neoantigen therapeutic agent described in the present invention. In some embodiments, a method of enhancing the immunogenicity of a tumor comprises administering to a subject a therapeutically effective amount of a neoantigen therapeutic agent described herein.

The present description also relates to methods of inhibiting tumor growth using a neoantigen therapeutic agent described in the present invention. In some embodiments, a method of inhibiting tumor growth includes contacting a mixture of cells with a neoantigen therapeutic agent in vitro . For example, an immortalized cell line or a cancer cell line mixed with immune cells ( eg T cells) is cultured in a medium to which a neoantigenic peptide has been added. In some embodiments, tumor cells are isolated from a patient sample, such as a tissue biopsy, pleural effusion, or blood sample mixed with immune cells ( eg , T cells), and cultured in media to which a neoantigen therapeutic agent has been added. In some embodiments, the neoantigen therapeutic agent enhances, stimulates, and/or improves the activity of immune cells. In some embodiments, the neoantigen therapeutic agent inhibits the growth of a tumor cell. In some embodiments, the neoantigen therapeutic agent activates the killing of tumor cells.

In some embodiments, the subject is a human. In some embodiments, the subject has a tumor or the subject has a tumor that has been at least partially removed.

In some embodiments, a method of inhibiting tumor growth includes redirecting an existing immune response to a new target, comprising administering to a subject a therapeutically effective amount of a neoantigenic therapeutic agent, wherein the existing immune response is directed against an antigenic peptide delivered to the tumor cell by the neoantigenic peptide. In some embodiments, the method of treatment includes the step of identifying one or more HLA subtypes expressed in a subject prior to administration of the peptide such that the peptide binds to at least one or more HLA subtypes specifically expressed by the subject. In some embodiments, if one of several mutant BTK peptides selected from Table 34 is administered to a subject, the subject is first determined to express an HLA subtype corresponding to the peptide from Table 34 such that the administered peptide binds to at least one or more HLA subtypes , specifically expressed by the subject. In some embodiments, the method includes determining that the subject expresses a protein encoded by the HLA-C14:02 allele, HLA-C14:03 allele, HLA-A33:03 allele, HLA-C04:01 allele, HLA-B15:09 allele or the HLA-B38:02 allele, where the therapeutic agent contains a mutant BTK peptide having the amino acid sequence EYMANGSLL (SEQ ID NO: 3207). In some embodiments, if the method comprises determining that the subject expresses a protein encoded by any of the HLA-C02:02 allele, HLA-C03:02 allele, HLA-B53:01 allele, HLA-C12:02 allele, HLA-C12 :03 alleles, HLA-A36:01 alleles, HLA-A26:01 alleles, HLA-A25:01 alleles, HLA-B57:01 alleles, HLA-A03:01 alleles, HLA-B46:01 alleles, HLA-B15: 03 alleles, HLA-A33:03 alleles, HLA-B35:03 alleles, or HLA-A11:01 alleles, wherein the therapeutic agent contains a mutant BTK peptide having the amino acid sequence MANGSLLNY (SEQ ID NO: 3208). In some embodiments, the method comprises determining that the subject expresses a protein encoded by any of the HLA-A02:04 allele, HLA-A02:03 allele, HLA-C03:02 allele, HLA-A03:01 allele, HLA-A32: 01 alleles, HLA-A02:07 alleles, HLA-C14:03 alleles, HLA-C14:02 alleles, HLA-A31:01 alleles, HLA-A30:02 alleles, HLA-A74:01 alleles, HLA-C06:02 alleles, HLA-B15:03 alleles, HLA-B46:01 alleles, HLA-B13:02 alleles, HLA-A25:01 alleles, HLA-A29:02 alleles, or HLA-C01:02 alleles, where the therapeutic agent contains a mutant BTK a peptide having the amino acid sequence SLLNYLREM (SEQ ID NO: 3209).

In some embodiments, the method includes determining that the subject expresses a protein encoded by any of the HLA-B14:02 allele, HLA-B49:01 allele, HLA-B44:03 allele, HLA-B44:02 allele, HLA-B37: 01 allele, HLA-B15:09 allele, HLA-B41:01 or HLA-B50:01 allele, where the therapeutic agent contains a mutant BTK peptide having the amino acid sequence TEYMANGSL (SEQ ID NO: 3210).

In some embodiments, the tumor contains cancer stem cells. In some embodiments, the frequency of cancer stem cells in a tumor is reduced by administration of a neoantigen therapeutic agent. In some embodiments, a method of reducing the frequency of cancer stem cells in a tumor in a subject is provided, comprising administering to the subject a therapeutically effective amount of a neoantigenic therapeutic agent.

Additionally, in some aspects, the present disclosure provides a method of reducing the tumorigenicity of a tumor in a subject, comprising administering to the subject a therapeutically effective amount of a neoantigenic therapeutic agent described herein. In some embodiments, the tumor contains cancer stem cells. In some embodiments, tumor tumorigenicity is reduced by reducing the frequency of cancer stem cells in the tumor. In some embodiments, the methods include the use of a neoantigen therapeutic agent described in the present invention. In some embodiments, the frequency of cancer stem cells in a tumor is reduced by administration of a neoantigen therapeutic agent described in the present invention.

In some embodiments, the tumor is a solid tumor. In some embodiments, the tumor is a tumor selected from the group consisting of: colorectal tumor, pancreatic tumor, lung tumor, ovarian tumor, liver tumor, breast tumor, kidney tumor, prostate tumor, neuroendocrine tumor, gastrointestinal tumor tract, melanoma, cervical tumors, bladder tumors, glioblastoma and head and neck tumors. In some embodiments, the tumor is a colorectal tumor. In some embodiments, the tumor is an ovarian tumor. In some embodiments, the tumor is a breast tumor. In some embodiments, the tumor is a lung tumor. In some embodiments, the tumor is a pancreatic tumor. In some embodiments, the tumor is melanoma. In some embodiments, the tumor is a solid tumor.

The present disclosure also relates to methods of treating cancer in a subject, comprising administering to the subject a therapeutically effective amount of a neoantigen therapeutic agent described herein.

In some embodiments, a method of treating cancer includes redirecting an immune response to a new target, where the method includes administering to a subject a therapeutically effective amount of a neoantigenic therapeutic agent, where the existing immune response is directed against an antigenic peptide delivered to the cancer cell by the neoantigenic peptide.

The present disclosure relates to methods of treating cancer comprising administering to a subject a therapeutically effective amount of a neoantigen therapeutic agent described herein ( eg , a subject in need of treatment). In some embodiments, the subject is a human. In some embodiments, the subject has a cancer. In some embodiments, the subject has had the tumor at least partially removed.

Subjects may be, for example, mammals, humans, pregnant women, the elderly, adults, adolescents, young people, children, toddlers, infants, newborns, or newborns under one month of age. The subject may be a patient. In some cases, the subject may be a person. In some cases, the subject may be a child (ie, a young person before puberty). In some cases, the subject may be an infant. In some cases, the subject may be a formula-fed infant. In some cases, the subject may be an individual participant in a clinical trial. In some cases, the subject may be a laboratory animal, such as a mammal or rodent. In some cases, the subject may be a mouse. In some cases, the subject may be obese or overweight.

In some embodiments, the subject has previously been treated with one or more different cancer treatments. In some embodiments, the subject has previously been treated with one or more of radiation therapy, chemotherapy, or immunotherapy. In some embodiments, the subject has been treated with one, two, three, four, or five lines of prior therapy. In some embodiments, the prior therapy is cytotoxic therapy.

In some embodiments, the cancer is a cancer selected from the group consisting of colorectal cancer, pancreatic cancer, lung cancer, ovarian cancer, liver cancer, breast cancer, kidney cancer, prostate cancer, gastrointestinal cancer, melanoma, cervical cancer, neuroendocrine cancer, bladder cancer, glioblastoma and head and neck cancer. In some embodiments, the cancer is pancreatic cancer. In some embodiments, the cancer is ovarian cancer. In some embodiments, the cancer is colorectal cancer. In some embodiments, the cancer is breast cancer. In some embodiments, the cancer is prostate cancer. In some embodiments, the cancer is lung cancer. In some embodiments, the cancer is melanoma. In some embodiments, the cancer is a solid cancer. In some embodiments, the cancer comprises a solid tumor.

In some embodiments, the cancer is a hematologic cancer. In some embodiments, the cancer is selected from the group consisting of: acute myelogenous leukemia (AML), Hodgkin lymphoma, multiple myeloma, T-cell acute lymphoblastic leukemia (T-ALL), chronic lymphocytic leukemia (CLL), hairy cell leukemia, chronic myelogenous leukemia leukemia (CML), non-Hodgkin's lymphoma, diffuse large B-cell lymphoma (DLBCL), mantle cell lymphoma (MCL) and cutaneous T-cell lymphoma (CTCL).

In some embodiments, the neoantigen therapeutic agent is administered as a combination therapy. Combination therapy with two or more therapeutic agents uses agents that work through different mechanisms of action, although this is not required. Combination therapy using agents with different mechanisms of action may have additive or synergistic effects. Combination therapy may allow a reduction in the dose of each agent used in monotherapy, thereby reducing toxic side effects and/or increasing the therapeutic index of the agent(s). Combination therapy may reduce the chance that resistant cancer will develop. In some embodiments, the combination therapy includes a therapeutic agent that affects the immune response ( eg , improves or activates the response) and a therapeutic agent that affects ( eg , inhibits or kills) tumor/cancer cells.

In some cases, the immunogenic pharmaceutical composition may be administered with an additional agent. In some embodiments, the neoantigen therapeutic agent may be administered with immunotherapy. An immunotherapy may be, for example, an antibody directed at an immune checkpoint. In some embodiments, the antibody is a bispecific antibody. The choice of additional agent may depend, at least in part, on the condition being treated. The additional agent may include, for example, an immune checkpoint inhibitor such as an anti-PD1, anti-CTLA4, anti-PD-L1, anti-CD40, or an anti-TIM3 agent (eg, anti-PD1, anti-CTLA4, anti- PD-L1, anti-CD40 or anti-TIM3 antibody); or any agents that provide a therapeutic effect against a pathogenic infection (eg, a viral infection), including, for example, drugs used to treat an inflammatory condition, such as NSAIDs, for example, ibuprofen, naproxen, acetaminophen, ketoprofen, or aspirin. For example, the immune checkpoint inhibitor may be a PD-1/PD-L1 antagonist selected from the group consisting of: nivolumab (ONO-4538/BMS-936558, MDX1 106, OPDIVO), pembrolizumab (MK-3475, KEYTRUDA), pidilizumab (CT-011), and MPDL328OA (ROCHE). As another example, the formulations may further contain one or more additives such as vitamin C, E or other antioxidants.

The methods described can be used to treat any type of cancer known in the art. Non-limiting examples of cancer treatable by the methods of the present disclosure may include melanoma (eg, metastatic malignant melanoma), kidney cancer (eg, clear cell carcinoma), prostate cancer (eg, hormone-refractory prostate adenocarcinoma), pancreatic adenocarcinoma, cancer breast, colon cancer, lung cancer (eg, non-small cell lung cancer), esophageal cancer, squamous cell carcinoma of the head and neck, liver cancer, ovarian cancer, cervical cancer, thyroid cancer, glioblastoma, glioma, leukemia, lymphoma and other malignancies neoplasms.

Additionally, the disease or condition presented herein includes refractory or relapsed malignancies, the growth of which can be inhibited using the treatment methods of the present disclosure. In some embodiments, the cancer treated by the treatment methods of the present disclosure is selected from the group consisting of carcinoma, squamous cell carcinoma, adenocarcinoma, sarcoma, endometrial cancer, breast cancer, ovarian cancer, cervical cancer, fallopian tube cancer, primary peritoneal cancer, colon cancer, colorectal cancer, anogenital squamous cell carcinoma, melanoma, renal cell carcinoma, lung cancer, non-small cell lung cancer, squamous cell lung cancer, stomach cancer, bladder cancer, gallbladder cancer, liver cancer, thyroid cancer, laryngeal cancer , salivary gland cancer, esophageal cancer, head and neck cancer, glioblastoma, glioma, squamous cell carcinoma of the head and neck, prostate cancer, pancreatic cancer, mesothelioma, sarcoma, hematological cancer, leukemia, lymphoma, neuroma and combinations thereof. In some embodiments, cancer treatable by the methods of the present disclosure includes, for example, carcinoma, squamous cell carcinoma (e.g., cervical canal, eyelid, connective tissue, vagina, lung, oral cavity, skin, bladder, tongue, larynx, and esophagus) and adenocarcinoma (eg, prostate, small intestine, endometrium, cervical canal, colon, lung, pancreas, pharynx, rectum, uterus, stomach, breast and ovary). In some embodiments, cancers to be treated by the methods of the present disclosure further include sarcoma (eg, myogenic sarcoma), leukemia, neuroma, melanoma, and lymphoma. In some embodiments, the cancer to be treated by the methods of the present disclosure is breast cancer. In some embodiments, the cancer to be treated by the treatment methods of the present disclosure is triple negative breast cancer (TNBC). In some embodiments, the cancer to be treated by the methods of the present disclosure is ovarian cancer. In some embodiments, the cancer to be treated by the methods of the present disclosure is colorectal cancer.

In some embodiments, the patient or population of patients to be treated with the pharmaceutical composition of the present disclosure has a solid tumor. In some embodiments, the solid tumor is melanoma, renal cell carcinoma, lung cancer, bladder cancer, breast cancer, cervical cancer, colon cancer, gallbladder cancer, laryngeal cancer, liver cancer, thyroid cancer, stomach cancer , salivary gland cancer, prostate cancer, pancreatic cancer or Merkel cell carcinoma. In some embodiments, the patient or population of patients to be treated with the pharmaceutical composition of the present disclosure has hematologic cancer. In some embodiments, the patient has a hematologic cancer, such as diffuse large B cell lymphoma (“DLBCL”), Hodgkin lymphoma (“HL”), non-Hodgkin lymphoma (“NHL”), follicular lymphoma (“FL”), acute myeloid leukemia (“AML”) or multiple myeloma (“MM”). In some embodiments, the patient or population of patients to be treated has a cancer selected from the group consisting of ovarian cancer, lung cancer, and melanoma.

Specific examples of cancer that can be prevented and/or treated in accordance with the present description include, but are not limited to, the following: renal cancer, kidney cancer, glioblastoma multiforme, metastatic breast cancer; breast carcinoma; breast sarcoma; neurofibroma; neurofibromatosis; childhood tumors; neuroblastoma; malignant melanoma; epidermal carcinomas; leukemias such as, but not limited to, acute leukemia, acute lymphocytic leukemia, acute myelocytic leukemia, such as myeloblastic, promyelocytic, myelomonocytic, monocytic, erythroleukemic leukemia and myelodysplastic syndrome, chronic leukemias, such as, but not limited to, chronic myelocytic (granulocytic) leukemia, chronic lymphocytic leukemia, hairy cell leukemia; true polycythemia; lymphomas such as, but not limited to, Hodgkin's disease, non-Hodgkin's disease; multiple myelomas, such as, but not limited to, smoldering multiple myeloma, nonsecretory myeloma, osteosclerotic myeloma, plasma cell leukemia, solitary plasmacytoma and extramedullary plasmacytoma; Waldenström's macroglobulinemia; monoclonal gammopathy of undetermined significance; benign monoclonal gammopathy; heavy chain disease; bone cancer and connective tissue sarcomas such as, but not limited to, bone sarcoma, myeloma of bone disease, multiple myeloma, cholesteatoma osteosarcoma of bone, Paget's disease of bone, osteosarcoma, chondrosarcoma, Ewing's sarcoma, malignant giant cell tumor, fibrosarcoma of bone, chordoma , parosteal sarcoma, soft tissue sarcoma, angiosarcoma (hemangiosarcoma), fibrosarcoma, Kaposi's sarcoma, leiomyosarcoma, liposarcoma, lymphangiosarcoma, neuroma, rhabdomyosarcoma and synovial sarcoma; brain tumors such as, but not limited to, glioma, astrocytoma, brainstem glioma, ependymoma, oligodendroglioma, non-glial tumor, acoustic neuroma, craniopharyngioma, medulloblastoma, meningioma, pineocytoma, pineoblastoma and primary brain lymphoma; breast cancer, including, but not limited to, adenocarcinoma, lobular (small cell) carcinoma, intraductal carcinoma, medullary breast cancer, mucinous breast cancer, tubular breast cancer, papillary breast cancer, Paget's disease (including juvenile Paget's disease) and inflammatory breast cancer; adrenal cancer such as, but not limited to, pheochromocytoma and adrenocortical carcinoma; thyroid cancer, such as, but not limited to, papillary or follicular thyroid cancer, medullary thyroid cancer and anaplastic thyroid cancer; pancreatic cancer such as, but not limited to, insulinoma, gastrinoma, glucagonoma, VIPoma, somatostatin-secreting tumor and carcinoid or islet cell tumor; pituitary cancer such as, but not limited to, Cushing's disease, prolactin-secreting tumor, acromegaly and diabetes insipidus; eye cancers such as, but not limited to, ocular melanoma such as iris melanoma, choroidal melanoma, and ciliary body melanoma, and retinoblastoma; vaginal cancer such as squamous cell carcinoma, adenocarcinoma and melanoma; vulvar cancer such as squamous cell carcinoma, melanoma, adenocarcinoma, basal cell carcinoma, sarcoma and Paget's disease; cervical cancer such as, but not limited to, squamous cell carcinoma and adenocarcinoma; uterine cancer, such as, but not limited to, endometrial carcinoma and uterine sarcoma; ovarian cancer such as, but not limited to, epithelial carcinoma, borderline tumor, germ cell tumor and stromal tumor; cervical carcinoma; esophageal cancer such as, but not limited to, squamous cell carcinoma, adenocarcinoma, adenoid cystic carcinoma, mucoepidermoid carcinoma, adenosquamous carcinoma, sarcoma, melanoma, plasmacytoma, verrucous carcinoma and oat cell (small cell) carcinoma; gastric cancer such as, but not limited to, adenocarcinoma, fungiform (polypoid), ulcerative, superficial spreading, diffuse spreading, malignant lymphoma, liposarcoma, fibrosarcoma and carcinosarcoma; colon cancer; colorectal cancer, colorectal cancer with KRAS mutation; colon carcinoma; rectal cancer; liver cancer such as, but not limited to, hepatocellular carcinoma and hepatoblastoma, gallbladder cancer such as adenocarcinoma; cholangiocarcinomas such as, but not limited to, papillary, nodular and diffuse; lung cancer such as KRAS mutation non-small cell lung cancer, non-small cell lung cancer, squamous cell carcinoma (epidermoid carcinoma), adenocarcinoma, large cell carcinoma and small cell lung cancer; lung carcinoma; testicular cancer, such as, but not limited to, germinal tumors, seminoma, anaplastic, classical (typical), spermatocytic, non-seminoma, embryonal carcinoma, teratoma carcinoma, choriocarcinoma (yolk sac tumor), prostate cancer, such as but not limited to them, androgen-independent prostate cancer, androgen-dependent prostate cancer, adenocarcinoma, leiomyosarcoma and rhabdomyosarcoma; penile cancer; oral cancer, such as, but not limited to, squamous cell carcinoma; basal cancer; salivary gland cancer such as, but not limited to, adenocarcinoma, mucoepidermoid carcinoma and adenoid cystic carcinoma; pharyngeal cancer, such as, but not limited to, squamous cell carcinoma and verricose carcinoma; skin cancer such as, but not limited to, basal cell carcinoma, squamous cell carcinoma and melanoma, superficial spreading melanoma, nodular melanoma, lentigo maligna melanoma, lentiginosis of the extremities; kidney cancer, such as, but not limited to, renal cell carcinoma, adenocarcinoma, hypernephroma, fibrosarcoma, transitional cell carcinoma (renal pelvis and/or ureter); kidney carcinoma; Wilms tumor; bladder cancer, such as, but not limited to, transitional cell carcinoma, squamous cell carcinoma, adenocarcinoma, carcinosarcoma. In addition, cancers include myxosarcoma, osteogenic sarcoma, endothelial sarcoma, lymphangioendotheliosarcoma, mesothelioma, synovioma, hemangioblastoma, epithelial carcinoma, cystadenocarcinoma, bronchogenic carcinoma, sweat gland carcinoma, sebaceous gland carcinoma, papillary carcinoma and papillary adenocarcinoma.

Cancers include, but are not limited to, B cell cancers such as multiple myeloma, Waldenström's macroglobulinemia, heavy chain diseases such as alpha chain disease, gamma chain disease, mu chain disease, benign monoclonal gammopathy and immunocytic amyloidosis, melanomas, breast cancer, lung cancer, bronchial cancer, colorectal cancer, prostate cancer ( eg , metastatic, hormone-refractory prostate cancer), pancreatic cancer, stomach cancer, ovarian cancer, bladder cancer, brain cancer, or central nervous system, peripheral nervous system cancer, esophageal cancer, cervical cancer, uterine or endometrial cancer, oral or pharyngeal cancer, liver cancer, kidney cancer, testicular cancer, biliary tract cancer, small intestine or appendix cancer, salivary gland cancer, thyroid cancer, adrenal cancer, osteosarcoma, chondrosarcoma, hematological tissue cancer and the like. Other non-limiting examples of types of cancer applicable to the methods covered herein include human sarcomas and carcinomas, for example , fibrosarcoma, myxosarcoma, liposarcoma, chondrosarcoma, osteogenic sarcoma, chordoma, angiosarcoma, endothelial sarcoma, lymphangiosarcoma, lymphangioendothelial sarcoma, synovioma, mesothelioma, Ewing's tumor , leiomyosarcoma, rhabdomyosarcoma, colon carcinoma, colorectal cancer, pancreatic cancer, breast cancer, ovarian cancer, squamous cell carcinoma, basal cell carcinoma, adenocarcinoma, sweat gland carcinoma, sebaceous gland carcinoma, papillary carcinoma, papillary adenocarcinomas, cystadenocarcinoma, medullary carcinoma, bronchogenic carcinoma, renal cell carcinoma, hepatoma, bile duct carcinoma, liver cancer, choriocarcinoma, seminoma, embryonal carcinoma, Wilms tumor, cervical cancer, bone cancer, brain tumor, testicular cancer, lung carcinoma, small cell lung carcinoma, urinary carcinoma bladder, epithelial carcinoma, glioma, astrocytoma, medulloblastoma, craniopharyngioma, ependymoma, pinealoma, hemangioblastoma, acoustic schwannoma, oligodendroglioma, meningioma, melanoma, neuroblastoma, retinoblastoma; leukemias, such as acute lymphocytic leukemia and acute myelocytic leukemia (myeloblastic, promyelocytic, myelomonocytic, monocytic and erythroleukemia); chronic leukemia (chronic myelocytic (granulocytic) leukemia and chronic lymphocytic leukemia); and polycythemia vera, lymphoma (Hodgkin's disease and non-Hodgkin's disease), multiple myeloma, Waldenström's macroglobulinemia and heavy chain disease. In some embodiments, the cancer whose phenotype is determined by the method of the present disclosure is an epithelial cancer, such as, but not limited to, bladder cancer, breast cancer, cervical cancer, colon cancer, gynecological cancers, kidney cancer, laryngeal cancer , lung cancer, oral cancer, head and neck cancer, ovarian cancer, pancreatic cancer, prostate cancer or skin cancer. In other embodiments, the cancer is breast cancer, prostate cancer, lung cancer, or colon cancer. In other embodiments, the epithelial cancer is non-small cell lung cancer, non-papillary renal cell carcinoma, cervical carcinoma, ovarian carcinoma ( eg , serous ovarian carcinoma), or breast carcinoma. Epithelial cancers can be characterized by various other pathways, including, but not limited to, serous, endometrioid, mucinous, clear cell, Brenner, or undifferentiated. In some embodiments, the present disclosure is used for the treatment, diagnosis, and/or prognosis of lymphoma or subtypes thereof, including, but not limited to, mantle cell lymphoma. Lymphoproliferative disorders are also considered proliferative diseases.

In some embodiments, the combination of an agent described in the present invention and at least one additional therapeutic agent produces additive or synergistic results. In some embodiments, the combination therapy results in an increase in the therapeutic index of the agent. In some embodiments, combination therapy provides an increase in the therapeutic index of the additional therapeutic agent(s). In some embodiments, the combination therapy results in a reduction in the toxicity and/or side effects of the agent. In some embodiments, the combination therapy provides a reduction in the toxicity and/or side effects of the additional therapeutic agent(s).

In some embodiments, in addition to administering the neoantigen therapeutic agent described herein, the method or treatment further comprises administering at least one additional therapeutic agent. The additional therapeutic agent may be administered before, simultaneously, and/or after administration of the agent. In some embodiments, the at least one additional therapeutic agent comprises 1, 2, 3, or more additional therapeutic agents.

Therapeutic agents that can be administered in combination with a neoantigen therapeutic agent described in the present invention include chemotherapeutic agents. Thus, in some embodiments, the method or treatment comprises administering an agent described herein in combination with a chemotherapeutic agent, or in combination with a cocktail of chemotherapeutic agents. Treatment with the agent may occur before, simultaneously with, or after the administration of chemotherapy. Combined administration may include co-administration, either in a single pharmaceutical formulation or using separate formulations, or sequential administration in any order, but usually for such a period of time that all active agents can exert their biological effects simultaneously. Drugs and dosage regimens for such chemotherapeutic agents may be used according to the manufacturer's instructions or as determined empirically by a practitioner. Drugs and dosing regimens for such chemotherapy are also described in Chemotherapy Source Book, 4th Edition, 2008, M. C. Perry, Editor, Lippincott, Williams & Wilkins, Philadelphia, PA.

Useful classes of chemotherapeutic agents include, for example, anti-tubulin agents, auristatins, DNA minor groove binding agents, DNA replication inhibitors, alkylating agents ( eg platinum complexes such as cisplatin, mono(platinum), bis(platinum) and trinuclear platinum complexes and carboplatin), anthracyclines, antibiotics, anti-folates, antimetabolites, chemotherapeutic sensitizers, duocarmycins, etoposides, fluorinated pyrimidines, ionophores, lexitropsins, nitrosoureas, platinols, purine antimetabolites, puromycins, radiation sensitizers, steroids, taxanes, topoisomerase inhibitors, alkaloids periwinkle or similar. In some embodiments, the second therapeutic agent is an alkylating agent, an antimetabolite, an antimitotic, a topoisomerase inhibitor, or an angiogenesis inhibitor.

Chemotherapeutic agents used herein include, but are not limited to, alkylating agents such as thiotepa and cyclophosphamide (CYTOXAN); alkylsulfonates such as busulfan, improsulfan and piposulfan; aziridines such as benzodopa, carbochon, meturedopa and uredopa; ethylenimines and methylmelamines, including altretamine, triethylnemelamine, triethylene phosphoramide, triethylene thiophosphoramide and trimethylol melamine; nitrogen mustards, such as chlorambucil, chlornaphasine, holophosphamide, estramustine, ifosfamide, mechlorethamine, mechlorethamine oxide hydrochloride, melphalan, novembiquine, phenesterine, prednimustine, trofosfamide, uramustine; nitrosoureas such as carmustine, chlorzotocin, fotemustine, lomustine, nimustine, ranimustine; antibiotics such as aclacinomycin, actinomycin, outramycin, azaserin, bleomycin, cactinomycin, calicheamicin, carabicin, caminomycin, carzinophylline, chromomycin, dactinomycin, daunorubicin, detorubicin, 6-diazo-5-oxo-L-norleucine, doxorubicin, epirubicin, esorubicin, idarubicin, marcellomycin, mitomycins mycophenolic acid, nogalamycin, olivomycins, peplomycin, potfiromycin, puromycin, kelamicin, rhodorubicin, streptonigrin, streptozocin, tubercidin, ubenimex, zinostatin, zorubicin; anti-metabolites such as methotrexate and 5-fluorouracil (5-FU); folic acid analogs such as denopterin, methotrexate, pteropterin, trimetrexate; purine analogues such as fludarabine, 6-mercaptopurine, thiamiprin, thioguanine; pyrimidine analogues such as antsitabine, azacitidine, 6-azauridine, carmofur, cytosine arabinoside, dideoxyuridine, doxifluridine, enocytabine, floxuridine, 5-FU; androgens such as calusterone, dromostanolone propionate, epithiostanol, mepithiostane, testolactone; drugs that suppress adrenal function, such as aminoglutethimide, mitotane, trilostane; folic acid replenishers such as folinic acid; aceglatone; aldophosphamide glycoside; aminolevulinic acid; amsacrine; bestrabucil; bisantrene; edatraxate; defofamine; demecolcine; diaziquon; elformitine; elliptinium acetate; ethoglucide; gallium nitrate; hydroxyurea; lentinan; lonidamine; mitoguazone; mitoxantrone; mopidamole; nitracrine; pentostatin; phenomet; pirarubicin; podophyllic acid; 2-ethylhydrazide; procarbazine; PSK; razoxane; sisofuran; spirogermanium; tenuazonic acid; triaziquon; 2,2',2''-trichlorotriethylamine;urethane;vindesine;dacarbazine;mannomustin;mitobronitol;mitolactol;pipobromance;gacytosine; arabinoside (Ara-C); taxoids, such as paclitaxel (TAXOL) and docetaxel (TAXOTERE); chlorambucil; gemcitabine; 6-thioguanine; mercaptopurine; platinum analogues such as cisplatin and carboplatin; vinblastine; platinum; etoposide (VP-16); ifosfamide; mitomycin C; mitoxantrone; vincristine; vinorelbine; navelbine; Novantrone; teniposide; daunomycin; aminopterin; ibandronate; CPT11; topoisomerase inhibitor RFS 2000; difluoromethylornithine (DMFO); retinoic acid; esperamycins; capecitabine (XELODA); and pharmaceutically acceptable salts, acids or derivatives of any of the foregoing. Chemotherapeutic agents also include antihormonal agents that regulate or inhibit the action of hormones on tumors, such as antiestrogens, including, for example, tamoxifen, raloxifene, aromatase inhibitory 4(5)-imidazoles, 4-hydroxytamoxifen, trioxifene, keoxifene, LY117018, onapristone and toremifene (FARESTON); and anti-androgens such as flutamide, nilutamide, bicalutamide, leuprolide and goserelin; and pharmaceutically acceptable salts, acids or derivatives of any of the foregoing. In some embodiments, the additional therapeutic agent is cisplatin. In some embodiments, the additional therapeutic agent is carboplatin.

In some embodiments, the chemotherapeutic agent is a topoisomerase inhibitor. Topoisomerase inhibitors are chemotherapeutic agents that interfere with the action of the topoisomerase enzyme ( eg topoisomerase I or II). Topoisomerase inhibitors include, but are not limited to, doxorubicin HCl, daunorubicin citrate, mitoxantrone HCl, actinomycin D, etoposide, topotecan HCl, teniposide (VM-26) and irinotecan, as well as pharmaceutically acceptable salts, acids or derivatives of any of them. In some embodiments, the additional therapeutic agent is irinotecan.

In some embodiments, the chemotherapeutic agent is an antimetabolite. An antimetabolite is a chemical substance with a structure that is similar to a metabolite required for normal biochemical reactions, but is different enough to interfere with one or more normal cellular functions, such as cell division. Antimetabolites include, but are not limited to, gemcitabine, fluorouracil, capecitabine, methotrexate sodium, ralitrexed, pemetrexed, tegafur, cytosine arabinoside, thioguanine, 5-azacytidine, 6-mercaptopurine, azathioprine, 6-thioguanine, pentostatin, fludarabine phosphate and cladribine, as well as pharmaceutically acceptable salts, acids or derivatives of any of them. In some embodiments, the additional therapeutic agent is gemcitabine.

In some embodiments, the chemotherapeutic agent is an antimitotic agent, including, but not limited to, agents that bind tubulin. In some embodiments, the agent is a taxane. In some embodiments, the agent is paclitaxel or docetaxel, or a pharmaceutically acceptable salt, acid, or derivative of paclitaxel or docetaxel. In some embodiments, the agent is paclitaxel (TAXOL), docetaxel (TAXOTERE), albumin-bound paclitaxel (ABRAXANE), DHA-paclitaxel, or PG-paclitaxel. In certain alternative embodiments, the antimitotic agent comprises a vinca alkaloid such as vincristine, vinblastine, vinorelbine, or vindesine, or pharmaceutically acceptable salts, acids, or derivatives thereof. In some embodiments, the antimitotic agent is an Eg5 kinesin inhibitor or a mitotic kinase inhibitor such as Aurora or Plk1. In some embodiments, the additional therapeutic agent is paclitaxel. In some embodiments, the additional therapeutic agent is albumin-bound paclitaxel.

In some embodiments, the additional therapeutic agent comprises an agent, such as a small molecule. For example, treatment may involve combined administration of an agent of the present disclosure with a small molecule that acts as an inhibitor against tumor-associated antigens, including, but not limited to, EGFR, HER2 (ErbB2) and/or VEGF. In some embodiments, an agent of the present disclosure is administered in combination with a protein kinase inhibitor selected from the group consisting of: gefitinib (IRESSA), erlotinib (TARCEVA), sunitinib (SUTENT), lapatinib, vandetanib (ZACTIMA), AEE788, CI-1033, cediranib (RECENTIN), sorafenib (NEXAVAR) and pazopanib (GW786034B). In some embodiments, the additional therapeutic agent comprises an mTOR inhibitor. In another embodiment, the additional therapeutic agent is chemotherapy or other inhibitors that reduce the number of Treg cells. In some embodiments, the therapeutic agent is cyclophosphamide or an anti-CTLA4 antibody. In another embodiment, the additional therapeutic agent reduces the presence of myeloid-derived suppressor cells. In a further embodiment, the additional therapeutic agent is carbotaxol. In another embodiment, the additional therapeutic agent shifts cells toward a T helmer 1 response. In a further embodiment, the additional therapeutic agent is ibrutinib.

In some embodiments, the additional therapeutic agent comprises a biological molecule, such as an antibody. For example, treatment may include combined administration of an agent of the present disclosure with antibodies against tumor-associated antigens, including, but not limited to, antibodies that bind EGFR, HER2/ErbB2 and/or VEGF. In some embodiments, the additional therapeutic agent is an antibody specific for a cancer stem cell marker. In some embodiments, the additional therapeutic agent is an antibody that is an angiogenesis inhibitor ( eg , anti-VEGF or VEGF receptor antibody). In some embodiments, the additional therapeutic agent is bevacizumab (AVASTIN), ramucirumab, trastuzumab (HERCEPTIN), pertuzumab (OMNITARG), panitumumab (VECTIBIX), nimotuzumab, zalutumumab, or cetuximab (ERBITUX).

The agents and compositions presented herein can be used alone or in combination with conventional therapeutic regimens, such as surgery, radiation, chemotherapy and/or bone marrow transplantation (autologous, syngeneic, allogeneic or unrelated). A variety of tumor antigens may be useful, for example in a significant proportion of cancer patients.

In some embodiments, at least one or more chemotherapeutic agents may be administered in addition to a composition containing an immunogenic vaccine. In some embodiments, one or more chemotherapeutic agents may belong to different classes of chemotherapeutic agents.

Examples of chemotherapeutic agents include, but are not limited to, alkylating agents such as nitrogen mustards ( eg, mechlorethamine (nitrogen mustard), chlorambucil, cyclophosphamide (Cytoxan®), ifosfamide and melphalan); nitrosoureas ( eg N-nitroso-N-methylurea, streptozocin, carmustine (BCNU), lomustine and semustine); alkylsulfonates ( eg busulfan); tetrazines ( eg dacarbazine (DTIC), mitozolomide and temozolomide (Temodar®)); aziridines ( eg thiotepa, mitomycin and diaziquone); and platinum-based drugs ( eg, cisplatin, carboplatin and oxaliplatin); non-classical alkylating agents such as procarbazine and altretamine (hexamethylmelamine); anti-metabolites such as 5-fluorouracil (5-FU), 6-mercaptopurine (6-MP), capecitabine (Xeloda®), cladribine, clofarabine, cytarabine (Ara-C®), decitabine, floxuridine, fludarabine, nelarabine, gemcitabine (Gemzar®), hydroxyurea, methotrexate, pemetrexed (Alimta®), pentostatin, thioguanine, Vidaza; tubulin polymerization inhibitors such as vinca alkaloids ( eg vincristine, vinblastine, vinorelbine, vindesine and vinflunine); taxanes ( eg paclitaxel (Taxol®), docetaxel (Taxotere®)); podophyllotoxin ( eg etoposide and teniposide); epothilones ( eg ixabepilone (Ixempra®)); estramustine (Emcyt®); antitumor antibiotics such as anthracyclines ( eg, daunorubicin, doxorubicin (Adriamycin®, epirubicin, idarubicin); actinomycin-D; and bleomycin; topoisomerase I inhibitors such as topotecan and irinotecan (CPT-11); topoisomerase II inhibitors such as etoposide (VP-16), teniposide, mitoxantrone, novobiocin, merbarone and aclarubicin; corticosteroids such as prednisone, methylprednisolone (Solumedrol®) and dexamethasone (Decadron®); L-asparaginase; bortezomib (Velcade®); immunotherapy agents such as rituximab (Rituxan®), alemtuzumab (Campath®), thalidomide, lenalidomide (Revlimid®), BCG, interleukin-2, interferon-alpha and cancer vaccines such as Provenge®; hormonal therapeutic agents such as fulvestrant (Faslodex®), tamoxifen , toremifene (Fareston®), anastrozole (Arimidex®), exemestane (Aromasin®), letrozole (Femara®), megestrol acetate (Megace®), estrogens, bicalutamide (Casodex®), flutamide (Eulexin®), nilutamide (Nilandron® ), leuprolide (Lupron®), and goserelin (Zoladex®); differentiating agents such as retinoids, tretinoin (ATRA or Atralin®), bexarotene (Targretin®) and arsenic oxide (Arsenox®); and targeted therapeutic agents such as imatinib (Gleevec®), gefitinib (Iressa®) and sunitinib (Sutent®). In some embodiments, the chemotherapy is a cocktail therapy. Examples of cocktail therapy include, but are not limited to, CHOP/R-CHOP (Rituxan, cyclophosphamide, hydroxydoxorubicin, vincristine, and prednisone), EPOCH (etoposide, prednisone, vincristine, cyclophosphamide, hydroxydoxorubicin), Hyper-CVAD (cyclophosphamide, vincristine, hydroxydoxorubicin, dexamethasone), FOLFOX (fluorouracil (5-FU), leucovorin, oxaliplatin), ICE (ifosfamide, carboplatin, etoposide), DHAP (high dose cytarabine [ara-C], dexamethasone, cisplatin), ESHAP (etoposide, methylprednisolone, cytarabine [ ara-C], cisplatin) and CMF (cyclophosphamide, methotrexate, fluorouracil).

In some embodiments, the immunogenic vaccine may be used in combination with a phosphoinositide 3-kinase (PI3 kinase, PI3K) inhibitor. For example, an immunogenic vaccine can be used in combination with Wortmannin, Demethoxyviridin, LY294002, Hibiscon C, Idelalisib, Copanlisib, Duvelisib, Tazelisib, Perifosine, Buparlisib, Duvelisib, Alpelisib (BYL719), Umbralisib, (TGR 1202), Copanlisib (BAY 80-694 6 ), PX-866, Dactolisib, CUDC-907, Voxtalisib (SAR245409, XL765), CUDC-907, ME-401, IPI-549, SF1126, RP6530, INK1117, pictilisib (GDC-0941), XL147 (SAR245408), Palomidom 529, GSK1059615, ZSTK474, PWT33597, IC87114, TG100–115, CAL263, RP6503, PI-103, GNE-477, AEZS-136 or any combination thereof.

In some embodiments, the dose of the Pi3 inhibitor of the Pi3 of Kinase, for example, vortmannin, demetoxiviridine, LY294002, hibisco C, Idalalisib, Kopanlisib, Duvelisib, Pilisib, Perifosin, Barlisib, Duvelisib, Alpelisib (BYL719), Umbralsib, (TGR 1202), BAA (BA Y 80-6946), PX-866, Dactolisiba, CUDC-907, Voxtalisib (SAR245409, XL765), CUDC-907, ME-401, IPI-549, SF1126, RP6530, INK1117, pictilisib (GDC-0941), XL147 (SAR245408 ), Palomide 529, GSK1059615, ZSTK474, PWT33597, IC87114, TG100–115, CAL263, RP6503, PI-103, GNE-477 or AEZS-136 used for human treatment may range from approximately 0.01 mg/kg to about 100 mg/kg per day (for example, from about 0.1 mg/kg to about 100 mg/kg per day, from about 0.1 mg/kg to about 50 mg/kg per day, from about 10 mg/kg kg per day or up to approximately 30 mg/kg per day). The desired dose may conveniently be administered in a single dose or in multiple doses at suitable intervals, for example in two, three, four or more sub-doses per day.

In some embodiments, the dose of the Pi3 inhibitor of the Pi3 of Kinase, for example, vortmannin, demetoxiviridine, LY294002, hibisco C, Idalalisib, Kopanlisib, Duvelisib, Pilisib, Perifosin, Barlisib, Duvelisib, Alpelisib (BYL719), Umbralsib, (TGR 1202), BAA (BA Y 80-6946), PX-866, Dactolisiba, CUDC-907, Voxtalisib (SAR245409, XL765), CUDC-907, ME-401, IPI-549, SF1126, RP6530, INK1117, pictilisib (GDC-0941), XL147 (SAR245408 ), Palomide 529, GSK1059615, ZSTK474, PWT33597, IC87114, TG100–115, CAL263, RP6503, PI-103, GNE-477 or AEZS-136 can be from about 1 ng/kg to about 100 mg/kg. Dose of a PI3 kinase inhibitor, e.g. Wortmannin, Demethoxyviridine, LY294002, Hibiscon C, Idelalisib, Copanlisib, Duvelisib, Tazelisib, Perifosine, Buparlisib, Duvelisib, Alpelisib (BYL719), Umbralisib, (TGR 1202), Copanlisib (BAY 80-6 946), PX-866, Dactolisiba, CUDC-907, Voxtalisib (SAR245409, XL765), CUDC-907, ME-401, IPI-549, SF1126, RP6530, INK1117, pictilisib (GDC-0941), XL147 (SAR245408), Palomida 529, GSK1059615, ZSTK474, PWT33597, IC87114, TG100-115, CAL263, RP6503, PI-103, GNE-477 or AEZS-136 may be any dose, including, but not limited to, approximately 1 mcg/kg, 25 mcg/kg, 50 mcg/kg, 75 mcg/kg, 100 mcg/kg, 125 mcg/kg, 150 mcg/kg, 175 mcg/kg, 200 mcg/kg, 225 mcg/kg, 250 mcg/kg, 275 mcg/kg , 300 mcg/kg, 325 mcg/kg, 350 mcg/kg, 375 mcg/kg, 400 mcg/kg, 425 mcg/kg, 450 mcg/kg, 475 mcg/kg, 500 mcg/kg, 525 mcg/kg , 550 mcg/kg, 575 mcg/kg, 600 mcg/kg, 625 mcg/kg, 650 mcg/kg, 675 mcg/kg, 700 mcg/kg, 725 mcg/kg, 750 mcg/kg, 775 mcg/kg , 800 mcg/kg, 825 mcg/kg, 850 mcg/kg, 875 mcg/kg, 900 mcg/kg, 925 mcg/kg, 950 mcg/kg, 975 mcg/kg, 1 mg/kg, 2.5 mg /kg, 5 mg/kg, 10 mg/kg, 15 mg/kg, 20 mg/kg, 25 mg/kg, 30 mg/kg, 35 mg/kg, 40 mg/kg, 45 mg/kg, 50 mg /kg, 60 mg/kg, 70 mg/kg, 80 mg/kg, 90 mg/kg or 100 mg/kg.

Method of administration of immunogenic vaccine and PI3 kinase inhibitor, for example, Wortmannin, Demethoxyviridine, LY294002, Hibiscon C, Idelalisib, Copanlisib, Duvelisib, Tazelisib, Perifosine, Buparlisib, Duvelisib, Alpelisib (BYL719), Umbralisib, (TGR 1202), Copanlisib (BAY) 80 -6946), PX-866, Dactolisiba, CUDC-907, Voxtalisib (SAR245409, XL765), CUDC-907, ME-401, IPI-549, SF1126, RP6530, INK1117, pictilisib (GDC-0941), XL147 (SAR245408) , Palomida 529, GSK1059615, ZSTK474, PWT33597, IC87114, TG100–115, CAL263, RP6503, PI-103, GNE-477 or AEZS-136 may be simultaneous or sequential, where the immunogenic vaccine and at least one additional pharmaceutically active agent are administered sequentially (or separately). For example, immunogenic vaccine and PI3 inhibitor kinase, for example, vortmannin, dememoxiviridine, LY294002, Hibisco C, Idalalisib, Kopanlisib, Duvelisib, Taselisib, Perifosin, Barlisib, Duvelisib, Alpelisib (BYL719), Umbralisib, (TGR 1202), Copmansib (TGR 1202), Kopentlysib (TGR 1202). Bay 80 -6946), PX-866, Dactolisib, CUDC-907, Voxtalisib (SAR245409, XL765), CUDC-907, ME-401, IPI-549, SF1126, RP6530, INK1117, pictilisib (GDC-0941), XL147 (SAR245408) , Palomide 529, GSK1059615, ZSTK474, PWT33597, IC87114, TG100–115, CAL263, RP6503, PI-103, GNE-477 or AEZS-136 may be presented in unit dosage form to be taken together or as separate substances (e.g. separate containers) for administration simultaneously or with some time difference. This time difference can be from 1 hour to 1 month, for example from 1 day to 1 week, for example from 48 hours to 3 days. In addition, it is possible to administer an immunogenic vaccine by a different route of administration than the PI3 kinase inhibitor, for example, Wortmannin, Demethoxyviridine, LY294002, Hibiscon C, Idelalisib, Copanlisib, Duvelisib, Tazelisib, Perifosine, Buparlisib, Duvelisib, Alpelisib (BYL719), Umbralisib, (TGR 1202), Copanlisiba (BAY 80-6946), PX-866, Dactolisiba, CUDC-907, Voxtalisib (SAR245409, XL765), CUDC-907, ME-401, IPI-549, SF1126, RP6530, INK1117, pictilisib ( GDC-0941), XL147 (SAR245408), Palomida 529, GSK1059615, ZSTK474, PWT33597, IC87114, TG100–115, CAL263, RP6503, PI-103, GNE-477 or AEZS-136. For example, it may be preferable to administer either an immunogenic vaccine or a PI3 kinase inhibitor, for example, Wortmannin, Demethoxyviridine, LY294002, Hibiscon C, Idelalisib, Copanlisib, Duvelisib, Tazelisib, Perifosine, Buparlisib, Duvelisib, Alpelisib (BYL719), Umbralisib, (TGR 1202 ), Copanlisib (BAY 80-6946), PX-866, Dactolisib, CUDC-907, Voxtalisib (SAR245409, XL765), CUDC-907, ME-401, IPI-549, SF1126, RP6530, INK1117, pictilisib (GDC-0941 ), XL147 (SAR245408), Palomid 529, GSK1059615, ZSTK474, PWT33597, IC87114, TG100–115, CAL263, RP6503, PI-103, GNE-477 or AEZS-136, intravenously, and the other administered systemically or orally. For example, the immunogenic vaccine is administered intravenously or subcutaneously, and the Pi3 inhibitor of kinase, for example, vortmannin, deemoxiviridine, LY294002, hibiscon C, Idalasib, Kopanlisib, Duvelisib, Taselisib, Perifosin, Barparlyisib, Duvelisib, Alpelisib (BYL719), TGRISIB (TGR 1202) , Copanlisib (BAY 80-6946), PX-866, Dactolisib, CUDC-907, Voxtalisib (SAR245409, XL765), CUDC-907, ME-401, IPI-549, SF1126, RP6530, INK1117, pictilisib (GDC-0941) , XL147 (SAR245408), Palomide 529, GSK1059615, ZSTK474, PWT33597, IC87114, TG100–115, CAL263, RP6503, PI-103, GNE-477 or AEZS-136, orally.

In some embodiments, the immunogenic vaccine is administered chronologically before the PI3 kinase inhibitor, e.g., Wortmannin, Demethoxyviridine, LY294002, Hibiscon C, Idelalisib, Copanlisib, Duvelisib, Tazelisib, Perifosine, Buparlisib, Duvelisib, Alpelisib (BYL719), Umbralisib, (TGR 120 2) , Copanlisiba (BAY 80-6946), PX-866, Dactolisiba, CUDC-907, Voxtalisib (SAR245409, XL765), CUDC-907, ME-401, IPI-549, SF1126, RP6530, INK1117, pictilisib (GDC-0941) , XL147 (SAR245408), Palomida 529, GSK1059615, ZSTK474, PWT33597, IC87114, TG100–115, CAL263, RP6503, PI-103, GNE-477 or AEZS-136. In some embodiments, the immunogenic vaccine is administered at 1-24 hours, 2-24 hours, 3-24 hours, 4-24 hours, 5-24 hours, 6-24 hours, 7-24 hours, 8-24 hours, 9 -24 hours, 10-24 hours, 11-24 hours, 12-24 hours, 1-30 days, 2-30 days, 3-30 days, 4-30 days, 5-30 days, 6-30 days, 7 -30 days, 8-30 days, 9-30 days, 10-30 days, 11-30 days, 12-30 days, 13-30 days, 14-30 days, 15-30 days, 16-30 days, 17 -30 days, 18-30 days, 19-30 days, 20-30 days, 21-30 days, 22-30 days, 23-30 days, 24-30 days, 25-30 days, 26-30 days, 27 -30 days, 28-30 days, 29-30 days, 1-4 weeks, 2-4 weeks, 3-4 weeks, 1-12 months, 2-12 months, 3-12 months, 4-12 months, 5 -12 months, 6-12 months, 7-12 months, 8-12 months, 9-12 months, 10-12 months, 11-12 months, or any combination thereof, before administration of a PI3 kinase inhibitor. In some embodiments, the immunogenic vaccine is administered over at least 1 hour, 2 hours, 3 hours, 4 hours, 5 hours, 6 hours, 7 hours, 8 hours, 9 hours, 10 hours, 11 hours, 12 hours, 1 day , 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9, days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days, 17 days, 18 days, 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, 25 days, 26 days, 27 days, 28 days, 29 days, 1 week, 2 weeks, three weeks, 4 weeks, 1 month , 2 months, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months, 12 months, or any combination thereof, before administration of a PI3 kinase inhibitor. For example, an immunogenic vaccine may be administered at least 1 hour, 2 hours, 3 hours, 4 hours, 5 hours, 6 hours, 7 hours, 8 hours, 9 hours, 10 hours, 11 hours, 12 hours, 1 day, 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9 days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days, 17 days, 18 days , 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, 25 days, 26 days, 27 days, 28 days, 29 days, 1 week, 2 weeks, three weeks, 4 weeks, 1 month, 2 months, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months, 12 months, or any combination thereof, before administration of Wortmannin, Demethoxyviridine, LY294002, Hibiscon C, Idelalisib, Kopanlisib, Duvelisib, Taselisib, Perifosin, Barlisib, Duvelisib, Alpelisib (BYL719), Umbralsib, (TGR 1202), Kopanlisib (Bay 80-6946), PX-866, DACLISIBA, CUDC-907, VASTALISIB (SAR245409, XL765, XL765, XL765), CU, Cu) DC -907, ME-401, IPI-549, SF1126, RP6530, INK1117, pictilisib (GDC-0941), XL147 (SAR245408), Palomida 529, GSK1059615, ZSTK474, PWT33597, IC87114, TG100–115, CAL26 3, RP6503, PI- 103, GNE-477 or AEZS-136.

In some embodiments, the immunogenic vaccine is administered in at most 1 hour, 2 hours, 3 hours, 4 hours, 5 hours, 6 hours, 7 hours, 8 hours, 9 hours, 10 hours, 11 hours, 12 hours, 1 day, 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9 days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days, 17 days , 18 days, 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, 25 days, 26 days, 27 days, 28 days, 29 days, 1 week, 2 weeks, three weeks, 4 weeks, 1 month, 2 months, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months, 12 months, or any combination thereof, before administration of a PI3 kinase inhibitor. For example, an immunogenic vaccine can be administered in at most 1 hour, 2 hours, 3 hours, 4 hours, 5 hours, 6 hours, 7 hours, 8 hours, 9 hours, 10 hours, 11 hours, 12 hours, 1 day, 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9 days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days, 17 days, 18 days, 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, 25 days, 26 days, 27 days, 28 days, 29 days, 1 week, 2 weeks, three weeks, 4 weeks, 1 month, 2 months, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months, 12 months, or any combination thereof, before administration of Wortmannin, Demethoxyviridine, LY294002, Hibiscon C, Idelalisib , Copanlisiba, Duvelisiba, Tazelisiba, Perifosina, Buparlisiba, Duvelisiba, Alpelisiba (BYL719), Umbralisiba, (TGR 1202), Copanlisiba (BAY 80-6946), PX-866, Dactolisiba, CUDC-907, Voxtalisiba (SAR245409, XL765), C AL263, RP6503, PI -103, GNE-477 or AEZS-136.

In some embodiments, the immunogenic vaccine is administered in about 1 hour, 2 hours, 3 hours, 4 hours, 5 hours, 6 hours, 7 hours, 8 hours, 9 hours, 10 hours, 11 hours, 12 hours, 1 day, 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9 days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days, 17 days, 18 days , 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, 25 days, 26 days, 27 days, 28 days, 29 days, 1 week, 2 weeks, three weeks, 4 weeks, 1 month, 2 months, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months, 12 months, or any combination thereof, before administration of a PI3 kinase inhibitor. For example, an immunogenic vaccine can be administered in approximately 1 hour, 2 hours, 3 hours, 4 hours, 5 hours, 6 hours, 7 hours, 8 hours, 9 hours, 10 hours, 11 hours, 12 hours, 1 day, 2 days , 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9, days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days, 17 days, 18 days, 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, 25 days, 26 days, 27 days, 28 days, 29 days, 1 week, 2 weeks, three weeks, 4 weeks, 1 month, 2 months , 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months, 12 months, or any combination thereof, before administration of Wortmannin, Demethoxyviridine, LY294002, Hibiscon C, Idelalisib, Copanlisib . 907, ME-401, IPI-549, SF1126, RP6530, INK1117, pictilisib (GDC-0941), XL147 (SAR245408), Palomida 529, GSK1059615, ZSTK474, PWT33597, IC87114, TG100–115, CAL26 3, RP6503, PI-103 , GNE-477 or AEZS-136.

In some embodiments, the immunogenic vaccine is administered chronologically at the same time as at least one additional pharmaceutically active agent.

In some embodiments, the immunogenic vaccine is administered chronologically after administration of a PI3 kinase inhibitor, e.g., Wortmannin, Demethoxyviridine, LY294002, Hibiscon C, Idelalisib, Copanlisib, Duvelisib, Tazelisib, Perifosine, Buparlisib, Duvelisib, Alpelisib (BYL719), Umbralisib, (TGR 12 02 ), Copanlisiba (BAY 80-6946), PX-866, Dactolisiba, CUDC-907, Voxtalisib (SAR245409, XL765), CUDC-907, ME-401, IPI-549, SF1126, RP6530, INK1117, pictilisib (GDC-0941 ), XL147 (SAR245408), Palomida 529, GSK1059615, ZSTK474, PWT33597, IC87114, TG100–115, CAL263, RP6503, PI-103, GNE-477 or AEZS-136. In some embodiments, the PI3 kinase inhibitor is administered at 1-24 hours, 2-24 hours, 3-24 hours, 4-24 hours, 5-24 hours, 6-24 hours, 7-24 hours, 8-24 hours, 9-24 hours, 10-24 hours, 11-24 hours, 12-24 hours, 1-30 days, 2-30 days, 3-30 days, 4-30 days, 5-30 days, 6-30 days, 7-30 days, 8-30 days, 9-30 days, 10-30 days, 11-30 days, 12-30 days, 13-30 days, 14-30 days, 15-30 days, 16-30 days, 17-30 days, 18-30 days, 19-30 days, 20-30 days, 21-30 days, 22-30 days, 23-30 days, 24-30 days, 25-30 days, 26-30 days, 27-30 days, 28-30 days, 29-30 days, 1-4 weeks, 2-4 weeks, 3-4 weeks, 1-12 months, 2-12 months, 3-12 months, 4-12 months, 5-12 months, 6-12 months, 7-12 months, 8-12 months, 9-12 months, 10-12 months, 11-12 months, or any combination thereof, before administration of an immunogenic vaccine. In some embodiments, the PI3 kinase inhibitor is administered over at least 1 hour, 2 hours, 3 hours, 4 hours, 5 hours, 6 hours, 7 hours, 8 hours, 9 hours, 10 hours, 11 hours, 12 hours, 1 day, 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9 days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days, 17 days , 18 days, 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, 25 days, 26 days, 27 days, 28 days, 29 days, 30 days, 1 week, 2 weeks, three weeks, 4 weeks, 1 month, 2 months, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months, 12 months, or any combination thereof, before administration of an immunogenic vaccine. For example, Wortmannin, Demethoxyviridine, LY294002, Hibiscon C, Idelalisib, Copanlisib, Duvelisib, Tazelisib, Perifosine, Buparlisib, Duvelisib, Alpelisib (BYL719), Umbralisib, (TGR 1202), Copanlisib (BAY 80-6946), PX-866, Dactoli sib , CUDC-907, Voxtalisib (SAR245409, XL765), CUDC-907, ME-401, IPI-549, SF1126, RP6530, INK1117, pictilisib (GDC-0941), XL147 (SAR245408), Palomid 529, GSK1059615, ZSTK 474, PWT33597 , IC87114, TG100–115, CAL263, RP6503, PI-103, GNE-477 or AEZS-136 can be administered at least 1 hour, 2 hours, 3 hours, 4 hours, 5 hours, 6 hours, 7 hours, 8 hours, 9 hours, 10 hours, 11 hours, 12 hours, 1 day, 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9 days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days, 17 days, 18 days, 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, 25 days, 26 days, 27 days, 28 days, 29 days, 30 days, 1 week, 2 weeks, 3 weeks, 4 weeks, 1 month, 2 months, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months , 12 months, or any combination thereof, before the introduction of an immunogenic vaccine.

In some embodiments, the PI3 kinase inhibitor is administered in at most 1 hour, 2 hours, 3 hours, 4 hours, 5 hours, 6 hours, 7 hours, 8 hours, 9 hours, 10 hours, 11 hours, 12 hours, 1 day, 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9 days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days, 17 days , 18 days, 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, 25 days, 26 days, 27 days, 28 days, 29 days, 30 days, 1 week, 2 weeks, three weeks, 4 weeks, 1 month, 2 months, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months, 12 months, or any combination thereof, before administration of an immunogenic vaccine. For example, Wortmannin, Demethoxyviridine, LY294002, Hibiscon C, Idelalisib, Copanlisib, Duvelisib, Tazelisib, Perifosine, Buparlisib, Duvelisib, Alpelisib (BYL719), Umbralisib, (TGR 1202), Copanlisib (BAY 80-6946), PX-866, Dactoli sib , CUDC-907, Voxtalisib (SAR245409, XL765), CUDC-907, ME-401, IPI-549, SF1126, RP6530, INK1117, pictilisib (GDC-0941), XL147 (SAR245408), Palomid 529, GSK1059615, ZSTK 474, PWT33597 , IC87114, TG100–115, CAL263, RP6503, PI-103, GNE-477 or AEZS-136 can be administered in at most 1 hour, 2 hours, 3 hours, 4 hours, 5 hours, 6 hours, 7 hours, 8 hours, 9 hours, 10 hours, 11 hours, 12 hours, 1 day, 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9 days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days, 17 days, 18 days, 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, 25 days, 26 days, 27 days, 28 days, 29 days, 30 days, 1 week, 2 weeks, 3 weeks, 4 weeks, 1 month, 2 months, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months , 12 months, or any combination thereof, before the introduction of an immunogenic vaccine.

In some embodiments, the PI3 kinase inhibitor is administered over about 1 hour, 2 hours, 3 hours, 4 hours, 5 hours, 6 hours, 7 hours, 8 hours, 9 hours, 10 hours, 11 hours, 12 hours, 1 day, 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9 days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days, 17 days, 18 days , 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, 25 days, 26 days, 27 days, 28 days, 29 days, 30 days, 1 week, 2 weeks, three weeks, 4 weeks, 1 month, 2 months, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months, 12 months, or any combination thereof, before administration of an immunogenic vaccine. For example, Wortmannin, Demethoxyviridine, LY294002, Hibiscon C, Idelalisib, Copanlisib, Duvelisib, Tazelisib, Perifosine, Buparlisib, Duvelisib, Alpelisib (BYL719), Umbralisib, (TGR 1202), Copanlisib (BAY 80-6946), PX-866, Dactoli sib , CUDC-907, Voxtalisib (SAR245409, XL765), CUDC-907, ME-401, IPI-549, SF1126, RP6530, INK1117, pictilisib (GDC-0941), XL147 (SAR245408), Palomid 529, GSK1059615, ZSTK 474, PWT33597 , IC87114, TG100–115, CAL263, RP6503, PI-103, GNE-477, or AEZS-136 can be administered in approximately 1 hour, 2 hours, 3 hours, 4 hours, 5 hours, 6 hours, 7 hours, 8 hours , 9 hours, 10 hours, 11 hours, 12 hours, 1 day, 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9 days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days, 17 days, 18 days, 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, 25 days, 26 days, 27 days, 28 days, 29 days , 30 days, 1 week, 2 weeks, 3 weeks, 4 weeks, 1 month, 2 months, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months, 12 months, or any combination thereof, before administration of an immunogenic vaccine.

In some embodiments, the invention provides a method of treating a condition or disease, comprising administering to a patient in need thereof a therapeutically effective amount of an immunogenic vaccine in combination with a therapeutically effective amount of a PI3 kinase inhibitor. For example, the invention relates to a method of treating a condition or disease comprising administering to a patient in need thereof a therapeutically effective amount of an immunogenic vaccine, in combination with a therapeutically effective amount of Wortmannin, Demethoxyviridine, LY294002, Hibiscon C, Idelalisib, Copanlisib, Duvelisib, Tazelisib, Perifosine, Buparlisiba, Duvelisiba, Alpelisiba (BYL719), Umbralisiba, (TGR 1202), Copanlisiba (BAY 80-6946), PX-866, Dactolisiba, CUDC-907, Voxtalisib (SAR245409, XL765), CUDC-907, ME-401, IPI -549, SF1126, RP6530, INK1117, pictilisib (GDC-0941), XL147 (SAR245408), Palomida 529, GSK1059615, ZSTK474, PWT33597, IC87114, TG100–115, CAL263, RP6503, PI-1 03, GNE-477 or AEZS- 136.

In some embodiments, the immunogenic vaccine is administered once, twice, or three times daily for 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17. 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29 or 30 consecutive days followed by 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, or 30 days of rest (eg, without administration of immunogenic vaccine/interruption of treatment ) at 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27 or 28 day course; and PI3 kinase inhibitor (eg, Wortmannin, Demethoxyviridin, LY294002, Hibiscon C, Idelalisib, Copanlisib, Duvelisib, Tazelisib, Perifosine, Buparlisib, Duvelisib, Alpelisib (BYL719), Umbralisib, (TGR 1202), Copanlisib (BAY 80-6946), PX-866, Dactolisib, CUDC-907, Voxtalisib (SAR245409, XL765), CUDC-907, ME-401, IPI-549, SF1126, RP6530, INK1117, pictilisib (GDC-0941), XL147 (SAR245408), Palomid 529, GSK1059615, ZSTK474, PWT33597, IC87114, TG100–115, CAL263, RP6503, PI-103, GNE-477, or AEZS-136) are administered before, simultaneously with, or after administration of an immunogenic vaccine on one or more days (eg, on day 1 course). In some embodiments, the combination therapy is administered for 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, or 13 cycles of 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27 or 28 days. In some embodiments, the combination therapy is administered over 1-12 or 13 courses of 28 days (eg, approximately 12 months).

In some embodiments, the invention provides a method of treating a condition or disease, comprising administering to a patient in need thereof a therapeutically effective amount of an immunogenic vaccine in combination with a therapeutically effective amount of a PI3 kinase inhibitor, e.g., Wortmannin, Demethoxyviridine, LY294002, Hibiscon C, Idelalisib, Copanlisib . 907, ME-401, IPI-549, SF1126, RP6530, INK1117, pictilisib (GDC-0941), XL147 (SAR245408), Palomida 529, GSK1059615, ZSTK474, PWT33597, IC87114, TG100–115, CAL26 3, RP6503, PI-103 , GNE-477 or AEZS-136, and a secondary active agent such as an immune checkpoint inhibitor. In some embodiments, the immunogenic vaccine is administered once, twice, or three times daily for 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17. 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29 or 30 consecutive days, followed by 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, or 30 days of rest (e.g., no immunogenic vaccine/suspension treatment) at 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24 , 25, 26, 27 or 28 day course; PI3 inhibitor Kinase (for example, vortmannin, dememoxiviridine, LY294002, Hibiscon C, IDALALISIB, Kopanlisib, Duvelisib, Taselisib, Perifosin, Barlisib, Duvelisib, Alpelisib (Byl719), Umbralsib, (TGR 1202), Popanlisib (Bay 80-6946), P X -866, Dactolisib, CUDC-907, Voxtalisib (SAR245409, XL765), CUDC-907, ME-401, IPI-549, SF1126, RP6530, INK1117, pictilisib (GDC-0941), XL147 (SAR245408), Palomid 529, GSK10 59615 , ZSTK474, PWT33597, IC87114, TG100–115, CAL263, RP6503, PI-103, GNE-477, or AEZS-136) administered before, simultaneously with, or after administration of an immunogenic vaccine on one or more days (eg, on day 1 of course 1 ), and the secondary agent is administered daily, weekly or monthly. In some embodiments, the combination therapy is administered over 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, or 13 courses of 1, 2, 3, 4, 5, 6, 7, 8 , 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27 or 28 days. In some embodiments, the combination therapy is administered over 1-12 or 13 courses of 28 days (eg, approximately 12 months).

In some embodiments, the immunogenic vaccine may be used in combination with cyclin-dependent kinase inhibitors, such as a CDK4 and/or CDK6 inhibitor. An example of such an inhibitor that can be used in combination with a present immunogenic vaccine is palbociclib (IBRANCE) (see, e.g. , Clin. Cancer Res.; 2015, 21(13); 2905–10). An example of such an inhibitor that can be used in combination with a present immunogenic vaccine is ribociclib. An example of such an inhibitor that can be used in combination with a present immunogenic vaccine is abemaciclib. An example of such an inhibitor that can be used in combination with a present immunogenic vaccine is seliciclib. An example of such an inhibitor that can be used in combination with a present immunogenic vaccine is dinaciclib. An example of such an inhibitor that can be used in combination with a present immunogenic vaccine is milciclib. An example of such an inhibitor that can be used in combination with a present immunogenic vaccine is roniciclib. An example of such an inhibitor that can be used in combination with a present immunogenic vaccine is atuveciclib. An example of such an inhibitor that can be used in combination with a present immunogenic vaccine is briciclib. An example of such an inhibitor that can be used in combination with a present immunogenic vaccine is riviciclib. An example of such an inhibitor that can be used in combination with a present immunogenic vaccine is seliciclib. An example of such an inhibitor that can be used in combination with a present immunogenic vaccine is trilaciclib. An example of such an inhibitor that can be used in combination with a present immunogenic vaccine is voruciclib. In some examples, the immunogenic vaccines of the present disclosure may be used in combination with a CDK4 and/or CDK6 inhibitor and with an agent that enhances the cytostatic activity of CDK4/6 inhibitors and/or with an agent that converts reversible cytostasis into irreversible cell growth arrest or death. Common cancer subtypes include NSCLC, melanoma, neuroblastoma, glioblastoma, liposarcoma, and mantle cell lymphoma.

In some embodiments, the dosage of a cyclin-dependent kinase inhibitor, e.g., seliciclib, ribociclib, abemaciclib, or palbociclib, used to treat a human may range from about 0.01 mg/kg to about 100 mg/kg per day (e.g., from about 0.1 mg/kg to about 100 mg/kg per day, from about 0.1 mg/kg to about 50 mg/kg per day, from about 10 mg/kg per day or to about 30 mg/kg per day day). The desired dose may conveniently be administered in a single dose or in multiple doses at suitable intervals, for example in two, three, four or more sub-doses per day.

In some embodiments, the dose of a cyclin-dependent kinase inhibitor, such as seliciclib, ribociclib, abemaciclib, or palbociclib, can be from about 1 ng/kg to about 100 mg/kg. The dose of a cyclin-dependent kinase inhibitor, e.g., seliciclib, ribociclib, abemaciclib, or palbociclib, can be any dose, including, but not limited to, about 1 mcg/kg, 25 mcg/kg, 50 mcg/kg, 75 mcg/kg, 100 µ µg/kg, 125 µg/kg, 150 µg/kg, 175 µg/kg, 200 µg/kg, 225 µg/kg, 250 µg/kg, 275 µg/kg, 300 µg/kg, 325 µg/kg , 350 mcg/kg, 375 mcg/kg, 400 mcg/kg, 425 mcg/kg, 450 mcg/kg, 475 mcg/kg, 500 mcg/kg, 525 mcg/kg, 550 mcg/kg, 575 mcg/kg , 600 mcg/kg, 625 mcg/kg, 650 mcg/kg, 675 mcg/kg, 700 mcg/kg, 725 mcg/kg, 750 mcg/kg, 775 mcg/kg, 800 mcg/kg, 825 mcg/kg , 850 mcg/kg, 875 mcg/kg, 900 mcg/kg, 925 mcg/kg, 950 mcg/kg, 975 mcg/kg, 1 mg/kg, 2.5 mg/kg, 5 mg/kg, 10 mg /kg, 15 mg/kg, 20 mg/kg, 25 mg/kg, 30 mg/kg, 35 mg/kg, 40 mg/kg, 45 mg/kg, 50 mg/kg, 60 mg/kg, 70 mg /kg, 80 mg/kg, 90 mg/kg or 100 mg/kg.

The method of administration of an immunogenic vaccine and a cyclin-dependent kinase inhibitor, for example, seliciclib, ribociclib, abemaciclib or palbociclib may be simultaneous or sequential, where the immunogenic vaccine and at least one additional pharmaceutically active agent are administered sequentially (or separately). For example, an immunogenic vaccine and a cyclin-dependent kinase inhibitor, such as seliciclib, ribociclib, abemaciclib, or palbociclib, may be presented in a unit dosage form for administration together or as separate substances (for example, in separate containers) for administration at the same time or with some difference in time. time. This time difference can be from 1 hour to 1 month, for example from 1 day to 1 week, for example from 48 hours to 3 days. It is also possible to administer an immunogenic vaccine by a route other than a cyclin-dependent kinase inhibitor, such as seliciclib, ribociclib, abemaciclib, or palbociclib. For example, it may be preferable to administer either an immunogenic vaccine or a cyclin-dependent kinase inhibitor, such as seliciclib, ribociclib, abemaciclib, or palbociclib, intravenously, and the other administered systemically or orally. For example, an immunogenic vaccine is administered intravenously or subcutaneously, and a cyclin-dependent kinase inhibitor, such as seliciclib, ribociclib, abemaciclib, or palbociclib, is administered orally.

In some embodiments, the immunogenic vaccine is administered chronologically before a cyclin-dependent kinase inhibitor, such as seliciclib, ribociclib, abemaciclib, or palbociclib. In some embodiments, the immunogenic vaccine is administered at 1-24 hours, 2-24 hours, 3-24 hours, 4-24 hours, 5-24 hours, 6-24 hours, 7-24 hours, 8-24 hours, 9 -24 hours, 10-24 hours, 11-24 hours, 12-24 hours, 1-30 days, 2-30 days, 3-30 days, 4-30 days, 5-30 days, 6-30 days, 7 -30 days, 8-30 days, 9-30 days, 10-30 days, 11-30 days, 12-30 days, 13-30 days, 14-30 days, 15-30 days, 16-30 days, 17 -30 days, 18-30 days, 19-30 days, 20-30 days, 21-30 days, 22-30 days, 23-30 days, 24-30 days, 25-30 days, 26-30 days, 27 -30 days, 28-30 days, 29-30 days, 1-4 weeks, 2-4 weeks, 3-4 weeks, 1-12 months, 2-12 months, 3-12 months, 4-12 months, 5 -12 months, 6-12 months, 7-12 months, 8-12 months, 9-12 months, 10-12 months, 11-12 months, or any combination thereof, before administration of a cyclin-dependent kinase inhibitor. In some embodiments, the immunogenic vaccine is administered over at least 1 hour, 2 hours, 3 hours, 4 hours, 5 hours, 6 hours, 7 hours, 8 hours, 9 hours, 10 hours, 11 hours, 12 hours, 1 day , 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9, days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days, 17 days, 18 days, 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, 25 days, 26 days, 27 days, 28 days, 29 days, 1 week, 2 weeks, three weeks, 4 weeks, 1 month , 2 months, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months, 12 months, or any combination thereof, before administration of a cyclin-dependent kinase inhibitor. For example, an immunogenic vaccine may be administered over at least 1 hour, 2 hours, 3 hours, 4 hours, 5 hours, 6 hours, 7 hours, 8 hours, 9 hours, 10 hours, 11 hours, 12 hours, 1 day, 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9 days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days, 17 days, 18 days, 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, 25 days, 26 days, 27 days, 28 days, 29 days, 1 week, 2 weeks, three weeks, 4 weeks, 1 month, 2 months, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months, 12 months, or any combination thereof, before administration of seliciclib, ribociclib, abemaciclib, or palbociclib.

In some embodiments, the immunogenic vaccine is administered in at most 1 hour, 2 hours, 3 hours, 4 hours, 5 hours, 6 hours, 7 hours, 8 hours, 9 hours, 10 hours, 11 hours, 12 hours, 1 day, 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9 days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days, 17 days , 18 days, 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, 25 days, 26 days, 27 days, 28 days, 29 days, 1 week, 2 weeks, three weeks, 4 weeks, 1 month, 2 months, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months, 12 months, or any combination thereof, before administration of a cyclin-dependent kinase inhibitor. For example, an immunogenic vaccine can be administered in at most 1 hour, 2 hours, 3 hours, 4 hours, 5 hours, 6 hours, 7 hours, 8 hours, 9 hours, 10 hours, 11 hours, 12 hours, 1 day, 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9 days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days, 17 days, 18 days, 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, 25 days, 26 days, 27 days, 28 days, 29 days, 1 week, 2 weeks, three weeks, 4 weeks, 1 month, 2 months, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months, 12 months, or any combination thereof, before administration of seliciclib, ribociclib, abemaciclib, or palbociclib.

In some embodiments, the immunogenic vaccine is administered in about 1 hour, 2 hours, 3 hours, 4 hours, 5 hours, 6 hours, 7 hours, 8 hours, 9 hours, 10 hours, 11 hours, 12 hours, 1 day, 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9 days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days, 17 days, 18 days , 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, 25 days, 26 days, 27 days, 28 days, 29 days, 1 week, 2 weeks, three weeks, 4 weeks, 1 month, 2 months, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months, 12 months, or any combination thereof, prior to management of a cyclin-dependent kinase inhibitor. For example, an immunogenic vaccine can be administered in approximately 1 hour, 2 hours, 3 hours, 4 hours, 5 hours, 6 hours, 7 hours, 8 hours, 9 hours, 10 hours, 11 hours, 12 hours, 1 day, 2 days , 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9, days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days, 17 days, 18 days, 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, 25 days, 26 days, 27 days, 28 days, 29 days, 1 week, 2 weeks, three weeks, 4 weeks, 1 month, 2 months , 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months, 12 months, or any combination thereof, before administration of seliciclib, ribociclib, abemaciclib, or palbociclib.

In some embodiments, the immunogenic vaccine is administered chronologically at the same time as at least one additional pharmaceutically active agent.

In some embodiments, the immunogenic vaccine is administered chronologically after a cyclin-dependent kinase inhibitor, such as seliciclib, ribociclib, abemaciclib, or palbociclib. In some embodiments, the cyclin-dependent kinase inhibitor is administered at 1-24 hours, 2-24 hours, 3-24 hours, 4-24 hours, 5-24 hours, 6-24 hours, 7-24 hours, 8-24 hours, 9-24 hours, 10-24 hours, 11-24 hours, 12-24 hours, 1-30 days, 2-30 days, 3-30 days, 4-30 days, 5-30 days, 6-30 days, 7-30 days, 8-30 days, 9-30 days, 10-30 days, 11-30 days, 12-30 days, 13-30 days, 14-30 days, 15-30 days, 16-30 days, 17-30 days, 18-30 days, 19-30 days, 20-30 days, 21-30 days, 22-30 days, 23-30 days, 24-30 days, 25-30 days, 26-30 days, 27-30 days, 28-30 days, 29-30 days, 1-4 weeks, 2-4 weeks, 3-4 weeks, 1-12 months, 2-12 months, 3-12 months, 4-12 months, 5-12 months, 6-12 months, 7-12 months, 8-12 months, 9-12 months, 10-12 months, 11-12 months, or any combination thereof, before administration of an immunogenic vaccine. In some embodiments, the cyclin-dependent kinase inhibitor is administered at least 1 hour, 2 hours, 3 hours, 4 hours, 5 hours, 6 hours, 7 hours, 8 hours, 9 hours, 10 hours, 11 hours, 12 hours before , 1 day, 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9 days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days, 17 days, 18 days, 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, 25 days, 26 days, 27 days, 28 days, 29 days, 30 days, 1 week, 2 weeks, three weeks , 4 weeks, 1 month, 2 months, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months, 12 months, or any combination thereof, before administration of an immunogenic vaccine. For example, seliciclib, ribociclib, abemaciclib, or palbociclib may be administered over at least 1 hour, 2 hours, 3 hours, 4 hours, 5 hours, 6 hours, 7 hours, 8 hours, 9 hours, 10 hours, 11 hours, 12 hours, 1 day, 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9 days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days , 17 days, 18 days, 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, 25 days, 26 days, 27 days, 28 days, 29 days, 30 days, 1 week, 2 weeks, 3 weeks, 4 weeks, 1 month, 2 months, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months, 12 months, or any combination thereof, before administration of an immunogenic vaccine .

In some embodiments, the cyclin-dependent kinase inhibitor is administered in at most 1 hour, 2 hours, 3 hours, 4 hours, 5 hours, 6 hours, 7 hours, 8 hours, 9 hours, 10 hours, 11 hours, 12 hours, 1 day, 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9 days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days, 17 days , 18 days, 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, 25 days, 26 days, 27 days, 28 days, 29 days, 30 days, 1 week, 2 weeks, three weeks, 4 weeks, 1 month, 2 months, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months, 12 months, or any combination thereof, before administration of an immunogenic vaccine. For example, seliciclib, ribociclib, abemaciclib, or palbociclib may be administered in at most 1 hour, 2 hours, 3 hours, 4 hours, 5 hours, 6 hours, 7 hours, 8 hours, 9 hours, 10 hours, 11 hours, 12 hours, 1 day, 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9 days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days , 17 days, 18 days, 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, 25 days, 26 days, 27 days, 28 days, 29 days, 30 days, 1 week, 2 weeks, 3 weeks, 4 weeks, 1 month, 2 months, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months, 12 months, or any combination thereof, before administration of an immunogenic vaccine .

In some embodiments, the cyclin-dependent kinase inhibitor is administered over about 1 hour, 2 hours, 3 hours, 4 hours, 5 hours, 6 hours, 7 hours, 8 hours, 9 hours, 10 hours, 11 hours, 12 hours, 1 day. , 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9, days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days, 17 days, 18 days, 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, 25 days, 26 days, 27 days, 28 days, 29 days, 30 days, 1 week, 2 weeks, three weeks, 4 weeks , 1 month, 2 months, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months, 12 months, or any combination thereof, before administration of an immunogenic vaccine. For example, seliciclib, ribociclib, abemaciclib, or palbociclib may be administered over approximately 1 hour, 2 hours, 3 hours, 4 hours, 5 hours, 6 hours, 7 hours, 8 hours, 9 hours, 10 hours, 11 hours, 12 hours, 1 day, 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9 days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days, 17 days, 18 days, 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, 25 days, 26 days, 27 days, 28 days, 29 days, 30 days, 1 week, 2 weeks, 3 weeks, 4 weeks, 1 month, 2 months, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months, 12 months, or any combination thereof, before administration of an immunogenic vaccine.

In some embodiments, the invention provides a method of treating a condition or disease, comprising administering to a patient in need thereof a therapeutically effective amount of an immunogenic vaccine in combination with a therapeutically effective amount of a cyclin-dependent kinase inhibitor. For example, a method of treating a condition or disease is provided, comprising administering to a patient in need thereof a therapeutically effective amount of an immunogenic vaccine in combination with a therapeutically effective amount of seliciclib, ribociclib, abemaciclib, or palbociclib.

In some embodiments, the immunogenic vaccine is administered once, twice, or three times daily for 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17. 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29 or 30 consecutive days followed by 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, or 30 days of rest (e.g., no immunogenic vaccine/suspension treatment) at 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24 , 25, 26, 27 or 28 day course; and a cyclin-dependent kinase inhibitor (eg, seliciclib, ribociclib, abemaciclib, or palbociclib) is administered before, concurrently with, or after administration of the immunogenic vaccine on one or more days (eg, day 1 of course 1). In some embodiments, the combination therapy is administered for 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, or 13 cycles of 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27 or 28 days. In some embodiments, the combination therapy is administered over 1-12 or 13 courses of 28 days (eg, approximately 12 months).

In some embodiments, the invention provides a method of treating a condition or disease, comprising administering to a patient in need thereof a therapeutically effective amount of an immunogenic vaccine in combination with a therapeutically effective amount of a cyclin-dependent kinase inhibitor, e.g., seliciclib, ribociclib, abemaciclib, or palbociclib, and a secondary an active agent such as an immune checkpoint inhibitor. In some embodiments, the immunogenic vaccine is administered once, twice, or three times daily for 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17. 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29 or 30 consecutive days followed by 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, or 30 days of rest (eg, without administration of immunogenic vaccine/interruption of treatment ) at 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27 or 28 day cycle; a cyclin-dependent kinase inhibitor (eg, seliciclib, ribociclib, abemaciclib, or palbociclib) is administered before, concurrently with, or after administration of an immunogenic vaccine on one or more days (eg, on day 1 of course 1), and a secondary agent is administered daily, weekly, or monthly . In some embodiments, the combination therapy is administered for 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, or 13 cycles of 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27 or 28 days. In some embodiments, the combination therapy is administered over 1-12 or 13 cycles of 28 days (eg, approximately 12 months).

In some embodiments, the additional therapeutic agent comprises a second immunotherapeutic agent. In some embodiments, the additional immunotherapeutic agent includes, but is not limited to, a colony-stimulating factor, interleukin, an antibody that blocks immunosuppressive functions ( e.g. , anti-CTLA-4 antibody, anti-CD28 antibody, anti-CD3 antibody, anti-PD- 1 antibody, anti-PD-L1 antibody, anti-TIGIT antibody), an antibody that enhances immune cell function ( eg , anti-GITR antibody, anti-OX-40 antibody, anti-CD40 antibody, or anti-4-1BB antibody) , toll-like receptor ( e.g. TLR4, TLR7, TLR9), soluble ligand ( e.g. GITRL, GITRL-Fc, OX-40L, OX-40L-Fc, CD40L, CD40L-Fc, 4-1BB ligand or 4-1BB ligand-Fc) or a member of the B7 family ( e.g. CD80, CD86). In some embodiments, the additional immunotherapy agent targets CTLA-4, CD28, CD3, PD-1, PD-L1, TIGIT, GITR, OX-40, CD-40, or 4-1BB.

In some embodiments, the additional therapeutic agent is an immune checkpoint inhibitor. In some embodiments, the immune checkpoint inhibitor is an anti-PD-1 antibody, an anti-PD-L1 antibody, an anti-CTLA-4 antibody, an anti-CD28 antibody, an anti-TIGIT antibody, an anti-LAG3 antibody, an anti-TIM3 antibody , anti-GITR antibody, anti-4-1BB antibody, or anti-OX-40 antibody. In some embodiments, the additional therapeutic agent is an anti-TIGIT antibody. In some embodiments, the additional therapeutic agent is an anti-PD-1 antibody selected from the group consisting of: nivolumab (OPDIVO), pembrolizumab (KEYTRUDA), pidilzumab, MEDI0680, REGN2810, BGB-A317, and PDR001. In some embodiments, the additional therapeutic agent is an anti-PD-L1 antibody selected from the group consisting of: BMS935559 (MDX-1105), atexolizumab (MPDL3280A), durvalumab (MEDI4736), and avelumab (MSB0010718C). In some embodiments, the additional therapeutic agent is an anti-CTLA-4 antibody selected from the group consisting of ipilimumab (YERVOY) and tremelimumab. In some embodiments, the additional therapeutic agent is an anti-LAG-3 antibody selected from the group consisting of: BMS-986016 and LAG525. In some embodiments, the additional therapeutic agent is an anti-OX-40 antibody selected from the group consisting of: MEDI6469, MEDI0562, and MOXR0916. In some embodiments, the additional therapeutic agent is an anti-4-1BB antibody selected from the group consisting of: PF-05082566.

In some embodiments, the neoantigen therapeutic agent may be administered in combination with a biological molecule selected from the group consisting of: adrenomedullin (AM), angiopoietin (Ang), BMP, BDNF, EGF, erythropoietin (EPO), FGF, GDNF, granulocyte colony-stimulating factor (G-CSF), granulocyte-macrophage colony-stimulating factor (GM-CSF), macrophage colony-stimulating factor (M-CSF), stem cell factor (SCF), GDF9, HGF, HDGF, IGF, migration stimulating factor, myostatin ( GDF-8), NGF, neurotrophins, PDGF, thrombopoietin, TGF-α, TGF-β, TNF-α, VEGF, PlGF, gamma-IFN, IL-1, IL-2, IL-3, IL-4, IL -5, IL-6, IL-7, IL-12, IL-15 and IL-18.

In some embodiments, treatment with a neoantigen therapeutic agent described in the present invention may be accompanied by surgical removal of tumors, removal of cancer cells, or any other surgical therapy deemed necessary by the attending physician.

In some embodiments, treatment includes administration of a neoantigen therapeutic agent described in the present invention in combination with radiation therapy. Treatment with the agent may occur before, simultaneously with, or after radiation therapy. Dosage regimens for such radiation therapy can be determined by the medical practitioner.

Combined administration may include co-administration, either in a single pharmaceutical formulation or using separate formulations, or sequential administration in any order, but usually for such an amount of time that all active agents can exert their biological activity simultaneously.

It should be appreciated that the combination of a neoantigen therapeutic agent described in the present invention and at least one additional therapeutic agent can be administered in any order or simultaneously. In some embodiments, the agent will be administered to patients who have previously been treated with a second therapeutic agent. In some other embodiments, the neoantigen therapeutic agent and the second therapeutic agent will be administered substantially simultaneously or simultaneously. For example, a subject may be given an agent while undergoing treatment with a second therapeutic agent (eg, chemotherapy). In some embodiments, the neoantigen therapeutic agent will be administered within 1 year of treatment with the second therapeutic agent. It will also be appreciated that two (or more) agents or treatments may be administered to a subject within a matter of hours or minutes (ie, substantially simultaneously).

For the treatment of a disease, the appropriate dosage of the neoantigen therapeutic agent described in the present invention depends on the type of disease being treated, the severity and course of the disease, the sensitivity of the disease, whether the agent is administered for therapeutic or prophylactic purposes, previous therapy, the patient's medical history and so on, all at the discretion of the attending physician. The neoantigen therapeutic agent may be administered once or over a series of treatments lasting from several days to several months, or until cure or reduction of the disease state (eg, reduction in tumor size) is achieved. Optimal dosing regimens can be calculated based on measurements of drug accumulation in the patient's body, and will vary depending on the relative potency of the individual agent. Your healthcare provider can determine optimal dosages, dosing techniques, and frequency of repetition.

In some embodiments, the neoantigen therapeutic agent may be administered at an initial higher “loading” dose followed by one or lower doses. In some embodiments, the frequency of administration may also vary. In some embodiments, the dosing regimen may include administering an initial dose followed by additional doses (or “maintenance” doses) once a week, once every two weeks, once every three weeks, or once a month. For example, the dosing regimen may include administration of an initial loading dose followed by a weekly maintenance dose of, for example, half the original dose. Or the dosing regimen may include administration of an initial loading dose followed by maintenance doses, for example, half the original dose every other week. Or, the dosing regimen may involve administering three initial doses over 3 weeks followed by maintenance doses, for example the same amount every other week.

As is known to those skilled in the art, administration of any therapeutic agent may result in side effects and/or toxicity. In some cases, side effects and/or toxicity are so severe that they prevent the administration of a particular agent at a therapeutically effective dose. In some cases, therapy must be discontinued and other agents may be tried. However, many agents within the same therapeutic class exhibit similar side effects and/or toxicities, meaning that the patient either must discontinue therapy or, if possible, suffer unpleasant side effects associated with the therapeutic agent.

In some embodiments, the dosage regimen may be limited to a certain number of administrations or “courses.” In some embodiments, the agent is administered over 3, 4, 5, 6, 7, 8 or more courses. For example, the agent is administered every 2 weeks for 6 courses, the agent is administered every 3 weeks for 6 courses, the agent is administered every 2 weeks for 4 courses, the agent is administered every 3 weeks for 4 courses, etc. Dosage regimens can be selected and modified markedly by those skilled in the art.

The present description relates to methods of administering to a subject a neoantigen therapeutic agent described in the present invention, including the use of a strategy of intermittent administration of one or more agents, which can reduce the side effects and/or toxicity associated with the administration of the agent, chemotherapeutic agent, etc. In some embodiments, a method of treating cancer in a human comprises administering to a subject a therapeutically effective dose of a neoantigen therapeutic agent in combination with a therapeutically effective dose of a chemotherapeutic agent, wherein one or both agents are administered according to an intermittent administration strategy. In some embodiments, a method of treating cancer in a human includes administering to a subject a therapeutically effective dose of a neoantigen therapeutic agent in combination with a therapeutically effective dose of a second immunotherapy agent, wherein one or both agents are administered according to an intermittent administration strategy. In some embodiments, the intermittent administration strategy includes administering an initial dose of a neoantigen therapeutic agent to a subject, and administering subsequent doses of the agent approximately once every 2 weeks. In some embodiments, the intermittent administration strategy includes administering an initial dose of a neoantigen therapeutic agent to a subject, and administering subsequent doses of the agent approximately once every 3 weeks. In some embodiments, the intermittent administration strategy includes administering an initial dose of a neoantigen therapeutic agent to a subject, and administering subsequent doses of the agent approximately once every 4 weeks. In some embodiments, the agent is administered using an intermittent administration strategy, and an additional therapeutic agent is administered weekly.

The present description relates to compositions containing a neoantigen therapeutic agent described in the present invention. The present description also relates to pharmaceutical compositions containing a neoantigen therapeutic agent described in the present invention and a pharmaceutically acceptable carrier. In some embodiments, the pharmaceutical compositions are used in immunotherapy. In some embodiments, the compositions are used to inhibit tumor growth. In some embodiments, the pharmaceutical compositions are used to inhibit the growth of a tumor in a subject ( eg , a human). In some embodiments, the compositions are used in the treatment of cancer. In some embodiments, the pharmaceutical compositions are used to treat cancer in a subject ( eg , a human).

The compositions are prepared for storage and use by combining the neoantigen therapeutic agent of the present disclosure with a pharmaceutically acceptable carrier ( eg , carrier or excipient). Those skilled in the art generally consider pharmaceutically acceptable carriers, excipients and/or stabilizers to be inactive ingredients of a formulation or pharmaceutical composition. Examples of compositions are listed in WO 2015/095811.

Suitable pharmaceutically acceptable carriers include, but are not limited to, non-toxic buffers such as phosphate, citrate and other organic acids; salts such as sodium chloride; antioxidants including ascorbic acid and methionine; preservatives such as octadecyldimethylbenzyl ammonium chloride, hexamethonium chloride, benzalkonium chloride, benzethonium chloride, phenol, butyl or benzyl alcohol, alkylparabens such as methyl or propylparaben, catechol, resorcinol, cyclohexanol, 3-pentanol, and m-cresol; low molecular weight polypeptides ( eg , less than about 10 amino acid residues); proteins such as serum albumin, gelatin or immunoglobulins; a hydrophilic polymer such as polyvinylpyrrolidone; amino acids such as glycine, glutamine, asparagine, histidine, arginine or lysine; carbohydrates such as monosaccharides, disaccharides, glucose, mannose or dextrins; chelating agents such as EDTA; sugars such as sucrose, mannitol, trehalose or sorbitol; salt-forming counterions such as sodium; metal complexes such as Zn-protein complexes; and nonionic surfactants such as TWEEN or polyethylene glycol (PEG). (Remington: Science and Practice of Pharmacy, 22nd Edition, 2012, Pharmaceutical Press, London). In some embodiments, the carrier is a 5% dextrose solution in water.

The pharmaceutical compositions described in the present invention can be administered in any number of ways for both local and systemic treatment. Administration may be local, epidermal or transdermal patches, ointments, lotions, creams, gels, drops, suppositories, sprays, liquids and powders; pulmonary, by inhalation or insufflation of powders or aerosols, including using a nebulizer, intratracheal and intranasal; oral; or parenteral, including intravenous, intraarterial, intratumoral, subcutaneous, intraperitoneal, intramuscular ( eg , injection or infusion), or intracranial ( eg , intrathecal or intraventricular).

The therapeutic composition may be in a unit dosage form. Such formulations include tablets, pills, capsules, powders, granules, solutions or suspensions in water or non-aqueous media, or suppositories.

Neoantigenic peptides described in the present invention can also be enclosed in microcapsules. Such microcapsules are prepared, for example, by coacervation or interfacial polymerization methods, for example, hydroxymethylcellulose or gelatin microcapsules and poly(methyl methacylate), respectively, in colloidal drug delivery systems (for example, liposomes, albumin microspheres, microemulsions, nanoparticles) or in macroemulsions, as described in Remington: Science and Practice of Pharmacy, 22nd Edition, 2012, Pharmaceutical Press, London.

In some embodiments, the pharmaceutical compositions include a neoantigen therapeutic agent described in the present invention in combination with liposomes. Methods for preparing liposomes are known to those skilled in the art. For example, some liposomes can be created by reverse phase evaporation with fat compositions containing phosphatidylcholine, cholesterol and PEG-derivatized phosphatidylethanolamine (PEG-PE). Liposomes can be extruded through filters of specific pore sizes to produce liposomes of the desired diameter.

In some embodiments, sustained release formulations may be prepared containing the neoantigenic peptides described herein. Suitable examples of sustained release formulations include semi-permeable matrices of solid hydrophobic polymers containing the agent, where the matrices are in the form of molded articles (eg, films or microcapsules). Examples of sustained release matrices include polyesters, hydrogels such as poly(2-hydroxyethyl methacrylate) or poly(vinyl alcohol), polylactides, L-glutamic acid-7-ethyl-L-glutamate copolymer, non-degradable ethylene vinyl acetate, degradable lactic-glycolic copolymer acids such as LUPRON DEPOT™ (injectable microspheres consisting of a copolymer of lactic-glycolic acid and leuprolide acetate), sucrose acetate isobutyrate and poly-D-(-)-3-hydroxybutyric acid.

The present description relates to methods of treatment including an immunogenic vaccine. The invention relates to methods for treating a disease (such as cancer or a viral infection). The method may include administering to a subject an effective amount of a composition comprising an immunogenic antigen. In some embodiments, the antigen comprises a viral antigen. In some embodiments, the antigen comprises a tumor antigen.

Non-limiting examples of vaccines that can be prepared include a peptide vaccine, a nucleic acid vaccine, an antibody vaccine, a T cell vaccine, and an antigen presenting cell vaccine.

Vaccine compositions can be formulated using one or more physiologically acceptable carriers, including excipients and excipients, which facilitate processing of the active agents into preparations that can be used pharmaceutically. The correct formulation may depend on the route of administration chosen. Any well known techniques, carriers and excipients can be used as appropriate and as understood in the art.

In some cases, the vaccine composition is formulated as a peptide-based vaccine, a nucleic acid-based vaccine, an antibody-based vaccine, or a cell-based vaccine. For example, the vaccine composition may include naked cDNA in cationic fat formulations; lipopeptides ( e.g. Vitiello, A. et al., J. Clin. Invest. 95:341, 1995), naked cDNA or peptides encapsulated, e.g. poly(DL-lactide-co-glycolide) (“PLG”) microspheres (see, for example , Eldridge, et al., Molec. Immunol. 28:287-294, 1991: Alonso et al, Vaccine 12:299-306, 1994; Jones et al, Vaccine 13:675-681, 1995 ); peptide compositions contained in immunostimulating complexes (ISCOMS) ( eg , Takahashi et al, Nature 344:873-875, 1990; Hu et al, Clin. Exp. Immunol. 113:235-243, 1998); or multiple antigenic peptide (MAP) systems (see, for example , Tam, JP, Proc. Natl Acad. Sci. USA 85:5409-5413, 1988; Tarn, JP, J. Immunol. Methods 196:17-32, 1996 ). Sometimes, the vaccine is formulated as a peptide vaccine or a nucleic acid vaccine, in which the nucleic acid encodes polypeptides. Sometimes, the vaccine is formulated as an antibody vaccine. Sometimes, the vaccine is formulated as a cell-based vaccine.

A disease-specific immunogenic neoantigenic peptide identified by its amino acid sequence can be used to develop a pharmaceutically acceptable composition. The source of the antigen may be, but is not limited to, natural or synthetic proteins, including glycoproteins, peptides and superantigens; antibody/antigen complexes; lipoproteins; RNA or its translation product; and DNA or a polypeptide encoded by DNA. The antigen source may also contain untransformed, transformed, transfected or transduced cells or cell lines. Cells can be transformed, transfected or transduced using any of a variety of expression vectors or retroviral vectors known to those skilled in the art that can be used to express recombinant antigens. Expression can also be achieved in any suitable host cell that has been transformed, transfected or transduced with an expression vector or retroviral vector containing molecules encoding the recombinant antigen(s). Any number of transfection, transformation and transduction protocols known to those skilled in the art may be used. Recombinant vaccinia vectors and cells infected with the vaccinia vector can be used as a source of antigen.

The composition may contain a synthetic disease-specific immunogenic neoantigenic peptide. The composition may contain two or more disease-specific immunogenic neoantigenic peptides. The composition may contain a disease-specific immunogenic peptide precursor (eg, protein, peptide, DNA and RNA). A disease-specific immunogenic peptide precursor can create or be created for an identified disease-specific immunogenic neoantigen peptide. In some embodiments, the therapeutic composition contains an immunogenic peptide precursor. The precursor to a disease-specific immunogenic peptide can be a prodrug. In some embodiments, a composition comprising a disease-specific immunogenic neoantigenic peptide may further include an adjuvant. For example, a neoantigen peptide can be used as a vaccine. In some embodiments, the immunogenic vaccine may comprise a pharmaceutically acceptable immunogenic neoantigen peptide. In some embodiments, the immunogenic vaccine may comprise a pharmaceutically acceptable precursor to an immunogenic neoantigen peptide (such as protein, peptide, DNA and RNA). In some embodiments, the method of treatment includes administering to a subject an effective amount of an antibody that specifically recognizes an immunogenic neoantigenic peptide. In some embodiments, the method of treatment includes administering to a subject an effective amount of a soluble TCR or TCR analogue that specifically recognizes an immunogenic neoantigen peptide.

The methods described in the present invention are particularly useful in the context of personalized medicine, where immunogenic neoantigenic peptides are used to develop therapeutic agents (such as vaccines or therapeutic antibodies) for the same individual. Thus, a method of treating a disease in a subject may comprise identifying an immunogenic neoantigenic peptide in the subject according to the methods described herein; and synthesis of the peptide (or its precursor); and administering a peptide or antibody specifically recognizing the peptide to the subject. In some embodiments, the immunogenic neoantigen expression pattern may serve as an essential basis for creating patient-specific vaccines. In some embodiments, the expression pattern of an immunogenic neoantigen can serve as an essential basis for creating a vaccine for a group of patients with a particular disease. In this way, specific diseases, for example specific types of tumors, can be selectively treated in a group of patients.

In some embodiments, the peptides described in the present invention are structurally normal antigens that can be recognized by autologous anti-disease T cells in large groups of patients. In some embodiments, the antigen expression pattern of a group of subjects with a disease who are determined to have the disease expressing structurally normal neoantigens.

In some embodiments, the peptides described in the present invention comprise a first peptide containing a first neo-epitope of a protein, and a second peptide containing a second neo-epitope of the same protein, wherein the first peptide is different from the second peptide, and where the first neo-epitope contains a mutation and the second neo-epitope contains the same mutation. In some embodiments, the peptides described in the present invention comprise a first peptide containing a first neo-epitope of a first region of a protein, and a second peptide containing a second neo-epitope of a second region of the same protein, wherein the first region contains at least one amino acid of the second region, wherein the first the peptide is different from the second peptide, and wherein the first neoepitope contains a first mutation and the second neoepitope contains a second mutation. In some embodiments, the first mutation and the second mutation are the same. In some embodiments, the mutation is selected from the group consisting of a point mutation, a splice site mutation, a frameshift mutation, a read-through mutation, a gene fusion mutation, and any combination thereof.

There are many ways to obtain immunogenic neoantigens. Proteins or peptides can be produced by any method known to those skilled in the art, including expression of proteins, polypeptides or peptides using standard molecular biological techniques, isolation of proteins or peptides from natural sources, in vitro translation or chemical synthesis of proteins or peptides. Typically, such disease-specific neoantigens can be produced in vitro or in vivo . Immunogenic neoantigens can be produced in vitro as peptides or polypeptides, which can then be formulated into a personalized vaccine or immunogenic composition and administered to a subject. In vitro production of immunogenic neoantigens may comprise peptide synthesis or expression of the peptide/polypeptide from a DNA or RNA molecule in any of a variety of bacterial, eukaryotic or viral recombinant expression systems, followed by purification of the expressed peptide/polypeptide. Alternatively, immunogenic neoantigens can be produced in vivo by introducing molecules ( eg , DNA, RNA, and viral expression systems) that encode the immunogenic neoantigen into a subject, whereby the encoded immunogenic neoantigens are expressed. In some embodiments, a polynucleotide encoding an immunogenic neoantigenic peptide may be used to produce the neoantigenic peptide in vitro .

In some embodiments, the polynucleotide comprises a sequence with at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72% , 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89 %, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the polynucleotide encoding the immunogenic neoantigen.

The polynucleotide may be, for example, DNA, cDNA, PNA, CNA, RNA, single- and/or double-stranded, native or stabilized forms of polynucleotides, or combinations thereof. The nucleic acid sequences encoding the immunogenic neoantigen peptide may or may not contain introns as long as the nucleic acid sequences encode the peptide. In some embodiments , in vitro translation is used to produce the peptide.

Also contemplated are expression vectors containing sequences encoding a neoantigen, as well as host cells containing the expression vector. Expression vectors suitable for use herein may contain at least one expression control element operably linked to a nucleic acid sequence. Expression control elements are inserted into the vector to control and regulate the expression of the nucleic acid sequence. Examples of expression control elements are well known in the art and include, for example, the lac system, phage lambda operator and promoter regions, yeast promoters, and promoters derived from polyoma, adenovirus, retrovirus, or SV40. Additional functional elements include, but are not limited to, leader sequences, stop codons, polyadenylation signals, and any other sequences necessary or preferred for proper transcription and subsequent translation of nucleic acid sequences in the host system. One skilled in the art will appreciate that the correct combination of expression control elements will depend on the host system chosen. It will further be understood that the expression vector must contain additional elements necessary for the transfer and subsequent replication of the expression vector containing the nucleic acid sequence in the host system. Examples of such elements include, but are not limited to, origins of replication and a selectable marker.

Neoantigenic peptides can be in the form of RNA or cDNA molecules encoding the desired neoantigenic peptides. One or more neoantigenic peptides according to the present description can be encoded by a single expression vector. Typically, the DNA is inserted into an expression vector, such as a plasmid, in the desired direction and in the correct reading frame for expression; if necessary, the DNA can be linked to suitable transcriptional and translational regulatory control nucleotide sequences recognized by the desired host ( e.g. , bacteria), although such controls are usually available in the expression vector. The vector is then introduced into the host bacterium for cloning using standard techniques. Useful expression vectors for eukaryotic hosts, especially mammalian or human, include, for example, vectors containing expression control sequences from SV40, bovine papillomavirus, adenovirus and cytomegalovirus. Useful expression vectors for bacterial hosts include known bacterial plasmids such as those from E. coli including pCR 1, pBR322, pMB9 and derivatives thereof, wider host range plasmids such as M13 and filamentous ssDNA phages.

In embodiments, the DNA sequence encoding the polypeptide of interest can be constructed by chemical synthesis using an oligonucleotide synthesizer. Such oligonucleotides can be designed based on the amino acid sequence of the desired polypeptide and the selection of codons that are favorable in the host cell in which the polypeptide of interest is produced. Standard methods can be used to synthesize isolated polynucleotide sequences encoding an isolated polypeptide of interest.

Suitable host cells for expression of the polypeptide include prokaryotes, yeast, insect cells or higher eukaryotic cells under the control of suitable promoters. Prokaryotes include gram-negative or gram-positive organisms such as E. coli or bacilli. Higher eukaryotic cells include stable cell lines derived from mammals. Cell-free translation systems can also be used. Suitable cloning and expression vectors for use with bacterial, fungal, yeast and mammalian cell hosts are well known in the art. Various mammalian or insect cell culture systems can be used to express the recombinant protein. Exemplary mammalian host cell lines include, but are not limited to, COS-7, L cell, C127, 3T3, Chinese hamster ovary (CHO), 293, HeLa, and BHK cell lines. Mammalian expression vectors may contain non-transcribed elements, such as an origin of replication, a suitable promoter and enhanced linker for the gene to be expressed, and other 5' or 3' flanking non-transcribed sequences, and 5' or 3' non-translated sequences, such as essential sites ribosome binding site, polyadenylation site, splice donor and acceptor sites, and transcription termination sequences.

Proteins produced by the transformed host can be purified by any suitable method. Such standard methods include chromatography ( eg , ion exchange, affinity and size distribution column chromatography, and the like), centrifugation, differential solubility, or any other standard protein purification technique. Affinity tags such as hexahistidine (SEQ ID NO: 3211), maltose binding domain, influenza virus sequence, glutathione S-transferase and the like can be attached to the protein for ease of purification by passing through a column of suitable affinity. Isolated proteins can also be physically characterized using techniques such as proteolysis, nuclear magnetic resonance, and x-ray crystallography.

The vaccine may contain a substance that binds the polypeptide sequence described in the present invention. The substance may be an antibody. The antibody vaccine can be formulated using any well known techniques, carriers and excipients, as appropriate and as understood in the art. In some embodiments, the peptides described in the present invention can be used to produce neoantigen-specific therapeutic agents, such as a therapeutic antibody. For example, neoantigens can be used to enhance and/or identify an antibody that specifically recognizes neoantigens. These antibodies can be used as therapeutic agents. The antibody may be a natural antibody, a chimeric antibody, a humanized antibody, or may be an antibody fragment. The antibody may recognize one or more polypeptides described in the present invention. In some embodiments, the antibody may recognize a polypeptide having a sequence of at most 40%, 50%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69 %, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% sequence identity to the polypeptide described in the present invention . In some embodiments, the antibody may recognize a polypeptide having a sequence of at least 40%, 50%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69 %, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the polypeptide described in the present invention. In some embodiments, the antibody may recognize a polypeptide sequence that is at least 30%, 40%, 50%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68 %, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% of the polypeptide length, described in the present invention. In some embodiments, the antibody may recognize a polypeptide sequence that is at most 30%, 40%, 50%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68 %, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% of the polypeptide length, described in the present invention.

Also contemplated herein is the use of nucleic acid molecules as carriers for delivering neoantigenic peptides/polypeptides to a subject in need thereof in vivo , in the form of, for example , DNA/RNA vaccines.

In some embodiments, the vaccine is a nucleic acid vaccine. In some embodiments, neoantigens can be administered to a subject using a plasmid. Plasmids can be introduced into animal tissues by a variety of methods, for example by injection or aerosol instillation of naked DNA onto the surface of mucous membranes such as the nasal and pulmonary mucosa. In some embodiments, physical delivery, such as a gene gun, may be used. The exact choice of expression vector may depend on which peptides/polypeptides will be expressed and is within the skill of those skilled in the art.

In some embodiments, the nucleic acid encodes an immunogenic peptide or a peptide precursor. In some embodiments, the nucleic acid vaccine comprises flanking sequences encoding an immunogenic peptide or a peptide precursor. In some embodiments, the nucleic acid vaccine contains more than one immunogenic epitope. In some embodiments, the nucleic acid vaccine is a DNA-based vaccine. In some embodiments, the nucleic acid vaccine is an RNA vaccine. In some embodiments, the RNA vaccine contains mRNA. In some embodiments, the RNA vaccine contains naked mRNA. In some embodiments, the RNA vaccine contains modified mRNA ( eg , protamine-protected mRNA, mRNA containing a 5' CAP structure, or mRNA containing modified nucleotides). In some embodiments, the RNA vaccine contains single-stranded mRNA.

The polynucleotide may be substantially pure or contained in a suitable vector or delivery system. Suitable vectors and delivery systems include virus, such as those based on adenovirus, vaccinia virus, retroviruses, herpesvirus, adeno-associated virus, or hybrids containing elements of more than one virus. Non-viral delivery systems include cationic fats and cationic polymer ( eg cationic liposomes.

One or more neoantigenic peptides can be encoded and expressed in vivo using a virus-based system. Viral vectors can be used as recombinant vectors herein, where part of the viral genome is removed to introduce new genes without destroying the infectivity of the virus. The viral vector of the present disclosure is a non-pathogenic virus. In some embodiments, the viral vector has tropism for a particular cell type in a mammal. In another embodiment, the viral vector of the present disclosure is capable of infecting professional antigen presenting cells such as dendritic cells and macrophages. In yet another embodiment of the present disclosure, the viral vector is capable of infecting any cell of a mammal. The viral vector can also infect tumor cells. Viral vectors used herein include, but are not limited to, poxvirus such as vaccinia virus, avipox virus, fowlpox virus and highly attenuated vaccinia virus (Ankara or MVA), retrovirus, adenovirus, baculovirus and the like.

The vaccine can be delivered in different ways. Routes of delivery may include oral (including buccal and sublingual), rectal, nasal, topical, transdermal patch, pulmonary, vaginal, suppository or parenteral (including intramuscular, intraarterial, intrathecal, intradermal, intraperitoneal, subcutaneous and intravenous) administration, or in the form, suitable for administration by aerosolization, inhalation or insufflation. General information on drug delivery systems can be found in Ansel et al., Pharmaceutical Dosage Forms and Drug Delivery Systems (Lippencott Williams & Wilkins, Baltimore Md. (1999). The vaccine described in the present invention can be administered into a muscle or can be injected by intradermal or subcutaneous injection or transdermally, such as by iontophoresis. Epidermal administration of the vaccine may be used.

In some cases, the vaccine may also be formulated to be administered through the nasal passages. Formulations suitable for nasal administration where the carrier is solid may include a coarse powder having a particle size, for example, in the range of about 10 to about 500 microns, which is administered in the same manner as snuff is administered, i.e., by rapid inhalation through the nasal passage from a container of powder held close to the nose. The formulation may be a nasal spray, nasal drops, or an aerosol administered via a nebulizer. The composition may include aqueous or oily solutions of the vaccine.

The vaccine may be a liquid preparation such as a suspension, syrup or elixir. The vaccine may also be a preparation for parenteral, subcutaneous, intradermal, intramuscular or intravenous administration ( eg injection), such as a sterile suspension or emulsion.

The vaccine may include material for a single immunization or may include material for multiple immunizations (ie, a set of “multiple doses”). The inclusion of a preservative is preferable in multiple dose regimens. As an alternative (or in addition) to including a preservative in multi-dose compositions, the compositions may be contained in a container having an aseptic adapter for removing the material.

The vaccine can be given in a dose of approximately 0.5 ml, although children can be given a half dose (ie approximately 0.25 ml). Sometimes the vaccine can be administered in a higher dose, for example approximately 1 ml.

The vaccine can be administered in the form of 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 or more course regimens. Sometimes the vaccine is administered as a 1, 2, 3 or 4-course regimen. Sometimes the vaccine is administered as a 1-course regimen. Sometimes the vaccine is administered as a 2-course regimen.

The administration of the first dose and the second dose may be separated by approximately 0 days, 1 day, 2 days, 5 days, 7 days, 14 days, 21 days, 30 days, 2 months, 4 months, 6 months, 9 months, 1 year, 1.5 years, 2 years, 3 years, 4 years or more.

The vaccine described in the present invention may be administered every 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 or more years. Sometimes, the vaccine described in the present invention is administered every 2, 3, 4, 5, 6, 7 or more years. Sometimes, the vaccine described in the present invention is administered every 4, 5, 6, 7 or more years. Sometimes, the vaccine described in the present invention is administered once.

The dosage examples are not limiting and are used only to illustrate specific dosage regimens for administering the vaccine described in the present invention. the effective amount for use in humans can be determined in animal models. For example, a human dose may be formulated to achieve blood, liver, local and/or gastrointestinal concentrations that have been found to be effective in animals. Based on animal data and other types of similar data, those skilled in the art can determine effective amounts of the vaccine composition suitable for humans.

An effective amount relative to an agent or combination of agents will generally mean dosage ranges, routes of administration, formulations, etc., that have been recommended or approved by any of the various medical or pharmaceutical regulatory or advisory organizations (e.g., FDA, AMA) or by the manufacturer or supplier.

In some aspects, the vaccine and kit described in the present invention can be stored at 2°C to 8°C. In some cases, the vaccine is not stored frozen. In some cases, the vaccine is stored at temperatures of -20°C or -80°C. In some cases, the vaccine is stored in an area protected from sunlight.

Sets

The neoantigen therapeutic agent described in the present invention may be presented in kit form along with instructions for use. Typically, the kit will include the desired neoantigen therapeutic agent in a container, in a unit dosage form, and instructions for use. The kit may also include additional therapeutic agents, for example, cytokines, lymphokines, immune checkpoint inhibitors, antibodies. Other kit components that may also be desirable include, for example, a sterile syringe, activator doses, and other desired excipients.

The present invention also provides kits and finished products for use with one or more of the methods described in the present invention. The kits may contain one or more neoantigenic polypeptides containing one or more neoepitopes. The kits may also contain nucleic acids that encode one or more peptides or proteins described herein, antibodies that recognize one or more peptides described herein, or APC-based cells activated by one or more peptides described herein. invention. The kits may additionally contain adjuvants, reagents and buffers necessary for vaccine production and delivery.

The kits may also include a carrier, package or container that is divided into compartments to receive one or more containers, such as vials, ampoules and the like, where each of the containers contains one of the individual elements, such as peptides and adjuvants, to be used in the method described in the present invention. Suitable containers include, for example, bottles, vials, syringes and tubes. Containers can be made from various materials such as glass or plastic.

The finished products shown here contain packaging materials. Examples of pharmaceutical packaging materials include, but are not limited to, blister packs, bottles, tubes, pouches, containers, vials, and any packaging material suitable for the composition selected and the intended mode of administration and treatment. The kit typically includes labels indicating the contents and/or instructions for use, and package inserts with instructions for use. A set of instructions is also usually included.

The present description will be described in more detail using specific examples. The following examples are offered for illustrative purposes and are not intended to limit the present description in any way. Those skilled in the art will readily recognize many non-critical parameters that may be changed or modified to provide alternative embodiments in accordance with the present disclosure. All patents, patent applications and printed publications listed herein are incorporated herein by reference in their entirety.

EXAMPLES

These examples are presented for illustrative purposes only and do not limit the scope of the claims presented here.

Example 1 – Calling CD4 responses ⁺ and CD8 ⁺ T cells

In vitro T cell induction is used to expand neoantigen-specific T cells. Mature professional APCs are obtained for these tests as follows. Monocytes are enriched from healthy human donor PBMC using a bead-based kit (Miltenyi). Enriched cells were seeded in GM-CSF and IL-4 to induce immature DCs. After 5 days, immature DCs are incubated at 37°C with peptide pools for 1 hour, then a cytokine maturation cocktail (GM-CSF, IL-1β, IL-4, IL-6, TNFα, PGE1β) is added. Peptide pools can include multiple mutations, both shortmer and longmer, to expand CD8 ⁺ and CD4 ⁺ T cells, respectively. Cells are incubated at 37°C until DC maturation.

After DC maturation, PBMCs (either pooled or enriched for T cells) are added to mature dendritic cells with proliferation cytokines. Cultures are monitored for peptide-specific T cells using a combination of functional assays and/or tetramer staining. Parallel immunogenicity assays with modified and original peptides allow comparison of the relative efficiency with which the peptides expand peptide-specific T cells.

Example 2 - Tetramer Color Assay

The MHC tetramer is purchased or produced locally and used to measure peptide-specific T cell expansion in immunogenicity assays. For evaluation, the tetramer is added to 1x10 ⁵ cells in PBS containing 1% FCS and 0.1% sodium azide (FACS buffer) according to the manufacturer's instructions. Cells are incubated in the dark for 20 minutes at room temperature. Antibodies specific for T cell markers such as CD8 are then added at the final concentration suggested by the manufacturer and the cells are incubated in the dark at 4°C for 20 minutes. Cells are washed with cold FACS buffer and resuspended in buffer containing 1% formaldehyde. Cell information was obtained on a FACS Calibur instrument (Becton Dickinson) and analyzed using Cellquest software (Becton Dickinson). To analyze tetramer-positive cells, lymphocyte gates are taken from forward and side scatter plots. Data are presented as the proportion of cells that were CD8 ⁺ /tetramer ⁺ .

Example 3 - Intracellular Cytokine Staining Assay

In the absence of well-established tetramer staining to identify antigen-specific T cell populations, antigen specificity can be assessed using assessment of cytokine production using well-established flow cytometry assays. Briefly, T cells are stimulated with a peptide of interest and compared to a control. Following stimulation, cytokine production by CD4 ⁺ T cells (eg, IFNγ and TNFα) is assessed by intracellular staining. These cytokines, especially IFNγ, can be used to identify stimulated cells. In FIG. 11 depicts FACS analysis of antigen-specific induction of IFNγ and TNFα levels in CD4+ cells from a healthy HLA-A02:01 donor stimulated with APCs loaded with or without GATA3 neoORF peptide.

Example 4 - ELISPOT Analysis

Peptide-specific T cells were functionally enumerated using an ELISPOT assay (BD Biosciences), which measures IFNγ release from T cells on a single-cell basis. Target cells (T2 or HLA-A0201 transfected with C1R) were injected with 10 μM peptide for 1 hour at 37°C and washed three times. 1x10 ⁵ peptide-added targets are co-cultured in wells of an ELISPOT plate with different concentrations of T cells (5x10 ² to 2x10 ³ ) taken from the immunogenic culture. Plates were processed according to the manufacturer's protocol and analyzed on an ELISPOT reader (Cellular Technology Ltd.) using the supplied software. Spots corresponding to the number of IFNγ-producing T cells are indicated as the absolute number of spots by the number of T cells plated. T cells expanded on modified peptides are tested not only for their ability to recognize targets to which the modified peptide has been introduced, but also for their ability to recognize targets to which the original peptide has been added. In FIG. 35 is a graph showing antigen-specific induction of IFNγ. IFNγ levels of two mock-transduced or transduced samples with a lentiviral expression vector encoding the GATA3 neoORF peptide are shown.

Example 5 - CD107 Staining Assay

CD107a and b are expressed on the cell surface of CD8 ⁺ T cells, followed by activation by a recognized peptide. Protease-containing T cell vacuoles have a fat bilayer that contains lysosome-associated membrane glycoproteins (“LAMPs”), which include the molecules CD107a and b. When cytotoxic T cells are activated through the T cell receptor, the membranes of these protease-containing vacuoles are mobilized and fuse with the plasma membrane of the T cell. The contents of the granules are released and this leads to the death of the target cell. As the vacuole membrane fuses with the plasma membrane, C107a and b appear on the cell surface and are therefore markers of degranulation. Since degranulation by CD107a and b staining is indicated on a single-cell basis, the assay is used for functional enumeration of peptide-specific T cells. To perform the assay, the peptide is added to HLA-A02:01-transfected C1R cells to a final concentration of 20 μM, the cells are incubated for 1 hour at 37°C and washed three times. 1x10 ⁵ C1R cells with added peptide are aliquoted into tubes, and antibodies specific for CD107a and b are added to the final concentration suggested by the manufacturer (Becton Dickinson). Antibodies are added before the T cells are added to “catch” the CD107 molecules when they temporarily appear on the surface during the assay. 1x10 ⁵ T cells from the immunogenic culture are then added and the samples are incubated for 4 hours at 37°C. T cells are then further stained for additional cell surface molecules such as CD8 and information is obtained on a FACS Calibur instrument (Becton Dickinson). Data are analyzed using the supplied Cellquest program and are shown as the proportion of CD8 ⁺ /CD107a and b ⁺ cells. In FIG. 34 is a graph showing the antigen-specific induction of the cytotoxic marker CD107a. The proportion of CD107a+ cells from the total number of CD8+ cells from two samples mock-transduced or transduced with a lentiviral expression vector encoding the GATA3 neoORF peptide is shown.

Example 6 - Cytotoxic Assays

Cytotoxic activity is measured using Method 1 or Method 2. Method 1 involves a chromium release assay. T2 target cells are labeled with Na ⁵¹ Cr for 1 hour at 37°C and washed, 5x1035 x 10 ³ T2 target cells are then added to varying numbers of T cells from the immunogenic culture. Chromium release was measured from the supernatant collected after 4 hours of incubation at 37°C. The proportion of specific lysis is calculated as:

Equation 10. Experimental release-spontaneous release/Total release-spontaneous release x 100.

In Method 2, cytotoxic activity is measured by detecting cleaved caspase 3 in target cells via flow cytometry. Target cancer cells are engineered to express the mutant peptide along with the appropriate MHC-I allele. Mock-transduced target cells (i.e., not expressing the mutant peptide) are used as negative controls. Cells are labeled with CFSE to distinguish them from stimulated PBMCs used as effector cells. Target and effector cells were co-cultured for 6 hours prior to collection. Intracellular staining is performed to detect the cleaved form of caspase 3 in CFSE-positive target cancer cells. The proportion of specific lysis is calculated as:

Equation 11. Experimental caspase 3 cleavage/spontaneous caspase 3 cleavage (measured in the absence of mutant peptide expression) x 100.

Cytotoxicity assay by Method 2 is presented in the Materials and Methods section of Example 25 of the present invention.

Example 7 - Improved CD8 ⁺ T Cell Responses in Vivo Using Longmers and Shortmers Sequentially

Vaccination with longmer peptides can induce both CD4 ⁺ and CD8 ⁺ T cell responses, depending on the processing and presentation of the peptides. Vaccination with minimal short-term epitopes focuses on generating CD8 ⁺ T cell responses but does not require peptide processing prior to antigen presentation. As such, any cell can easily present an epitope, not just professional antigen-presenting cells (APCs). This can lead to tolerance of T cells that contact healthy cells presenting antigens as part of peripheral tolerance. To circumvent this, prime immunization with Longmer primes CD8 ⁺ T cells only with APCs that can process and present peptides. Subsequent immunizations enhance CD8 ⁺ T cell responses.

In vivo immunogenicity assays

Nineteen 8- to 12-week-old female C57BL/6 mice (Taconic Biosciences) were randomly assigned to treatment groups upon admission. Animals are acclimatized for three (3) days before the start of the study. Animals are fed sterile LabDiet™ 5053 rodent food and sterile water is provided ad libitum . Animals in Group 1 serve as an adjuvant-only control and are administered polyinosinic:polycytidylic acid (polyI:C) alone at a dose of 100 μg in a 0.1 ml volume by subcutaneous injection (SC) on days 0, 7, and 14 Animals in group 2 were administered 50 μg of each of the six long-mer peptides (described below) along with polyI:C at a dose of 100 μg s.c. in a volume of 0.1 ml on days 0, 7 and 14. Animals in group 3 were administered 50 μg of each of the six long-term peptides (described below) together with polyI:C at a dose of 100 μg s.c. in a volume of 0.1 ml on day 0 and molar equivalents of the corresponding shortmer peptides (described below) together with polyI:C at a dose of 100 μg s.c. in a volume of 0.1 ml on days 7 and 14. Animals are weighed and general health is monitored daily. Animals are sacrificed with a CO2 overdose on day 21 of study completion if the animal loses >30% of its body weight compared to day 0; or if the animal is found in agony. At sacrifice, spleens are collected and processed into single-cell suspensions using standard protocols. Briefly, spleens were mechanically disrupted through a 70 μM filter, pelleted, and lysed with ACK lysis buffer (Sigma) before resuspension in cell culture medium.

Peptides

Six previously identified mouse neoantigens are used based on their demonstrated ability to induce CD8 ⁺ T cell responses. For each neoantigen, a shortmer (8-11 amino acids) corresponding to the minimal epitope was determined. A longmer corresponding to 20-27 amino acids surrounding the mutation is used.

ELISPOT

The ELISPOT assay (Mouse IFNγ ELISPOT Reasy-SET-Go; EBioscience) was performed according to the kit protocol. Briefly, the day before analysis, 96-well filter plates (0.45 μM hydrophobic PVDF membrane; EMD Millipore) are activated (35% EtOH), washed (BFBS), and coated with immobilized antibody (1:250; 4°CO /N). On the day of analysis, wells are washed and blocked (medium; 2 hours at 37°C). Approximately 2x10 ⁵ cells per 100 μl are added to the wells along with 100 μl of 10 mM test peptide pool (shortmer) or PMA/ionomycin positive control antigen or vehicle. Cells are incubated with antigen overnight (16-18 hours) at 37°C. The next day, the cell suspension is removed and the wells are washed once with PBS and twice with deionized water. For all wash steps in the remainder of the assay, wells are soaked for 3 minutes at each wash step. The wells are then washed three times with wash buffer (BFBS+0.05% Tween-20) and identifying antibody (1:250) is added to all wells. The plates are incubated for two hours at room temperature. The identifying antibody solution is removed and the wells are washed three times with buffer. Avidin-HRP (1:250) was added to all wells and the plates were incubated for one hour at room temperature. The conjugate solution is removed and the wells are washed three times with wash buffer, then once with PBS. Substrate (3-amino-9-ethylcarbazole, 0.1 M in acetate buffer, H ₂ O ₂ ) is added to all wells and spot development is monitored (approximately 10 minutes). The substrate reaction is stopped by washing the wells with water and the plates are air dried overnight. The plates were analyzed on an ELISPOT reader (Cellular Technology Ltd.) using the supplied software. Spots corresponding to the number of IFNγ-producing T cells are shown as the absolute number of spots per number of T cells plated.

Example 8 - Determination of GATA3 neoORF peptides by mass spectrometry

293T cells were transduced with a lentiviral vector encoding different regions of the GATA3 neoORF-encoded peptides. 50-700 million transduced cells expressing peptides encoded by the GATA3 neoORF sequence are cultured and the peptides are eluted from HLA-peptide complexes using an acid wash. The eluted peptides are then analyzed by MS/MS. For 293T cells expressing HLA-A02:01 protein, the peptides VLPEPHLAL (SEQ ID NO: 3212), SMLTGPPARV (SEQ ID NO: 3213) and MLTGPPARV (SEQ ID NO: 3214) were determined by mass spectrometry ( FIG. 5 ). For 293T cells expressing HLA-B07:02 protein, the peptides KPKRDGYMF (SEQ ID NO: 3215) and KPKRDGYMFL (SEQ ID NO: 3216) were determined by mass spectrometry ( FIG. 5 ). For 293T cells expressing HLA-B08:01 protein, the ESKIMFATL peptide (SEQ ID NO: 3217) was determined by mass spectrometry ( FIG. 5 ).

Example 9 - GATA3 neoORF produces strong epitopes on multiple alleles.

A variety of peptides containing the neo-epitopes in Table 4 below are expressed or loaded into antigen presenting cells (APC). Then mass spectrometry is carried out and the affinity of neoepitopes with the indicated HLA alleles and the stability of neoepitopes with HLA alleles are determined.

Table 4 lists typical GATA3 neoORF epitopes produced on multiple alleles

Allele Neoepitope Common (C) or variable (V) area Observed MHC affinity (nM) Observed MHC stability (h) A02.01 AIQPVLWTT (SEQ ID NO: 3218) V 8 1.5 MLTGPPARV (SEQ ID NO: 3219) C eleven 5.8 SMLTGPPARV (SEQ ID NO: 3220) C 14 21.7 VLPEPHLAL (SEQ ID NO: 3221) V 16 1.1 TLQRSSLWCL (SEQ ID NO: 3222) C 118 0.5 YMFLKAESKI (SEQ ID NO: 3223) C 141 0.6 ALQPLQPHA (SEQ ID NO: 3224) V 604 1.5 A03:01 KIMFATLQR (SEQ ID NO: 3225) C 3 5.6 VLWTTPPLQH (SEQ ID NO: 3226) V 16 0.3 YMFLKAESK (SEQ ID NO: 3227) C 80 0.3 A11:01 KIMFATLQR (SEQ ID NO: 3228) C 23 8.9 VLWTTPPLQH (SEQ ID NO: 3229) V 4539 0 YMFLKAESK (SEQ ID NO: 3230) C 1729 0 A24:02 MFLKAESKI (SEQ ID NO: 3231) C 332 0.2 YMFLKAESKI (SEQ ID NO: 3232) C 6,995 1.2 B07:02 FATLQRSSL (SEQ ID NO: 3233) C 14 0.7 EPHLALQPL (SEQ ID NO: 3234) V 17 7.2 KPKRDGYMF (SEQ ID NO: 3235) C 28 8.6 KPKRDGYMFL (SEQ ID NO: 3236) C 98 3.3 QPVLWTTPPL (SEQ ID NO: 3237) V 109 1.4 GPPARVPAV (SEQ ID NO: 3238) C 221 1.6 MFATLQRSSL (SEQ ID NO: 3239) V 267 0 B08:01 EPHLALQPL (SEQ ID NO: 3240) V 12 0 ESKIMFATL (SEQ ID NO: 3241) C 18 1.3 FLKAESKIM (SEQ ID NO: 3242) C 22 1.2 FATLQRSSL (SEQ ID NO: 3243) C 27 0 YMFLKAESKI (SEQ ID NO: 3244) C 32 0.4 IMKPKRDGYM (SEQ ID NO: 3245) C 33 0.4 MFATLQRSSL (SEQ ID NO: 3246) C 53 0 FLKAESKIMF (SEQ ID NO: 3247) C 82 0 LHFCRSSIM (SEQ ID NO: 3248) C 119 0

Example 10 – Multiple Neoepitopes Induce CD8+ T Cell Responses

PBMC samples from a human donor are used to perform antigen-specific T cell induction. CD8 ⁺ T cell induction is analyzed after T cell production. Cell samples can be taken at different time points for analysis. pMHC multimer is used to monitor the proportion of antigen-specific CD8 ⁺ T cells in induction cultures. On FIG. 9A-9C and 10A-10B depict exemplary results showing the proportion of antigen-specific memory CD8 ⁺ T cells induced with both SMLTGPPARV (SEQ ID NO: 3249) and MLTGPPARV (SEQ ID NO: 3250), respectively. In FIG. 9A depicts an exemplary result of a T cell response assay using PBMC from 6 different healthy donors, showing the proportion of antigen-specific CD8 ⁺ T cells that respond to the MLTGPPARV (SEQ ID NO: 3251) peptide analyzed by flow cytometry after stimulation or induction. An increase in the proportion of antigen-specific T cells is observed. In FIG. 9B depicts an exemplary result of a T cell response assay using PBMC from a healthy donor, showing the proportion of antigen-specific CD8 ⁺ T cells that respond to the SMLTGPPARV (SEQ ID NO: 3252) peptide analyzed by flow cytometry after stimulation or induction. An increase in the proportion of antigen-specific T cells is observed. Of the five healthy donors tested, 4 showed an increase in the proportion of antigen-specific CD8 ⁺ T cells that respond to the MLTGPPARV (SEQ ID NO: 3253) peptide. T cell response analysis using PBMC from 3 different healthy donors showed an increase in the proportion of antigen-specific CD8 ⁺ T cells that respond to VLPEPHLAL (SEQ ID NO: 3254) peptide analyzed by flow cytometry after stimulation or induction in one of the three donors . In FIG. 9C depicts a typical T cell response using PBMC from HLA-A02:01, HLA-A03:01 HLA-A11:01, HLA-B07:02 and HLA-B08:01 healthy donors, showing the proportion of antigen-specific CD8 ⁺ T cells that respond to SMLTGPPARV (SEQ ID NO: 3255), MLTGPPARV (SEQ ID NO: 3256), KIMFATLQR (SEQ ID NO: 3257), KPKRDGYMFL (SEQ ID NO: 3258), KPKRDGYMF (SEQ ID NO: 3259 ) or ESKIMFATL (SEQ ID NO: 3260) peptide analyzed by flow cytometry after stimulation or induction. In FIG. 10A depicts an exemplary T cell response using PBMC from an HLA-B07:02 healthy donor, showing the proportion of antigen-specific CD8 ⁺ T cells that respond to the KPKRDGYMFLKAESKIMFATLQRSSLWCLCSNH stimulatory peptide (SEQ ID NO: 3261) (KPKRDGYMF minimal epitopes analyzed ( SEQ ID NO: 3262) and KPKRDGYMFL (SEQ ID NO: 3263)). In FIG. 10B depicts an exemplary T cell response using PBMC from an HLA-A02:01 healthy donor, showing the proportion of antigen-specific CD8 ⁺ T cells that respond to the stimulatory peptide SMLTGPPARVPAVPFDLH (SEQ ID NO: 3264) (SMLTGPPARV minimal epitopes analyzed ( SEQ ID NO: 3265) and MLTGPPARV (SEQ ID NO: 3266)).

Example 11 - Cytotoxicity Assay of Induced T Cells

Cytotoxicity assays are used to evaluate whether induced T cell cultures can kill antigen-expressing tumor colonies. In this example, the expression of active caspase 3 on live and dead tumor cells is measured to quantify early cell death and dead tumor cells. In FIG. 33 induced CD8 ⁺ responses are capable of killing antigen-expressing tumor targets. The proportion of live caspase-A positive target cells in two samples, mock-transduced or transduced with a lentiviral expression vector encoding the GATA3 neoORF peptide, is shown.

Example 12 - Peptide Synthesis

The peptides in Table 5 below were synthesized and purified. Predicted and determined molecular weights are shown. Crude impurities and final impurities for the indicated peptides are also shown.

Table 5

ID Sequences Theoretical MM Certain MM Unrefined impurities Final impurities L7 EPCSMLTGPPARVPAVPFDLH (SEQ ID NO: 3267) 2234.6 2235.2 47% 97.4% L8 GPPARVPAVPFDLHFCRSSIMKPKRD (SEQ ID NO: 3268) 2922.5 2923.5 51% 99.5% L9 LHFCRSSIMKPKRDGYMFLKAESKI (SEQ ID NO: 3269) 2986.6 2987.7 37% 98.1% L10 KPKRDGYMFLKAESKIMFATLQR (SEQ ID NO: 3270) 2759.3 2760.3 53% 92.6% L10b KPKRDGYMFLKAESKIMFAT (SEQ ID NO: 3271) 2361.9 2362.4 41% 97.6% L10b-4K KKKKKPKRDGYMFLKAESKIMFAT (SEQ ID NO: 3272) 2874.5 2874.9 57% 85.7% L10c KPKRDGYMFLKAESKI (SEQ ID NO: 3273) 1911.3 1911.4 69% 98.4% L11 FLKAESKIMFATLQRSSLWCL (SEQ ID NO: 3274) 2473.0 2473.0 66% 86% L11b YMFLKAESKIMFATLQRSSLWCL (SEQ ID NO: 3275) 2767.4 2767.2 37% 80.0% L11c YMFLKAESKIMFATLQRSS (SEQ ID NO: 3276) 2251.7 2252.4 38% 95.9% L11c-4K KKKKYMFLKAESKIMFATLQRSS (SEQ ID NO: 3277) 2764.3 2764.8 45% 82.0% L11d KAESKIMFATLQRSSLWCL (SEQ ID NO: 3278) 2212.7 2213.0 32% 96.6% L11d-4K KKKKKAESKIMFATLQRSSLWCL (SEQ ID NO: 3279) 2725.3 2725.8 28% 82.3% L11e DGYMFLKAESKIMFAT (SEQ ID NO: 3280) 1852.2 1852.3 39% 91.6% L11f FLKAESKIMFATLQRS (SEQ ID NO: 3281) 1870.2 1870.2 62% 95.0% L11g ESKIMFATLQRSSLWC (SEQ ID NO: 3282) 1900.2 1900.2 41% 91.0% L11h FLKAESKIMFATLQR (SEQ ID NO: 3283) 1783.1 1783.8 35% 84% L11i ESKIMFATLQRSSL (SEQ ID NO: 3284) 1610.87 1610.80 75% 97% L12 KIMFATLQRSSLWCLCSNH (SEQ ID NO: 3285) 2238.7 2238.6 31% 68.0% L12-4K KKKKKIMFATLQRSSLWCLCSNH (SEQ ID NO: 3286) 2751.3 2751.8 49% 75.7% L12b MFATLQRSSLWCLCSNH (SEQ ID NO: 3287) 1997.3 1997.8 47% 98.7% L12b-4K KKKKMFATLQRSSLWCLCSNH (SEQ ID NO: 3288) 2510 2510.4 39% 92.7% L12c MFATLQRSSLWCLC (SEQ ID NO: 3289) 1659.0 1659 57% 90% L12d TLQRSSLWCLCSNH (SEQ ID NO: 3290) 1647.9 1648 60% 99% L14 SMLTGPPARVPAVPFDLH (SEQ ID NO: 3291) 1905.2 1905.3 64.5% 99.5% L15 KPKRDGYMFLKAESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 3292) 3890.58 3891 37% 96% L15b KPKRDGYMFLKAESKIMFATLQRSSLWCL (SEQ ID NO: 3293) 3449.1 3449.5 42% 87% L15c DLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWCL (SEQ ID NO: 3294) 4639.5 4640.4 40% 90%

Example 13 - Solubility Tests of Synthetic GATA3 neoORF Peptide

The solubility of each peptide in Table 6 below is tested in different specified solutions. SS=sodium succinate. Formulation A tested included 4% DMSO, 5 mM sodium succinate (SS) in D5W. Composition B tested included no DMSO, 5 mM SS in D5W. Composition C tested included no DMSO, 0.25 mM SS in D5W. The synthesis of L15 33mer, which contains two cysteines, is carried out using the creation of pseudoproline building blocks through the conjugation of ES, AT and SS side chains in the sequence. This allows L15 to be purified to 95% purity and prevents aggregation during solid-phase peptide synthesis.

Table 6 below lists the peptide solubilities

ID Subsequence A.A. 5 mM SS in D5W wt/4% DMSO 0.5 mM SS in D5W wt/ 4% DMSO 0.75 mM SS in D5W wt/4% DMSO 0.25 mM SS in D5W wt/ 4% DMSO Poly
ICLC
+ 0.5 mM SS in D5W wt/ 4% DMSO Poly
ICLC
+ 0.75 mM SS in D5W wt/ 4% DMSO Poly
ICLC
+ 0.25 mM SS in D5W wt/ 4% DMSO Poly
ICLC
+5 mM SS in D5W wt/ 4% DMSO 0.25mM SS in D5W wt/0 DMSO Poly
ICLC
+ 0.25 mM SS in D5W wt/0 DMSO 5mM SS in D5W wt/0 DMSO Poly
ICLC
+ 5 mM SS in D5W wt/0 DMSO 7 EPCSMLTGPP
ARVPAVPFDLH
(SEQ ID NO: 3295) 21 Yes Yes Yes Yes Yes Yes Yes Yes Yes Yes Yes 14 SMLTGPPAR
VPAVPFDLH
(SEQ ID NO: 3296) 18 Yes Yes Yes Yes Yes Yes Yes Yes Yes Yes 8 GPPARVPAVPFDL
HF C RSSIMKPKRD
(SEQ ID NO: 3297) 26 Yes Yes Yes Yes Yes Yes Yes Yes Yes Yes Yes 9 LHF C RSSIMKPKR
DGYMFLKAESKI
(SEQ ID NO: 3298) 25 Yes Yes Yes Yes Yes Yes Yes Yes Yes 10 KPKRDGYMFLKA
ESKIMFATLQR
(SEQ ID NO: 3299) 23 Yes Yes No No eleven FLKAESKIMFA
TLQRSSLWCL
(SEQ ID NO: 3300) 21 No 12 KIMFATLQRS
SLWCLCSNH
(SEQ ID NO: 3301) 19 10b KPKRDGYMFL
KAESKIMFAT
(SEQ ID NO: 3302) 20 Yes Yes Yes No No 11b YMFLKAESKIMF
ATLQRSSLWCL
(SEQ ID NO: 3303) 23 11c YMFLKAESKI
MFATLQRSS
(SEQ ID NO: 3304) 19 Yes Yes Yes No No 11d KAESKIMFA
TLQRSSLWCL
(SEQ ID NO: 3305) 19 Yes Yes Yes Yes Yes 12b MFATLQRSS
LWCLCSNH
(SEQ ID NO: 3306) 17 Yes Yes Yes No No 10b-4K KKKKKPKRDGYM
FLKAESKIMFAT
(SEQ ID NO: 3307) 25 Yes 11c-4K KKKKYMFLKAES
KIMFATLQRSS
(SEQ ID NO: 3308) 23 11d-4K KKKKKAESKIMF
ATLQRSSLWCL
(SEQ ID NO: 3309) 23 Yes 12b-4K KKKKMFATLQR
SSLWCLCSNH
(SEQ ID NO: 3310) 20 Yes 12-4K KKKKKIMFATLQ
RSSLWCLCSNH
(SEQ ID NO: 3311) 23 Yes L10c KPKRDGYMF
LKAESKI
(SEQ ID NO: 3312) 16 Yes Yes Yes Yes Yes Yes Yes L11e DGYMFLKAE
SKIMFAT
(SEQ ID NO: 3313) 16 No No L11f FLKAESKIM
FATLQRS
(SEQ ID NO: 3314) 16 Yes Yes Yes Yes L11g ESKIMFATL
QRSSLWC
(SEQ ID NO: 3315) 16 No Yes No L11h FLKAESKIM
FATLQR
(SEQ ID NO: 3316) 15 L11i ESKIMFATL
QRSSL
(SEQ ID NO: 3317) 14 Yes Yes L12c MFATLQR
SSLWCLC
(SEQ ID NO: 3318) 14 No No L12d TLQRSSLW
CLCSNH
(SEQ ID NO: 3319) 14 Yes Yes Yes Yes Yes L15 KPKRDGYMFLKAE
SKIMFATLQRSSL
WCLCSNH
(SEQ ID NO: 3320) 33 No Yes Yes L15b KPKRDGYMFLK
AESKIMFATL
QRSSLWCL
(SEQ ID NO: 3321) 29 L15c DLHFCRSSIMKPK
RDGYMFLKAESKI
MFATLQRSSLWCL
(SEQ ID NO: 3322) 39 10b-4K KKKKKPKRDGYM
FLKAESKIMFAT
(SEQ ID NO: 3323) 24 Yes 11c-4K KKKKYMFLKAES
KIMFATLQRSS
(SEQ ID NO: 3324) 23 11d-4K KKKKKAESKIMF
ATLQRSSLWCL
(SEQ ID NO: 3325) 23 Yes 12b-4K KKKKMFATLQR
SSLWCLCSNH
(SEQ ID NO: 3326) 21 Yes 12-4K KKKKKIMFATLQ
RSSLWCLCSNH
(SEQ ID NO: 3327) 23 Yes

Example 14 - Design of Pools of Synthetic GATA3 neoORF Peptide for Administration to Subjects

Different pools of the indicated GATA3 peptides are created according to Table 7 below. For example, “Design 1” contains three peptide pools, where pool 1 contains three peptides (i.e., L7, L8 and L14), pool 2 contains two peptides (i.e., L9 and L10c) and pool 3 contains two peptide (ie, L15 and L11f). For example, “Design 6” contains two peptide pools, where pool 1 contains four peptides (i.e., L7, L8, L9 and L14) and pool 2 contains two peptides (i.e., L15 and L11f). For example, “Design 10” contains four peptide pools, where pool 1 contains five peptides (i.e., L7, L8, L9, L10c and L14), pool 2 contains one peptide (i.e., L15), pool 3 contains one peptide (ie, L11f) and pool 4 contains one peptide (ie, L11i). The concentration of each peptide in the pools can be modified by one skilled in the art of producing peptide formulations. Table 7 below lists a description of the GATA3 pool designs.

Table 7

# Design 1 Design 2 Design 3 Design 4 Design 5 Design 6 Design 7 Design 8 Design 9 Design 10 Design 11 3 pools 3 pools 3 pools 2 pools 4 pools 2 pools 3 pools 4 pools 3 pools 4 pools 3 pools 1 L7 1 1 1 1 1 1 1 1 1 1 1 2 L14 1 1 1 1 1 1 1 1 1 1 1 3 L8 1 2 2 1 2 1 2 1 1 1 1 4 L9 2 2 2 1 2 1 2 1 1 1 1 5 L15 3 3 3 2 4 2 3 2 2 2 2 6 L11f 3 3 3 2 3 2 3 3 3 3 N/A 7 L10c 2 2 1 1 2 N/A N/A 4 1 1 1 8 L11i N/A N/A N/A N/A N/A N/A N/A N/A N/A 4 3

Example 15 - Synthesis of GATA3 neoORF peptide

A typical synthesis is carried out with a target of 700 mg of crude product. The following Fmoc amino acids with suitable side chain protection are used to construct the L7 peptide (EPCSMLTGPPARVPAVPFDLH (SEQ ID NO: 3328)): Fmoc-Ala-OH ∙ H ₂ O, Fmoc-Cys(Trt)-OH, Fmoc-Asp(OtBu) -OH, Fmoc-Glu(OtBu)-OH, Fmoc-Gly-OH, Fmoc-Leu-OH, Fmoc-Met-OH, Fmoc-Pro-OH, Fmoc-Arg(Pbf)-OH, Fmoc-Ser(tBu )-OH, Fmoc-Thr(tBu)-OH and Fmoc-Val-OH. The C-terminal histidine is introduced into the sequence by preloading into the resin using either H-His(Trt)-2Cl-Trt resin or Fmoc-His(Trt)-Wang resin. Fmoc-Asp(OMpe)-OH can be used instead of Fmoc-Asp(OtBu)-OH to improve synthesis, for example to minimize aspartamide formation for “DG” sequence combinations.

Peptide sequences are blown with dimethylformamide (DMF) and drained twice. The synthesis begins with deprotection of the N-α-FMOC protecting group using 20% piperidine in DMF with nitrogen dispersed in the mixture. After drainage, the resin is washed with DMF. A 0.4 M amino acid solution is then added along with 0.4 M HCTU and 0.8 M DIEA. The coupling reaction is carried out with nitrogen dispersed in the mixture, followed by drainage of the reaction vessel (RV). The addition of amino acid, HCTU and DIEA is repeated for two coupling cycles at the same mixing and drainage parameters as in the first coupling cycle. The resin is then washed again with DMF. This cycle is repeated for each amino acid residue. The final deprotection method removes the N-terminal Fmoc via 20% piperidine in DMF and the resin is washed with DMF followed by MeOH washes. The resin is kept in the instrument under nitrogen until removed.

For microwave synthesis, the same starting Fmoc amino acid is used, using only Fmoc-His(Trt)-Wang resin (not H-His(Trt)-2Cl Trt resin) to introduce the C-terminal histidine.

On a microwave synthesizer, the resin is blown into DMF until it is transferred through the HT line into the microwave reaction vessel (RV). While in RV, the Fmoc-His(Trt)-OH loaded resin is treated with 25% pyrrolidine in DMF to remove N-α-FMOC at 85°C/90W, then 100°C/20W. The RV is then drained and flushed with DMF and drained again. Programmed Fmoc amino acids are added (0.5 M in DMF) to the RV along with 4 M DIC and 0.25 M Oxymapure. This coupling reaction is continued at 105°C/288W heating, then at 105°C/73W heating. This first deprotection is initially diluted with DMF, however this step is not required for any subsequent deprotections since RV already contains DMF from the coupling reaction, washed, and coupling cycles are repeated for each residue until the peptide is synthesized. For arginine residues, a double coupling step is carried out, where after one coupling the solution is drained and the coupling step is repeated before deprotection. Final deprotection of the N-terminal Fmoc group is performed as described above, except draining and washing with DMF twice before transferring through DMF back to the original HT resin position.

After synthesis, the resin is transferred to a frit syringe using DMF, washed with MeOH and dried using a vacuum manifold. The resin is then cleaved using Reagent K (82.5% trifluoroacetic acid (TFA), 5% water, 5% thioanisole, 5% phenol and 2.5% ethanedhiol) using a vertical holder on an oscillating shaker for three hours at room temperature .

The digestion cocktail is then passed through a filtered syringe frit into cold diethyl ether or cold methyl tertiary butyl ether (MTBE). Each syringe is then washed with a 95:5 solution of trifluoroacetic acid:water while stirring. The wash is then added to the remainder of the cocktail/ether mixture. The mixture is then centrifuged. After distilling off the ether, another wash based on cold ether is added. The container is shaken and centrifuged again. This is repeated to thoroughly rinse the cake. The final wash is distilled off and the cake is dried in a vacuum dryer. A sample of the cake is dissolved in a solvent ( eg DMSO, DMF, water or acetonitrile) and analyzed by UPLC-MS for identification, purity and retention time. Other peptides such as L14 (SMLTGPPARVPAVPFDLH (SEQ ID NO: 3329)), L8 (GPPARVPAVPFDLHFCRSSIMKPKRD (SEQ ID NO: 3330)), L10c (KPKRDGYMFLKAESKI (SEQ ID NO: 3331)), L11h (FLKAESKIMFATLQR (SEQ ID NO: 3332) ) and L11i (ESKIMFATLQRSSL (SEQ ID NO: 3333)) are prepared in a similar manner using amino acids and preloaded resins specific for these sequences.

Example 16 - Synthesis of GATA3 neoORF peptide

The following Fmoc amino acids are used in the synthesis of peptide L15 (KPKRDGYMFLKAESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 3334)): Fmoc-Ala-OH ∙ H ₂ O, Fmoc-Cys(Trt)-OH, Fmoc-Asp(OtBu)-OH, Fmoc- Glu(OtBu)-OH, Fmoc-Phe-OH, Fmoc-Gly-OH, Fmoc-Ile-OH, Fmoc-Lys(Boc)-OH, Fmoc-Leu-OH, Fmoc-Met-OH, Fmoc-Asn( Trt)-OH, Fmoc-Pro-OH, Fmoc-Gln(Trt)-OH, Fmoc-Arg(Pbf)-OH, Fmoc-Ser(tBu)-OH, Fmoc-Thr(tBu)-OH, Fmoc-Trp (Boc)-OH, and Fmoc-Tyr(tBu)-OH. The C-terminal histidine is introduced into the sequence by preloading into the resin using either H-His(Trt)-2Cl-Trt resin or Fmoc-His(Trt)-Wang resin. Fmoc-Asp(OMpe)-OH can be used instead of Fmoc-Asp(OtBu)-OH to improve synthesis, for example to minimize aspartamide formation for “DG” sequence combinations. If serine (Ser, S) and threonine (Thr, T) residues are present, amino acid dipeptides (pseudoprolines) are introduced to improve yield, such as Fmoc-Ser(tBu)-Ser(psi(Me,Me)pro)-OH instead of “ SS”, Fmoc-Ala-Thr(psi(Me,Me)pro)-OH instead of “AT”, and Fmoc-Glu(OtBu)-Ser(psi(Me,Me)pro)-OH instead of “ES”. For some L15 syntheses, a combination of all three pseudoprolines is used (i.e., Fmoc-Ser(tBu)-Ser(psi(Me,Me)pro)-OH instead of “SS”, Fmoc-Ala-Thr(psi(Me, Me)pro)-OH instead of “AT”, and Fmoc-Glu(OtBu)-Ser(psi(Me,Me)pro)-OH) instead of “ES”). For other L15 syntheses, use the following pseudoproline and pseudoproline combinations, respectively: Fmoc-Ala-Thr(psi(Me,Me)pro)-OH instead of “AT” and Fmoc-Glu(OtBu)-Ser(psi(Me,Me) pro)-OH instead of “ES”; Fmoc-Ser(tBu)-Ser(psi(Me,Me)pro)-OH instead of “SS” and Fmoc-Glu(OtBu)-Ser(psi(Me,Me)pro)-OH instead of “ES”; Fmoc-Ser(tBu)-Ser(psi(Me,Me)pro)-OH instead of “SS” and Fmoc-Ala-Thr(psi(Me,Me)pro)-OH instead of “AT”; Fmoc-Ala-Thr(psi(Me,Me)pro)-OH instead of “AT”; Fmoc-Glu(OtBu)-Ser(psi(Me,Me)pro)-OH) instead of “ES”; and Fmoc-Ser(tBu)-Ser(psi(Me,Me)pro)-OH instead of “SS”.

The peptide sequences are inflated with DMF and drained twice. The synthesis begins with deprotection of the N-α-FMOC group using 20% piperidine in DMF with nitrogen dispersed in the mixture. After drainage, the resin is washed with DMF. A 0.4 M amino acid solution is then added along with 0.4 M HCTU and 0.8 M DIEA. The coupling reaction is carried out with nitrogen dispersed in the mixture, followed by drainage of the reaction vessel (RV). The addition of amino acid, HCTU and DIEA is repeated for two coupling cycles at the same mixing and drainage parameters as in the first coupling cycle. The resin is then washed again with DMF. This cycle is repeated for each amino acid residue. The final deprotection method removes the N-terminal Fmoc via 20% piperidine in DMF and the resin is washed with DMF followed by MeOH washes. The resin is kept in the instrument under nitrogen until removed.

The microwave synthesis uses the same starting materials, using only Fmoc-His(Trt)-Wang resin (not H-His(Trt)-2Cl-Trt resin) to introduce the C-terminal histidine.

On a microwave synthesizer, the resin is blown into DMF until it is transferred through the HT line into the microwave reaction vessel (RV). While in the RV, the Fmoc-His(Trt) loaded resin is treated with 25% pyrrolidine in DMF to remove N-α-FMOC at 85°C/90W, then 100°C/20W. This first deprotection is initially diluted with DMF, however this step is not required for any subsequent deprotections since the RV already contains DMF from the coupling reaction. The RV is then drained and flushed with DMF and drained again. Programmed Fmoc amino acids are added (0.5 M in DMF) to the RV along with 4 M DIC and 0.25 M Oxymapure. This coupling reaction is continued at 105°C/288W heating, then at 105°C/73W heating. Deprotection, washing, and coupling cycles are repeated for each residue until the peptide is synthesized. For arginine residues, a double coupling step is carried out, where after one coupling the solution is drained and the coupling step is repeated before deprotection. The final deprotection of the N-terminal Fmoc group is carried out in the same manner as all other deprotection steps, except for draining and washing with DMF twice before transferring through DMF back to the original HT resin.

After synthesis, the resin is transferred to a frit syringe using DMF, washed with MeOH and dried using a vacuum manifold. The resin is then cleaved using Reagent K (82.5% trifluoroacetic acid (TFA), 5% water, 5% thioanisole, 5% phenol and 2.5% ethanedhiol) using a vertical holder on an oscillating shaker for three hours at room temperature .

The digestion cocktail is then passed through a filtered syringe frit into cold diethyl ether (or cold MTBE). Each syringe is then washed with a 95:5 solution of trifluoroacetic acid:water while stirring. The wash is then added to the remainder of the cocktail/ether mixture. The mixture is then centrifuged. After distilling off the ether, another wash based on cold ether is added. The container is shaken and centrifuged again. This is repeated to thoroughly rinse the cake. The final wash is distilled off and the cake is dried in a vacuum dryer. A cake sample is dissolved in a solvent ( eg DMSO, DMF, water or acetonitrile) and analyzed by UPLC-MS for identification, purity and retention time.

Other peptides, such as L9 (LHFCRSSIMKPKRDGYMFLKAESKI (SEQ ID NO: 3335)), are prepared in a similar way, using amino acids and preloaded resins specific for these sequences, as well as pseudoproline derivatives where serine (Ser, S) or threonine (Thr) are present , T) residues and Fmoc-Asp(OMpe)-OH as described above.

Example 17 - Solubility Studies

Multiple GATA3 peptides with neoepitopes were first tested for solubility using 5 mM sodium succinate (SS) in D5W with 4% DMSO. Based on the initial results, the formulation strategy was improved by adjusting the concentration of sodium succinate (SS) and the amount of DMSO, resulting in the selection of 7 peptides. Pooling strategies for these peptides were determined to determine solubility and compatibility with polyICLC. Based on these results, three pools were selected. Each of two pools with only one peptide in 0.25mM SS in D5W and a third pool with 5 peptides in 5mM SS in D5W. The pH of the pool after combining with polyICLC was pH 5.0-6.0 in all cases and there was minimal loss during filtration.

The peptides were screened for the following studies, all of which are listed in Table 8 .

Table 8

Name Subsequence Molecular mass Theoretical content of TPA Theoretical % peptide content % Purity L7 EPCSMLTGPPARVPAVPFDLH (SEQ ID NO: 3336) 2234.6 13.3 80.3 97 L8 GPPARVPAVPFDLHFCRSSIMKPKRD (SEQ ID NO: 3337) 2922.4 21.5 72.1 100 L9 LHFCRSSIMKPKRDGYMFLKAESKI (SEQ ID NO: 3338) 2986.6 23.4 70.2 98 L10B KPKRDGYMFLKAESKIMFAT (SEQ ID NO: 3339) 2361.8 22.5 71.1 98 L11C YMFLKAESKIMFATLQRSS (SEQ ID NO: 3340) 2251.7 16.8 76.8 93 L11D KAESKIMFATLQRSSLWCL (SEQ ID NO: 3341) 2212.6 17.1 76.5 92 L12B MFATLQRSSLWCLCSNH (SEQ ID NO: 3342) 1997.3 14.6 79.0 93 L10 KPKRDGYMFLKAESKIMFATLQR (SEQ ID NO: 3343) 2759.3 22.4 71.2 93 L10c KPKRDGYMFLKAESKI (SEQ ID NO: 3344) 1911.3 26.4 67.2 98 L11 FLKAESKIMFATLQRSSLWCL (SEQ ID NO: 3345) 2473.0 15.6 78.0 86 L11e DGYMFLKAESKIMFAT (SEQ ID NO: 3346) 1852.2 15.6 78.0 92 L11f FLKAESKIMFATLQRS (SEQ ID NO: 3347) 1870.2 19.6 74.0 95 L11g ESKIMFATLQRSSLWC (SEQ ID NO: 3348) 1900.2 15.3 78.3 91 L12c MFATLQRSSLWCLC (SEQ ID NO: 3349) 1659.0 12.1 81.5 90 L12d TLQRSSLWCLCSNH (SEQ ID NO: 3350) 1647.9 17.2 76.4 99 L15 KPKRDGYMFLKAESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 3351) 3890.6 19.0 74.6 98 L14 SMLTGPPARVPAVPFDLH (SEQ ID NO: 3352) 1905.2 15.2 78.4 99 L11i ESKIMFATLQRSSL (SEQ ID NO: 3353) 1610.9 17.5 76.1 96

All buffers are received daily. D5W is prepared by weighing dextrose and adding milliQ water in dextrose until a suitable volume is reached. For example, water is added up to 12.5 g of dextrose to achieve a total volume of 250 ml. To obtain 50 mL of 5 mM SS in D5W by weighing, 67.54 mg of SS was weighed and added to D5W to achieve a total volume of 50 mL. To obtain 0.25 mM SS in D5W, 2.5 ml of 5 mM SS in D5W is diluted with 47.5 ml of D5W.

The % peptide content for each peptide is determined as follows: the total theoretical TFC is equal to the sum of the number of positive charges (N-terminus, Arg, Lys and His). This amount is entered into the following equation, where MW is the molecular weight of the peptide:

Equation 1. % TPA=100*((%TPA*114.02)/((%TPA*114.02)+MM))

This value is then used to calculate the percentage of peptide content using 6.45% as the theoretical water content:

Equation 2. %Peptide=100-%TPA-6.45%

The target gross mass for these experiments is calculated using the equation below.

Equation 3. Target total mass = (13.2*10000)/(% peptide content*% purity)

Peptides were weighed into 15-mL or 50-mL conical tubes using a Mettler Toledo XP105 Delta Mass analytical balance, and the actual total mass was recorded and used to determine the amount of DMSO required to obtain 50 mg/mL. The calculation is shown below:

Equation 4: DMSO (µL) = (Actual total mass (mg)*264 µL)/(Target total mass (mg))

The stock solution is then diluted to 2 mg/mL (1 part DMSO stock, 24 parts buffer) in a suitable formulation buffer.

Peptide masses and percentages are calculated as described above, and a suitable buffer is added directly to the peptides. The target total mass calculated using Equation 3 and the volume of buffer used to obtain 2 mg/mL peptide was calculated using Equation 5.

Equation 5: Buffer (ml) = (Actual total mass (mg) * 6.6 (ml)/(Target total mass (mg))

The peptides are then further diluted 1:4 with buffer to obtain 0.4 mg/ml or, only where indicated, buffer is added directly to the dry peptide to obtain 0.4 mg/ml. In the latter case, Equation 6 is used to determine the appropriate volume of buffer to be added.

Equation 6: Buffer (ml) = (Actual total mass (mg) * 33 (ml)/(Target total mass (mg))

Peptides are dissolved by inverting conical tubes, but not by sonication or shaking.

To combine 5 peptides, an equal volume from each 2 mg/mL stock solution was combined to yield 0.4 mg/mL of each peptide. If less than 5 peptides are combined, equal volumes of peptides are combined, then the solution is diluted with a suitable buffer to obtain 0.4 mg/ml of each peptide. The pool is turned over 3-5 times to mix. The formulated peptides are transferred into glass vials to visualize solubility. Photographs are taken every two hours to note any changes in appearance.

PolyICLC is produced commercially. The pools are combined in a 3:1 ratio of peptide to polyICLC using 150 μl of polyICLC with 450 μl of peptide pool in a 2 ml glass vial. The solution is inverted 3-5 times to mix and photographs are taken every two hours for 6 hours to note any changes in appearance. All pH measurements are performed using a Mettler Toledo inLab Micro pH meter, which is calibrated each day before use and 100 µl of the test sample is removed and added to a pH microcentrifuge tube. The sample is then discarded. Samples by UPLC-MS (Waters Acquity H-Class m mass spectrometer Acquity QDa). A 2 μg injection of each sample was assayed in duplicate using an 8-minute gradient from 10:90 solvent A:B to 50:50 solvent A:B (A: 0.1% TFA/water, B: 0.1% TFA:acetonitrile) . The initial solubility of peptides in a standard composition is determined for each peptide at 0.4 mg/ml and 2 mg/ml. Although photographs are taken, they do not always clearly show solubility as the gels were often clear or the peptides produced small glassy particles when dissolved. The solubility of the peptides in 5 mM SS/D5W with 4% DMSO is shown in Table 9 .

Table 9 below lists the peptide solubility and appearance in 5 mM SS/D5W with 4% DMSO

Peptide name Peptide solubility (at 2 mg/ml) (D/N) Type of composition (at 2 mg/ml) Peptide solubility (at 0.4 mg/ml) (D/N) Type of composition (at 0.4 mg/ml) L7 D transparent D transparent L8 D transparent D transparent L9 D transparent D transparent L15 N turbid N Cloudy after 4 hours L14 D transparent D transparent L10 D transparent D transparent L10c D transparent D transparent L11 N cloudy, sediment N Glassy particles L11e N cloudy, coarse sediment N Glassy particles L11f N turbid N Glassy particles L11g N turbid N Glassy particles L12c N cloudy, coarse sediment N Glassy particles L12d D transparent D transparent

Peptides that were insoluble in 5 mM SS were tested using 0.25 mM SS in D5W with 4% DMSO. The results are summarized in Table 10 . Many of these peptides that were insoluble in 5 mM SS were soluble at a concentration of 0.4 mg/ml in 0.25 mM SS/D5W with 4% DMSO after 6 hours, and were tested in subsequent studies using this low concentration SS.

Table 10 lists the peptide solubility and appearance in 0.25 mM SS/D5W with 4% DMSO

Peptide name Peptide solubility (at 2 mg/ml) (D/N) Type of composition (at 2 mg/ml) Peptide solubility (at 0.4 mg/ml) (D/N) Type of composition (at 0.4 mg/ml) L15 D transparent D transparent L11 H (glassy particles) glass particles D transparent L11e N gel N glassy particles L11f D transparent D transparent L11g N (gelation over time) gelation over time D transparent L12c N large particles N turbid L12d D transparent D transparent

Based on these results, peptides L7, L8, L9, L14, L10c, L11d, L11f, and L15 were selected for formulation studies. Formulations without DMSO were tested as a means of improving the stability of formulated peptides and to slow down the dimerization of cysteine-containing peptides. All peptides were tested (L7, L8, L9, L14, L10c, L11d, L11f, and L15) at a concentration of 0.4 mg/mL in 0.25 mM SS and were soluble without DMSO after 6 h. Peptides L7, L8, L9, L10c, L12d and L14 were tested at 5 mM SS and were also soluble without DMSO after 6 h. The pH values of the peptide formulations in 0.25 mM SS/D5W and 5 mM SS/D5W are listed in Table 11 .

Table 11 below shows the pH of 0.4 mg/ml peptide formulations in 0.25 mM SS/D5W and 5 mM SS/D5W

Peptide name pH in 5mM SS/D5W pH at 0.25mM SS/D5W L7 6.4 4.5 L8 6.4 5.0 L9 6.4 4.6 L10c 6.4 4.3 L11f N/A 5.0 L14 6.4 4.2 L15 N/A 4.8

Since all peptides listed in Table 11 were soluble in 0.25 mM SS, initial pool designs were examined using a lower concentration of SS. The pools have also been designed with individual mental solubility. Since L15 and L11f were soluble in low SS, these two peptides were combined. The first three pool designs are shown in Table 12 .

Table 12 below shows the original peptide pools in 0.25 mM SS/D5W

Peptide name Design 1 Design 2 Design 3 3 pools 3 pools 3 pools L7 1 1 1 L14 1 1 1 L8 1 2 2 L9 2 2 2 L15 3 3 3 L11f 3 3 3 L10c 2 2 1

All peptides remained soluble after combining. The pH values of the peptide pools with or without the addition of polyICLC are given in Table 13 .

Table 13 below lists the pH of the peptide pools from Table 12 with or without the addition of polyICLC

Pool Pool pH pH pool with polyICLC Design 1 Pool 1 3.4 4.7 Pool 2 3.8 5.1 Pool 3 4.0 5.5 Design 2 Pool 1 3.7 5.0 Pool 2 3.6 4.8 Pool 3 4.0 5.5 Design 3 Pool 1 3.5 4.7 Pool 2 3.9 5.5 Pool 3 4.0 5.5

Pools from each design are then mixed with polyICLC to test their compatibility with the adjuvant. Pool 3 and each pool containing the L10c peptide precipitated when combined with polyICLC. Additionally, pools with 3 peptides have a pH below 5.0 when combined with polyICLC, suggesting that buffering should be higher if the pool contains more than two peptides.

Since L7, L8, L9, L10c, and L14 were all water soluble in 5 mM SS, they are tested in high SS concentration pools. Three pools are tested with these five peptides. One pool was without L10c, one included only L10c, and the third included all five peptides. Since L11f and L15 were not soluble at such a high concentration, they are formulated in 0.25 mM SS. However, due to the sediment observed, they were formulated at 0.4 mg/mL separately rather than in the same pool. Each of the peptides was soluble in their respective formulations. These pools were also compatible with polyICLC by imaging, and all pH values after pooling with polyICLC were between 5.0 and 6.3 ( Table 14 ), which are suitable for subcutaneous administration.

Table 14 lists the pH of peptide pools without polyICLC compared to the pH of peptide pools with polyICLC

Pool Pool pH without polyICLC pH pool with polyICLC Pool 1 5.6 5.6 Pool 2 5.4 5.5 L10c 6.4 6.3 L11f 5.0 5.9 L15 4.8 6.0

Peptide L11i was tested in D5W with different concentrations of succinate without DMSO. The peptide was found to be soluble in all concentrations of SS at 0.4 mg/mL. Some precipitation was observed at 2 mg/mL in the higher SS concentration. All samples appeared identical when combined with polyICLC. pH values of formulations of 2 mg/ml or 0.4 mg/ml L11i peptide in 0.25 mM SS, 0.5 mM SS or 5 mM SS without polyICLC and 0.4 mg/ml L11i peptide in 0.25 mM SS, 0.5 mM SS or 5 mM SS with polyICLC are shown in Table 15 .

Table 15 lists the pH of 2 mg/ml or 0.4 mg/ml L11i peptide in 0.25 mM SS, 0.5 mM SS and 5 mM SS without polyICLC and 0.4 mg/ml in 0.25 mM SS. 0.5 mM SS and 5 mM SS with polyICLC

pH 2mg/ml L11i peptide 0.4 mg/ml L11i peptide 0.4 mg/ml L11i peptide with polyICLC 5mM SS 5.8 6.7 6.6 0.5mM SS 4.1 5.8 6.1 0.25mM SS 3.7 5.3 6.1

Final pools from the results include Pool 1 (L7, L8, L9, L10c and L14 in 5 mM SS/D5W), pool 2 (either L11i or L11f in 0.25 mM SS/D5W) and pool 3 (L15 in 0, 25 mM SS/D5W). Each of these pools is tested for retention on a 0.2 μM filter from Pall (HP1002). The sample before filtration, as well as the sample after each of the 2 filtrations, are analyzed by UPLC-MS. Less than 3% of L11f and L11i are lost after the first filtration step, and no additional peptide is lost after the second filtration step. Only 4.9% of L15 is lost after the first filtration and then 1.3% is lost after the second filtration. Less than 3% overall of each peptide in Pool 1 is lost after two filtration steps.

Conclusions

A number of potential GATA3 peptides were tested for solubility in formulation buffer containing 5 mM SS/D5W with 4% DMSO. Peptides that were insoluble in 5 mM SS were also tested at lower SS concentrations. Based on these results, seven peptides were selected, where five were soluble in 5 mM SS (L7, L8, L9, L10c, and L14) and others were soluble in lower concentrations (L11f, L11i, and L15). DMSO removal has also been tested and may improve solubility and retard disulfide formation, which can interfere with UPLC analysis. Each of the selected peptides was soluble without DMSO.

Based on the solubility results, 3 pool designs are created using 0.25 mM SS/D5W. Although the pools were soluble, some were incompatible with polyICLC. In some cases, precipitate was observed when pools containing L10c were mixed with polyICLC. The same observation was made when combining a pool containing both L11f and L15 with polyICLC. Based on these results, a fourth set of pools was created. The first pool contained L7, L8, L9, L10c, and L14 in 5 mM SS/D5W and was polyICLC compatible. Peptides L15 and L11f or L11i are left as separate peptides to be prepared by dissolving directly in 0.4 mg/ml with 0.25 mM SS/D5W. All of these pools had a pH greater than 5.0 when mixed with polyICLC, which is acceptable for subcutaneous administration.

Example 18: Prevalence of GATA3 neoORF mutations

This example characterizes the prevalence and translational evidence of the GATA3 neoORF mutation. The vaccine consists of a pool of long peptides that span a novel open reading frame in GATA3 (GATA binding protein 3), which is only present in cells that have certain frameshift mutations in this gene. Depending on the starting position of the frameshift mutation, the resulting open reading frames may vary in length, but they all share a common translated region “GATA3 neoORF”. In FIG. 13 shows a typical amino acid sequence of the general translated region. Any genetic frameshift mutation that gives a GATA3 neoORF translated sequence is a “GATA3 neoORF mutation.” Publicly available genomic and proteomic datasets are examined for GATA3 neoORF mutation prevalence and translational evidence for GATA3 neoORF

Materials and methods

Datasets

MSK-IMPACT Breast Cancer Dataset: The MSK-IMPACT Breast Cancer Dataset (Razavi et al., 2018) is a public dataset available on the cBioPortal for Cancer Genomics (http://www.cbioportal.org/study?id =breast_msk_2018). This dataset contains sequencing data using MSK-IMPACT, a hybridization capture-based next-generation sequencing assay that analyzes all protein-coding exons between 341 and 468 tumor-associated genes, for a total of 1918 breast cancer samples and matched normal samples from 1756 patients. Publicly available mutation and clinical data, which include ER status, HER2 status and overall survival, are downloaded for this study.

TCGA Breast Cancer Proteome Dataset: The TCGA Breast Cancer Proteome Dataset (NCI CPTAC et al., 2016) is a public dataset available on the CPTAC Data Portal (https://cptac-data-portal.georgetown.edu/cptac /s/S015). This dataset contains tandem mass spectrometry data from the global proteome of 105 TCGA breast cancer patients obtained using iTRAQ protein quantification methods. Publicly available raw data was downloaded for this study.

Mutation prevalence analysis

Identification of GATA3 neoORF: Each GATA3 gene mutation event from the MSK-IMPACT breast cancer dataset is mapped to the GATA3 transcript ENST00000346208.3 from the human genome (hg19, GRCh37 Genome Reference Consortium Human Reference 37) and then translated in silico into full-length protein. If the full-length protein contains a GATA3 neoORF sequence, the sample that contains this mutation event is labeled GATA3 neoORF positive.

Prevalence of GATA3 neoORF: For all subjects in the cohort, if the subject has at least one sequenced tumor sample that was identified as GATA3 neoORF positive, the subject is considered GATA3 neoORF positive. GATA3 neoORF prevalence is defined as the proportion of GATA3 neoORF positive subjects in the cohort.

Peptide identification from proteomics data

Protein Sequence Database: The Protein Sequence Database contains 63,691 protein sequences from the UCSC Protein Sequence Database (Feb. 2009 human reference sequence, GRCh37/hg19) and one full-length protein, which contains the GATA3 neoORF sequence.

Peptide identification: Raw data from the breast cancer TCGA proteome dataset were analyzed using the Comet search engine (http://comet-ms.sourceforge.net), an open-source software package for interpreting tandem mass spectra. Comet (version 2017.01 rev.2) is used to search all MS/MS spectra from the TCGA breast cancer proteome dataset against the UCSC protein sequence database. MS/MS spectra with precursor ions up to +6 are allowed in the search. The mass error tolerance for precursor ions was ±10 parts per million (ppm), and an m/z bin width of 0.02 was used to fragment the ions. All searches were limited to trypsin, so that each peptide matching the experimental spectrum had to match the enzyme's cleavage specificity, i.e. C-terminal side of lysines or arginines. A maximum of 2 undercuts is allowed. A fixed modification of +144.1021 Da is used to the N-terminus of the peptide and each lysine residue, as expected for iTRAQ labeling. Variable modifications included up to two oxidized methionine residues per peptide. Fixed modification +57.021464 Yes is used for all cysteines for urea-methylated cysteines. During the search, decoy peptides are automatically generated as part of the Comet search engine to estimate the false discovery rate of the decoy target. Search results are processed by Percolator (version 3.02.0) to calculate peptide-level q-values, typically a measure of the probability of false identification of a peptide using tandem mass spectrometry data. A standard threshold (q-value <0.01) is used to accept peptides identified from the data set such that less than 1% of the accepted peptides were likely false discoveries.

Evidence for GATA3 neoORF translation: Peptides specifically derived from a protein sequence containing the GATA3 neoORF and not from another protein in the UCSC protein sequence database are called GATA3 neoORF specific peptides. Identification of GATA3 neoORF-specific peptides is considered evidence of GATA3 neoORF translation.

results

Prevalence of GATA3 neoORF mutations in breast cancer

From the MSK-IMPACT breast cancer dataset of 1,756 patients, mutation prevalence analysis is performed (Materials and Methods from section 1 above) and 91 patients are identified who were GATA3 neoORF positive. Of these 91 patients, 77 patients were described as HR+Her2(-), and 62 patients were described as metastatic at diagnosis. The prevalence of GATA3 neoORF positive patients in each subgroup is presented in Table 16 below. Among HR+Her2(-) patients, GATA3 neoORF positive patients had no statistical difference in overall survival compared to all HR+Her2(-) patients (regardless of GATA3 neoORF status) (p-value=0.246) ( FIG. 14 ).

Table 16 below shows the prevalence of GATA3 neoORF

Number of patients Number of patients positive for GATA3 neoORF Prevalence all patients 1.756 91 5.2% HR+Her2(-) 1.272 77 6.1% HR+Her2(-) metastatic 856 62 7.2%

Table 17 below shows GATA3 neoORF specific peptides and other peptides mapped to canonical GATA3 identified from the TCGA breast cancer proteome dataset

# Peptide sequence Matched proteins 1 HGLEPCSMLTGPPAR (SEQ ID NO: 3354) GATA3 neoORF 2 RDGYMFLK (SEQ ID NO: 3355) GATA3 neoORF 3 SSIMKPK (SEQ ID NO: 3356) GATA3 neoORF 4 AGTSCANCQTTTTTLWR (SEQ ID NO: 3357) GATA3 5 ALGSHHTASPWNLSPFSK (SEQ ID NO: 3358) GATA3 6 DGTGHYLCNACGLYHK (SEQ ID NO: 3359) GATA2, GATA3, GATA4, GATA5 7 DVSPDPSLSTPGSAGSAR (SEQ ID NO: 3360) GATA3 8 ECVNCGATSTPLWR (SEQ ID NO: 3361) GATA3 9 EGIQTR (SEQ ID NO: 3362) GATA2, GATA3, GATA4, GATA6 10 EGIQTRNR (SEQ ID NO: 3363) GATA2, GATA3 eleven KEGIQTR (SEQ ID NO: 3364) GATA2, GATA3, GATA4, GATA6 12 KVHDSLEDFPK (SEQ ID NO: 3365) GATA3 13 LHNINRPLTMK (SEQ ID NO: 3366) GATA3 14 LHNINRPLTMKK (SEQ ID NO: 3367) GATA3 15 MNGQNRPLIKPK (SEQ ID NO: 3368) GATA2, GATA3 16 NANGDPVCNACGLYYK (SEQ ID NO: 3369) GATA2, GATA3 17 NSSFNPAALSR (SEQ ID NO: 3370) GATA3 18 RAGTSCANCQTTTTTLWR (SEQ ID NO: 3371) GATA3 19 RDGTGHYLCNACGLYHK (SEQ ID NO: 3372) GATA2, GATA3, GATA4, GATA5 20 SSTEGRECVNCGATSTPLWR (SEQ ID NO: 3373) GATA3 21 VHDSLEDFPK (SEQ ID NO: 3374) GATA3 22 YQVPLPDSMK (SEQ ID NO: 3375) GATA3

A study of a breast cancer genomic dataset found that GATA3 neoORF is prevalent in 6-7% of patients with HR+Her2(-) breast cancer depending on their metastatic status. Multiple GATA3 neoORF specific peptides, along with other peptides that map to canonical GATA3, have been identified, indicating translation of the GATA3 neoORF. Together, these results demonstrate that GATA3 neoORF mutation is common in HR+Her2(-) breast cancer and, if present, GATA3 neoORF can be translated to produce protein products.

Example 19 Calculation of GATA3 neoORF epitope among HLA types

This example provides an estimate of the typical number of epitopes that might be expected from the GATA3 neoORF in a patient population and by different HLA types.

Materials and methods

All peptides (lengths 8-11) with a common GATA3 neoORF region (as defined in EXAMPLE 18) are assessed for presentation likelihood using an in silico prediction algorithm that jointly considers gene expression, HLA binding potential, and protesome processing potential. The algorithm combines the three variables into an overall presentation prediction through a logistic regression fit on HLA-I monoallelic mass spectrometry profiling data. The following assumptions and tools were used to define the three input variables:

Expression

Based on Cancer Genome Atlas (TCGA) RNA-Seq data, breast cancer samples have an average GATA3 expression of ~700 transcripts per million (TPM). Assuming that the mutant and wild-type allele contribute equally to overall GATA3 expression, we calculated that the neoORF transcript would be expressed at 350 TPM.

HLA binding potential

US allele frequencies are entered based on ethnic-specific frequencies and the estimate that the US population is 62.3% European, 13.3% African American, 6.8% Asian/Pacific, and 17.6% Hispanic ( Table 18 ). For the 21 most common HLA-A alleles and the 49 most common HLA-B alleles, peptide binding predictions are made using the NetMHCpan-3.0 tool (21 and 49 alleles provide 95% population coverage for HLA-A and HLA-B, respectively) .

Processing potential

The processing potential predictor was trained using publicly available mass spectrometry-based HLA-I profiling data, such as those described in Abelin. J. et al. Immunity, 2017, Bassani-Sternberg, M. et al Molecular & Cellular Proteomics 2015, neural network configurations that determine processing potential based on the upstream and downstream sequence context of each peptide.

To model the number of epitopes per patient, mock HLA genotypes were created by randomly drawing two HLA-A and two HLA-B alleles (with replacement to account for homozygosity) according to their overall US frequencies ( Table 18 ). Most mock patients had 4 different alleles, but because homozygosity was allowed, some mock patients only had 2 or 3 different alleles. For each peptide-allele pair in a mock patient, a Bernoulli “coin toss” was performed, parameterized by the estimated probability of presentation (derived from the model described above); a positive result is taken as an indication that the peptide will be presented on this allele. For each mock patient, the total number of unique positive peptides was summed to determine the total number of reactive epitopes (meaning that a peptide present on multiple alleles in a mock patient was counted only once). The results are further rejected by counting nested epitopes (eg, a positive 9mer is entirely contained within a positive 10mer) as a single epitope. Ten thousand patients were stimulated in this way using the statistical programming language R.

Table 18 below lists the frequency of alleles used in stimulation

Allele Europeans African Americans Natives of the Asia-Pacific region Spaniards US average A*02:01 29.6% 12.5% 9.5% 19.4% 24.2% A*01:01 17.2% 4.7% 5.1% 6.7% 12.9% A*03:01 14.3% 8.1% 2.6% 7.9% 11.6% A*24:02 8.7% 2.2% 18.2% 12.3% 9.1% A*11:01 5.6% 1.6% 17.9% 4.6% 5.8% A*29:02 3.3% 3.6% 0.1% 4.2% 3.3% A*23:01 1.7% 10.8% 0.2% 3.7% 3.1% A*68:01 2.5% 3.7% 1.9% 4.7% 3.0% A*26:01 2.9% 1.4% 3.9% 2.9% 2.8% A*32:01 3.1% 1.4% 1.3% 2.7% 2.7% A*31:01 2.4% 1.0% 3.2% 4.8% 2.7% A*30:01 1.3% 6.9% 2.1% 2.1% 2.3% A*30:02 0.9% 6.2% 0.1% 2.8% 1.9% A*68:02 0.8% 6.5% 0.0% 2.5% 1.8% A*33:03 0.1% 4.5% 9.4% 1.3% 1.5% A*25:01 1.9% 0.5% 0.1% 0.9% 1.4% A*33:01 1.0% 2.1% 0.1% 2.0% 1.3% A*02:06 0.2% 0.0% 4.8% 3.9% 1.1% A*02:05 0.8% 1.9% 0.3% 1.5% 1.0% A*74:01 0.0% 5.2% 0.1% 0.8% 0.8% A*02:02 0.1% 4.2% 0.0% 0.7% 0.7% B*07:02 14.0% 7.3% 2.6% 5.5% 10.8% B*08:01 12.5% 3.8% 1.6% 4.5% 9.2% B*44:02 9.0% 2.1% 0.8% 3.3% 6.5% B*35:01 5.7% 6.5% 4.3% 6.4% 5.8% B*44:03 5.0% 5.4% 4.2% 6.1% 5.2% B*15:01 6.7% 1.0% 3.5% 2.9% 5.0% B*51:01 4.5% 2.2% 6.3% 5.8% 4.6% B*40:01 5.6% 1.3% 8.0% 1.4% 4.5% B*18:01 4.6% 3.6% 1.2% 4.0% 4.1% B*14:02 3.1% 2.2% 0.1% 4.1% 3.0% B*57:01 3.8% 0.5% 2.1% 1.2% 2.8% B*27:05 3.3% 0.7% 0.8% 1.7% 2.5% B*13:02 2.6% 1.0% 2.3% 1.2% 2.1% B*53:01 0.3% 11.2% 0.1% 1.6% 2.0% B*38:01 2.2% 0.2% 0.5% 1.9% 1.7% B*40:02 1.0% 0.4% 3.1% 4.9% 1.7% B*49:01 1.3% 2.8% 0.1% 2.4% 1.6% B*52:01 1.0% 1.4% 3.7% 2.7% 1.5% B*35:03 1.6% 0.4% 2.4% 1.4% 1.4% B*58:01 0.5% 3.5% 5.8% 1.5% 1.4% B*55:01 1.7% 0.4% 0.5% 1.1% 1.4% B*15:03 0.1% 6.2% 0.0% 1.6% 1.2% B*45:01 0.4% 4.5% 0.2% 1.5% 1.1% B*37:01 1.3% 0.5% 1.5% 0.6% 1.1% B*50:01 0.8% 0.9% 0.7% 1.5% 0.9% B*39:01 1.0% 0.4% 1.3% 1.0% 0.9% B*35:02 1.1% 0.1% 0.2% 1.1% 0.9% B*42:01 0.0% 5.5% 0.0% 0.6% 0.8% B*14:01 0.8% 0.9% 0.3% 0.9% 0.8% B*39:06 0.5% 0.2% 0.0% 2.0% 0.7% B*58:02 0.0% 4.1% 0.0% 0.5% 0.6% B*57:03 0.0% 3.4% 0.0% 0.7% 0.6% B*48:01 0.1% 0.0% 2.0% 2.2% 0.6% B*41:01 0.4% 0.5% 0.1% 1.3% 0.5% B*15:10 0.0% 3.0% 0.1% 0.5% 0.5% B*07:05 0.2% 0.7% 2.0% 0.5% 0.5% B*56:01 0.5% 0.2% 0.8% 0.4% 0.5% B*39:05 0.0% 0.0% 0.1% 2.3% 0.4% B*41:02 0.4% 0.7% 0.0% 0.6% 0.4% B*46:01 0.0% 0.0% 6.1% 0.0% 0.4% B*35:08 0.4% 0.0% 0.2% 0.9% 0.4% B*15:17 0.3% 0.6% 0.5% 0.7% 0.4% B*35:12 0.0% 0.0% 0.0% 1.9% 0.3% B*15:16 0.0% 1.7% 0.0% 0.5% 0.3% B*81:01 0.0% 2.0% 0.1% 0.3% 0.3% B*40:06 0.0% 0.0% 3.7% 0.3% 0.3% B*35:17 0.0% 0.0% 0.0% 1.6% 0.3% B*15:02 0.0% 0.1% 3.6% 0.0% 0.3% B*38:02 0.0% 0.0% 3.7% 0.0% 0.2%

results

The analysis described in the "Methods" section showed that 95% of patients could present ≥2 HLA-I epitopes from the GATA3 neoORF ( FIG. 15 ). GATA3 neoORF has multiple HLA-I-presented epitopes regardless of the patient's HLA genotype based on the details presented above. This demonstrates the effectiveness of therapies inducing T cell responses against these predicted neoantigens. A subset of predicted epitopes is selected for validation of the following studies, detailed in Examples 20, 21, 22, 23 below.

Example 20 Biochemical Epitope Measurements

The example below presents biochemical validation of the affinity of epitopes from GATA3neoORF. A large number of epitopes can bind to many HLA alleles (as described in Example 19). In this example, epitopes are assessed for their ability to bind to several common HLA alleles, namely HLA-A02:01, HLA-B07:02 and HLA-B08:01. Both the affinity and stability of binding between epitopes and their predicted HLAs are assessed.

Affinity is a measure of the strength of an epitope's binding to HLA. Strong binding (usually defined as <500 nM) is an important characteristic for a neoantigen that can be targeted by a T cell. This occurs because the neoantigen must be presented on the surface of tumor cells, and therefore must outcompete other antigens produced by the tumor cell for the binding pocket of one of the HLA molecules, since only one peptide can bind to a single HLA molecule at a time. In addition, it has been shown that immunogenic epitopes tend to have strong affinity for their specific HLA.

Stability is a measure of how long a given epitope remains associated with recognized HLA. Stable binding (usually defined as >1 hour) is also an important characteristic for a neoantigen that can be targeted by T cells. Epitopes must remain associated with tumor cells on the cell surface in order to be recognized by T cells. In addition, like affinity, it has previously been shown that immunogenic epitopes tend to bind stably to their specific HLA.

To assess the stability and affinity of epitopes for their HLA-recognized molecules, peptides are synthesized at >70% purity (by UV area % analysis) and diluted to 20 mM or less, and their affinity and stability are measured.

This example presents the binding affinity and stability between 14 epitopes and HLA-recognized molecules. Four epitopes were studied on HLA-A02:01, five epitopes were studied on HLA-B07:02, and eight epitopes were studied on HLA-B08:01 (three epitopes were studied on both HLA-B07:02 and HLA-B08:01). All peptides showed strong binding through affinities ranging from 9.5 nM to 242.8 nM. Stability ranges from 0 hours to 21.7 hours, with at least one epitope on each allele exceeding 1 hour. These results indicate that there is at least one strong GATA3 neoORF-derived epitope per allele.

Materials and methods

Selection of epitopes for biochemical measurements

Multiple epitopes derived from the GATA3 neoORF were selected to confirm their ability to bind to a specific common HLA allele, namely HLA-A02:01, HLA-B07:02, or HLA-B08:01. These epitopes are thought to range from weak to strong binders.

Solid phase peptide synthesis

Peptides are prepared on a 5 μM scale using solid-phase peptide synthesis on the Intavis Peptide Synthesizer. Fmoc deprotection was carried out using 20% piperidine in DMF and washed with pure DMF. All amino acids were combined twice for 15 minutes at room temperature using 60 μl of 0.5 M amino acids (6 eq.), 55 μl of 0.5 M HCTU (5.5 eq.), 5 μl of NMP (0.5 eq. ) and 14 µl 4 M NMM (11.2 eq). After each double coupling cycle, acetyl capping is accomplished by adding 100 µl of DIEA solution (first as a 2M solution in NMP and then diluted to 12.5% using DMF) and 6.25% acetic anhydride in DMF for 15 minutes followed by vacuum drainage and rinsing with DMF. Deprotection, wash, double coupling, acetyl capping, wash cycle is repeated for each amino acid in the sequence. Final deprotection was carried out with 20% piperidine in DMF, and final washes with DMF, EtOH and DCM. The final drainage is completed within 5 minutes on the instrument, after which the bottom of the plate is washed with DCM.

Peptide degradation

Peptides are digested using a solution of 92.5% TFA, 2.5% TIPS, 2.5% H ₂ O, 2.5% EDT. After 1 hour, the plates are drained under vacuum into a 1.2 ml Micronic tube rack. After a total of 3 hours, the peptides are precipitated with cold diethyl ether via centrifugation.

UPLC-UV-MS analysis of peptides

Crude peptides are dried and resuspended in 1:1 ACN:H ₂ O containing 0.1% TFA and stored at -80°C until completely frozen. The peptides are then lyophilized to isolate the peptide in powder form. Peptide powders are first dissolved in pure DMSO and then diluted 3:1 in DMSO:H ₂ O for UPLC-UV-MS analysis. UV tracking is carried out at a wavelength of 214 nm with a mass detector interval of 200-1250 Da. The UPLC-UV-MS method used for peptides less than 9 amino acids in length involves a gradient of 0-100% mobile phase B (0.085% TFA in acetonitrile, with a corresponding mobile phase of 0.1% TFA in water) for 5 minutes per UPLC column 2.1x50 mm 1.7 µM BEH Acquity UPLC, and the method for peptides greater than 9 amino acids involves a gradient of 10-80% mobile phase B over 8 minutes on a UPLC column 2.1x100 mm 1.7 µM BEH Acquity UPLC.

Determination of peptide concentration by method A214

Crude peptides are dissolved in pure DMSO at concentrations of 2-5 mg/ml for evaluation by method A214. The peak area of the peptide in the UPLC-UV chromatogram was proportional to the amount of peptide introduced for analysis and the extinction coefficient of the peptide at the detection wavelength. Therefore, the concentration of a peptide can be determined by comparing its UV peak area with the UV peak area of a reference peptide of known concentration, taking into account appropriate extinction coefficients. The following equation is used to calculate the peptide concentration:

Equation 7

where C is the concentration of the peptide sample in mM, C _ref is the concentration of the reference peptide in mM, A _sam is the UV peak area of the peptide sample, A _ref is the UV peak area of the reference peptide, E _ref is the extinction coefficient of the reference peptide in M ^-1 cm ^-1 E _sam is the extinction coefficient of the peptide sample in M ^-1 cm ^-1 , V _sam is the injection volume of the sample, and V _ref is the injection volume of the reference peptide.

The extinction coefficient of a peptide at 214 nm is predicted by combining the extinction coefficients of individual amino acids and peptide bonds. The reference peptide with the sequence RAKFKQLL (SEQ ID NO: 3376) (peptide ID LS-18) at 0.2 mg/ml was run sequentially with the crude peptide samples on UPLC-UV-MS. The UV peak areas and calculated extinction coefficients are then used to calculate the peptide concentration in mM.

Affinity measurements

The binding affinity of a peptide to HLA molecules is measured by assessing its ability to compete with a specific radiolabeled peptide for the binding pocket on the HLA molecule. This was accomplished by purifying HLA molecules and incubating them with multiple concentrations of the peptide of interest and a high affinity binding peptide that is radiolabeled. After 2 days of incubation, unbound radiolabeled peptide is separated by size-separation gel filtration chromatography, and the proportion of HLA molecules that have radiolabeled peptide is determined. Peptides that have a low proportion of radiolabeled peptide at the end of the assay have strong affinity for HLA. Quantitatively, the concentration of peptide of interest required to inhibit radiolabeled peptide binding by 50% can be determined by regression analysis of inhibition over multiple concentrations. This IC50 measurement is used as an approximation of the true binding affinity.

In the first wave of peptides analyzed, the actual concentrations of the peptides were known based on A214 measurements, and any necessary concentration-based corrections were made. In the second wave of peptides analyzed, the concentration of all peptides was assumed to be 20 mM, and initial IC50s were calculated based on this assumption, with adjustments made later for the actual concentration. For peptides with an actual concentration below 20 mM, the measured IC50s were corrected by multiplying the actual concentration determined by method A214 and dividing by 20 mM.

Stability measurements

To measure the stability of peptide binding to MHC class I, synthetic genes encoding biotinylated MHC-I heavy and light chains were expressed in E. coli and purified from inclusion bodies by standard methods. The light chain (β2m) was radiolabeled with iodine (125I) and combined with the purified MHC-I heavy chain and the peptide of interest at 18°C to initiate the formation of the pMHC-I complex. These reactions are carried out in streptavidin-coated plates to bind biotinylated MHC-I heavy chains to the surface, and the radiolabeled light chain is measured to monitor complex formation. Dissociation is initiated by adding higher concentrations of unlabeled light chain and incubation at 37°C. Stability is defined as the length of time in hours required for half of the complexes to dissociate, as measured by a scintillation counter. Double measurements are taken. The average of the two measurements is taken as stability.

results

Affinity measurements

Table 19 below shows epitope affinity measurements.

Wave Peptide sequence HLA allele Actual peptide concentration (mM) Measured IC50 (nM) Adjusted IC50 (nM) 2 MLTGPPARV (SEQ ID NO: 3377) A02:01 13.7 15.4 10.6 1 SMLTGPPARV (SEQ ID NO: 3378) A02:01 20.0 15.4 15.4 2 TLQRSSLWCL (SEQ ID NO: 3379) A02:01 8.4 281.2 117.7 1 YMFLKAESKI (SEQ ID NO: 3380) A02:01 20.0 165.9 165.9 2 FATLQRSSL (SEQ ID NO: 3381) B07:02 20.0 14.0 14.0 2 KPKRDGYMF (SEQ ID NO: 3382) B07:02 20.0 28.2 28.2 2 KPKRDGYMFL (SEQ ID NO: 3383) B07:02 17.0 115.2 98.1 2 GPPARVPAV (SEQ ID NO: 3384) B07:02 15.7 281.9 221.2 2 MFATLQRSSL (SEQ ID NO: 3385) B07:02 15.2 350.3 266.9 2 ESKIMFATL (SEQ ID NO: 3386) B08:01 15.2 23.3 17.7 2 FLKAESKIM (SEQ ID NO: 3387) B08:01 20.0 21.9 21.9 2 FATLQRSSL (SEQ ID NO: 3388) B08:01 19.4 27.5 26.6 1 YMFLKAESKI (SEQ ID NO: 3389) B08:01 20.0 32.0 32.0 2 IMKPKRDGYM (SEQ ID NO: 3390) B08:01 16.5 40.2 33.2 2 MFATLQRSSL (SEQ ID NO: 3391) B08:01 20.0 53.4 53.4 2 FLKAESKIMF (SEQ ID NO: 3392) B08:01 18.3 90.0 82.3 2 LHFCRSSIM (SEQ ID NO: 3393) B08:01 14.2 167.3 118.7

*Note: The actual peptide concentration and measured IC50 presented here are rounded from the raw data, but adjusted IC50 values were calculated using the unrounded raw data.

Stability measurements

Table 20 below provides stability measurements

Wave Subsequence HLA allele Experiment 1 half-life (hours) Experiment 2 half-life (hours) Average half-life (hours) 2 TLQRSSLWCL (SEQ ID NO: 3394) A02.01 0.5 0.5 0.5 2 MLTGPPARV (SEQ ID NO: 3395) A02.01 5.8 5.8 5.8 1 YMFLKAESKI (SEQ ID NO: 3396) A02:01 0.6 0.6 0.6 1 SMLTGPPARV (SEQ ID NO: 3397) A02:01 21.7 21.8 21.7 2 KPKRDGYMFL (SEQ ID NO: 3398) B07.02 3.3 3.3 3.3 2 KPKRDGYMF (SEQ ID NO: 3399) B07.02 8.3 9.0 8.6 2 FATLQRSSL (SEQ ID NO: 3400) B07.02 0.7 0.6 0.7 2 MFATLQRSSL (SEQ ID NO: 3401) B07.02 0.0 0.0 0.0 2 GPPARVPAV (SEQ ID NO: 3402) B07.02 1.5 1.8 1.6 2 FLKAESKIMF (SEQ ID NO: 3403) B08.01 0.0 0.0 0.0 2 FATLQRSSL (SEQ ID NO: 3404) B08.01 0.0 0.0 0.0 2 MFATLQRSSL (SEQ ID NO: 3405) B08.01 0.0 0.0 0.0 2 ESKIMFATL (SEQ ID NO: 3406) B08.01 1.0 1.6 1.3 2 FLKAESKIM (SEQ ID NO: 3407) B08.01 0.8 1.5 1.2 2 LHFCRSSIM (SEQ ID NO: 3408) B08.01 0.0 0.0 0.0 2 IMKPKRDGYM (SEQ ID NO: 3409) B08.01 0.4 0.4 0.4 1 YMFLKAESKI (SEQ ID NO: 3410) B08:01 0.4 0.5 0.4

In Example 20 , predicted epitopes from the GATA3 neoORF on a variety of common HLA molecules (HLA-A02:01, HLA-B07:02, HLA-B08:01) are assessed. All epitopes were determined to have strong affinity (<500 nM). A subset of these epitopes are also stable binders (>1 hour) with at least one strong binder on each of the HLA alleles assessed. These data indicate that GATA3 neoORF epitopes are present in multiple HLA alleles.

Example 21: Creation of a cell line with a GATA3 mutation and an HLA allele

This example describes the generation of a cell line with a GATA binding protein 3 (GATA3) mutation, a novel open reading frame (neoORF), and a significant predominance of HLA alleles, HLA-A02:01 and HLA-B07:02. This cell line can be used as an in vitro surrogate for tumor cells that contain GATA3 neoORF mutations. Cell lines that naturally have a specific GATA3 neoORF in focus are not readily available, but are generated by stable lentiviral transduction of a commonly used cell line, HEK293T. This cell line was chosen because it naturally expresses two of the known HLA alleles, HLA-A02:01 and HLA-B07:02. This modified cell line was used for functional assays with T cells ( Example 25 and Example 26 ). Additionally, this cell line is used to validate neoantigens processing/presenting from the GATA3 neoORF on multiple HLA alleles ( Example 22 ). For these studies, the HLA allele is transiently transfected into the modified cell line.

Materials and methods

Overview of cell line generation with GATA3 mutation

Generation of GATA3 mutation transduced HEK 293T cells involves (a) designing a plasmid encoding the GATA3 mutation, obtaining a lentivirus, transducing the GATA3 mutation into a colony of HEK 293T cells, and selecting the transduced cells. These steps for creating a cell line with a GATA3 mutation are described below.

Cell lines and cultures

HEK 293T cell colonies were purchased from American Type Culture Collection (Rockford, MD, USA) and maintained in DMEM 10% FBS and Pen/Strep.

Design of a plasmid encoded by the GATA3 mutation

GATA3 gene mutation

For efficient expression of the GATA3 gene plasmid construct, mutations, 600 bp. wild-type GATA binding protein 3 (GATA3) sequences 1473 to 2074 (which contains DNA coding sequence (CDS) sequence 558 to 1892) are obtained from NCBI reference sequence: NM_001002295.01. The GATA3 mutation sequence is then created by deleting 2 nucleotides at 1734 and 1735 from the reference sequence ( FIG. 16 ). The GATA3 mutation sequence then translates into a frameshift at amino acid position 87 from the wild-type sequence ( FIG. 17 ). This DNA construct can span 87 residues of the wild-type GATA3 amino acid sequence and 114 residues of the GATA3 neoORF amino acid sequence with a frameshift caused by the deletion.

Plasmid design with GATA3 mutation

GATA3 mutation sequences were codon-optimized, synthesized and cloned into the pCDH-CMV-Puro vector (Genescript) (FIG. 18).

Obtaining Lentivirus

Lenti-X 293T cells (ClonTech) are cultured in complete culture medium (DMEM containing 10% FBS, Pen/Strep) and transfected with a GATA3 mutation-encoded lentiviral plasmid to produce lentivirus for the GATA3 mutation gene. The day before transfection, ^8x105 cells are seeded per well of a 6-well plate. The culture medium is changed on the day of transfection. 4 μg of lentiviral engineered plasmid and 4.6 μl of lentiviral packaging plasmid mixture (Sigma-Aldrich) were mixed in Opti-MEM (Thermo Fisher). The mixture is mixed with 10 μl FuGENE HD (Promega) and added directly to the cells. After 24 hours, the medium is replaced with fresh complete culture medium. The supernatant containing lentivirus was collected 72 hours after transfection.

Transduction of GATA3 mutations

5x10 ⁵ HEK 293T cells (ATCC) were seeded in 2 ml of DMEM containing 6 μg/ml polybrene and 10% FBS in a 12-well plate. 130 μl of supernatant containing GATA3 lentivirus is added directly to the cells. Cells are incubated in a 5% CO ₂ incubator. The medium is replaced with DMEM with 10% FCS and Pen/Strep after 24 hours.

Choice of pyromycin

Treatment with a 1 μg/ml concentration of pyromycin begins on day 2 after transduction of lentivirus with the GATA3 mutation. Cells were cultured and propagated using DMEM with 10% FCS, Pen/Strep and 1 μg/ml Pyromycin until harvested.

Transfection of HLA-coding constructs

1.5 x 10 ⁷ GATA3 mutation transduced HEK 293T cells are seeded in a T175 flask. 15 μg of HLA-A02:01, HLA-B07:02, or HLA-B08.01 encoded plasmids (Genewiz) were mixed with 70 μl of Fugene HD (Promega) and incubated at room temperature for 15 minutes. Mixtures of each HLA type plasmid and Fugene HD were added to GATA3 mutation-transduced HEK 293T cells in a T175 transfection flask. HEK 293T cells transfected with 3 different HLAs and transduced with the GATA3 mutation were cultured for 48 hours and then harvested.

Collection of GATA3 mutation-transduced and HLA-transfected cells

Cells are washed with 1x PBS and 0.25% Trypsin-EDTA (Thermo-Fisher scientific) is added. After 3 minutes of incubation at 37°C, cells are resuspended and collected with DMEM with 10% FBS and Pen/Strep. The washing steps are carried out 3 times and include centrifugation at 1500 rpm. for 5 min, then suspended with PBS buffer. The debris is flash frozen on dry ice in 70% ethanol. Frozen debris was stored at -80°C in a freezer for proteomics analysis.

results

GATA3 mutant-transduced HEK 293T were used as target cells to evaluate GATA3-specific TCR functional assays, and as material to evaluate GATA mutation presentation on HLA-A02.01 by mass spectrometry ( Example 22 ). Below are results demonstrating the generation of GATA3 mutant expressing HEK 293T cells.

Plasmid construct with GATA3 mutation

A GATA3 mutation-encoded plasmid construct is generated and evaluated through DNA sequencing on GENEWIZ. DNA sequencing data on the final plasmid encoded by the GATA3 mutation are 100% identical to the engineered sequence of the gene with the GATA3 mutation ( FIG. 19 ). After digestion with restriction endonuclease AflII, two DNA disks are observed between 5000 bp. and 3000 bp on track 2 analysis by gel electrophoresis. These disks correlate with the expected size of 4243 bp. and 3424 bp, respectively ( FIG. 20 ).

Transduction and collection of GATA3 mutations

HEK 293T cells are used to transduce the GATA3 mutation. Transduced cells are cultured until the total cell number reaches 200x10 ⁶ cells. On the day of collection, 1x10 ⁶ cells are used to express HLA Class I and HLA Class II on a flow cytometer ( FIG. 21 ). 99.5% of cells were HLA-Class I positive. 193 x 10 ⁶ cells are frozen for proteomics analysis.

HLA transfection

GATA3 mutation-transduced HEK 293T cells were transiently transfected with BAP-tagged HLA-A02.01, BAP-tagged HLA-B07.02, and BAP-tagged HLA-B08.01-encoded expression plasmids. Transfected cells are cultured for 48 hours and harvested. On the day of collection, 1x10 ⁶ cells are used to express HLA-A02.01 and HLA-I class using flow cytometry ( FIG. 22 ). Non-transfected ( FIG. 22A ), HLA-A02.01 transfected ( FIG. 22B ), HLA-B07.02 transfected ( FIG. 22C ) and HLA-B08.01 transfected ( FIG. 22C ) GATA3 HEK293T cells. All transfected cells overexpress HLA-A02.01 and HLA-I class.

A modified cell line is created that expresses the GATA3 neoORF upon stable transduction of a lentivirus containing the mutated GATA3 gene in HEK293T cells. HEK 293T cells transduced with the GATA3 mutation express HLA-I class. This cell line is then used as a target for functional assays with T cells specific for the GATA3 neoantigen ( Example 25 and Example 26 ). Then, after transfection with several common HLA alleles, these cell lines showed a broader distribution of HLA class I and HLA-A:02 expression levels, and are used to assess the processing and presentation of multiple neoantigens on these alleles ( Example 22 ).

Example 22 Evaluation of GATA3 neoORF peptide epitopes by mass spectrometry

This example provides validation of the endogenous processing and presentation of predicted peptide epitopes derived from the novel open reading frame (neoORF) GATA binding protein 3 (GATA3) common region for binding to HLA-A*02:01, HLA-B*07:02 and HLA-B*08:01 heterodimer, mass spectrometry. HEK293T cells are engineered to stably express the GATA3 neoORF and transiently transfected to express biotin acceptor peptide (BAP)-tagged HLA alleles of interest. Prediction of allele-specific peptide epitopes and generation of HEK293T cells are described in Example 19 and Example 21 , respectively. HLA-peptide complexes are isolated from cell lysates by affinity adsorption of a biotinylated BAP tag expressed on the alpha chain of each HLA class I heterodimer. Peptide ligands are isolated from HLA-peptide complexes by acid treatment and desalted by reverse phase liquid chromatography. HLA peptide ligands are then separated by nanoliquid chromatography coupled to high-resolution tandem mass spectrometry (nLC-MS/MS). Predicted peptide epitopes derived from the GATA3 neoORF are subjected to targeted nLC-MS/MS, whereby a priori knowledge of the precursor mass of each peptide epitope is used to select the theoretical monoisotopic mass of each peptide epitope for fragmentation by high-energy collisional dissociation (HCD) and subsequent peptide sequencing. GATA3 neoORF peptide epitopes are matched from the acquired tandem mass spectra (MS/MS) using a database matching algorithm to a database containing GATA3 neoORF, and using precursor mass spectral comparison (MS) and MS/MS spectra corresponding to their synthetic peptides analogues.

In total, five peptide epitopes from the general GATA3 neoORF region that bind to three different HLA heterodimers were detected by nLC-MS/MS in engineered HEK293T cells. For HLA-A*02:01, the following two of the four targeted peptide epitopes were identified: SMLTGPPARV (SEQ ID NO: 3411) and MLTGPPARV (SEQ ID NO: 3412). For HLA-B*07:02, the following two of the five targeted peptide epitopes were identified: KPKRDGYMF (SEQ ID NO: 3413) and KPKRDGYMFL (SEQ ID NO: 3414). For HLA-B*08:01, one of eight targeted peptide epitopes was identified as follows: ESKIMFATL (SEQ ID NO: 3415). Determination and identification of these peptide epitopes using nLC-MS/MS from cells expressing GATA3 neoORF demonstrated that they are endogenously processed and then bound by the HLA heterodimer.

Materials and methods

Peptides: Synthesize ¹² C ¹⁴ N synthetic peptides corresponding to GATA3 neoORF peptide epitopes.

Table 21 below provides a list of synthetic peptides corresponding to GATA3 neoORF predicted peptide epitopes.

Allele Subsequence Length Theoretical molecular weight HLA-A*02:01 SMLTGPPARV (SEQ ID NO: 3416) 10 1027.5484 HLA-A*02:01 MLTGPPARV (SEQ ID NO: 3417) 9 940.5164 HLA-B*07:02 KPKRDGYMF (SEQ ID NO: 3418) 9 1140.5750 HLA-B*07:02 KPKRDGYMFL (SEQ ID NO: 3419) 10 1253.6590 HLA-B*08:01 ESKIMFATL (SEQ ID NO: 3420) 9 1054.5368

Cell culture

Generation of engineered HEK293T cells that stably express the GATA3 neoORF and transient transfection of each affinity-tagged (BAP-tagged) allele are described in Example 21 . Table 22 lists the samples and numbers of cells used for targeted nLC-MS/MS.

Table 22 below shows samples for targeted nLC-MS/MS

Allele Cell type Number of cells (x10 ⁶ ) Affinity adsorption type HLA-A*02:01 HEK293T 55 affinity-labeled HLA-B*07:02 HEK293T 61 affinity-labeled HLA-B*08:01 HEK293T 60 affinity-labeled

Affinity adsorption of affinity-labeled (BAP-labeled) HLA-peptide complexes

Frozen debris containing BAP-tagged HLA molecules are thawed on ice for 20 min, then gently lysed by hand pipetting in cold lysis buffer [20 mM Tris-Cl pH 8, 100 mM NaCl, 6 mM MgCl ₂ , 1.5% ( v/v) Triton X-100, 60 mM octyl BD-glucopitanoside, 0.2 mM 2-iodoacetamide, 1 mM EDTA pH 8, 1 mM PMSF, 1X EDTA-free complete protease inhibitor cocktail] in a ratio of 1, 2 ml lysis buffer per 50x10 ⁶ cells. Lysates are incubated inverted at 4°C for 15 min and benzonase nuclease is added at a ratio of ≥250 units of benzonase per 50 x 10 ⁶ cells to digest DNA/RNA, then centrifuged at 15,000 x g at 4°C for 20 min to remove cellular debris and insoluble materials. Cleared supernatants are transferred to new tubes and BAP-tagged HLA molecules are biotinylated by inversion incubation at room temperature for 10 min in a 1.5 ml tube with 0.56 µM biotin, 1 mM ATP/1 mM magnesium acetate and 3 µM BirA . The supernatants are incubated by inversion at 4°C for 30 min in a volume corresponding to 200 μl of Pierce NeutrAvidin high performance agarose bead resin suspension on 50 x 10 ⁶ cells for affinity enriched biotinylated-HLA-peptide complexes. Finally, the HLA-bound resin is washed four times with 1 ml of cold wash buffer (20 mM Tris-Cl pH 8, 100 mM NaCl, 60 mM octyl BD-glucopyranoside, 0.2 mM 2-iodoacetamide, 1 mM EDTA, pH 8), then washed four times with 1 ml of cold wash 10 mM Tris-Cl pH 8. Between washes, the HLA-bound resin was mixed gently by hand, then pelletized by centrifugation at 1500 xg at 4°C for 1 min. NeutrAvidin beaded agarose resin is washed three times with 1 ml of cold PBS before use. The washed HLA-bound resin is stored at -80°C for less than one week, then eluted with HLA peptide.

Desalting, reduction and alkylation of HLA peptide

HLA peptides are eluted from affinity-labeled (BAP-labeled) HLA complexes and simultaneously desalted using a Sep-Pak solid-phase extraction system. Briefly, Sep-Pak cartridges are attached to a 24-position solid-phase extraction manifold, activated twice with 200 μL of methanol, then 100 μL of 50% (v/v) acetonitrile/0.1% (v/v) formic acid. , then washed four times with 500 µl 1% (v/v) formic acid. To dissociate HLA peptides from affinity-labeled (BAP-labeled) HLA molecules and improve binding of peptides to the tC18 solid phase, 400 μl of 3% (v/v) acetonitrile/5% (v/v) formic acid is added into tubes containing HLA-linked beaded agarose resin. The suspension is mixed by pipetting, then transferred to Sep-Pak cartridges. The tubes and pipette are washed with 1% (v/v) formic acid (2x200 µl) and the wash is transferred to cartridges. 100 femtomoles of the Pierce peptide retention time calibration mixture are added to the cartridges as a loading control. The beaded agarose resin is incubated twice for 5 min with 200 μl of 10% (v/v) acetic acid to further dissociate HLA peptides from affinity-labeled (BAP-labeled) HLA molecules, then washed four times with 500 μl 1% (v/v) formic acid. HLA peptides are eluted with tC18 into new 1.5 ml microtubes by fractionation steps with 250 µl 15% (v/v) acetonitrile/1% (v/v) formic acid, then 250 µl 30% (v/v) .) acetonitrile/1% (v/v) formic acid. Solutions are used for activation, sample loading, washing and gravity elution, and vacuum (≥-2.5 ^psi ) is used to remove remaining eluate from the cartridges. Eluates containing HLA peptides are frozen, dried by vacuum centrifugation and stored at -80°C, then subjected to reduction, alkylation and a second desalting.

Reduction and alkylation of cysteine-containing HLA peptides is carried out in 1.5 ml microtubes as follows. Dried peptides were solubilized in 200 μl of 10 mM Tris-Cl pH 8, then reconstituted by incubation with 5 mM dithiothreitol at 60°C for 30 min with shaking at 1000 rpm. in ThermoMixer. Reduced thiols are alkylated by incubation with 15 mM 2-iodoacetamide at room temperature for 30 min in the dark. Any unreacted 2-iodoacetamide is quenched by incubating with 5 mM dithiothreitol for 15 min at room temperature in the dark. Samples are desalted immediately after reduction and alkylation.

Secondary desalting of HLA peptide samples is carried out using internal inline StageTips packaged using two 16 gauge Empore C18 solid phase extraction disc punches. StageTips are activated twice with 100 µl methanol, then 50 µl 99.9% (v/v) acetonitrile/0.1% (v/v) formic acid, then washed three times with 100 µl 1% (v/v) vol.) formic acid. The peptide solution was acidified by adding 200 μL of 3% (v/v) acetonitrile/5% (v/v) and loaded onto StageTips. Tubes and pipette tips are washed with 200 µl 3% (v/v) acetonitrile/5% (v/v) followed by 1% (v/v) formic acid (2x100 µl) and the washes are transferred to StageTips. StageTips are washed five times with 100 μL 1% (v/v) formic acid. Peptides are eluted into 1.5 ml microtubes using a stepwise gradient of 20 µl 15% (v/v) acetonitrile/1% (v/v) formic acid, then two 20 µl portions of 30% (v/v) formic acid. ) acetonitrile/1% (v/v) formic acid. Sample loading, washing and elution are carried out in a centrifuge with a maximum speed of 1800-3500 x g at room temperature. The eluates are frozen, dried by vacuum centrifugation and stored at -80°C.

HLA peptide sequencing via nLC-MS/MS

All nLC-MS/MS analyzes use the same liquid chromatography separation conditions described below. Peptides are chromatographically separated using an EASY-nLC 1200 System equipped with a 75 µM i.d. PicoFrit nanospray column with a 10 µM emitter, packaged at ~1000 psi ² helium to ~35 cm using ReproSil-Pur 120Ǻ C18-AQ packaging material 1.9 µM, and heated at 60°C during separation. The column is equilibrated with a 10X volume of solvent A layer [3% (v/v) acetonitrile/0.1% (v/v) formic acid], samples loaded into 4 μl of 3% (v/v) acetonitrile/ 5% (v/v) formic acid, and the peptides were eluted with a linear gradient of 6-40% solvent B [80% (v/v) acetonitrile/0.1% (v/v) formic acid] in for 84 min, 40-60% solvent B for 9 min, then incubate in 90% solvent B for 5 min and 50% solvent B for 9 min to wash the column. Linear gradients were run at 200 nL/min.

Peptides were eluted into an Orbitrap Fusion Lumos Tribrid Mass Spectrometer equipped with a Nanospray Flex Ion source at 2.5 kV. Full-range MS is acquired at a resolution of 15,000 from 300-1800 m / z with the goal of automated trap fill control (AGC) of 4x10 ⁵ and a maximum injection time of 50 milliseconds. After each MS scan, an MS/MS scan is then performed according to the mass inclusion list ( Table 23 ) containing the calculated ion masses ( m/z ) of GATA3 neoORF-targeted peptide epitopes and their predicted charge states ( z ). Additional calculated ion masses have been included for peptides that meet the following criteria: i) multiple charge states are expected due to the presence of one or more basic residues in the sequence and/or ii) peptides containing amino acids that are expected to be modified during sample processing, such as cysteine, methionine and N-terminal glutamine. The maximum injection time varies from 100 milliseconds to 120 milliseconds to maintain a cycle time of 2-2.8 seconds at the chromatographic peak. MS/MS scans are acquired at 15000 resolution from 110 to 1300-1500 m/z , using an isolation width of 1 m/z , HCD normalized collision energy of 34, and a target AGC of 1x 10 ⁵ .

Table 23 provides a list of inclusion masses of GATA3 neoORF peptide epitopes for each HLA allele

# Allele Peptide sequence* m/z z 1 HLA-A*02:01 MLTGPPARV (SEQ ID NO: 3421) 471.2655 2 2 HLA-A*02:01 mlTGPPARV (SEQ ID NO: 3422) 479.2629 2 3 HLA-A*02:01 SMLTGPPARV (SEQ ID NO: 3423) 514.7815 2 4 HLA-A*02:01 SmlTGPPARV (SEQ ID NO: 3424) 522.7790 2 5 HLA-A*02:01 TLQRSSLWCamcL (SEQ ID NO: 3425) 421.8887 3 6 HLA-A*02:01 TLQRSSLWCamcL (SEQ ID NO: 3426) 632.3294 2 7 HLA-A*02:01 TLQRSSLWCcysL (SEQ ID NO: 3427) 442.5495 3 8 HLA-A*02:01 TLQRSSLWCcysL (SEQ ID NO: 3428) 663.3207 2 9 HLA-A*02:01 TLQRSSLWCL (SEQ ID NO: 3429) 402.8815 3 10 HLA-A*02:01 TLQRSSLWCL (SEQ ID NO: 3430) 603.8186 2 eleven HLA-A*02:01 YMFLKAESKI (SEQ ID NO: 3431) 410.5581 3 12 HLA-A*02:01 YmFLKAESKI (SEQ ID NO: 3432) 415.8898 3 13 HLA-A*02:01 YMFLKAESKI (SEQ ID NO: 3433) 615.3336 2 14 HLA-A*02:01 YmFLKAESKI (SEQ ID NO: 3434) 623.3310 2 1 HLA-B*07:02 FATLQRSSL (SEQ ID NO: 3435) 511.7851 2 2 HLA-B*07:02 GPPARVPAV (SEQ ID NO: 3436) 432.2585 2 3 HLA-B*07:02 KPKRDGYMF (SEQ ID NO: 3437) 381.1989 3 4 HLA-B*07:02 KPKRDGYmF (SEQ ID NO: 3438) 386.5306 3 5 HLA-B*07:02 KPKRDGYMF (SEQ ID NO: 3439) 571.2948 2 6 HLA-B*07:02 KPKRDGYmF (SEQ ID NO: 3440) 579.2922 2 7 HLA-B*07:02 KPKRDGYMFL (SEQ ID NO: 3441) 418.8936 3 8 HLA-B*07:02 KPKRDGYmFL (SEQ ID NO: 3442) 424.2253 3 9 HLA-B*07:02 KPKRDGYMFL (SEQ ID NO: 3443) 627.8368 2 10 HLA-B*07:02 KPKRDGYmFL (SEQ ID NO: 3444) 635.8343 2 eleven HLA-B*07:02 MFATLQRSSL (SEQ ID NO: 3445) 577.3053 2 12 HLA-B*07:02 mFATLQRSSL (SEQ ID NO: 3446) 585.3028 2 1 HLA-B*08:01 ESKIMFATL (SEQ ID NO: 3447) 520.2783 2 2 HLA-B*08:01 ESKImFATL (SEQ ID NO: 3448) 528.2757 2 3 HLA-B*08:01 FATLQRSSL (SEQ ID NO: 3449) 511.7851 2 4 HLA-B*08:01 FLKAESKIM (SEQ ID NO: 3450) 356.2037 3 5 HLA-B*08:01 FLKAESKIm (SEQ ID NO: 3451) 361.5353 3 6 HLA-B*08:01 FLKAESKIM (SEQ ID NO: 3452) 533.8019 2 7 HLA-B*08:01 FLKAESKIm (SEQ ID NO: 3453) 541.7994 2 8 HLA-B*08:01 FLKAESKIMF (SEQ ID NO: 3454) 405.2265 3 9 HLA-B*08:01 FLKAESKImF (SEQ ID NO: 3455) 410.5581 3 10 HLA-B*08:01 IMKPKRDGYM (SEQ ID NO: 3456) 413.5510 3 eleven HLA-B*08:01 ImKPKRDGYM (SEQ ID NO: 3457) 418.8826 3 12 HLA-B*08:01 ImKPKRDGYm (SEQ ID NO: 3458) 424.2143 3 13 HLA-B*08:01 IMKPKRDGYM (SEQ ID NO: 3459) 619.8228 2 14 HLA-B*08:01 ImKPKRDGYM (SEQ ID NO: 3460) 627.8203 2 15 HLA-B*08:01 ImKPKRDGYm (SEQ ID NO: 3461) 635.8178 2 16 HLA-B*08:01 LHFCamcRSSIM (SEQ ID NO: 3462) 384.1881 3 17 HLA-B*08:01 LHFCamcRSSIm (SEQ ID NO: 3463) 389.5197 3 18 HLA-B*08:01 LHFCamcRSSIM (SEQ ID NO: 3464) 575.7784 2 19 HLA-B*08:01 LHFCamcRSSIm (SEQ ID NO: 3465) 583.7759 2 20 HLA-B*08:01 LHFCcysRSSIM (SEQ ID NO: 3466) 606.7698 2 21 HLA-B*08:01 LHFCcysRSSIm (SEQ ID NO: 3467) 614.7672 2 22 HLA-B*08:01 MFATLQRSSL (SEQ ID NO: 3468) 577.3053 2 23 HLA-B*08:01 mFATLQRSSL (SEQ ID NO: 3469) 585.3028 2 24 HLA-B*08:01 YMFLKAESKI (SEQ ID NO: 3470) 410.5581 3 25 HLA-B*08:01 YmFLKAESKI (SEQ ID NO: 3471) 415.8898 3 26 HLA-B*08:01 YMFLKAESKI (SEQ ID NO: 3472) 615.3336 2 27 HLA-B*08:01 YmFLKAESKI (SEQ ID NO: 3473) 623.3310 2 *caps m=oxidized methionine, Camc=ureamethylated cysteine, Ccys=cysteinylated cysteine

Database Search

Mass spectra are interpreted using the Spectrum Mill software package. MS/MS spectra were excluded from the search if they did not have an MH+ precursor in the 600–2000 Da range, had a precursor charge of >5, or had <4 detected peaks. The merging of similar spectra with the same precursor m/z obtained in the same chromatographic peak is disabled. MS/MS spectra were analyzed against a database that contained all UCSC Genome Browser genes with genome annotation of hg19 and its protein-coding transcripts (63,691 entries) combined with the full-length GATA3 neoORF sequence and 150 common contaminants. Before database searching, all MS/MS were required to pass a spectral quality filter with a sequence tag length >2 (i.e., a minimum of 3 masses separated by the mass of the amino acid in the chain). The minimum spina bifida score is set to 5 and the “ESI QExactive HLA v2” scoring scheme is used. All spectra were examined using non-enzyme specificity, a fixed modification of carbamidomethylation of cysteine (Camc) and the following variable modifications: oxidized methionine (m), pyroglutamic acid and cysteinylation (Ccys). The precursor and product mass tolerances are set to 0.1 Da and 10 ppm, respectively, and the minimum peak intensity consensus is set to 30%. Peptide spectrum matches (PSMs) for individual spectra were automatically developed as confidently assigned using Spectrum Mill's autovalidation module to apply target-decoy based FDR scoring at the PSM rank to set scoring threshold criteria. An automatic threshold strategy using a minimum sequence length of 7, automatic filtering by variable range precursor mass, and Rank1-Rank2 score and delta score thresholds were optimized for all nLC-MS/MS runs for the HLA allele, resulting in a PSM FDR score of < 1% for each charge state of the predecessor.

The equation

The experimental monoisotopic molecular mass (MW) of each peptide epitope is calculated according to the following equation, where m/z is the mass-to-charge ratio of the peptide epitope detected by the mass spectrometer, z is the charge of the peptide epitope, and 1.007276 is the monoisotopic molecular mass of the proton.

Equation 8. Experimental MM = (( m/z ) × (z)) – ((z) × (1.007276))

RESULTS

Targeted nLC-MS/MS was used to validate endogenous processing of GATA3 neoORF-derived peptide epitopes that were predicted to bind to HLA-A*02:01, HLA-B*07:02, and HLA-B*08:01. Five peptide epitopes derived from the general GATA3 neoORF region were detected in HEK293T cells for three alleles ( FIG . 23 ).

For the HLA-A*02:01 heterodimer, five peptides derived from the general region of the GATA3 neoORF are targeted by nLC-MS/MS. Two peptides from the general region, SMLTGPPARV (SEQ ID NO: 3474) and MLTGPPARV (SEQ ID NO: 3475), were successfully identified by database searches and spectral compatibility with their synthetic peptide partners. Theoretical and experimental monoisotopic molecular masses for each peptide epitope with associated mass error are shown in Table 24 . The skeletal cleavage score and estimated peak intensity from the Spectrum Mill database search engine are shown in Table 25 . The backbone cleavage score indicates the number of fragment-specific ions generated by the HCD, whereas the peak intensity score indicates the percentage of ion current in the MS/MS spectrum as explained by the search interpretation.

Table 24 below lists the theoretical and experimental molecular masses with mass error

Allele Subsequence* Theoretical MM (Yes) Experimental MM (Yes) Mass error (Yes) HLA-A*02:01 SMLTGPPARV (SEQ ID NO: 3476) 1027.5484 1027.5570 0.0086 HLA-A*02:01 MLTGPPARV (SEQ ID NO: 3477) 940.5164 940.5126 -0.0038 HLA-B*07:02 KPKRDGYMF (SEQ ID NO: 3478) 1140.5750 1140.5748 -0.0002 HLA-B*07:02 KPKRDGYMFL (SEQ ID NO: 3479) 1253.6590 1253.6514 -0.0076 HLA-B*08:01 ESKImFATL (SEQ ID NO: 3480) 1054.5368 1054.5370 0.0002 *capital m means methionine oxidation.

Table 25 shows the interpretation criteria from the database search

Allele Sequence coverage map*
Key: /y-ion, \b-ion, | b- and y-ions Assessment of skeletal clefts Estimated peak intensity (%) HLA-A*02:01 S M|L|T/G/P/P R V (SEQ ID NO: 3481) 5/9 78.5 HLA-A*02:01 M/L|T/G/P/P R V (SEQ ID NO: 3482) 5/8 83.6 HLA-B*07:02 K/P|K/R D G Y|M|F (SEQ ID NO: 3483) 5/8 81.1 HLA-B*07:02 K/P/K R D G Y\M|F\L (SEQ ID NO: 3484) 5/9 72.2 HLA-B*08:01 E S K\I m\F\A/T/L (SEQ ID NO: 3485) 5/8 73.9 *capital m means methionine oxidation.

Each MS/MS spectrum generated on an endogenously processed peptide epitope was matched to an MS/MS spectrum generated using the corresponding synthetic peptide. In FIG. 24 shows a spectral comparison of the MS/MS spectrum for the endogenously processed peptide epitope SMLTGPPARV (SEQ ID NO: 3486) ( FIG. 24A bottom ) and the MS/MS spectrum of its corresponding synthetic peptide ( FIG. 24A top ). In FIG. 24B shows an alternative image of an identical spectral match. These top-down plots were created using the top 45 or 50 most abundant ions for 9mer and 10mer peptide epitopes, respectively (http://orgmassspec.github.io/).

In FIG. 25 shows a comparison of MS/MS spectra for the HLA-A*02:01 endogenously processed peptide MLTGPPARV (SEQ ID NO: 3487).

For HLA-B*07:02, five peptide epitopes derived from the general GATA3 neoORF region are targeted by nLC-MS/MS. Two peptide epitopes from the common region, KPKRDGYMF (SEQ ID NO: 3488) and KPKRDGYMFL (SEQ ID NO: 3489), were successfully identified by database searches and spectral compatibility with their synthetic peptides. Theoretical and experimental molecular masses for each peptide epitope with associated mass error are shown in Table 24 . The skeletal cleavage score and estimated peak intensity from the search engine are shown in Table 25 .

In FIG. 26 and FIG. 27 shows a comparison of the spectra for the HLA-B*07:02 peptide epitopes KPKRDGYMF (SEQ ID NO: 3490) and KPKRDGYMFL (SEQ ID NO: 3491), respectively.

For HLA-B*08:01, eight peptide epitopes derived from the general GATA3 neoORF region are targeted by nLC-MS/MS. One peptide epitope from the general region, ESKIMFATL (SEQ ID NO: 3492), was successfully identified by database searching and spectral matching to the corresponding synthetic peptide. This peptide is determined with the sulfoxide form of methionine, which gives a mass shift of 15999 Da, indicating the addition of oxygen from the side chain. Oxidation of methionine (shown with a capital m) to the sulfoxide form is a common result of sample processing. The theoretical and experimental molecular mass for ESKImFATL (SEQ ID NO: 3493) with associated mass error is shown in Table 24 . The skeletal cleavage score and estimated peak intensity from the search engine are shown in Table 25 .

In FIG. 28 shows a comparison of spectra for the HLA-B*08:01 peptide epitope ESKImFATL (SEQ ID NO: 3494).

Targeted nLC-MS/MS was used to validate the processing and presentation of five peptide epitopes derived from the general GATA3 neoORF region that were predicted to bind to HLA-A*02:01, HLA-B*07:02 and HLA-B* 08:01 heterodimer. HLA class I heterodimer is purified from HEK293T cells stably expressing GATA3 neoORF using an affinity tag that is genetically expressed on the alpha chain of each HLA class I heterodimer. Each affinity-tagged heterodimer (BAP-tagged HLA allele) was transiently transfected into HEK293T cells expressing GATA3 neoORF as described in RP19-005. The correct linear sequence for each target peptide epitope is confirmed by nLC-MS/MS by peptide sequencing. All MS/MS spectra are interpreted using the Spectrum Mill database search engine, which matches experimental MS/MS spectra to peptides from a database containing >63,000 entries, including the full-length GATA3 neoORF. The molecular mass for each observed peptide epitope is calculated to within ±0.01 Da of its theoretical molecular mass. Interpretation of the experimental MS/MS spectra revealed that ≥72% of the ion current in the MS/MS spectra could be explained by sequence-specific fragment ions. Further confirmation of the sequence of the endogenously processed peptide epitope was performed by spectral comparison with the MS/MS spectrum of the corresponding synthetic peptide, which showed identical fragment ion masses and backbone cleavage patterns. Together, targeted nLC-MS/MS confirms that HLA-A*02:01 peptide epitopes SMLTGPPARV (SEQ ID NO: 3495) and MLTGPPARV (SEQ ID NO: 3496), HLA-B*07:02 peptide epitopes KPKRDGYMF (SEQ ID NO: 3497) and KPKRDGYMFL (SEQ ID NO: 3498) and the HLA-B*08:01 peptide epitope ESKIMFATL (SEQ ID NO: 3499) are endogenously processed in HEK293T cells and then bound by the HLA heterodimer.

Example 23 Immunogenicity on MHC I

This example evaluates the immunogenicity of GATA3 neoORF on different, most common HLA alleles. GATA3 neoORF is a frameshift mutation occurring before the natural stop codon, causing the protein to be extended by at least 61 new amino acids. Immunogenicity is assessed in vitro by inducing PBMC from a healthy donor (HD) against predicted minimal epitopes specific for HLA-A02:01, A03:01, A24:02, B07:02, or B08:01.

Materials and methods

Table 26 lists the peptide pools derived based on allele restriction

Peptide pool Subsequence Peptide length Ultimate purity Experimental MM HLA allele A02.01 SMLTGPPARV (SEQ ID NO: 3500) 10 100% 1028.1 A02.01 YMFLKAESKI (SEQ ID NO: 3501) 10 100% 1229.4 B08.01/ A02.01/ A24.02 VLPEPHLAL (SEQ ID NO: 3502) 9 100% 988.4 A02.01 TLQRSSLWCL (SEQ ID NO: 3503) 10 98% 1206.5 A02.01 MLTGPPARV (SEQ ID NO: 3504) 9 100% 941.3 A02.01 A03.01 YMFLKAESK (SEQ ID NO: 3505) 9 80% 1116.2 A03.01 KIMFATLQR (SEQ ID NO: 3506) 9 71% 1107.3 A03.01 VLWTTPPLQH (SEQ ID NO: 3507) 10 85% 1191.3 A03.01 A24.02 YMFLKAESKI (SEQ ID NO: 3508) 10 85% 1229.4 B08.01/ A02.01/ A24.02 MFLKAESKI (SEQ ID NO: 3509) 9 86% 1066.3 A24.02 YMFLKAESK (SEQ ID NO: 3510) 9 80% 1116.2 A03.01/ A24.02 KIMFATLQR (SEQ ID NO: 3511) 9 71% 1107.3 A03.01/ A24.02 VLWTTPPLQH (SEQ ID NO: 3512) 10 85% 1191.3 A03.01/ A24.02 B07.02 KPKRDGYMFL (SEQ ID NO: 3513) 10 71% 1254.3 B07.02 FATLQRSSL (SEQ ID NO: 3514) 9 83% 1022.2 B08.01/ B07.02 EPHLALQPL (SEQ ID NO: 3515) 9 81% 1017.2 B08.01/ B07.02 KPKRDGYMF (SEQ ID NO: 3516) 9 73% 1141.2 B07.02 GPPARVPAV (SEQ ID NO: 3517) 9 81% 863.0 B07.02 B08.01-1 FATLQRSSL (SEQ ID NO: 3518) 9 83% 1022.2 B08.01/ A24.02 ESKIMFATL (SEQ ID NO: 3519) 9 76% 1039.2 B08.01/ B07.02 FLKAESKIM (SEQ ID NO: 3520) 9 78% 1066.2 B08.01/ B07.02 EPHLALQPL (SEQ ID NO: 3521) 9 81% 1017.2 B08.01 B08.01-2 YMFLKAESKI (SEQ ID NO: 3522) 10 85% 1229.4 B08.01/ A02.01/ A24.02 MFATLQRSSL (SEQ ID NO: 3523) 10 80% 1153.2 B08.01/ B07.02 IMKPKRDGYM (SEQ ID NO: 3524) 10 74% 1238.4 B08.01 FLKAESKIMF (SEQ ID NO: 3525) 10 71% 1213.3 B08.01

Table 27 lists information about a healthy donor

Healthy donor ID Type I class HLA-A HLA-B HLA-C HD44 11:01:01 24:02:01 13:01:01 40:01:02 03:04:01 N/A HD45 03:01 68:01:02 39:01:01 51:08:01 07:02:01 16:02:01 HD48 02:06:01 29:02:01 07:02:01 48:01:01 07:02:01 08:03:01 HD50 02:01:01 68:03:01 35:01:01 51:01:01 07:02:01 16:02:01 HD56 01:01:01 68:01:02 08:01:01 40:08 03:04:01 07:01:01

N/A = donor is homozygous for a specific allele. Epitope-targeted alleles are highlighted in bold.

Induction using FMS-like tyrosine kinase 3 (FLT3L) ligand to stimulate DCs

FLT3L stimulation is carried out in the following way. PBMCs are thawed and resuspended at 5x10 ⁷ cells/ml in AIM-V medium. Benzonase (Sigma-Aldrich 70746) is added at 25-29 U/µl and incubated at 37°C for 30 min - 1 hour. CD14/CD25 depletion is carried out to remove monocytes (CD14) and T regulatory cells (CD25) according to the protocol manufacturer (Miltenyi Biotec, Inc 130-050-201, 130-092-983). Cells at 2x10 ⁶ cells/ml are resuspended in AIM-V medium with FLT3L (CellGenix 1415-050) at 50 ng/ml and seeded at 2 ml per well in a 24-well plate overnight. The peptide diluted in AIM-V is added at a final concentration of 2 μM and the wells are mixed gently. Cells are incubated with the peptide for 1 hour at 37°C.

Add maturation cocktail with tumor necrosis factor (TNF-a) (1000 U/ml) (CellGenix1406-050), IL-1b (10 ng/ml) (CellGenix1411-050), prostaglandin-E 1 (PGE-1) ( 0.5 μg/ml) and IL-7 (0.5 ng/ml) and incubated at 37°C overnight. After incubating the maturation cocktail overnight, FBS is added to each well at a final concentration of 10% by volume and mixed. Co-culture is introduced every 2-3 days, starting on day 5, by carefully replacing 75% of the medium with fresh Roswell Park Memorial Institute 1640 (RPMI) + 10% FBS with sufficient IL-7 and IL-15 for a final concentration of 5 ng/ml into the hole. For administrations after the first, the medium is changed to fresh 20/80+10% FCS with sufficient IL-7 and IL-15 for a final concentration of 5 ng/ml per well. The onset of mDC formation began on day 4.

Formation of mature dendritic cells (mDC)

PBMCs are thawed and resuspended at 5x10 ⁷ cells/ml in dendritic cell (DC) medium (Cellgenix 20801-0500). Benzonase is added (sigma-aldrich 70746) in an amount of 25-29 U/ml and incubated at 37°C for 30 minutes - 1 hour.

Isolation of monocytes by sorting is carried out according to the manufacturer's protocol (Miltenyi biotec, Inc 130-096-537). Cells are seeded in 6-well plates 3x10 ⁶ cells/well in 2 ml DC medium with granulocyte-macrophage colony-stimulating factor (GM-CSF) (800 U/ml) (CellGenix 1412-050) and IL-4 (400 U/ml) (CellGenix 1403-050) and incubated at 37°C for 5 days.

Loading and maturation of the peptide is carried out as follows. immDC from the wells are collected by pipetting and pelletized by centrifugation at 1200 rpm. within 5 minutes. Cells are resuspended in 1 ml DC medium. Cells are separated into pools with 0.2x10 ⁶ (or 0.5x10 ⁶ ) cells per well for each pool and incubated for 1 hour at 37°C with 1.6 μM peptide (0.4 μM final concentration). 800 μl (or 2 ml) DC medium is added per well to peptide-loaded immDCs and seeded in a 6-well plate with the following cytokines and incubated at 37°C for 2 days: IL-4 (400 U/ml) (CellGenix 1403 -050), GM-CSF (800 U/ml) (CellGenix 1412-050), TNF-a (10 ng/ml) (CellGenix1406-050), IL-1b (10 ng/ml) (CellGenix1411-050), PGE-1 (0.5 μg/ml) (Cayman from Czech republic), IL-6 (10 ng/ml) (CellGenix 1004-50).

Mature dendritic cells mediated long-term stimulation (mDC LTS)

On day 12, FLT3L-stimulated T cells were added. DCs are resuspended in 1 ml 20/80. The co-culture wells are collected and counted, and the cells are resuspended at 5x10 ⁶ /ml in 20/80. 1 ml of naive T cells is added to mDC in a ratio of 10:1 (T cells:mDC) with the cytokines IL-7 (5 ng/ml) IL-15 (5 ng/ml). Add medium to a final volume of 5 ml per well. Cocultures are incubated at 37°C. The coculture is loaded every 2-3 days, starting from the 15th day. Cells are propagated in larger flasks if necessary.

Equation 9: Medium to be added (ml) = (current volume (ml)×(180-glucose))/60

Cultures are restimulated on day 23 on new mDCs. DCs are resuspended in 1 ml 20/80. Coculture wells are harvested and cells are resuspended at 2e6/ml (or 5e6/ml) at 20/80. 1 ml of naive T cells is added to mDC in a ratio of 10:1 (T cells:mDC) with the cytokines IL-7 (5 ng/ml) IL-15 (5 ng/ml). The medium is added to a final volume of 5 ml per well. The coculture is incubated at 37°C. The coculture is loaded every 2-3 days. Cells are propagated in larger flasks if necessary.

Equation 9: Medium to be added (ml) = (current volume (ml)×(180-glucose))/60

On day 31, cells are frozen in 1 ml of freezing medium (90% FCS, 10% DMSO). Cells are stored overnight at -80°C in a CoolCell Freeze Container (VWR 75779-816) and then transferred to liquid nitrogen for long-term storage.

Multimer creation and analysis

Monomer for peptide exchange

An HLA MHC class I monomer loaded with UV cleavable peptide is created internally. The monomer is resuspended at 100 μg/ml in filtered PBS, and the analytical peptides are resuspended at 10 mg/ml in DMSO, and the UV-cleavable peptide is exchanged for individual analytical peptides in a ratio of 1 μl of peptide:50 μl of monomer under UV irradiation for 1 h at 4 °C. The exchanged monomer is centrifuged at 3600 rpm. and the supernatant is collected.

Fluorochrome conjugation

50 μl of pMHC is combined with streptavidin-labeled fluorochrome on ice for 30 min in the dark according to the conjugation ratio of each of the following fluorochromes (CR): PE (BioLegend 405203) (CR: 2); APC (BioLegend 405207) (CR: 3); BV421 (BioLegend 405226) (CR: 2); QD605 (Life Technologies Q10101 MP) (CR: 2); QD705 (Life Technologies Q10161 MP) (CR: 2); BUV395 (BD 564176) (CR: 2); BV650 (BD 563855) (CR: 2). Each pMHC is cleaved and conjugated to two separate fluorochromes. Biotin (Avidity BIO200) + 0.5% azide was added at a ratio of 1:20 and the multimer was stored at 4°C in the dark for 1 to 3 days. Flow cytometry data were obtained at days 11 and 22 and after freezing. ~2x10 ⁶ cells are collected in a propylene 96-well V-bottom plate in benzonase medium (sigma-aldrich 70746) at 25-29 U/μl and incubated at 37°C for 30 min - 1 h.

Cells were stained with all of the following fluorochrome-conjugated multimers loaded with induced peptides in 50 μl of filtered phosphate-buffered saline (PBS) for 15 min at 37°C in the dark. PE (BioLegend 405203) 1 µl; APC (BioLegend 405207) 3 µl; BV421 (BioLegend 405226) 1 µl; QD605 (Life Technologies Q10101 MP) 4.5 µl; QD705 (Life Technologies Q10161 MP) 4.5 µl; BUV395 (BD 564176) 3.5 µl; BV650 (BD 563855) 2.5 µl. Samples are stained with the following surface antibodies for 30 min on ice in the dark. Analyze on LSR-Fortessa for differentiation cluster (CD)8(+) / CD4(-) / CD14(-) / CD16(-) / CD19(-)/ dead(-) / multimer_1(+) / multimer_2 (+) /irrelevant multimer(-): CD8-FITC (Biolegend 344704) 2 µl, CD4-AF700 (BD 557922) 1 µl, CD14-AF700 (BD 557923) 1 µl, CD19-AFF700 (BD 557921) 1 µl, CD16-AF700 (BD 557920) 1 µl, Live dead stain (Molecular probes L-23101) 0.1 µl.

results

Each sample is stained with two multimers for each donor peptide raised against a unique fluorochrome combination. Positive inductions were defined as at least 10 events that were positive for at least 1 specific fluorochrome combination and negative for irrelevant fluorochrome combinations. Data are collected after each stimulation, and a positive result for two stimulations is considered a positive induction. In FIG. 29A and FIG. 29B shows typical induction of CD8+ neoantigen GATA3 responses.

Table 28 shows the proportion of positive responses to GATA3 neoantigen CD8+

Inducing peptide Allele Number of wells with reactive TCR Number of wells tested Proportion of positive inductions MLTGPPARV (SEQ ID NO: 3526) A02:01 5 5 100% SMLTGPPARV (SEQ ID NO: 3527) A02:01 1 5 20% GPPARVPAV (SEQ ID NO: 3528) B07:02 1 5 20% KPKRDGYMF (SEQ ID NO: 3529) B07:02 1 5 20% ESKIMFATL (SEQ ID NO: 3530) B08:01 1 5 20%

Table 28 shows the proportion of replicates that induce naïve CD8+ T cells, confirmed for two independent stimulations.

These results indicate that there is at least one minimal epitope in the GATA3 neoORF that can confer CD8+ specific induction in vitro for 4 of the 5 HLAs analyzed. The results indicate broad immunogenicity of the GATA3 neoORF across all HLAs and identify immunogenic minimal neoantigen epitopes specific to significantly abundant HLAs.

Example 24 Immunogenicity on MHC II

This example evaluates the CD4 immunogenicity of longmer peptides (>15 amino acids) specific to the GATA3 neoORF. An in vitro induction assay against five different healthy donors with minimal HLA-II class overlap is used to predict in vivo CD4 immunogenicity.

Materials and methods

Table 29 below lists the inducing peptides

Peptide pool Subsequence Peptide length Ultimate purity Molecular mass L1 PGRPLQTHVLPEPHLALQPLQPHADHA (SEQ ID NO: 3531) 27 95% 2971.2 APAIQPVLWTTPPLQHGHRHGLEPCS (SEQ ID NO: 3532) 26 90% 2843.4 PPARVPAVPFDLHFCRSSIMKPKRD (SEQ ID NO: 3533) 25 93% 2865.8 L2 EPHLALQPLQPHADHAHADAPAIQPV (SEQ ID NO: 3534) 26 92% 2774.2 TPPLQHGHRHGLEPCSMLTGPPARVPA (SEQ ID NO: 3535) 27 96% 2857.8 DLHFCRSSIMKPKRDGYMFLKAESK (SEQ ID NO: 3536) 25 88% 2989.0 KAESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 3537) 24 100% 1810.0 L3 HADHAHADAPAIQPVLWTTPPLQH (SEQ ID NO: 3538) 24 94% 2624.1 EPCSMLTGPPARVPAVPFDLHFCR (SEQ ID NO: 3539) 24 98% 2641.4 KPKRDGYMFLKAESKIMFATLQRS (SEQ ID NO: 3540) 24 98% 2846.8

Table 30 below provides information for healthy donors

Healthy donor ID HD41 HD44 HD63 HD47 HD56 Class II allele HLA-DPA1 01:03:01 02:02:02 01:03:01 01:03:01 01:03:01 01:04:01 02:02:02 01:03:01 01:03:01 02:01:02 HLA-DPB1 05:01:01 05:01:01 04:01:01 04:01:01 01:01:01 107:01 05:01:01 04:01:01 15:01:01 04:02:01 HLA-DQA1 03:03:01 01:02:02 02:01:01 05:01:01 03:01:01 01:03:01 05:08 04:01:01 05:05:01 05:01:01 HLA-DQB1 01:03:01 03:01:01 02:02:01 02:01:01 02:01:01 01:03:01 05:02:01 04:02:01 03:01:01 03:02:01 HLA-DRB1 04:05:01 12:01:01 07:01:01 03:01:01 03:01:01 11:01:01 16:02:01 08:02:01 11:02:01 04:04:01 HLA-DRB345 02:02:01 01:01:02 01:01:01 02:02:01 01:01:02 01:03:01 01:01:01 not present 02:02:01 01:03:01

Creation of mature dendritic cells (mDC)

Monocyte isolation

PBMCs are thawed and resuspended at 5x10 ⁷ cells/ml in dendritic cell (DC) medium (Cellgenix 20801-0500). Benzonase (sigma-aldrich 70746) is added at 25-29 U/μl and incubated at 37°C for 30 min - 1 hour. Monocytes are isolated by sorting according to the manufacturer's protocol (Miltenyi biotec, Inc 130-096-537). Cells were seeded in 6-well plates at 3x10 ⁶ cells/well in 2 ml DC medium with GM-CSF (800 U/ml) and IL-4 (400 U/ml) and incubated at 37°C for 5 days.

Peptide loading and maturation

immDCs are collected from wells by pipetting and pelletized by centrifugation at 1200 rpm. within 5 minutes. Cells are resuspended at 1 in DC medium. Cells are separated into pools with 0.2x10 ⁶ (or 0.5x10 ⁶ ) cells per well for each pool and incubated for 1 hour at 37°C with 1.6 μM peptide (0.4 μM final concentration). 800 μl (or 2 ml) DC medium is added per well for peptide-loaded immDCs and seeded in a 24 (or 6) well plate with the following cytokines and incubated at 37°C for 2 days; IL-4 (400 U/ml) (CellGenix 1403-050), GM-CSF (800 U/ml) (CellGenix 1412-050), TNF-a (10 ng/ml) (CellGenix1406-050), IL-1b (10 ng/ml) (CellGenix1411-050), PGE-1 (0.5 µg/ml) (Cayman from Czech republic), IL-6 (10 ng/ml) (CellGenix 1004-50)

Long term stimulation (LTS)

Naïve T cells are added. PBMCs are thawed and resuspended at 5x10 ⁷ cells/ml in DC medium (Cellgenix 20801-0500). Add benzonase (sigma-aldrich 70746) at 25-29 U/µl and incubate at 37°C for 30 min - 1 hour.

CD14/CD25 depletion was performed to remove monocytes (CD14) and T regulatory cells (CD25) according to the manufacturer's protocol (Miltenyi Biotec, Inc 130-050-201, 130-092-983). 1 ml of naïve T cells was added to mDC in a 10:1 ratio (T cells:mDC) with the cytokines IL-7 (5 ng/ml; CellGenix) IL-15 (5 ng/ml; CellGenix). The coculture is incubated at 37°C. mDC are either resuspended at 20/80 or maintained in DC media with cytokines.

The coculture is loaded every 2-3 days starting on day 5, then either method 1 or method 2 below (2.3.2.1.1 or 2.3.2.1.2) is used. Cells are propagated in larger flasks if necessary. For method 1, the addition medium is calculated as (ml) = (current volume (ml)×(180-glucose))/60. For method 2, a glucometer is used to check if the medium is yellow. If glucose remains high (>90 mg/dL), 100 µl of 20x IL-7 and IL-15 is added to the well. If glucose is low (<90 mg/dL), cells are expanded to a 6-well plate (4 ml/well) and 1x IL-15 and IL-7 are added. If glucose is very low (<60 mg/dL), multiply to 6 mL/well in a 6-well plate. On days 6 and 13 or 14, new mDCs are created.

On days 13 and 21 or 22, cultures on new mDCs are restimulated. The coculture wells are collected and counted, and the cells are resuspended at 2x10 ⁶ /ml (or 5x10 ⁶ /ml) at 20/80. 1 ml of naive T cells is added to mDC in a ratio of 10:1 (T cells:mDC) with the cytokines IL-7 (5 ng/ml) IL-15 (5 ng/ml). The coculture is incubated at 37°C. mDC are either resuspended at 20/80 or maintained in DC media with cytokines. At day 28 or 29, cells are frozen in 1 ml of freezing medium (90% FBS, 10% DMSO). Cells are stored overnight at -80°C in a CoolCell Freeze Container (VWR 75779-816) and then transferred to liquid nitrogen for long-term storage.

CD4 secondary immune response assay

Either generate new mDCs or thaw fresh PBMCs from the same induction donor. Seed cells at 0.26/well PBMC and 0.02x10 ⁶ /well mDC in a 96-well u-bottom plate with peptide or DMSO at 0.8 µM final concentration. The induction sample is added to the wells at a ratio of 1:1 induction:PBMC or 10:1 induction:mDC and incubated at 32°C for 20-24 hours.

Flow cytometry data

Golgy stop (BD 554724) and Golgy plug (BD 555029) were added to the cultures according to the manufacturer's protocol and incubated for 4 hours. Cells are stained with CD4-BV786 (BD 563877), CD8-AF700 (BD 561453), CD14-FITC (BD 340682), CD16-FITC (BD 340704), CD19-FITC (BD 340864), Live dead stain (Molecular probes L- 23101) for 20 minutes. Samples are fixed using the Fixation/Permeabilization kit (BD 554714) according to the manufacturer's protocol. Cells were stained with IFN-y-PE (Biolegend 502508) for 20 minutes. The analysis is carried out on LSR-Fortessa for CD4 (+) / CD8 (-) / CD14 (-) / CD16 (-) / CD19 (-), Dead (-) / IFNy (+).

results

Antigen-specific CD4 T cells were identified using flow cytometry ( FIG. 30A and FIG. 30B ). At least one GATA3 neoORF induction of a specific peptide is identified in each healthy donor.

Specific reactive peptides are identified through the secondary immune response of induced cells against individual peptides and comparison with the secondary immune response without the peptide. Each induction sample is first assayed against the induction pool, and positive samples are then induced to produce a secondary immune response against individual peptides. All samples are processed on duplicate plates, and if the average proportion of CD4+/IFNy+ induction samples with peptide is more than 2% compared to the same sample without peptide, the sample is considered affected.

Table 31 shows the proportion of CD4 neoantigen GATA3 responses

Inducing peptide HD41 HD44 HD56 HD47 HD63 EPHLALQPLQPHADHAHADAPAIQPV (SEQ ID NO: 3541) 0% 20% 0% 0% 0% APAIQPVLWTTPPLQHGHRHGL EPCS (SEQ ID NO: 3542) 0% 0% 0% 20% 0% PPARVPAVPFDLHFCRSSIMKPKRD (SEQ ID NO: 3543) 0% 20% 20% 0% 0% DLHFCRSSIMKPKRDGYMFLKAESK (SEQ ID NO: 3544) 40% 0% 20% 40% 20% KPKRDGYMFLKAESKIMFATLQRS (SEQ ID NO: 3545) 0% 40% 0% 0% 0% LKAESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 3546) 20% 0% 0% 0% 0%

Sequences in bold are in the GATA3 NeoOrf region common to all patients

At least one CD4 specific response was observed for the common GATA3 neoORF region in all healthy donors tested. These donors have a wide range of HLA MHC class II alleles, indicating that the ability to generate a CD4 GATA3 response is not allele dependent.

Example 25 Functional Assays with Induced CD8+ T Cells

This example demonstrates the ability of CD8+ T cells specific for neoantigens derived from GATA binding protein 3 (GATA3) novel open reading frame (neoORF) to kill cells having a suitable GATA3 neoORF mutation. The induction of neoantigen-specific CD8+ T cells is described previously in Example 23, and the creation of a cell line having a GATA3 neoORF mutation is described in Example 21.

In this example, CD8+ T cells specific for one epitope from the GATA3 neoORF presented on HLA-A02:01 (covered by the peptide sequence MLTGPPARV (SEQ ID NO: 3547)) are selected for this detailed analysis. Briefly, induced CD8+ T cells are cocultured with target cells either transduced with GATA3 neoORF or left untreated as a negative control. Following coculture, target cells are assessed for expression of caspase 3, a cell death marker, as a measure of CD8+ T cell-induced cytotoxicity. The increased caspase 3 on target cells expressing GATA3 neoORF compared to untreated cells represents specific killing due to the recognized epitope being presented on the surface of the target cell. In addition, CD8+ T cells are assessed for the expression of CD107a, a marker of T cell activation, to measure antigen-specific T cell activation. To further evaluate antigen-specific recognition of GATA3-induced PBMCs, IFN-γ, a cytokine produced by a CD8+ cytotoxic T cell upon antigen recognition, was also measured in the supernatant.

In total, four different populations of CD8+ T cells specific for the GATA3 neoORF epitope on HLA-A02:01 are tested for their ability to kill target cells harboring the mutation. In all four cases, increased caspase 3 was observed on target cells harboring the GATA3 neoORF compared to target cells without the mutation. Increased caspase 3 demonstrates the ability of CD8+ T cells specific for epitopes from GATA3 neoORF to kill cells harboring a GATA3 neoORF mutation.

Materials and methods

Cytotoxicity Assay

Colonies of HEK 293T cells were purchased from American Type Culture Collection (Rockford, MD, USA) and maintained in DMEM, 10% FBS and Pen/Strep. The lentivirus-encoded GATA3 gene is generated and transduced into HEK 293T cells. GATA3-transduced HEK 293T cells were maintained with 1 μg/ml puromycin in complete medium for over 2 weeks. Additional details are described in Example 21.

1 x 10 ⁷ target cells in 1 ml are added to 1 µl of Tag-it Violet (Biolegend) followed by incubation in a 5% CO ₂ incubator for 20 minutes, washing twice with 5 ml of culture medium with 10% FBS, and resuspending cells at 1 x 10 ⁶ cells in a culture medium.

Induced PBMC vials are thawed by placing them in a 37°C water bath. Then 1 ml of FTS is added to each vial. Cells are transferred to a 50 ml conical tube containing 15 ml AIM-V culture medium, 10% FCS and Pen/Strep. Cells are centrifuged at 1500 rpm. for 5 min and resuspended in 5 ml of culture medium. Cells were incubated for 1 hour and 30 minutes at 37°C in a 5% CO ₂ incubator, then 5 μl of benzonase (Millipore Sigma) was added and then incubated for 30 minutes at 37°C in a 5% CO ₂ incubator. The incubated cells are centrifuged again and, after removing the supernatant, resuspended in 5 ml of AIM-V medium. The number of cells is counted using a Vi-CELL counter (Beckman coulter).

Cells are centrifuged and resuspended in 40 μl of MACS buffer per 1 x 10 ⁷ target cells. CD8+ positive cells were negatively enriched according to the Human CD8+ T Cell Isolation Kit (Miltenyi Biotec). CD8+ cells are resuspended at 2.5 x 10 ⁶ cells in 1 ml of AIM-V medium. 5 x 10 ⁴ target cells per well are seeded in 50 μl of culture medium in a 96-well flat-bottom plate and cultured overnight at 37°C in a 5% CO ₂ incubator. GATA3-induced and CD8+ enriched cells were seeded above target cells at 2.5 x 10 ⁵ cells per well in 100 μl of AIM-V medium. Cocultured cells are incubated for 6 hours at 37°C in a 5% CO ₂ incubator.

Coculture culture supernatants were collected and IFN-γ concentration assessed using V-PLEX Human IFN-γ assays according to the manufacturer's protocol (Meso Scale Discovery).

The suspension cells are transferred to a new staining plate and the adherent cells are transferred after adding 50 μl of trypsin per well, incubated at 37°C and resuspended with AIM V medium. The cells are pooled, centrifuged and washed with FACS buffer. 50 µl of antibody mixture (anti-CD3-BUV8052, anti-CD4-BV711, anti-CD107a-BV786, anti-CD8+-PE-cy5 and Live/Dead IR dye; BD) is added to each sample, then incubated for 30 min on ice. Cells are washed with 100 μl FACS buffer. Intracellular caspase-3 staining was performed according to the manufacturer's instructions for the Cytofix/Cytoperm kit (BD) with 2 μl of caspase-3 antibody. Stained cells were analyzed on a Fortessa II (BD).

results

Cytotoxicity assay of GATA3-induced PBMCs

PBMCs from three different healthy donors (HD47, HD50 and HD51) were induced by GATA3 HLA-A:02 neoantigen peptide MLTGPPARV (SEQ ID NO: 3548) by a long-term stimulation method. This epitope:allele combination was determined to be optimal for testing in a cytotoxicity assay compared to other epitope:alleles related to GATA3 neoORF, taking into account allele frequency and cell number. In FIG. 31A-31D show GATA3 specific CD8+ T cells via multimer staining. These T cells are selected as effector cells for cytotoxicity assays.

GATA3 transduced HEK293T cells are used as target cells ( Example 21 ). Also, non-transduced HEK 293T cells were used as a negative control. After 6 hours of effector and target cell coculture, an average of 3.3%, 3.7%, 2.5%, and 2.8% caspase-3 positive cells were found in 4 experiments in non-transduced target cells, and an average of 4.4%, 5.2%, 6.3% and 6.9% of caspase-3 positive cells were found in GATA3 transduced cells, respectively ( FIG. 32 ). Significantly more caspase-3 positive target cells were found in coculture with GATA3-induced PBMCs from HD51 ( FIG. 33 ). A higher frequency of CD107a-expressed CD8+ T cells was observed when GATA3-transduced HEK293T cells were co-cultured with 2 of GATA-induced healthy donor PBMCs (sample 1 and sample 2) ( FIG. 34 ). Higher levels of IFN-γ were detected under the same co-culture conditions with 2 of the GATA-induced healthy donor PBMCs (sample 1 and sample 2) ( FIG. 35 ).

An in vitro cytotoxicity assay is used to evaluate the ability of GATA3 neoORF-specific CD8+ T cells to recognize and kill cells harboring a GATA3 frameshift mutation. PBMCs comprising frameshifted GATA3 neoantigen-specific T cells to HLA-A02:01 derived from healthy donors stimulated with the frameshifted GATA3 peptide MLTGPPARV (SEQ ID NO: 3549) are tested as representative of the T cell types which can be induced from GATA3 frameshift vaccines. These T cells lead to the death of the tumor cell, which is confirmed by analyzing the presence of the target cell death marker, caspase-3. Results from CD8+ T cell activation marker D107a and cytokine IFN-γ assays also suggest that these peptide-induced T cells may recognize and kill cells that naturally process and present GATA3 frameshift neoantigens.

Example 26 TCR Cloning and Functional Assays

The example below shows neoantigen-specific CD8+ T cell receptor (TCR) cloning from the GATA3 neoORF on HLA-A02:01 and functional assays. Induction of neoantigen-specific CD8+ T cells is described in Example 23 . Specific CD8+ T cells were isolated using fluorescence-activated cell sorting (FACS), and the TCR sequence was identified using the 10x Genomics and MiSeq platforms. Selected TCRs are then recombinantly expressed in T cell colonies to functionally characterize the TCR and assess neoantigen processing and surface presentation on cells harboring the GATA3 neoORF mutation, the creation of which is described in Example 21 .

The TCR is characterized by an avidity below 40 nM. This demonstrates that it is possible to generate CD8+ T cells with TCRs to GATA3 neoantigens. In addition, the TCR is capable of recognizing processed and presented neoantigen on the surface of HEK293T cells harboring the GATA3 neoORF mutation, as supported by the results in Example 22 , demonstrating the processing and presentation of GATA3 neoantigens on the surface of cells harboring the mutation.

Materials and methods

In FIG. Figures 36-38 provide an overview of TCR cloning and functional analysis. GATA3 CD8+ T cells are sorted by multimer.

GATA3 neoORF specific T cells are induced and expanded (Example 23). Induced cells are stained with GATA3 9mer peptide multimer and surface antibodies (CD8, CD4, CD14, CD16, CD19 and near-IR fluorescent reactive dye). GATA3 specific T cells that were positive for GATA3 multimer and CD8 were sorted using FACS ARIA fusion (BD) and collected into a 1.5 ml tube containing 2% FCS in PBS.

Single T cell TCR sequencing using 10x Genomics and MiSeq

After sorting, the collected cells are immediately processed by single cell barcoding and cDNA generation using Chromium Single Cell V(D)J Reagent Kits (10x Genomics). TCR sequence enrichment and library construction were performed according to the manufacturer's protocol. Sequencing is performed at 10 pM scale with the MiSeq 300 cycles reagent kit and MiSeq (Illumina). Analysis of TCR sequence and clonal properties was carried out using the Cell ranger program and the Loupe VDJ browser (10x Genomics).

Synthesis and cloning of the TCR gene

The selected TCR sequences are codon-optimized for the mammalian system. TCR DNA sequences were synthesized and cloned into a lentiviral vector (pCDH-EF1ɑ-Puro, System Biosciences) from GENEWIZ (NJ, USA). The lentiviral vector contains the EF1ɑ promoter followed by TCR beta, furin cleavage site, F2A, TCR alpha, T2A and a pyromycin resistance site ( FIG. 40 )

Obtaining Lentivirus

To obtain a lentivirus encoding the GATA3 neoORF TCR gene, a lentiviral vector, packaging plasmids and fresh HEK 293T cells (ATCC) are used by transfection. Transfection and collection details are described in Example 21 .

Transduction into Jurkat cells or PBMCs

Modified Jurkat cells (J.RT3-T3.5, ATCC), which lack TCR beta, are modified to express the CD8+ alpha chain of an lntivirus encoding the CD8+ alpha gene. Modified Jurkat cells are used to transduce GATA3 TCR lentivirus. 1.8 x 10 ⁶ Jurkat cells are seeded in 1.2 ml of RPMI-1640 medium with 10% FCS and 6 μg/ml polybrene in a 24-well plate. Then 0.6 ml of GATA3 specific TCR lentivirus is added to the cells, the plate is centrifuged at 2400 rpm. for 45 minutes at 32°C. Cells are incubated in a 5% CO2 incubator for 24 hours. Transduced Jurkat cells were maintained in RPMI-1640 medium with 10% FCS with 1 μg/ml puromycin for 10 days.

IL-2 release assay with peptide titration

To assess the sensitivity of the TCR that has been cloned into Jurkat cells, a peptide titration assay is performed. Jurkat cells specifically secrete IL-2 in response to TCR signaling. Since the Jurkat cells used in this assay do not have an endogenous TCR beta, the TCR on the surface of these cells is a specifically cloned TCR. Peptides are added at a wide range of concentrations to target HEK293T cells with the relevant HLA (HLA-A02:01), but not GATA3 mutation, to assess maximum IL-2 secretion, and to estimate the peptide concentration required to release 50% of this maximum secretion (EC50). This EC50 is taken as the TCR avidity. 20,000 unmodified HEK 293T cells that endogenously express HLA:A02.01 were plated in a 96-well plate supplemented with 100 μl of GATA3 peptide or irrelevant peptide at a concentration of 20 μM to 2 pM in DMEM with 10% FBS. After overnight incubation at 37°C, 200,000 GATA3 neoORF specific TCR transduced Jurkat cells were added to each well in a 10:1 ratio of TCR transduced Jurkat cells to peptide-loaded HEK 293T cells. The coculture is incubated in a 5% CO2 incubator at 37°C for 24 hours. 50 μl of supernatant from each well was collected and the human IL-2 concentration was measured with a Meso scale discovery kit according to the manufacturer's protocol.

IL-2 release assay with target cells transduced with GATA3 mutation

To assess the ability of the TCR to recognize truly processed and presented neoantigen, TCR-transduced Jurkat cells and target HEK 293T cells were cocultured. In this system, however, no peptides are added exogenously. Instead, cell lines transduced with either the GATA3 neoORF or an irrelevant gene are used as targets. Thus, for TCR-transduced Jurkat cells to recognize their targets, the GATA3 neoantigen must be processed and presented on the surface of the target cell.

20,000 HEK 293T cells transduced with the GATA3 mutation or irrelevant gene were seeded in a 96-well plate. After overnight incubation, 200,000 GATA3 specific TCR transduced Jurkat cells are added to each well. The coculture is incubated in a 5% CO2 incubator at 37°C for 24 hours. 50 μl of supernatant from each well was collected and the human IL-2 concentration was measured with a Meso scale discovery kit according to the manufacturer's protocol (Meso Scale Discovery).

results

GATA3 specific TCR cells Jurkat

GATA3 Sorting of Specific CD8+ T Cells

2.1% GATA3 specific CD8+ T cells were detected in well #5 of healthy donor 42 using GATA3 HLA-A02 multimer after long-term stimulation of GATA3 neoORF with the MLTGPPARV peptide (SEQ ID NO: 3550). 5402 double multimer positive cells were sorted using FACSARIA ( FIG. 39 ). Sorted cells are processed by single cell barcoding using the 10X Genomics V(D)J kit. Paired TCR alpha and beta sequences were analyzed using the Loupe V(D)J browser. The dominant clonotype (clonotype1) has the CALDIYGNNRLAF (SEQ ID NO: 3551) and CASSLDFVLAGSYSYEQFF (SEQ ID NO: 3552) CDR3 TCR alpha and beta amino acid sequences, respectively. Clonotype 2 has the same TCR beta sequence as clonotype 1, without the TCR alpha sequence. Clonotype 4 has the same TCR alpha sequence as clonotype 1, without the TCR beta sequence. The combined proportion of clonotypes 1, 2 and 4 is 82.5% of all TCR clonotypes, and other clonotypes account for less than 1% ( Table 32 ).

Table 32 below shows a typical GATA3 specific TCR clonotype analysis

clonotype_id Frequency Share CDR3 Amino acid sequence clonotype1 1178 48% TRA:CALDIYGNNRLAF (SEQ ID NO: 3553);TRB:CASSLDFVLAGSYSYNEQFF (SEQ ID NO: 3554) clonotype2 848 34% TRB:CASSLDFVLAGSYSYNEQFF (SEQ ID NO: 3555) clonotype4 12 0.5% TRA:CALDIYGNNRLAF (SEQ ID NO: 3556) clonotype3 12 0.5% TRA:CAEKVPNTGNQFYF (SEQ ID NO: 3557);TRB:CASSSLGTVRTEAFF (SEQ ID NO: 3558) clonotype5 10 0.4% TRA:CAVEAYNFNKFYF (SEQ ID NO: 3559);TRB:CASRSENTIYF (SEQ ID NO: 3560) clonotype6 10 0.4% TRA:CILSDSGNTPLVF (SEQ ID NO: 3561);TRB:CASSDWAVSGNTIYF (SEQ ID NO: 3562) clonotype7 9 0% TRA:CAGAANAGGTSYGKLTF (SEQ ID NO: 3563);TRB:CASSQAQGANYGYTF (SEQ ID NO: 3564) clonotype9 7 0% TRA:CAEIPTFSGGYNKLIF (SEQ ID NO: 3565);TRB:CASSLAGQETQYF (SEQ ID NO: 3566) clonotype8 7 0% TRA:CLRGGSTLGRLYF (SEQ ID NO: 3567);TRB:CASSLYPTGGSGMDEQYF (SEQ ID NO: 3568) clonotype10 6 0% TRA:CAVRDGNTGGFKTIF (SEQ ID NO: 3569);TRB:CASSELKTGGAFF (SEQ ID NO: 3570)

Synthesis and cloning of GATA3 specific TCR DNA

Clonotype 1 TCR alpha and beta sequences are codon-optimized according to human codon frequency for maximum expression in human cell line and PBMC (Table 32). The TCR gene-encoded lentiviral plasmid ( FIG. 40 ) is assessed by DNA sequencing and restriction endonuclease digestion. The DNA sequence data of the final GATA3 neoORF specific TCR encoded plasmid is 100% identical to the TCR alpha and beta codon optimized sequence (bold in FIG. 41 ). After digestion with restriction endonuclease AflII, two DNA disks are observed; one disk between 6000 bp and 5000 bp, and another disc between 4000 bp. and 3000 bp These discs correlate with the expected size of 5590 bp. and 3424 bp, respectively ( FIG. 42 ).

Table 33 below shows GATA3 specific TCR alpha and beta DNA sequences and codon optimized sequences.

Clonotype 1 TCR alpha Clonotype 1 TCR alpha codon-optimized ATGGCTTTTTGGCTGAGAAGGCTGGGTCTACATTTCAGGCCACATTTGGGGAGACGAATGGAGTCATTCCTGGGAGGTGTTTTGCTGATTTTGTGGCTTCAAGTGGACTGGGTGAAGAGCCAAAAGATAGAACAGAATTCCGAGGCCCTGAACATTCAGGAGGGTAAAACGGCCACCCTGACCTGCAACTATACAAACTATTCTCCAGCATACTTACAGTGGTACCGACAAGATCCAGGAAGAGGCCCTG TTTTCTTGCTACTCATACGTGAAAATGAGAAAGAAAAAAGGAAAGAAAGACTGAAGGTCACCTTTGATACCACCCTTAAACAGAGTTTGTTTCATATCACAGCCTCCCAGCCTGCAGACTCAGCTACCTACCTCTGTGCTCTAGACATTTATGGGAACAACAGACTCGCTTTTGGGAAGGGGAACCAAGTGGTGGTCATACCA (SEQ ID NO: 3571) ATGGCCTTCTGGCTGAGGAGACTGGGTTTACACTTCAGACCCCATTTAGGCAGAAGAATGGAGAGCTTTTTAGGCGGCGTGCTGCTGATTTTATGGCTGCAAGTTGACTGGGTGAAGAGCCAGAAGATCGAGCAGAACAGCGAGGCTTTAAACATTCAAGAAGGCAAGACAGCCACTTTAACTTGTAACTATACCAACTACTCCCCCGCTTATTTACAGTGGTACAGACAAGATCCCGGCAGAGGCCCCG TGTTTTTTACTGCTGATTCGTGAGAACGAGAAGGAAGAGGAAGGAGAGACTGAAGGTGACCTTCGACACCACTTTAAAGCAGTCTTTATTCCACATCACCGCCAGCCAGCCCGCTGATAGCGCCACCTATTTATGCGCTTTAGACATCTACGGCAACAATCGTCTGGCCTTCGGCAAGGGCAACCAAGTTGTGGTGATCCCC (SEQ ID NO: 3573) Clonotype 1 TCR beta Clonotype 1 TCR beta codon-optimized ATGGGAATCAGGCTCCTCTGTCGTGTGGCCTTTTGTTTCCTGGCTGTAGGCCTCGTAGATGTGAAAGTAACCCAGAGCTCGAGATATCTAGTCAAAAGGACGGGAGAGAAAGTTTTTCTGGAATGTGTCCAGGATATGGACCATGAAAATATGTTCTGGTATCGACAAGACCCAGGTCTGGGGCTACGGCTGATCTATTTCTCATATGATGTTAAAATGAAAGAAAAGGAGATATCCTGAGGGGTA CAGTGTCTCTAGAGAGAAGAAGGAGCGCTTCTCCCTGATTCTGGAGTCCGCCAGCACCAACCAGACATCTATGTACCTCTGTGCCAGCAGTTTAGATTTTGTGCTAGCGGGGTCCTACTCCTACAATGAGCAGTTCTTCGGGCCAGGGACACGGCTCACCGTGCTAG (SEQ ID NO: 3572) ATGGGCATTCGTCTGCTGTGTCGTGTGGCCTTCTGCTTTTTAGCCGTGGGTTTAGTGGACGTGAAGGTGACCCAGTCCTCTCGTTATTTAGTGAAGAGGACCGGCGAGAAGGTGTTTTTAGAATGCGTGCAAGATATGGACCACGAGAACATGTTCTGGTACAGACAAGATCCCGGACTGGGTTTAAGGCTGATCTACTTCAGCTACGACGTGAAGATGAAGGAGAAGGGCGACATCCCCGA GGGCTACTCCGTGTCTCGTGAGAAGAAGGAGAGGTTCTCTTTAATTTTAGAGTCCGCCAGCACCAACCAGACCAGCATGTATTTATGCGCCAGCTCTTTAGACTTTGTGCTGGCCGGCAGCTACAGCTACAACGAGCAGTTCTTCGGCCCCGGCACCAGACTGACCGTGCTG (SEQ ID NO: 3574)

Expression of GATA3 specific TCR

For Jurkat cells expressing the GATA3 specific TCR, the lentiviral system is used after transfecting a colony of HEK 293T cells with the GATA3 specific TCR construct and the lentivirus is transduced into Jurkat cells. Transduced and pyromycin-selected Jurkat cells were stained with GATA3 multimer-PE and GATA3 multimer-BV650 and compared with non-transduced Jurkat cells to verify expression of the GATA3 specific TCR. 73.1% of cells were positive for both GATA3 multimer-PE and GATA3 multimer-BV650, indicating expression of the GATA3 neoORF specific TCR ( FIG. 43 )

Peptide titration test

To verify that the recombinant TCR is functional, peptide concentrations ranging from 20 μM to 0.2 pM are tested with GATA3-specific TCR-transduced Jurkat cells. IL-2 secretion levels from Jurkat cells showed a non-linear correlation with GATA3 peptide concentration with an observed _EC50 of 37.85 nM ( FIG. 44 ).

Analysis of IL-2 release for GATA3 specific TCR transduced Jurkat

To verify endogenous antigen recognition with GATA3 mutation using GATA3 mutation-specific Jurkat TCRs, HEK 293T cells with the transduced mutation are used as target cells and cocultured with GATA3 TCR transduced Jurkat cells. IL-2 levels were higher in the GATA3 mutation peptide-loaded group of HEK 293T cells (circles) compared to the irrelevant peptide-loaded group (triangles) in FIG. 45 . IL-2 levels were also higher in the group of target cells transduced with the GATA3 mutation (squares) compared to the group of target cells transduced with an irrelevant gene (inverted triangles) in FIG. 45 .

In this study, TCRs were cloned from CD8+ T cells specific for the GATA3 neoantigen presented on HLA-A02:01. TCR avidity is determined to be less than 40 nM by peptide titration (EC50), and the TCR is able to recognize a cell line expressing the GATA3 neoORF. These data support the generation of CD8+ T cells that have efficient TCRs that can recognize cells with the GATA3 neoORF mutation.

Examples 27 - Example 41 described below refer to mutant BTK and mutant EGFR peptides

Example 27 Intracellular Cytokine Staining Assay

Induction of BTK neoantigen-specific CD4+ and CD8+ T cell responses and tetramer staining assays were performed as described in Example 1 and Example 2 . Induction of EGFR neoantigen-specific CD4+ and CD8+ T cell responses and tetramer staining assays were performed as described in Example 1 and Example 2. In the absence of established tetramer staining to identify antigen-specific T cell populations, antigen specificity can be assessed using a score cytokine production using established flow cytometry assays. Briefly, T cells are stimulated with a peptide of interest and compared to a control. Following stimulation, cytokine production by CD4+ T cells (eg, IFNγ and TNFα) is assessed by intracellular staining. These cytokines, especially IFNγ, can be used to identify stimulated cells. FACS analysis was performed for antigen-specific induction of IFNγ and TNFα levels of CD4+ cells from a healthy donor stimulated with APCs loaded with or without mutant BTK. FACS analysis is performed for antigen-specific induction of IFNγ and TNFα levels of CD4+ cells from a healthy donor stimulated with APCs loaded with or without mutant EGFR peptide.

Example 28 - ELISPOT Analysis

Peptide-specific T cells were functionally enumerated using the ELISPOT assay (BD Biosciences), which measures IFNγ release from T cells on a single-cell basis. Target cells (T2 or HLA-A0201 transfected with C1R) are activated with 10 μM peptide for 1 hour at 37°C and washed three times. 1x10 ⁵ peptide-activated targets are co-stimulated in wells of an ELISPOT plate with different concentrations of T cells (5x10 ² -2x10 ³ ) taken from the immunogenic culture. Plates were processed according to the manufacturer's protocol and analyzed on an ELISPOT reader (Cellular Technology Ltd.) using the supplied software. Spots corresponding to the number of IFNγ-producing T cells are described as the absolute number of spots per number of T cells plated. T cells expanded on modified peptides are tested not only for their ability to recognize targets activated by the modified peptide, but also for their ability to recognize targets activated by the original peptide. Determine IFNγ levels in mock-transduced or transduced samples with a lentiviral expression vector encoding a mutant BTK peptide or a mutant EGFR peptide.

Example 29 – CD107 Staining Assay

CD107a and b are expressed on the cell surface of CD8 ⁺ T cells after activation by a recognized peptide. Protease-containing T cell vacuoles have a fatty bilayer that contains lysosomal-associated membrane glycoproteins (“LAMPs”), which include the molecules CD107a and b. When cytotoxic T cells are activated through the T cell receptor, the membranes of these protease-containing vacuoles are mobilized and fuse with the T cell plasma membrane. The granular contents are released and this leads to the death of the target cell. Upon fusion of the granule membrane with the plasma membrane, C107a and b are exposed on the cell surface and therefore become markers of degranulation. Since degranulation by CD107a and b staining has been described on a single-cell basis, the assay is used for functional enumeration of peptide-specific T cells. To perform the assay, the peptide is added to HLA-A02:01-transfected C1R cells to a final concentration of 20 μM, the cells are incubated for 1 hour at 37°C and washed three times. 1x10 ⁵ C1R peptide activated cells are aliquoted into tubes and CD107a and b specific antibodies are added to the final concentration suggested by the manufacturer (Becton Dickinson). Antibodies are added before the addition of T cells to “catch” CD107 molecules as they temporarily appear on the surface during the assay. 1x10 ⁵ T cells from the immunogenic culture are then added and the samples are incubated for 4 hours at 37°C. T cells are then stained for additional cell surface molecules such as CD8, and data are acquired on a FACS Calibur instrument (Becton Dickinson). Data were analyzed using the supplied Cellquest program and results are shown as the proportion of CD8 ⁺ /CD107a and b ⁺ cells.

Example 30 - Cytotoxicity Assays

Cytotoxic activity is measured using Method 1 or Method 2. Method 1 includes a chromium release assay. T2 target cells are labeled with Na ⁵¹ Cr for 1 hour at 37°C and washed, 5x10 ³ T2 target cells are then added to varying numbers of T cells from the immunogenic culture. Chromium release was measured from the supernatant collected after 4 hours of incubation at 37°C. The proportion of specific lysis is calculated as:

Equation 10. Experimental release - spontaneous release/Total release - spontaneous release x 100.

In method 2, cytotoxic activity is measured by detecting cleaved caspase 3 in target cells by flow cytometry. Target cancer cells are engineered to express the mutant peptide along with the appropriate MHC-I allele. Mock-transduced target cells (i.e., not expressing the mutant peptide) are used as a negative control. Cells are labeled with CFSE to separate them from stimulated PBMCs used as effector cells. Targets and effector cells are cocultured for 6 hours and then harvested. Intracellular staining is performed to detect the cleaved form of caspase 3 in CFSE-positive target cancer cells. The proportion of specific lysis is calculated as:

Equation 11. Experimental caspase 3 cleavage/spontaneous caspase 3 cleavage (measured in the absence of mutant peptide expression) x 100.

Method 2 of the cytotoxicity assay is presented in the Materials and Methods section of Example 25 of this specification.

Example 31 - Enhanced CD8 ⁺ T Cell Responses in Vivo with Longmer and Shortmer Sequential Application

Vaccination with longmer peptides can induce both CD4 ⁺ and CD8 ⁺ T cell responses, depending on the processing and presentation of the peptides. Vaccination with minimal short-term epitopes focuses on generating CD8 ⁺ T cell responses but does not require peptide processing prior to antigen presentation. As such, any cell can easily present an epitope, not just professional antigen-presenting cells (APCs). This can lead to tolerance of T cells that contact healthy cells presenting antigens as part of peripheral tolerance. To circumvent this, prime immunization with longmer allows priming of CD8 ⁺ T cells to only APCs that can process and present peptides. Subsequent immunizations enhance initial CD8 ⁺ T cell responses.

In vivo immunogenicity assays

Nineteen 8- to 12-week-old female C57BL/6 mice (Taconic Biosciences) were randomly assigned to treatment groups upon admission. Animals are acclimatized for three (3) days before the start of the study. Animals are fed sterile LabDiet™ 5053 rodent food and sterile water is provided ad libitum . Animals in Group 1 serve as an adjuvant-only control and are administered polyinosinic:polycytidylic acid (polyI:C) alone at a dose of 100 μg in a 0.1 ml volume by subcutaneous injection (SC) on days 0, 7, and 14 Animals in group 2 were administered 50 μg of each of the six long-mer peptides (described below) along with polyI:C at a dose of 100 μg s.c. in a volume of 0.1 ml on days 0, 7 and 14. Animals in group 3 were administered 50 μg of each of the six long-term peptides (described below) together with polyI:C at a dose of 100 μg s.c. in a volume of 0.1 ml on day 0 and molar equivalents of the corresponding shortmer peptides (described below) together with polyI:C at a dose of 100 μg s.c. in a volume of 0.1 ml on days 7 and 14. Animals are weighed and general health is monitored daily. Animals are sacrificed with a CO2 overdose on day 21 of study completion if the animal loses >30% of its body weight compared to day 0; or if the animal is found in agony. At sacrifice, spleens are collected and processed into single-cell suspensions using standard protocols. Briefly, spleens were mechanically disrupted through a 70 μM filter, pelleted, and lysed with ACK lysis buffer (Sigma) before resuspension in cell culture medium.

Peptides

Six previously identified mouse neoantigens are used based on their demonstrated ability to induce CD8 ⁺ T cell responses. For each neoantigen, a shortmer (8-11 amino acids) corresponding to the minimal epitope was determined. A longmer corresponding to 20-27 amino acids surrounding the mutation is used.

ELISPOT

The ELISPOT assay (Mouse IFNγ ELISPOT Reasy-SET-Go; EBioscience) was performed according to the kit protocol. Briefly, the day before analysis, 96-well filter plates (0.45 μM hydrophobic PVDF membrane; EMD Millipore) are activated (35% EtOH), washed (BFBS), and coated with immobilized antibody (1:250; 4°CO /N). On the day of analysis, wells are washed and blocked (medium; 2 hours at 37°C). Approximately 2x10 ⁵ cells per 100 μl are added to the wells along with 100 μl of 10 mM test peptide pool (shortmer) or PMA/ionomycin positive control antigen or vehicle. Cells are incubated with antigen overnight (16-18 hours) at 37°C. The next day, the cell suspension is removed and the wells are washed once with PBS and twice with deionized water. For all wash steps in the remainder of the assay, wells are soaked for 3 minutes at each wash step. The wells are then washed three times with wash buffer (BFBS+0.05% Tween-20) and identifying antibody (1:250) is added to all wells. The plates are incubated for two hours at room temperature. The identifying antibody solution is removed and the wells are washed three times with buffer. Avidin-HRP (1:250) was added to all wells and the plates were incubated for one hour at room temperature. The conjugate solution is removed and the wells are washed three times with wash buffer, then once with PBS. Substrate (3-amino-9-ethylcarbazole, 0.1 M in acetate buffer, H ₂ O ₂ ) is added to all wells and spot development is monitored (approximately 10 minutes). The substrate reaction is stopped by washing the wells with water and the plates are air dried overnight. The plates were analyzed on an ELISPOT reader (Cellular Technology Ltd.) using the supplied software. Spots corresponding to the number of IFNγ-producing T cells are shown as the absolute number of spots per number of T cells seeded.

Example 32 – Determination of Mutant BTK Peptides by Mass Spectrometry

293T cells are transduced with a lentiviral vector encoding different regions of the mutant BTK peptide. 50-100 million transduced cells expressing peptides encoded by the mutant BTK peptide are cultured and the peptides are eluted from the HLA-peptide complexes using an acid wash. The eluted peptides are then analyzed by MS/MS.

Example 33 Mutant BTK peptides produce strong epitopes on multiple alleles.

Multiple peptides containing neoepitopes are expressed or loaded into antigen presenting cells (APCs). Then mass spectrometry is carried out, and the affinity of neoepitopes for the indicated HLA alleles and the stability of neoepitopes with HLA alleles are determined.

Example 34 Multiple BTK Neoepitopes Induce CD8+ T Cell Responses

PBMC samples from a human donor can be used to perform antigen-specific T cell induction. CD8 ⁺ T cell induction was analyzed after T cell production. Cell samples can be taken at different time points for analysis. pMHC multimer is used to monitor the proportion of antigen-specific CD8 ⁺ T cells in induction cultures.

Example 35 Predicted HLA Specificity of Mutant BTK Neopeptides

BTK specific neopeptides are run through the proprietary RECON algorithm to predict HLA specificity. Neopeptides are ranked based on predicted binding affinity. Table 38 shows the specificity for alleles, which are further ranked by affinity from high to low. A lower ranking value indicates stronger affinity. Table 38 also shows that the mutant BTK neopeptides identified and characterized in the present invention have strong epitopes with multiple alleles.

Table 38 depicts allelic specificity, which is further ranked by affinity from high to low

BTK, C481S IFIITEYMANGSLLNYLREMRHR (SEQ ID NO: 3575) PEPTIDE ALLELE RANK ANGSLLNY (SEQ ID NO: 3576) HLA-A36:01 24 ANGSLLNYL (SEQ ID NO: 3577) HLA-C15:02 14 ANGSLLNYL (SEQ ID NO: 3578) HLA-C08:01 19 ANGSLLNYL (SEQ ID NO: 3579) HLA-C06:02 19 ANGSLLNYL (SEQ ID NO: 3580) HLA-A02:04 21 ANGSLLNYL (SEQ ID NO: 3581) HLA-C12:02 25 ANGSLLNYL (SEQ ID NO: 3582) HLA-B44:02 26 ANGSLLNYL (SEQ ID NO: 3583) HLA-C17:01 27 ANGSLLNYL (SEQ ID NO: 3584) HLA-B38:01 27 ANGSLLNYLR (SEQ ID NO: 3585) HLA-A74:01 19 ANGSLLNYLR (SEQ ID NO: 3586) HLA-A31:01 26 EYMANGSL (SEQ ID NO: 3587) HLA-C14:02 13 EYMANGSL (SEQ ID NO: 3588) HLA-C14:03 13 EYMANGSL (SEQ ID NO: 3589) HLA-A24:02 25 EYMANGSLL (SEQ ID NO: 3590) HLA-A24:02 3 EYMANGSLL (SEQ ID NO: 3591) HLA-A23:01 9 EYMANGSLL (SEQ ID NO: 3592) HLA-C14:02 eleven EYMANGSLL (SEQ ID NO: 3593) HLA-C14:03 12 EYMANGSLL (SEQ ID NO: 3594) HLA-A33:03 19 EYMANGSLL (SEQ ID NO: 3595) HLA-C04:01 20 EYMANGSLL (SEQ ID NO: 3596) HLA-B15:09 22 EYMANGSLL (SEQ ID NO: 3597) HLA-B38:01 23 EYMANGSLLN (SEQ ID NO: 3598) HLA-A24:02 24 EYMANGSLLN (SEQ ID NO: 3599) HLA-A23:01 27 EYMANGSLLNY (SEQ ID NO: 3600) HLA-A29:02 27 GSLLNYLR (SEQ ID NO: 3601) HLA-A31:01 16 GSLLNYLR (SEQ ID NO: 3602) HLA-A74:01 23 GSLLNYLREM (SEQ ID NO: 3603) HLA-B58:02 15 GSLLNYLREM (SEQ ID NO: 3604) HLA-B57:01 27 ITEYMANGS (SEQ ID NO: 3605) HLA-A01:01 23 ITEYMANGSL (SEQ ID NO: 3606) HLA-A01:01 20 ITEYMANGSLL (SEQ ID NO: 3607) HLA-A01:01 21 MANGSLLNY (SEQ ID NO: 3608) HLA-C02:02 1 MANGSLLNY (SEQ ID NO: 3609) HLA-C03:02 2 MANGSLLNY (SEQ ID NO: 3610) HLA-B53:01 2 MANGSLLNY (SEQ ID NO: 3611) HLA-B35:01 4 MANGSLLNY (SEQ ID NO: 3612) HLA-A29:02 eleven MANGSLLNY (SEQ ID NO: 3613) HLA-C12:02 eleven MANGSLLNY (SEQ ID NO: 3614) HLA-C12:03 eleven MANGSLLNY (SEQ ID NO: 3615) HLA-A30:02 12 MANGSLLNY (SEQ ID NO: 3616) HLA-A36:01 12 MANGSLLNY (SEQ ID NO: 3617) HLA-A26:01 16 MANGSLLNY (SEQ ID NO: 3618) HLA-A01:01 17 MANGSLLNY (SEQ ID NO: 3619) HLA-B15:01 17 MANGSLLNY (SEQ ID NO: 3620) HLA-A25:01 18 MANGSLLNY (SEQ ID NO: 3621) HLA-B57:01 19 MANGSLLNY (SEQ ID NO: 3622) HLA-B58:01 22 MANGSLLNY (SEQ ID NO: 3623) HLA-A03:01 23 MANGSLLNY (SEQ ID NO: 3624) HLA-B46:01 23 MANGSLLNY (SEQ ID NO: 3625) HLA-B15:03 24 MANGSLLNY (SEQ ID NO: 3626) HLA-A33:03 25 MANGSLLNY (SEQ ID NO: 3627) HLA-B35:03 28 MANGSLLNY (SEQ ID NO: 3628) HLA-A11:01 28 MANGSLLNYL (SEQ ID NO: 3629) HLA-C17:01 17 MANGSLLNYL (SEQ ID NO: 3630) HLA-C02:02 18 MANGSLLNYL (SEQ ID NO: 3631) HLA-B35:01 18 MANGSLLNYL (SEQ ID NO: 3632) HLA-C03:03 21 MANGSLLNYL (SEQ ID NO: 3633) HLA-C08:01 24 MANGSLLNYL (SEQ ID NO: 3634) HLA-B35:03 24 MANGSLLNYL (SEQ ID NO: 3635) HLA-C12:02 25 MANGSLLNYL (SEQ ID NO: 3636) HLA-C01:02 26 MANGSLLNYL (SEQ ID NO: 3637) HLA-C03:04 28 MANGSLLNYL (SEQ ID NO: 3638) HLA-C08:02 28 MANGSLLNYLR (SEQ ID NO: 3639) HLA-A33:03 24 MANGSLLNYLR (SEQ ID NO: 3640) HLA-A74:01 28 NGSLLNYL (SEQ ID NO: 3641) HLA-B14:02 19 NGSLLNYLR (SEQ ID NO: 3642) HLA-A68:01 14 NGSLLNYLR (SEQ ID NO: 3643) HLA-A33:03 16 NGSLLNYLR (SEQ ID NO: 3644) HLA-A31:01 25 NGSLLNYLR (SEQ ID NO: 3645) HLA-A74:01 26 SLLNYLREM (SEQ ID NO: 3646) HLA-A02:04 5 SLLNYLREM (SEQ ID NO: 3647) HLA-A02:01 13 SLLNYLREM (SEQ ID NO: 3648) HLA-A02:03 16 SLLNYLREM (SEQ ID NO: 3649) HLA-C03:02 16 SLLNYLREM (SEQ ID NO: 3650) HLA-A03:01 19 SLLNYLREM (SEQ ID NO: 3651) HLA-A32:01 20 SLLNYLREM (SEQ ID NO: 3652) HLA-A02:07 20 SLLNYLREM (SEQ ID NO: 3653) HLA-C14:03 20 SLLNYLREM (SEQ ID NO: 3654) HLA-C14:02 20 SLLNYLREM (SEQ ID NO: 3655) HLA-A31:01 21 SLLNYLREM (SEQ ID NO: 3656) HLA-A30:02 22 SLLNYLREM (SEQ ID NO: 3657) HLA-A74:01 22 SLLNYLREM (SEQ ID NO: 3658) HLA-C06:02 24 SLLNYLREM (SEQ ID NO: 3659) HLA-B15:03 25 SLLNYLREM (SEQ ID NO: 3660) HLA-B46:01 25 SLLNYLREM (SEQ ID NO: 3661) HLA-B13:02 25 SLLNYLREM (SEQ ID NO: 3662) HLA-A25:01 26 SLLNYLREM (SEQ ID NO: 3663) HLA-A29:02 28 SLLNYLREM (SEQ ID NO: 3664) HLA-C01:02 28 SLLNYLREMR (SEQ ID NO: 3665) HLA-A74:01 14 SLLNYLREMR (SEQ ID NO: 3666) HLA-A31:01 20 TEYMANGSL (SEQ ID NO: 3667) HLA-B40:01 8 TEYMANGSL (SEQ ID NO: 3668) HLA-B40:02 8 TEYMANGSL (SEQ ID NO: 3669) HLA-B14:02 eleven TEYMANGSL (SEQ ID NO: 3670) HLA-B49:01 14 TEYMANGSL (SEQ ID NO: 3671) HLA-B44:03 16 TEYMANGSL (SEQ ID NO: 3672) HLA-B44:02 17 TEYMANGSL (SEQ ID NO: 3673) HLA-B37:01 19 TEYMANGSL (SEQ ID NO: 3674) HLA-B18:01 20 TEYMANGSL (SEQ ID NO: 3675) HLA-B15:09 23 TEYMANGSL (SEQ ID NO: 3676) HLA-B41:01 25 TEYMANGSL (SEQ ID NO: 3677) HLA-B50:01 25 TEYMANGSLL (SEQ ID NO: 3678) HLA-B40:01 7 TEYMANGSLL (SEQ ID NO: 3679) HLA-B44:03 15 TEYMANGSLL (SEQ ID NO: 3680) HLA-B49:01 17 TEYMANGSLL (SEQ ID NO: 3681) HLA-B44:02 21 TEYMANGSLL (SEQ ID NO: 3682) HLA-B40:02 24 TEYMANGSLLNY (SEQ ID NO: 3683) HLA-B44:03 21 YMANGSLL (SEQ ID NO: 3684) HLA-B15:09 14 YMANGSLL (SEQ ID NO: 3685) HLA-C03:04 15 YMANGSLL (SEQ ID NO: 3686) HLA-C03:03 16 YMANGSLL (SEQ ID NO: 3687) HLA-C17:01 16 YMANGSLL (SEQ ID NO: 3688) HLA-C03:02 21 YMANGSLL (SEQ ID NO: 3689) HLA-C14:03 22 YMANGSLL (SEQ ID NO: 3690) HLA-C14:02 23 YMANGSLL (SEQ ID NO: 3691) HLA-C04:01 24 YMANGSLL (SEQ ID NO: 3692) HLA-C02:02 26 YMANGSLL (SEQ ID NO: 3693) HLA-A01:01 26 YMANGSLLN (SEQ ID NO: 3694) HLA-A29:02 25 YMANGSLLN (SEQ ID NO: 3695) HLA-A01:01 25 YMANGSLLNY (SEQ ID NO: 3696) HLA-A01:01 6 YMANGSLLNY (SEQ ID NO: 3697) HLA-A29:02 10 YMANGSLLNY (SEQ ID NO: 3698) HLA-A36:01 16 YMANGSLLNY (SEQ ID NO: 3699) HLA-A03:01 16 YMANGSLLNY (SEQ ID NO: 3700) HLA-B46:01 18 YMANGSLLNY (SEQ ID NO: 3701) HLA-A25:01 19 YMANGSLLNY (SEQ ID NO: 3702) HLA-B15:01 20 YMANGSLLNY (SEQ ID NO: 3703) HLA-A26:01 20 YMANGSLLNY (SEQ ID NO: 3704) HLA-A30:02 21 YMANGSLLNY (SEQ ID NO: 3705) HLA-A32:01 24

Example 36: Affinity and Stability of Mutant BTK Neopeptides

A variety of neoepitope-containing peptides in the table below are either expressed or loaded into antigen-presenting cells. Then mass spectrometry is carried out and the affinity of neoepitopes for the indicated HLA alleles is determined, and the stability of neoepitopes with HLA alleles is determined.

Table 39 shows the corresponding affinity and stability of the mutant BTK peptides.

Gene HLA allele Peptide sequence Affinity (nM) Stability (1/2 h) BTK, C481S A01.01 YMANGSLLNY (SEQ ID NO: 3706) 13.24495 0.866167 BTK, C481S A01.01 MANGSLLNY (SEQ ID NO: 3707) 439,029 0.216408 BTK, C481S A03.01 MANGSLLNY (SEQ ID NO: 3708) 35.62463 0.237963 BTK, C481S A03.01 YMANGSLLNY (SEQ ID NO: 3709) 95.93212 0.279088 BTK, C481S A11.01 MANGSLLNY (SEQ ID NO: 3710) 535.6333 N.B. BTK, C481S A11.01 YMANGSLLNY (SEQ ID NO: 3711) 974.2881 N.B. BTK, C481S A24.02 EYMANGSLL (SEQ ID NO: 3712) 4.961145 5.716141 BTK_C481S A02.01 SLLNYLREM (SEQ ID NO: 3713) 67.69132 3.043604 BTK_C481S A02.01 MANGSLLNYL (SEQ ID NO: 3714) 1006.566 0 BTK_C481S A02.01 YMANGSLLN (SEQ ID NO: 3715) 3999.442 0 BTK_C481S B07.02 SLLNYLREM (SEQ ID NO: 3716) 865.8805 0 BTK_C481S B07.02 MANGSLLNYL (SEQ ID NO: 3717) 16474.59 0 BTK_C481S B08.01 SLLNYLREM (SEQ ID NO: 3718) 959.6542 0 BTK_C481S B08.01 MANGSLLNYL (SEQ ID NO: 3719) 18463.09 0

Example 37 – Determination of mutant EGFR peptides by mass spectrometry

293T cells are transduced with a lentiviral vector encoding different regions of the mutant EGFR peptide. 50-100 million transduced cells expressing peptides encoded by the mutant EGFR peptide are cultured and the peptides are eluted from the HLA-peptide complexes using an acid wash. The eluted peptides are then analyzed by MS/MS.

Example 38 - Mutant EGFR peptides produce strong epitopes on multiple alleles.

Multiple peptides containing neoepitopes are expressed or loaded into antigen presenting cells (APCs). Then mass spectrometry is carried out, and the affinity of neoepitopes for the indicated HLA alleles and the stability of neoepitopes with HLA alleles are determined.

Example 39 - Multiple EGFR Neoepitopes Induce CD8+ T Cell Responses

PBMC samples from a human donor can be used to perform antigen-specific T cell induction. CD8 ⁺ T cell induction was analyzed after T cell production. Cell samples can be taken at different time points for analysis. pMHC multimer is used to monitor the proportion of antigen-specific CD8 ⁺ T cells in induction cultures.

Example 40 – HLA Predicted Specificity of Mutant EGFR Neopeptides

Specific neopeptides are run through the proprietary RECON algorithm to predict HLA specificity. Neopeptides are ranked based on predicted binding affinity. Table 43 shows the specificity for alleles, which are further ranked by affinity from high to low. A lower ranking value indicates stronger affinity. Table 43 also shows that the mutant EGFR neopeptides identified and characterized in the present invention have strong epitopes with multiple alleles.

Table 43

PEPTIDE ALLELE RANK LIMQLMPF (SEQ ID NO: 3720) HLA-C03:02 5 LTSTVQLIM (SEQ ID NO: 3721) HLA-C12:03 10 HLA-A01:01 13 HLA-C15:02 13 HLA-B57:01 14 HLA-B57:03 15 HLA-A36:01 16 HLA-C12:02 18 HLA-C03:03 19 HLA-B58:02 21 QLIMQLMPF (SEQ ID NO: 3722) HLA-B15:01 15 HLA-A26:01 21 STVQLIMQL (SEQ ID NO: 3723) HLA-A68:02 1 HLA-C15:02 2 HLA-A25:01 3 HLA-B57:03 4 HLA-C12:02 4 HLA-A26:01 5 HLA-C12:03 6 HLA-C06:02 7 HLA-C03:03 8 HLA-A30:01 9 HLA-C02:02 9 HLA-A11:01 10 HLA-A32:01 10 HLA-A02:04 10 HLA-A68:01 eleven HLA-B15:09 eleven HLA-C03:04 12 HLA-B38:01 18 HLA-B57:01 19 HLA-A02:03 20 HLA-C08:01 21 HLA-B35:01 21 HLA-B40:01 21 STVQLIMQLM (SEQ ID NO: 3724) HLA-A26:01 15 HLA-B57:01 17 TSTVQLIMQL (SEQ ID NO: 3725) HLA-C15:02 17 TVQLIMQL (SEQ ID NO: 3726) HLA-C17:01 eleven HLA-B08:01 12 HLA-B42:01 13 HLA-B14:02 15 HLA-B37:01 15 HLA-B15:09 17 TVQLIMQLM (SEQ ID NO: 3727) HLA-B35:03 21 VQLIMQLM (SEQ ID NO: 3728) HLA-B52:01 8 HLA-B14:02 19 HLA-B37:01 19

Example 41 Affinity and Stability of Mutant EGFR Neopeptides

A variety of neoepitope-containing peptides in the table below are either expressed or loaded into antigen-presenting cells. Then mass spectrometry is carried out and the affinity of neoepitopes for the indicated HLA alleles is determined, and the stability of neoepitopes with HLA alleles is determined. Table 44 shows the corresponding affinity and stability of the mutant EGFR peptides.

Table 44

Gene HLA Allele Peptide sequence Affinity (nM) Stability (1/2 h) EGFR, T790M A01.01 LTSTVQLIM (SEQ ID NO: 3729) 2891.111 0.103721 EGFR_T790M A01.01 CLTSTVQLIM (SEQ ID NO: 3730) 8276.876 0 EGFR_T790M A02.01 MQLMPFGCLL (SEQ ID NO: 3731) 16.26147 0.381118 EGFR_T790M A02.01 MQLMPFGCL (SEQ ID NO: 3732) 116.3352 0.368273 EGFR_T790M A02.01 LIMQLMPFGC (SEQ ID NO: 3733) 132.4766 0.381284 EGFR_T790M A02.01 QLIMQLMPF (SEQ ID NO: 3734) 192.8406 0.34067 EGFR_T790M A02.01 CLTSTVQLIM (SEQ ID NO: 3735) 537.1391 0 EGFR_T790M A02.01 IMQLMPFGCL (SEQ ID NO: 3736) 653.1065 0.515559 EGFR_T790M A02.01 IMQLMPFGC (SEQ ID NO: 3737) 1205.368 0.370112 EGFR_T790M A02.01 LIMQLMPFG (SEQ ID NO: 3738) 3337.708 0 EGFR_T790M A02.01 VQLIMQLMPF (SEQ ID NO: 3739) 4942.892 0 EGFR_T790M A02.01 QLIMQLMPFG (SEQ ID NO: 3740) 5214.668 0 EGFR_T790M A02.01 STVQLIMQL (SEQ ID NO: 3741) 7256.773 0 EGFR_T790M A24.02 QLIMQLMPF (SEQ ID NO: 3742) 2030.807 0.368673 EGFR_T790M A24.02 VQLIMQLMPF (SEQ ID NO: 3743) 4103.131 0 EGFR_T790M A24.02 IMQLMPFGCL (SEQ ID NO: 3744) 14119.38 0 EGFR_T790M A24.02 MQLMPFGCLL (SEQ ID NO: 3745) 18857.47 0 EGFR_T790M B07.02 MQLMPFGCL (SEQ ID NO: 3746) 1589.188 0 EGFR_T790M B08.01 QLIMQLMPF (SEQ ID NO: 3747) 330.1933 0 EGFR_T790M B08.01 IMQLMPFGCL (SEQ ID NO: 3748) 427.3913 0 EGFR_T790M B08.01 MQLMPFGCL (SEQ ID NO: 3749) 4931.727 0 EGFR_T790M B08.01 MQLMPFGCLL (SEQ ID NO: 3750) 11244.9 0 EGFR_T790M B08.01 VQLIMQLMPF (SEQ ID NO: 3751) 16108.18 0 EGFR_T790M B08.02 QLIMQLMPF (SEQ ID NO: 3752) 5590.3 ND

--->

LIST OF SEQUENCES

<110> NEON THERAPEUTICS, INC.

<120> NEOANTIGENS AND THEIR APPLICATION

<130> 50401-731.601

<140>PCT/US2019/038061

<141>2019-06-19

<150> 62/801,981

<151> 2019-02-06

<150> 62/800,700

<151> 2019-02-04

<150> 62/800,792

<151> 2019-02-04

<150> 62/789,162

<151> 2019-01-07

<150> 62/726,804

<151> 2018-09-04

<150> 62/702,567

<151> 2018-07-24

<150> 62/687,191

<151> 2018-06-19

<160> 3872

<170> Patent In version 3.5

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Cys Gln Thr Thr Thr Thr Thr Leu Trp Arg Arg Asn Ala Asn Gly Asp

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Pro Val Cys Asn Ala Cys Gly Leu Tyr Tyr Lys Leu His Asn Ile Asn

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Arg Pro Leu Thr Met Lys Lys Glu Gly Ile Gln Thr Arg Asn Arg Lys

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Met Ser Ser Lys Ser Lys Lys Cys Lys Lys Val His Asp Ser Leu Glu

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Asp Phe Pro Lys Asn Ser Ser Phe Pro Gly Arg Pro Leu Gln Thr His

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Val Leu Pro Glu Pro His Leu Ala Leu Gln Pro Leu Gln Pro His Ala

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Asp His Ala His Ala Asp Ala Pro Ala Ile Gln Pro Val Leu Trp Thr

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Thr Pro Pro Leu Gln His Gly His Arg His Gly Leu Glu Pro Cys Ser

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Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

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His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

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Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

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Ser Leu Trp Cys Leu Cys Ser Asn His

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Arg His Gly Leu Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg

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1 5 10

<210> 47

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 47

Tyr Met Phe Leu Lys Ala Glu Ser Lys

15

<210> 48

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 48

Lys Ile Met Phe Ala Thr Leu Gln Arg

15

<210> 49

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 49

Phe Ala Thr Leu Gln Arg Ser Ser Leu

15

<210> 50

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 50

Glu Pro His Leu Ala Leu Gln Pro Leu

15

<210> 51

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 51

Gln Pro Val Leu Trp Thr Thr Pro Pro Leu

1 5 10

<210> 52

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 52

Gly Pro Pro Ala Arg Val Pro Ala Val

15

<210> 53

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 53

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 54

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 54

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 55

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 55

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 56

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 56

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10

<210> 57

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 57

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 58

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 58

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10

<210> 59

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 59

Leu His Phe Cys Arg Ser Ser Ile Met

15

<210> 60

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 60

Glu Pro His Leu Ala Leu Gln Pro Leu

15

<210> 61

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 61

Phe Ala Thr Leu Gln Arg Ser Ser Leu

15

<210> 62

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 62

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 63

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 63

Phe Leu Lys Ala Glu Ser Lys Ile Met

15

<210> 64

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 64

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 65

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 65

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 66

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 66

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

<210> 67

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 67

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His

<210> 68

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 68

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His

20

<210> 69

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 69

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala Glu Ser Lys Ile

20 25

<210> 70

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 70

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

20 25

<210> 71

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 71

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

20 25 30

His

<210> 72

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 72

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 73

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 73

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

<210> 74

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 74

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His

<210> 75

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 75

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His

20

<210> 76

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 76

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala Glu Ser Lys Ile

20 25

<210> 77

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 77

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

20 25

<210> 78

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 78

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

20 25 30

His

<210> 79

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 79

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

1 5 10

<210> 80

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 80

Val Leu Pro Glu Pro His Leu Ala Leu

15

<210> 81

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 81

His Val Leu Pro Glu Pro His Leu Ala Leu

1 5 10

<210> 82

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 82

Ala Leu Gln Pro Leu Gln Pro His Ala

15

<210> 83

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 83

Ala Ile Gln Pro Val Leu Trp Thr Thr

15

<210> 84

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 84

Ala Pro Ala Ile Gln Pro Val Leu Trp Thr Thr

1 5 10

<210> 85

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 85

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 86

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 86

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 87

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 87

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 88

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 88

Met Phe Leu Lys Ala Glu Ser Lys Ile

15

<210> 89

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 89

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 90

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 90

Val Leu Trp Thr Thr Pro Pro Leu Gln His

1 5 10

<210> 91

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 91

Tyr Met Phe Leu Lys Ala Glu Ser Lys

15

<210> 92

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 92

Lys Ile Met Phe Ala Thr Leu Gln Arg

15

<210> 93

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 93

Phe Ala Thr Leu Gln Arg Ser Ser Leu

15

<210> 94

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 94

Glu Pro His Leu Ala Leu Gln Pro Leu

15

<210> 95

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 95

Gln Pro Val Leu Trp Thr Thr Pro Pro Leu

1 5 10

<210> 96

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 96

Gly Pro Pro Ala Arg Val Pro Ala Val

15

<210> 97

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 97

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 98

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 98

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 99

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 99

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 100

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 100

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10

<210> 101

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 101

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 102

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 102

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10

<210> 103

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 103

Leu His Phe Cys Arg Ser Ser Ile Met

15

<210> 104

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 104

Glu Pro His Leu Ala Leu Gln Pro Leu

15

<210> 105

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 105

Phe Ala Thr Leu Gln Arg Ser Ser Leu

15

<210> 106

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 106

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 107

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 107

Phe Leu Lys Ala Glu Ser Lys Ile Met

15

<210> 108

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 108

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 109

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 109

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

1 5 10

<210> 110

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 110

Val Leu Pro Glu Pro His Leu Ala Leu

15

<210> 111

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 111

His Val Leu Pro Glu Pro His Leu Ala Leu

1 5 10

<210> 112

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 112

Ala Leu Gln Pro Leu Gln Pro His Ala

15

<210> 113

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 113

Ala Ile Gln Pro Val Leu Trp Thr Thr

15

<210> 114

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 114

Ala Pro Ala Ile Gln Pro Val Leu Trp Thr Thr

1 5 10

<210> 115

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 115

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 116

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 116

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 117

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 117

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 118

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 118

Met Phe Leu Lys Ala Glu Ser Lys Ile

15

<210> 119

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 119

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 120

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 120

Val Leu Trp Thr Thr Pro Pro Leu Gln His

1 5 10

<210> 121

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 121

Tyr Met Phe Leu Lys Ala Glu Ser Lys

15

<210> 122

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 122

Lys Ile Met Phe Ala Thr Leu Gln Arg

15

<210> 123

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 123

Phe Ala Thr Leu Gln Arg Ser Ser Leu

15

<210> 124

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 124

Glu Pro His Leu Ala Leu Gln Pro Leu

15

<210> 125

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 125

Gln Pro Val Leu Trp Thr Thr Pro Pro Leu

1 5 10

<210> 126

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 126

Gly Pro Pro Ala Arg Val Pro Ala Val

15

<210> 127

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 127

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 128

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 128

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 129

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 129

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 130

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 130

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10

<210> 131

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 131

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 132

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 132

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10

<210> 133

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 133

Leu His Phe Cys Arg Ser Ser Ile Met

15

<210> 134

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 134

Glu Pro His Leu Ala Leu Gln Pro Leu

15

<210> 135

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 135

Phe Ala Thr Leu Gln Arg Ser Ser Leu

15

<210> 136

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 136

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 137

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 137

Phe Leu Lys Ala Glu Ser Lys Ile Met

15

<210> 138

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 138

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 139

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 139

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His

20

<210> 140

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 140

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His

<210> 141

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 141

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

20 25

<210> 142

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 142

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

20 25

<210> 143

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 143

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

20 25 30

His

<210> 144

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 144

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

1 5 10 15

<210> 145

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 145

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

<210> 146

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 146

Ile Phe Ile Ile Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10 15

Leu Arg Glu Met Arg His Arg

20

<210> 147

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 147

Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 148

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 148

Ala Asn Gly Ser Leu Leu Asn Tyr Leu

15

<210> 149

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 149

Ala Asn Gly Ser Leu Leu Asn Tyr Leu Arg

1 5 10

<210> 150

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 150

Glu Tyr Met Ala Asn Gly Ser Leu

15

<210> 151

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 151

Glu Tyr Met Ala Asn Gly Ser Leu Leu Asn

1 5 10

<210> 152

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 152

Glu Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 153

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 153

Gly Ser Leu Leu Asn Tyr Leu Arg

15

<210> 154

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 154

Gly Ser Leu Leu Asn Tyr Leu Arg Glu Met

1 5 10

<210> 155

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 155

Ile Thr Glu Tyr Met Ala Asn Gly Ser

15

<210> 156

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 156

Ile Thr Glu Tyr Met Ala Asn Gly Ser Leu

1 5 10

<210> 157

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 157

Ile Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu

1 5 10

<210> 158

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 158

Met Ala Asn Gly Ser Leu Leu Asn Tyr Leu

1 5 10

<210> 159

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 159

Met Ala Asn Gly Ser Leu Leu Asn Tyr Leu Arg

1 5 10

<210> 160

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 160

Asn Gly Ser Leu Leu Asn Tyr Leu

15

<210> 161

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 161

Asn Gly Ser Leu Leu Asn Tyr Leu

15

<210> 162

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 162

Ser Leu Leu Asn Tyr Leu Arg Glu Met Arg

1 5 10

<210> 163

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 163

Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu

1 5 10

<210> 164

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 164

Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 165

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 165

Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 166

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 166

Tyr Met Ala Asn Gly Ser Leu Leu Asn

15

<210> 167

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 167

Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 168

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 168

Ala Asn Gly Ser Leu Leu Asn Tyr Leu

15

<210> 169

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 169

Ala Asn Gly Ser Leu Leu Asn Tyr Leu Arg

1 5 10

<210> 170

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 170

Glu Tyr Met Ala Asn Gly Ser Leu

15

<210> 171

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 171

Glu Tyr Met Ala Asn Gly Ser Leu Leu Asn

1 5 10

<210> 172

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 172

Glu Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 173

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 173

Gly Ser Leu Leu Asn Tyr Leu Arg

15

<210> 174

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 174

Gly Ser Leu Leu Asn Tyr Leu Arg Glu Met

1 5 10

<210> 175

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 175

Ile Thr Glu Tyr Met Ala Asn Gly Ser

15

<210> 176

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 176

Ile Thr Glu Tyr Met Ala Asn Gly Ser Leu

1 5 10

<210> 177

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 177

Ile Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu

1 5 10

<210> 178

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 178

Met Ala Asn Gly Ser Leu Leu Asn Tyr Leu

1 5 10

<210> 179

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 179

Met Ala Asn Gly Ser Leu Leu Asn Tyr Leu Arg

1 5 10

<210> 180

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 180

Asn Gly Ser Leu Leu Asn Tyr Leu

15

<210> 181

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 181

Asn Gly Ser Leu Leu Asn Tyr Leu

15

<210> 182

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 182

Ser Leu Leu Asn Tyr Leu Arg Glu Met Arg

1 5 10

<210> 183

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 183

Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu

1 5 10

<210> 184

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 184

Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 185

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 185

Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 186

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 186

Tyr Met Ala Asn Gly Ser Leu Leu Asn

15

<210> 187

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 187

Ile Phe Ile Ile Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10 15

Leu Arg Glu Met Arg His Arg

20

<210> 188

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 188

Ile Asp Ile Ile Met Lys Ile Arg Asn Ala

1 5 10

<210> 189

<211> 30

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<400> 189

Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe

1 5 10 15

Phe Phe Phe Phe Ile Ile Phe Phe Ile Phe Phe Trp Met Cys

20 25 30

<210> 190

<211> 30

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<400> 190

Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe

1 5 10 15

Phe Phe Phe Phe Phe Phe Phe Phe Ala Ala Phe Trp Phe Trp

20 25 30

<210> 191

<211> 30

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<400> 191

Ile Phe Phe Ile Phe Phe Ile Ile Phe Phe Phe Phe Phe Phe Phe Phe

1 5 10 15

Phe Phe Phe Phe Ile Ile Ile Ile Ile Ile Ile Trp Glu Cys

20 25 30

<210> 192

<211> 30

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<400> 192

Phe Ile Phe Phe Phe Ile Ile Phe Phe Phe Phe Phe Ile Phe Phe Phe

1 5 10 15

Phe Phe Ile Phe Ile Ile Ile Ile Ile Ile Phe Trp Glu Cys

20 25 30

<210> 193

<211> 8

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 193

Trp Gln Ala Gly Ile Leu Ala Arg

15

<210> 194

<211> 7

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 194

His Ser Tyr Thr Thr Ala Glu

15

<210> 195

<211> 8

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 195

Pro Leu Thr Glu Glu Lys Ile Lys

15

<210> 196

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 196

Gly Ala Leu His Phe Lys Pro Gly Ser Arg

1 5 10

<210> 197

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 197

Arg Arg Ala Asn Lys Asp Ala Thr Ala Glu

1 5 10

<210> 198

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 198

Lys Ala Phe Ile Ser His Glu Glu Lys Arg

1 5 10

<210> 199

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 199

Thr Asp Leu Ser Ser Arg Phe Ser Lys Ser

1 5 10

<210> 200

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 200

Phe Asp Leu Gly Gly Gly Thr Phe Asp Val

1 5 10

<210> 201

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 201

Cys Leu Leu Leu His Tyr Ser Val Ser Lys

1 5 10

<210> 202

<211> 9

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 202

Met Thr Glu Tyr Lys Leu Val Val Val

15

<210> 203

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 203

Lys Lys Asn Lys Lys Asp Asp Ile Lys Asp

1 5 10

<210> 204

<211> 30

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<400> 204

Ala Gly Asn Asp Asp Asp Asp Asp Asp Asp Asp Asp Asp Asp Asp Asp

1 5 10 15

Asp Asp Asp Asp Lys Lys Asp Lys Asp Asp Asp Asp Asp Asp

20 25 30

<210> 205

<211> 30

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<400> 205

Ala Gly Asn Lys Lys Lys Lys Lys Lys Lys Asn Asn Asn Asn Asn Asn

1 5 10 15

Asn Asn Asn Asn Asn Asn Asn Asn Asn Asn Asn Asn Asn Asn

20 25 30

<210> 206

<211> 30

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<400> 206

Ala Gly Arg Asp Asp Asp Asp Asp Asp Asp Asp Asp Asp Asp Asp Asp

1 5 10 15

Asp Asp Asp Asp Asp Asp Asp Asp Asp Asp Asp Asp Asp Asp

20 25 30

<210> 207

<211> 9

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 207

Gly Lys Ser Ala Leu Thr Ile Gln Leu

15

<210> 208

<211> 7

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 208

Gly Lys Ser Ala Leu Thr Ile

15

<210> 209

<211> 8

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 209

Gln Gly Gln Asn Leu Lys Tyr Gln

15

<210> 210

<211> 8

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 210

Ile Leu Gly Val Leu Leu Leu Ile

15

<210> 211

<211> 8

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 211

Glu Lys Glu Gly Lys Ile Ser Lys

15

<210> 212

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 212

Ala Ala Ser Asp Phe Ile Phe Leu Val Thr

1 5 10

<210> 213

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 213

Lys Glu Leu Lys Gln Val Ala Ser Pro Phe

1 5 10

<210> 214

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 214

Lys Lys Lys Leu Ile Asn Glu Lys Lys Glu

1 5 10

<210> 215

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 215

Lys Lys Cys Asp Ile Ser Leu Gln Phe Phe

1 5 10

<210> 216

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 216

Lys Ser Thr Ala Gly Asp Thr His Leu Gly

1 5 10

<210> 217

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 217

Ala Thr Phe Tyr Val Ala Val Thr Val Pro

1 5 10

<210> 218

<211> 30

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<400> 218

Leu Thr Ile Gln Leu Ile Gln Asn His Phe Val Asp Glu Tyr Asp Pro

1 5 10 15

Thr Ile Glu Asp Ser Tyr Arg Lys Gln Val Val Ile Asp Gly

20 25 30

<210> 219

<211> 30

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<400> 219

Thr Ile Gln Leu Ile Gln Asn His Phe Val Asp Glu Tyr Asp Pro Thr

1 5 10 15

Ile Glu Asp Ser Tyr Arg Lys Gln Val Val Ile Asp Gly Glu

20 25 30

<210> 220

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 220

Leu Ile Met Gln Leu Met Pro Phe

15

<210> 221

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 221

Thr Val Gln Leu Ile Met Gln Leu

15

<210> 222

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 222

Thr Ser Thr Val Gln Leu Ile Met Gln Leu

1 5 10

<210> 223

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 223

Thr Val Gln Leu Ile Met Gln Leu Met

15

<210> 224

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 224

Val Gln Leu Ile Met Gln Leu Met

15

<210> 225

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 225

Ser Thr Val Gln Leu Ile Met Gln Leu

15

<210> 226

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 226

Leu Thr Ser Thr Val Gln Leu Ile Met

15

<210> 227

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 227

Leu Ile Met Gln Leu Met Pro Phe

15

<210> 228

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 228

Thr Val Gln Leu Ile Met Gln Leu

15

<210> 229

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 229

Thr Ser Thr Val Gln Leu Ile Met Gln Leu

1 5 10

<210> 230

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 230

Thr Val Gln Leu Ile Met Gln Leu Met

15

<210> 231

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 231

Val Gln Leu Ile Met Gln Leu Met

15

<210> 232

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 232

Ser Thr Val Gln Leu Ile Met Gln Leu

15

<210> 233

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 233

Leu Thr Ser Thr Val Gln Leu Ile Met

15

<210> 234

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 234

Ser Thr Val Gln Leu Ile Met Gln Leu

15

<210> 235

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 235

Leu Ile Met Gln Leu Met Pro Phe

15

<210> 236

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 236

Leu Thr Ser Thr Val Gln Leu Ile Met

15

<210> 237

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 237

Thr Val Gln Leu Ile Met Gln Leu

15

<210> 238

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 238

Thr Ser Thr Val Gln Leu Ile Met Gln Leu

1 5 10

<210> 239

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 239

Thr Val Gln Leu Ile Met Gln Leu Met

15

<210> 240

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 240

Val Gln Leu Ile Met Gln Leu Met

15

<210> 241

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 241

Ser Thr Val Gln Leu Ile Met Gln Leu

15

<210> 242

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 242

Leu Ile Met Gln Leu Met Pro Phe

15

<210> 243

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 243

Leu Thr Ser Thr Val Gln Leu Ile Met

15

<210> 244

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 244

Thr Val Gln Leu Ile Met Gln Leu

15

<210> 245

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 245

Thr Ser Thr Val Gln Leu Ile Met Gln Leu

1 5 10

<210> 246

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 246

Thr Val Gln Leu Ile Met Gln Leu Met

15

<210> 247

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 247

Val Gln Leu Ile Met Gln Leu Met

15

<210> 248

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 248

Ile Asp Ile Ile Met Lys Ile Arg Asn Ala

1 5 10

<210> 249

<211> 30

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<400> 249

Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe

1 5 10 15

Phe Phe Phe Phe Ile Ile Phe Phe Ile Phe Phe Trp Met Cys

20 25 30

<210> 250

<211> 30

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<400> 250

Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe Phe

1 5 10 15

Phe Phe Phe Phe Phe Phe Phe Phe Ala Ala Phe Trp Phe Trp

20 25 30

<210> 251

<211> 30

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<400> 251

Ile Phe Phe Ile Phe Phe Ile Ile Phe Phe Phe Phe Phe Phe Phe Phe

1 5 10 15

Phe Phe Phe Phe Ile Ile Ile Ile Ile Ile Ile Trp Glu Cys

20 25 30

<210> 252

<211> 30

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<400> 252

Phe Ile Phe Phe Phe Ile Ile Phe Phe Phe Phe Phe Ile Phe Phe Phe

1 5 10 15

Phe Phe Ile Phe Ile Ile Ile Ile Ile Ile Phe Trp Glu Cys

20 25 30

<210> 253

<211> 8

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 253

Trp Gln Ala Gly Ile Leu Ala Arg

15

<210> 254

<211> 7

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 254

His Ser Tyr Thr Thr Ala Glu

15

<210> 255

<211> 8

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 255

Pro Leu Thr Glu Glu Lys Ile Lys

15

<210> 256

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 256

Gly Ala Leu His Phe Lys Pro Gly Ser Arg

1 5 10

<210> 257

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 257

Arg Arg Ala Asn Lys Asp Ala Thr Ala Glu

1 5 10

<210> 258

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 258

Lys Ala Phe Ile Ser His Glu Glu Lys Arg

1 5 10

<210> 259

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 259

Thr Asp Leu Ser Ser Arg Phe Ser Lys Ser

1 5 10

<210> 260

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 260

Phe Asp Leu Gly Gly Gly Thr Phe Asp Val

1 5 10

<210> 261

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 261

Cys Leu Leu Leu His Tyr Ser Val Ser Lys

1 5 10

<210> 262

<211> 9

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 262

Met Thr Glu Tyr Lys Leu Val Val Val

15

<210> 263

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 263

Lys Lys Asn Lys Lys Asp Asp Ile Lys Asp

1 5 10

<210> 264

<211> 30

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<400> 264

Ala Gly Asn Asp Asp Asp Asp Asp Asp Asp Asp Asp Asp Asp Asp Asp

1 5 10 15

Asp Asp Asp Asp Lys Lys Asp Lys Asp Asp Asp Asp Asp Asp

20 25 30

<210> 265

<211> 30

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<400> 265

Ala Gly Asn Lys Lys Lys Lys Lys Lys Lys Asn Asn Asn Asn Asn Asn

1 5 10 15

Asn Asn Asn Asn Asn Asn Asn Asn Asn Asn Asn Asn Asn Asn

20 25 30

<210> 266

<211> 30

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<400> 266

Ala Gly Arg Asp Asp Asp Asp Asp Asp Asp Asp Asp Asp Asp Asp Asp

1 5 10 15

Asp Asp Asp Asp Asp Asp Asp Asp Asp Asp Asp Asp Asp Asp

20 25 30

<210> 267

<211> 9

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 267

Gly Lys Ser Ala Leu Thr Ile Gln Leu

15

<210> 268

<211> 7

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 268

Gly Lys Ser Ala Leu Thr Ile

15

<210> 269

<211> 8

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 269

Gln Gly Gln Asn Leu Lys Tyr Gln

15

<210> 270

<211> 8

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 270

Ile Leu Gly Val Leu Leu Leu Ile

15

<210> 271

<211> 8

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 271

Glu Lys Glu Gly Lys Ile Ser Lys

15

<210> 272

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 272

Ala Ala Ser Asp Phe Ile Phe Leu Val Thr

1 5 10

<210> 273

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 273

Lys Glu Leu Lys Gln Val Ala Ser Pro Phe

1 5 10

<210> 274

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 274

Lys Lys Lys Leu Ile Asn Glu Lys Lys Glu

1 5 10

<210> 275

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 275

Lys Lys Cys Asp Ile Ser Leu Gln Phe Phe

1 5 10

<210> 276

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 276

Lys Ser Thr Ala Gly Asp Thr His Leu Gly

1 5 10

<210> 277

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 277

Ala Thr Phe Tyr Val Ala Val Thr Val Pro

1 5 10

<210> 278

<211> 30

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<400> 278

Leu Thr Ile Gln Leu Ile Gln Asn His Phe Val Asp Glu Tyr Asp Pro

1 5 10 15

Thr Ile Glu Asp Ser Tyr Arg Lys Gln Val Val Ile Asp Gly

20 25 30

<210> 279

<211> 30

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<400> 279

Thr Ile Gln Leu Ile Gln Asn His Phe Val Asp Glu Tyr Asp Pro Thr

1 5 10 15

Ile Glu Asp Ser Tyr Arg Lys Gln Val Val Ile Asp Gly Glu

20 25 30

<210> 280

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 280

Leu Ile Met Gln Leu Met Pro Phe

15

<210> 281

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 281

Leu Thr Ser Thr Val Gln Leu Ile Met

15

<210> 282

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 282

Gln Leu Ile Met Gln Leu Met Pro Phe

15

<210> 283

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 283

Ser Thr Val Gln Leu Ile Met Gln Leu

15

<210> 284

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 284

Ser Thr Val Gln Leu Ile Met Gln Leu Met

1 5 10

<210> 285

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 285

Thr Ser Thr Val Gln Leu Ile Met Gln Leu

1 5 10

<210> 286

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 286

Thr Val Gln Leu Ile Met Gln Leu

15

<210> 287

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 287

Thr Val Gln Leu Ile Met Gln Leu Met

15

<210> 288

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 288

Val Gln Leu Ile Met Gln Leu Met

15

<210> 289

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 289

Ser Thr Val Gln Leu Ile Met Gln Leu Met

1 5 10

<210> 290

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 290

Gln Leu Ile Met Gln Leu Met Pro Phe

15

<210> 291

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 291

Ser Thr Val Gln Leu Ile Met Gln Leu Met

1 5 10

<210> 292

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 292

Gln Leu Ile Met Gln Leu Met Pro Phe

15

<210> 293

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 293

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 294

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 294

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 295

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 295

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 296

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 296

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 297

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 297

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 298

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 298

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 299

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 299

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

<210> 300

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 300

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His

<210> 301

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 301

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His

20

<210> 302

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 302

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala Glu Ser Lys Ile

20 25

<210> 303

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 303

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

20 25

<210> 304

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 304

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

20 25 30

His

<210> 305

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 305

Glu Pro Cys Ser Met Leu Thr Gly

15

<210> 306

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 306

Pro Cys Ser Met Leu Thr Gly Pro

15

<210> 307

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 307

Cys Ser Met Leu Thr Gly Pro Pro

15

<210> 308

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 308

Ser Met Leu Thr Gly Pro Pro Ala

15

<210> 309

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 309

Met Leu Thr Gly Pro Pro Ala Arg

15

<210> 310

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 310

Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 311

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 311

Thr Gly Pro Pro Ala Arg Val Pro

15

<210> 312

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 312

Gly Pro Pro Ala Arg Val Pro Ala

15

<210> 313

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 313

Pro Pro Ala Arg Val Pro Ala Val

15

<210> 314

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 314

Pro Ala Arg Val Pro Ala Val Pro

15

<210> 315

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 315

Ala Arg Val Pro Ala Val Pro Phe

15

<210> 316

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 316

Arg Val Pro Ala Val Pro Phe Asp

15

<210> 317

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 317

Val Pro Ala Val Pro Phe Asp Leu

15

<210> 318

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 318

Pro Ala Val Pro Phe Asp Leu His

15

<210> 319

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 319

Ala Val Pro Phe Asp Leu His Phe

15

<210> 320

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 320

Val Pro Phe Asp Leu His Phe Cys

15

<210> 321

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 321

Pro Phe Asp Leu His Phe Cys Arg

15

<210> 322

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 322

Phe Asp Leu His Phe Cys Arg Ser

15

<210> 323

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 323

Asp Leu His Phe Cys Arg Ser Ser

15

<210> 324

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 324

Leu His Phe Cys Arg Ser Ser Ile

15

<210> 325

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 325

His Phe Cys Arg Ser Ser Ile Met

15

<210> 326

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 326

Phe Cys Arg Ser Ser Ile Met Lys

15

<210> 327

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 327

Cys Arg Ser Ser Ile Met Lys Pro

15

<210> 328

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 328

Arg Ser Ser Ile Met Lys Pro Lys

15

<210> 329

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 329

Ser Ser Ile Met Lys Pro Lys Arg

15

<210> 330

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 330

Ser Ile Met Lys Pro Lys Arg Asp

15

<210> 331

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 331

Ile Met Lys Pro Lys Arg Asp Gly

15

<210> 332

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 332

Met Lys Pro Lys Arg Asp Gly Tyr

15

<210> 333

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 333

Lys Pro Lys Arg Asp Gly Tyr Met

15

<210> 334

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 334

Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 335

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 335

Lys Arg Asp Gly Tyr Met Phe Leu

15

<210> 336

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 336

Arg Asp Gly Tyr Met Phe Leu Lys

15

<210> 337

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 337

Asp Gly Tyr Met Phe Leu Lys Ala

15

<210> 338

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 338

Gly Tyr Met Phe Leu Lys Ala Glu

15

<210> 339

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 339

Tyr Met Phe Leu Lys Ala Glu Ser

15

<210> 340

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 340

Met Phe Leu Lys Ala Glu Ser Lys

15

<210> 341

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 341

Phe Leu Lys Ala Glu Ser Lys Ile

15

<210> 342

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 342

Leu Lys Ala Glu Ser Lys Ile Met

15

<210> 343

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 343

Lys Ala Glu Ser Lys Ile Met Phe

15

<210> 344

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 344

Ala Glu Ser Lys Ile Met Phe Ala

15

<210> 345

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 345

Glu Ser Lys Ile Met Phe Ala Thr

15

<210> 346

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 346

Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 347

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 347

Lys Ile Met Phe Ala Thr Leu Gln

15

<210> 348

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 348

Ile Met Phe Ala Thr Leu Gln Arg

15

<210> 349

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 349

Met Phe Ala Thr Leu Gln Arg Ser

15

<210> 350

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 350

Phe Ala Thr Leu Gln Arg Ser Ser

15

<210> 351

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 351

Ala Thr Leu Gln Arg Ser Ser Leu

15

<210> 352

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 352

Thr Leu Gln Arg Ser Ser Leu Trp

15

<210> 353

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 353

Leu Gln Arg Ser Ser Leu Trp Cys

15

<210> 354

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 354

Gln Arg Ser Ser Leu Trp Cys Leu

15

<210> 355

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 355

Arg Ser Ser Leu Trp Cys Leu Cys

15

<210> 356

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 356

Ser Ser Leu Trp Cys Leu Cys Ser

15

<210> 357

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 357

Ser Leu Trp Cys Leu Cys Ser Asn

15

<210> 358

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 358

Glu Pro Cys Ser Met Leu Thr Gly Pro

15

<210> 359

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 359

Pro Cys Ser Met Leu Thr Gly Pro Pro

15

<210> 360

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 360

Cys Ser Met Leu Thr Gly Pro Pro Ala

15

<210> 361

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 361

Ser Met Leu Thr Gly Pro Pro Ala Arg

15

<210> 362

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 362

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 363

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 363

Leu Thr Gly Pro Pro Ala Arg Val Pro

15

<210> 364

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 364

Thr Gly Pro Pro Ala Arg Val Pro Ala

15

<210> 365

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 365

Gly Pro Pro Ala Arg Val Pro Ala Val

15

<210> 366

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 366

Pro Pro Ala Arg Val Pro Ala Val Pro

15

<210> 367

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 367

Pro Ala Arg Val Pro Ala Val Pro Phe

15

<210> 368

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 368

Ala Arg Val Pro Ala Val Pro Phe Asp

15

<210> 369

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 369

Arg Val Pro Ala Val Pro Phe Asp Leu

15

<210> 370

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 370

Val Pro Ala Val Pro Phe Asp Leu His

15

<210> 371

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 371

Pro Ala Val Pro Phe Asp Leu His Phe

15

<210> 372

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 372

Ala Val Pro Phe Asp Leu His Phe Cys

15

<210> 373

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 373

Val Pro Phe Asp Leu His Phe Cys Arg

15

<210> 374

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 374

Pro Phe Asp Leu His Phe Cys Arg Ser

15

<210> 375

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 375

Phe Asp Leu His Phe Cys Arg Ser Ser

15

<210> 376

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 376

Asp Leu His Phe Cys Arg Ser Ser Ile

15

<210> 377

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 377

Leu His Phe Cys Arg Ser Ser Ile Met

15

<210> 378

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 378

His Phe Cys Arg Ser Ser Ile Met Lys

15

<210> 379

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 379

Phe Cys Arg Ser Ser Ile Met Lys Pro

15

<210> 380

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 380

Cys Arg Ser Ser Ile Met Lys Pro Lys

15

<210> 381

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 381

Arg Ser Ser Ile Met Lys Pro Lys Arg

15

<210> 382

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 382

Ser Ser Ile Met Lys Pro Lys Arg Asp

15

<210> 383

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 383

Ser Ile Met Lys Pro Lys Arg Asp Gly

15

<210> 384

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 384

Ile Met Lys Pro Lys Arg Asp Gly Tyr

15

<210> 385

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 385

Met Lys Pro Lys Arg Asp Gly Tyr Met

15

<210> 386

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 386

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 387

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 387

Pro Lys Arg Asp Gly Tyr Met Phe Leu

15

<210> 388

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 388

Lys Arg Asp Gly Tyr Met Phe Leu Lys

15

<210> 389

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 389

Arg Asp Gly Tyr Met Phe Leu Lys Ala

15

<210> 390

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 390

Asp Gly Tyr Met Phe Leu Lys Ala Glu

15

<210> 391

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 391

Gly Tyr Met Phe Leu Lys Ala Glu Ser

15

<210> 392

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 392

Tyr Met Phe Leu Lys Ala Glu Ser Lys

15

<210> 393

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 393

Met Phe Leu Lys Ala Glu Ser Lys Ile

15

<210> 394

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 394

Phe Leu Lys Ala Glu Ser Lys Ile Met

15

<210> 395

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 395

Leu Lys Ala Glu Ser Lys Ile Met Phe

15

<210> 396

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 396

Lys Ala Glu Ser Lys Ile Met Phe Ala

15

<210> 397

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 397

Ala Glu Ser Lys Ile Met Phe Ala Thr

15

<210> 398

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 398

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 399

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 399

Ser Lys Ile Met Phe Ala Thr Leu Gln

15

<210> 400

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 400

Lys Ile Met Phe Ala Thr Leu Gln Arg

15

<210> 401

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 401

Ile Met Phe Ala Thr Leu Gln Arg Ser

15

<210> 402

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 402

Met Phe Ala Thr Leu Gln Arg Ser Ser

15

<210> 403

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 403

Phe Ala Thr Leu Gln Arg Ser Ser Leu

15

<210> 404

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 404

Ala Thr Leu Gln Arg Ser Ser Leu Trp

15

<210> 405

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 405

Thr Leu Gln Arg Ser Ser Leu Trp Cys

15

<210> 406

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 406

Leu Gln Arg Ser Ser Leu Trp Cys Leu

15

<210> 407

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 407

Gln Arg Ser Ser Leu Trp Cys Leu Cys

15

<210> 408

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 408

Arg Ser Ser Leu Trp Cys Leu Cys Ser

15

<210> 409

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 409

Ser Ser Leu Trp Cys Leu Cys Ser Asn

15

<210> 410

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 410

Ser Leu Trp Cys Leu Cys Ser Asn His

15

<210> 411

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 411

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro

1 5 10

<210> 412

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 412

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala

1 5 10

<210> 413

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 413

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg

1 5 10

<210> 414

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 414

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 415

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 415

Met Leu Thr Gly Pro Pro Ala Arg Val Pro

1 5 10

<210> 416

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 416

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala

1 5 10

<210> 417

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 417

Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10

<210> 418

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 418

Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10

<210> 419

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 419

Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10

<210> 420

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 420

Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10

<210> 421

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 421

Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10

<210> 422

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 422

Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10

<210> 423

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 423

Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10

<210> 424

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 424

Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10

<210> 425

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 425

Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10

<210> 426

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 426

Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10

<210> 427

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 427

Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10

<210> 428

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 428

Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10

<210> 429

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 429

Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10

<210> 430

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 430

Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10

<210> 431

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 431

His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10

<210> 432

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 432

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10

<210> 433

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 433

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10

<210> 434

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 434

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10

<210> 435

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 435

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10

<210> 436

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 436

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10

<210> 437

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 437

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10

<210> 438

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 438

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10

<210> 439

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 439

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 440

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 440

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10

<210> 441

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 441

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10

<210> 442

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 442

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

1 5 10

<210> 443

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 443

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

1 5 10

<210> 444

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 444

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

1 5 10

<210> 445

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 445

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 446

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 446

Met Phe Leu Lys Ala Glu Ser Lys Ile Met

1 5 10

<210> 447

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 447

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10

<210> 448

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 448

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

1 5 10

<210> 449

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 449

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

1 5 10

<210> 450

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 450

Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

1 5 10

<210> 451

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 451

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

1 5 10

<210> 452

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 452

Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

1 5 10

<210> 453

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 453

Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

1 5 10

<210> 454

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 454

Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

1 5 10

<210> 455

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 455

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 456

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 456

Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp

1 5 10

<210> 457

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 457

Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

1 5 10

<210> 458

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 458

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

1 5 10

<210> 459

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 459

Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys

1 5 10

<210> 460

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 460

Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser

1 5 10

<210> 461

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 461

Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

1 5 10

<210> 462

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 462

Ser Ser Leu Trp Cys Leu Cys Ser Asn His

1 5 10

<210> 463

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 463

Ser Leu Trp Cys Leu Cys Ser Asn His

15

<210> 464

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 464

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala

1 5 10

<210> 465

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 465

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg

1 5 10

<210> 466

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 466

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 467

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 467

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro

1 5 10

<210> 468

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 468

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala

1 5 10

<210> 469

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 469

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10

<210> 470

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 470

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10

<210> 471

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 471

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10

<210> 472

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 472

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10

<210> 473

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 473

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10

<210> 474

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 474

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10

<210> 475

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 475

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10

<210> 476

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 476

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10

<210> 477

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 477

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10

<210> 478

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 478

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10

<210> 479

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 479

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10

<210> 480

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 480

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10

<210> 481

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 481

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10

<210> 482

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 482

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10

<210> 483

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 483

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10

<210> 484

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 484

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10

<210> 485

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 485

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10

<210> 486

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 486

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10

<210> 487

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 487

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10

<210> 488

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 488

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10

<210> 489

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 489

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10

<210> 490

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 490

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10

<210> 491

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 491

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 492

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 492

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10

<210> 493

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 493

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10

<210> 494

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 494

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

1 5 10

<210> 495

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 495

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

1 5 10

<210> 496

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 496

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

1 5 10

<210> 497

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 497

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 498

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 498

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

1 5 10

<210> 499

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 499

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10

<210> 500

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 500

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

1 5 10

<210> 501

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 501

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

1 5 10

<210> 502

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 502

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

1 5 10

<210> 503

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 503

Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

1 5 10

<210> 504

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 504

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

1 5 10

<210> 505

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 505

Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

1 5 10

<210> 506

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 506

Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

1 5 10

<210> 507

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 507

Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 508

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 508

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp

1 5 10

<210> 509

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 509

Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

1 5 10

<210> 510

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 510

Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

1 5 10

<210> 511

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 511

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys

1 5 10

<210> 512

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 512

Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser

1 5 10

<210> 513

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 513

Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

1 5 10

<210> 514

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 514

Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn His

1 5 10

<210> 515

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 515

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg

1 5 10

<210> 516

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 516

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 517

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 517

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro

1 5 10

<210> 518

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 518

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala

1 5 10

<210> 519

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 519

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10

<210> 520

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 520

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10

<210> 521

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 521

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10

<210> 522

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 522

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10

<210> 523

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 523

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10

<210> 524

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 524

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10

<210> 525

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 525

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10

<210> 526

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 526

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10

<210> 527

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 527

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10

<210> 528

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 528

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10

<210> 529

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 529

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10

<210> 530

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 530

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10

<210> 531

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 531

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10

<210> 532

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 532

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10

<210> 533

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 533

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10

<210> 534

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 534

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10

<210> 535

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 535

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10

<210> 536

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 536

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10

<210> 537

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 537

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10

<210> 538

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 538

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10

<210> 539

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 539

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10

<210> 540

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 540

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10

<210> 541

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 541

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 542

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 542

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10

<210> 543

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 543

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10

<210> 544

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 544

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

1 5 10

<210> 545

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 545

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

1 5 10

<210> 546

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 546

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

1 5 10

<210> 547

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 547

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 548

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 548

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

1 5 10

<210> 549

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 549

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10

<210> 550

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 550

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

1 5 10

<210> 551

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 551

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

1 5 10

<210> 552

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 552

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

1 5 10

<210> 553

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 553

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

1 5 10

<210> 554

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 554

Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

1 5 10

<210> 555

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 555

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

1 5 10

<210> 556

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 556

Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

1 5 10

<210> 557

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 557

Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 558

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 558

Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp

1 5 10

<210> 559

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 559

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

1 5 10

<210> 560

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 560

Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

1 5 10

<210> 561

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 561

Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys

1 5 10

<210> 562

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 562

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser

1 5 10

<210> 563

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 563

Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

1 5 10

<210> 564

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 564

Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn His

1 5 10

<210> 565

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 565

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 566

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 566

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro

1 5 10

<210> 567

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 567

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala

1 5 10

<210> 568

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 568

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10

<210> 569

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 569

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10

<210> 570

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 570

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10

<210> 571

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 571

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10

<210> 572

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 572

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10

<210> 573

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 573

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10

<210> 574

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 574

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10

<210> 575

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 575

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10

<210> 576

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 576

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10

<210> 577

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 577

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10

<210> 578

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 578

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10

<210> 579

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 579

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10

<210> 580

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 580

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10

<210> 581

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 581

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10

<210> 582

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 582

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10

<210> 583

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 583

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10

<210> 584

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 584

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10

<210> 585

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 585

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10

<210> 586

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 586

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10

<210> 587

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 587

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10

<210> 588

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 588

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10

<210> 589

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 589

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10

<210> 590

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 590

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 591

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 591

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10

<210> 592

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 592

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10

<210> 593

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 593

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

1 5 10

<210> 594

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 594

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

1 5 10

<210> 595

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 595

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

1 5 10

<210> 596

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 596

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 597

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 597

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

1 5 10

<210> 598

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 598

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10

<210> 599

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 599

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

1 5 10

<210> 600

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 600

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

1 5 10

<210> 601

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 601

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

1 5 10

<210> 602

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 602

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

1 5 10

<210> 603

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 603

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

1 5 10

<210> 604

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 604

Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

1 5 10

<210> 605

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 605

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

1 5 10

<210> 606

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 606

Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 607

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 607

Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp

1 5 10

<210> 608

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 608

Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

1 5 10

<210> 609

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 609

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

1 5 10

<210> 610

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 610

Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys

1 5 10

<210> 611

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 611

Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser

1 5 10

<210> 612

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 612

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

1 5 10

<210> 613

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 613

Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn His

1 5 10

<210> 614

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 614

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro

1 5 10

<210> 615

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 615

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala

1 5 10

<210> 616

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 616

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10

<210> 617

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 617

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10

<210> 618

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 618

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10

<210> 619

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 619

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10

<210> 620

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 620

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10

<210> 621

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 621

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10

<210> 622

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 622

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10

<210> 623

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 623

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10

<210> 624

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 624

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10

<210> 625

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 625

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10

<210> 626

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 626

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10

<210> 627

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 627

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10

<210> 628

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 628

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10

<210> 629

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 629

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10

<210> 630

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 630

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10

<210> 631

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 631

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10

<210> 632

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 632

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10

<210> 633

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 633

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10

<210> 634

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 634

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10

<210> 635

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 635

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10

<210> 636

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 636

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10

<210> 637

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 637

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10

<210> 638

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 638

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 639

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 639

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10

<210> 640

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 640

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10

<210> 641

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 641

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

1 5 10

<210> 642

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 642

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

1 5 10

<210> 643

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 643

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

1 5 10

<210> 644

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 644

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 645

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 645

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

1 5 10

<210> 646

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 646

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10

<210> 647

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 647

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

1 5 10

<210> 648

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 648

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

1 5 10

<210> 649

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 649

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

1 5 10

<210> 650

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 650

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

1 5 10

<210> 651

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 651

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

1 5 10

<210> 652

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 652

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

1 5 10

<210> 653

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 653

Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

1 5 10

<210> 654

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 654

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 655

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 655

Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp

1 5 10

<210> 656

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 656

Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

1 5 10

<210> 657

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 657

Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

1 5 10

<210> 658

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 658

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys

1 5 10

<210> 659

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 659

Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser

1 5 10

<210> 660

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 660

Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

1 5 10

<210> 661

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 661

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn His

1 5 10

<210> 662

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 662

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala

1 5 10 15

<210> 663

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 663

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

<210> 664

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 664

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10 15

<210> 665

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 665

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10 15

<210> 666

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 666

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

<210> 667

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 667

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10 15

<210> 668

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 668

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10 15

<210> 669

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 669

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10 15

<210> 670

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 670

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

<210> 671

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 671

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

<210> 672

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 672

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10 15

<210> 673

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 673

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10 15

<210> 674

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 674

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10 15

<210> 675

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 675

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10 15

<210> 676

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 676

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10 15

<210> 677

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 677

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10 15

<210> 678

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 678

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10 15

<210> 679

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 679

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10 15

<210> 680

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 680

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10 15

<210> 681

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 681

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

<210> 682

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 682

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

<210> 683

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 683

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10 15

<210> 684

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 684

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10 15

<210> 685

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 685

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10 15

<210> 686

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 686

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10 15

<210> 687

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 687

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10 15

<210> 688

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 688

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

1 5 10 15

<210> 689

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 689

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

1 5 10 15

<210> 690

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 690

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

1 5 10 15

<210> 691

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 691

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

<210> 692

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 692

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

1 5 10 15

<210> 693

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 693

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10 15

<210> 694

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 694

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

1 5 10 15

<210> 695

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 695

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

1 5 10 15

<210> 696

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 696

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

1 5 10 15

<210> 697

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 697

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

1 5 10 15

<210> 698

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 698

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

1 5 10 15

<210> 699

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 699

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

1 5 10 15

<210> 700

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 700

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

1 5 10 15

<210> 701

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 701

Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10 15

<210> 702

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 702

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp

1 5 10 15

<210> 703

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 703

Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

1 5 10 15

<210> 704

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 704

Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

1 5 10 15

<210> 705

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 705

Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys

1 5 10 15

<210> 706

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 706

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser

1 5 10 15

<210> 707

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 707

Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

1 5 10 15

<210> 708

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 708

Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn His

1 5 10 15

<210> 709

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 709

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

<210> 710

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 710

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10 15

<210> 711

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 711

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10 15

<210> 712

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 712

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

<210> 713

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 713

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10 15

<210> 714

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 714

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10 15

<210> 715

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 715

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10 15

<210> 716

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 716

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

<210> 717

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 717

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

<210> 718

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 718

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10 15

<210> 719

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 719

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10 15

<210> 720

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 720

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10 15

<210> 721

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 721

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10 15

<210> 722

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 722

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10 15

<210> 723

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 723

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10 15

<210> 724

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 724

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10 15

<210> 725

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 725

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10 15

<210> 726

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 726

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10 15

<210> 727

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 727

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

<210> 728

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 728

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

<210> 729

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 729

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10 15

<210> 730

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 730

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10 15

<210> 731

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 731

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10 15

<210> 732

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 732

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10 15

<210> 733

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 733

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10 15

<210> 734

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 734

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

1 5 10 15

<210> 735

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 735

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

1 5 10 15

<210> 736

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 736

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

1 5 10 15

<210> 737

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 737

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

<210> 738

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 738

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

1 5 10 15

<210> 739

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 739

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10 15

<210> 740

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 740

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

1 5 10 15

<210> 741

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 741

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

1 5 10 15

<210> 742

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 742

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

1 5 10 15

<210> 743

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 743

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

1 5 10 15

<210> 744

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 744

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

1 5 10 15

<210> 745

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 745

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

1 5 10 15

<210> 746

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 746

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

1 5 10 15

<210> 747

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 747

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10 15

<210> 748

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 748

Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp

1 5 10 15

<210> 749

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 749

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

1 5 10 15

<210> 750

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 750

Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

1 5 10 15

<210> 751

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 751

Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys

1 5 10 15

<210> 752

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 752

Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser

1 5 10 15

<210> 753

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 753

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

1 5 10 15

<210> 754

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 754

Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn His

1 5 10 15

<210> 755

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 755

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro

<210> 756

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 756

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10 15

Phe

<210> 757

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 757

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10 15

Asp

<210> 758

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 758

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu

<210> 759

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 759

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10 15

His

<210> 760

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 760

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10 15

Phe

<210> 761

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 761

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10 15

Cys

<210> 762

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 762

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg

<210> 763

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 763

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

Ser

<210> 764

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 764

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10 15

Ser

<210> 765

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 765

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10 15

Ile

<210> 766

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 766

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10 15

Met

<210> 767

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 767

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10 15

Lys

<210> 768

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 768

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10 15

Pro

<210> 769

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 769

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10 15

Lys

<210> 770

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 770

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10 15

Arg

<210> 771

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 771

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10 15

Asp

<210> 772

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 772

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10 15

Gly

<210> 773

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 773

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr

<210> 774

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 774

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met

<210> 775

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 775

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10 15

Phe

<210> 776

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 776

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10 15

Leu

<210> 777

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 777

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10 15

Lys

<210> 778

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 778

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10 15

Ala

<210> 779

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 779

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10 15

Glu

<210> 780

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 780

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

1 5 10 15

Ser

<210> 781

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 781

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

1 5 10 15

Lys

<210> 782

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 782

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

1 5 10 15

Ile

<210> 783

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 783

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met

<210> 784

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 784

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

1 5 10 15

Phe

<210> 785

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 785

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10 15

Ala

<210> 786

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 786

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

1 5 10 15

Thr

<210> 787

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 787

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

1 5 10 15

Leu

<210> 788

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 788

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

1 5 10 15

Gln

<210> 789

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 789

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

1 5 10 15

Arg

<210> 790

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 790

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

1 5 10 15

Ser

<210> 791

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 791

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

1 5 10 15

Ser

<210> 792

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 792

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

1 5 10 15

Leu

<210> 793

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 793

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10 15

Trp

<210> 794

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 794

Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp

1 5 10 15

Cys

<210> 795

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 795

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

1 5 10 15

Leu

<210> 796

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 796

Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

1 5 10 15

Cys

<210> 797

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 797

Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys

1 5 10 15

Ser

<210> 798

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 798

Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser

1 5 10 15

Asn

<210> 799

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 799

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

1 5 10 15

His

<210> 800

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 800

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe

<210> 801

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 801

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10 15

Phe Asp

<210> 802

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 802

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10 15

Asp Leu

<210> 803

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 803

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His

<210> 804

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 804

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10 15

His Phe

<210> 805

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 805

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10 15

Phe Cys

<210> 806

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 806

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10 15

CysArg

<210> 807

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 807

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser

<210> 808

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 808

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

Ser Ser

<210> 809

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 809

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10 15

Ser Ile

<210> 810

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 810

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10 15

Ile Met

<210> 811

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 811

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10 15

Met Lys

<210> 812

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 812

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10 15

Lys Pro

<210> 813

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 813

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10 15

Pro Lys

<210> 814

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 814

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10 15

Lys Arg

<210> 815

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 815

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10 15

Arg Asp

<210> 816

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 816

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10 15

Asp Gly

<210> 817

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 817

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10 15

Gly Tyr

<210> 818

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 818

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met

<210> 819

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 819

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe

<210> 820

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 820

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10 15

Phe Leu

<210> 821

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 821

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10 15

Leu Lys

<210> 822

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 822

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10 15

Lys Ala

<210> 823

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 823

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10 15

Ala Glu

<210> 824

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 824

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10 15

Glu Ser

<210> 825

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 825

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

1 5 10 15

Ser Lys

<210> 826

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 826

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

1 5 10 15

Lys Ile

<210> 827

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 827

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

1 5 10 15

Ile Met

<210> 828

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 828

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe

<210> 829

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 829

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

1 5 10 15

Phe Ala

<210> 830

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 830

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10 15

Ala Thr

<210> 831

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 831

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

1 5 10 15

Thr Leu

<210> 832

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 832

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

1 5 10 15

Leu Gln

<210> 833

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 833

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

1 5 10 15

Gln Arg

<210> 834

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 834

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

1 5 10 15

Arg Ser

<210> 835

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 835

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

1 5 10 15

Ser Ser

<210> 836

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 836

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

1 5 10 15

Ser Leu

<210> 837

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 837

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

1 5 10 15

Leu Trp

<210> 838

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 838

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10 15

Trp Cys

<210> 839

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 839

Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp

1 5 10 15

Cys Leu

<210> 840

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 840

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

1 5 10 15

Leu Cys

<210> 841

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 841

Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

1 5 10 15

Cys Ser

<210> 842

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 842

Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys

1 5 10 15

Ser Asn

<210> 843

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 843

Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser

1 5 10 15

Asn His

<210> 844

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 844

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp

<210> 845

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 845

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10 15

Phe Asp Leu

<210> 846

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 846

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10 15

Asp Leu His

<210> 847

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 847

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His Phe

<210> 848

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 848

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10 15

His Phe Cys

<210> 849

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 849

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10 15

Phe CysArg

<210> 850

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 850

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10 15

Cys Arg Ser

<210> 851

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 851

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser

<210> 852

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 852

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

Ser Ser Ile

<210> 853

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 853

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10 15

Ser Ile Met

<210> 854

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 854

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10 15

Ile Met Lys

<210> 855

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 855

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10 15

Met Lys Pro

<210> 856

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 856

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10 15

Lys Pro Lys

<210> 857

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 857

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10 15

Pro Lys Arg

<210> 858

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 858

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10 15

Lys Arg Asp

<210> 859

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 859

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10 15

Arg Asp Gly

<210> 860

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 860

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10 15

Asp Gly Tyr

<210> 861

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 861

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10 15

Gly Tyr Met

<210> 862

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 862

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met Phe

<210> 863

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 863

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu

<210> 864

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 864

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10 15

Phe Leu Lys

<210> 865

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 865

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10 15

Leu Lys Ala

<210> 866

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 866

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10 15

Lys Ala Glu

<210> 867

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 867

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10 15

Ala Glu Ser

<210> 868

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 868

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10 15

Glu Ser Lys

<210> 869

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 869

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

1 5 10 15

Ser Lys Ile

<210> 870

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 870

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

1 5 10 15

Lys Ile Met

<210> 871

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 871

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

1 5 10 15

Ile Met Phe

<210> 872

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 872

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala

<210> 873

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 873

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

1 5 10 15

Phe Ala Thr

<210> 874

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 874

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10 15

Ala Thr Leu

<210> 875

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 875

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

1 5 10 15

Thr Leu Gln

<210> 876

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 876

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

1 5 10 15

Leu Gln Arg

<210> 877

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 877

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

1 5 10 15

Gln Arg Ser

<210> 878

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 878

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

1 5 10 15

Arg Ser Ser

<210> 879

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 879

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

1 5 10 15

Ser Ser Leu

<210> 880

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 880

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

1 5 10 15

Ser Leu Trp

<210> 881

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 881

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

1 5 10 15

Leu Trp Cys

<210> 882

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 882

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10 15

Trp CysLeu

<210> 883

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 883

Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp

1 5 10 15

Cys Leu Cys

<210> 884

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 884

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

1 5 10 15

Leu Cys Ser

<210> 885

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 885

Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

1 5 10 15

Cys Ser Asn

<210> 886

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 886

Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys

1 5 10 15

Ser Asn His

<210> 887

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 887

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu

20

<210> 888

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 888

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10 15

Phe Asp Leu His

20

<210> 889

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 889

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10 15

Asp Leu His Phe

20

<210> 890

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 890

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His Phe Cys

20

<210> 891

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 891

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10 15

His Phe Cys Arg

20

<210> 892

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 892

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10 15

Phe Cys Arg Ser

20

<210> 893

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 893

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10 15

Cys Arg Ser Ser

20

<210> 894

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 894

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile

20

<210> 895

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 895

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

Ser Ser Ile Met

20

<210> 896

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 896

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10 15

Ser Ile Met Lys

20

<210> 897

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 897

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10 15

Ile Met Lys Pro

20

<210> 898

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 898

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10 15

Met Lys Pro Lys

20

<210> 899

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 899

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10 15

Lys Pro Lys Arg

20

<210> 900

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 900

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10 15

Pro Lys Arg Asp

20

<210> 901

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 901

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10 15

Lys Arg Asp Gly

20

<210> 902

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 902

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10 15

Arg Asp Gly Tyr

20

<210> 903

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 903

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10 15

Asp Gly Tyr Met

20

<210> 904

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 904

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10 15

Gly Tyr Met Phe

20

<210> 905

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 905

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met Phe Leu

20

<210> 906

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 906

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys

20

<210> 907

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 907

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10 15

Phe Leu Lys Ala

20

<210> 908

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 908

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10 15

Leu Lys Ala Glu

20

<210> 909

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 909

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10 15

Lys Ala Glu Ser

20

<210> 910

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 910

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10 15

Ala Glu Ser Lys

20

<210> 911

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 911

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10 15

Glu Ser Lys Ile

20

<210> 912

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 912

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

1 5 10 15

Ser Lys Ile Met

20

<210> 913

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 913

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

1 5 10 15

Lys Ile Met Phe

20

<210> 914

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 914

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

1 5 10 15

Ile Met Phe Ala

20

<210> 915

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 915

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr

20

<210> 916

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 916

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

1 5 10 15

Phe Ala Thr Leu

20

<210> 917

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 917

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10 15

Ala Thr Leu Gln

20

<210> 918

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 918

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

1 5 10 15

Thr Leu Gln Arg

20

<210> 919

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 919

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

1 5 10 15

Leu Gln Arg Ser

20

<210> 920

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 920

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

1 5 10 15

Gln Arg Ser Ser

20

<210> 921

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 921

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

1 5 10 15

Arg Ser Ser Leu

20

<210> 922

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 922

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

1 5 10 15

Ser Ser Leu Trp

20

<210> 923

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 923

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

1 5 10 15

Ser Leu Trp Cys

20

<210> 924

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 924

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

1 5 10 15

Leu Trp Cys Leu

20

<210> 925

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 925

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10 15

Trp Cys Leu Cys

20

<210> 926

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 926

Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp

1 5 10 15

Cys Leu Cys Ser

20

<210> 927

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 927

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

1 5 10 15

Leu Cys Ser Asn

20

<210> 928

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 928

Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

1 5 10 15

Cys Ser Asn His

20

<210> 929

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 929

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His

20

<210> 930

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 930

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10 15

Phe Asp Leu His Phe

20

<210> 931

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 931

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10 15

Asp Leu His Phe Cys

20

<210> 932

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 932

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His Phe Cys Arg

20

<210> 933

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 933

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10 15

His Phe Cys Arg Ser

20

<210> 934

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 934

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10 15

Phe Cys Arg Ser Ser

20

<210> 935

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 935

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10 15

Cys Arg Ser Ser Ile

20

<210> 936

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 936

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met

20

<210> 937

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 937

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

Ser Ser Ile Met Lys

20

<210> 938

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 938

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10 15

Ser Ile Met Lys Pro

20

<210> 939

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 939

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10 15

Ile Met Lys Pro Lys

20

<210> 940

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 940

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10 15

Met Lys Pro Lys Arg

20

<210> 941

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 941

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10 15

Lys Pro Lys Arg Asp

20

<210> 942

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 942

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10 15

Pro Lys Arg Asp Gly

20

<210> 943

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 943

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10 15

Lys Arg Asp Gly Tyr

20

<210> 944

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 944

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10 15

Arg Asp Gly Tyr Met

20

<210> 945

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 945

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10 15

Asp Gly Tyr Met Phe

20

<210> 946

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 946

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10 15

Gly Tyr Met Phe Leu

20

<210> 947

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 947

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met Phe Leu Lys

20

<210> 948

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 948

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala

20

<210> 949

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 949

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10 15

Phe Leu Lys Ala Glu

20

<210> 950

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 950

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10 15

Leu Lys Ala Glu Ser

20

<210> 951

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 951

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10 15

Lys Ala Glu Ser Lys

20

<210> 952

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 952

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10 15

Ala Glu Ser Lys Ile

20

<210> 953

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 953

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10 15

Glu Ser Lys Ile Met

20

<210> 954

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 954

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

1 5 10 15

Ser Lys Ile Met Phe

20

<210> 955

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 955

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

1 5 10 15

Lys Ile Met Phe Ala

20

<210> 956

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 956

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

1 5 10 15

Ile Met Phe Ala Thr

20

<210> 957

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 957

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu

20

<210> 958

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 958

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

1 5 10 15

Phe Ala Thr Leu Gln

20

<210> 959

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 959

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10 15

Ala Thr Leu Gln Arg

20

<210> 960

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 960

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

1 5 10 15

Thr Leu Gln Arg Ser

20

<210> 961

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 961

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

1 5 10 15

Leu Gln Arg Ser Ser

20

<210> 962

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 962

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

1 5 10 15

Gln Arg Ser Ser Leu

20

<210> 963

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 963

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

1 5 10 15

Arg Ser Ser Leu Trp

20

<210> 964

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 964

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

1 5 10 15

Ser Ser Leu Trp Cys

20

<210> 965

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 965

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

1 5 10 15

Ser Leu Trp Cys Leu

20

<210> 966

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 966

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

1 5 10 15

Leu Trp Cys Leu Cys

20

<210> 967

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 967

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10 15

Trp Cys Leu Cys Ser

20

<210> 968

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 968

Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp

1 5 10 15

Cys Leu Cys Ser Asn

20

<210> 969

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 969

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

1 5 10 15

Leu Cys Ser Asn His

20

<210> 970

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 970

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His Phe

20

<210> 971

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 971

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10 15

Phe Asp Leu His Phe Cys

20

<210> 972

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 972

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10 15

Asp Leu His Phe Cys Arg

20

<210> 973

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 973

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His Phe Cys Arg Ser

20

<210> 974

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 974

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10 15

His Phe Cys Arg Ser Ser

20

<210> 975

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 975

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10 15

Phe Cys Arg Ser Ser Ile

20

<210> 976

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 976

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10 15

Cys Arg Ser Ser Ile Met

20

<210> 977

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 977

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys

20

<210> 978

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 978

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

Ser Ser Ile Met Lys Pro

20

<210> 979

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 979

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10 15

Ser Ile Met Lys Pro Lys

20

<210> 980

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 980

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10 15

Ile Met Lys Pro Lys Arg

20

<210> 981

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 981

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10 15

Met Lys Pro Lys Arg Asp

20

<210> 982

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 982

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10 15

Lys Pro Lys Arg Asp Gly

20

<210> 983

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 983

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10 15

Pro Lys Arg Asp Gly Tyr

20

<210> 984

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 984

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10 15

Lys Arg Asp Gly Tyr Met

20

<210> 985

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 985

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10 15

Arg Asp Gly Tyr Met Phe

20

<210> 986

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 986

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10 15

Asp Gly Tyr Met Phe Leu

20

<210> 987

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 987

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10 15

Gly Tyr Met Phe Leu Lys

20

<210> 988

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 988

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met Phe Leu Lys Ala

20

<210> 989

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 989

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala Glu

20

<210> 990

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 990

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10 15

Phe Leu Lys Ala Glu Ser

20

<210> 991

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 991

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10 15

Leu Lys Ala Glu Ser Lys

20

<210> 992

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 992

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10 15

Lys Ala Glu Ser Lys Ile

20

<210> 993

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 993

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10 15

Ala Glu Ser Lys Ile Met

20

<210> 994

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 994

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10 15

Glu Ser Lys Ile Met Phe

20

<210> 995

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 995

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

1 5 10 15

Ser Lys Ile Met Phe Ala

20

<210> 996

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 996

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

1 5 10 15

Lys Ile Met Phe Ala Thr

20

<210> 997

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 997

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

1 5 10 15

Ile Met Phe Ala Thr Leu

20

<210> 998

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 998

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln

20

<210> 999

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 999

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

1 5 10 15

Phe Ala Thr Leu Gln Arg

20

<210> 1000

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 1000

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10 15

Ala Thr Leu Gln Arg Ser

20

<210> 1001

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 1001

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

1 5 10 15

Thr Leu Gln Arg Ser Ser

20

<210> 1002

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 1002

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

1 5 10 15

Leu Gln Arg Ser Ser Leu

20

<210> 1003

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 1003

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

1 5 10 15

Gln Arg Ser Ser Leu Trp

20

<210> 1004

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 1004

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

1 5 10 15

Arg Ser Ser Leu Trp Cys

20

<210> 1005

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 1005

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

1 5 10 15

Ser Ser Leu Trp Cys Leu

20

<210> 1006

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 1006

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

1 5 10 15

Ser Leu Trp Cys Leu Cys

20

<210> 1007

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 1007

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

1 5 10 15

Leu Trp Cys Leu Cys Ser

20

<210> 1008

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 1008

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10 15

Trp Cys Leu Cys Ser Asn

20

<210> 1009

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 1009

Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp

1 5 10 15

Cys Leu Cys Ser Asn His

20

<210> 1010

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1010

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His Phe Cys

20

<210> 1011

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1011

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10 15

Phe Asp Leu His Phe Cys Arg

20

<210> 1012

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1012

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10 15

Asp Leu His Phe Cys Arg Ser

20

<210> 1013

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1013

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His Phe Cys Arg Ser Ser

20

<210> 1014

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1014

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10 15

His Phe Cys Arg Ser Ser Ile

20

<210> 1015

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1015

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10 15

Phe Cys Arg Ser Ser Ile Met

20

<210> 1016

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1016

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10 15

Cys Arg Ser Ser Ile Met Lys

20

<210> 1017

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1017

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys Pro

20

<210> 1018

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1018

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

Ser Ser Ile Met Lys Pro Lys

20

<210> 1019

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1019

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10 15

Ser Ile Met Lys Pro Lys Arg

20

<210> 1020

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1020

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10 15

Ile Met Lys Pro Lys Arg Asp

20

<210> 1021

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1021

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10 15

Met Lys Pro Lys Arg Asp Gly

20

<210> 1022

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1022

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10 15

Lys Pro Lys Arg Asp Gly Tyr

20

<210> 1023

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1023

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10 15

Pro Lys Arg Asp Gly Tyr Met

20

<210> 1024

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1024

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10 15

Lys Arg Asp Gly Tyr Met Phe

20

<210> 1025

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1025

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10 15

Arg Asp Gly Tyr Met Phe Leu

20

<210> 1026

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1026

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10 15

Asp Gly Tyr Met Phe Leu Lys

20

<210> 1027

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1027

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10 15

Gly Tyr Met Phe Leu Lys Ala

20

<210> 1028

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1028

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met Phe Leu Lys Ala Glu

20

<210> 1029

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1029

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala Glu Ser

20

<210> 1030

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1030

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10 15

Phe Leu Lys Ala Glu Ser Lys

20

<210> 1031

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1031

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10 15

Leu Lys Ala Glu Ser Lys Ile

20

<210> 1032

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1032

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10 15

Lys Ala Glu Ser Lys Ile Met

20

<210> 1033

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1033

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10 15

Ala Glu Ser Lys Ile Met Phe

20

<210> 1034

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1034

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10 15

Glu Ser Lys Ile Met Phe Ala

20

<210> 1035

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1035

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

1 5 10 15

Ser Lys Ile Met Phe Ala Thr

20

<210> 1036

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1036

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

1 5 10 15

Lys Ile Met Phe Ala Thr Leu

20

<210> 1037

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1037

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

1 5 10 15

Ile Met Phe Ala Thr Leu Gln

20

<210> 1038

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1038

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg

20

<210> 1039

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1039

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

1 5 10 15

Phe Ala Thr Leu Gln Arg Ser

20

<210> 1040

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1040

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10 15

Ala Thr Leu Gln Arg Ser Ser

20

<210> 1041

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1041

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

1 5 10 15

Thr Leu Gln Arg Ser Ser Leu

20

<210> 1042

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1042

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

1 5 10 15

Leu Gln Arg Ser Ser Leu Trp

20

<210> 1043

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1043

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

1 5 10 15

Gln Arg Ser Ser Leu Trp Cys

20

<210> 1044

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1044

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

1 5 10 15

Arg Ser Ser Leu Trp Cys Leu

20

<210> 1045

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1045

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

1 5 10 15

Ser Ser Leu Trp Cys Leu Cys

20

<210> 1046

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1046

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

1 5 10 15

Ser Leu Trp Cys Leu Cys Ser

20

<210> 1047

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1047

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

1 5 10 15

Leu Trp Cys Leu Cys Ser Asn

20

<210> 1048

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 1048

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10 15

Trp Cys Leu Cys Ser Asn His

20

<210> 1049

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1049

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His Phe Cys Arg

20

<210> 1050

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1050

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10 15

Phe Asp Leu His Phe Cys Arg Ser

20

<210> 1051

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1051

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10 15

Asp Leu His Phe Cys Arg Ser Ser

20

<210> 1052

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1052

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His Phe Cys Arg Ser Ser Ile

20

<210> 1053

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1053

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10 15

His Phe Cys Arg Ser Ser Ile Met

20

<210> 1054

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1054

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10 15

Phe Cys Arg Ser Ser Ile Met Lys

20

<210> 1055

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1055

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10 15

Cys Arg Ser Ser Ile Met Lys Pro

20

<210> 1056

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1056

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys Pro Lys

20

<210> 1057

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1057

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

Ser Ser Ile Met Lys Pro Lys Arg

20

<210> 1058

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1058

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10 15

Ser Ile Met Lys Pro Lys Arg Asp

20

<210> 1059

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1059

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10 15

Ile Met Lys Pro Lys Arg Asp Gly

20

<210> 1060

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1060

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10 15

Met Lys Pro Lys Arg Asp Gly Tyr

20

<210> 1061

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1061

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10 15

Lys Pro Lys Arg Asp Gly Tyr Met

20

<210> 1062

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1062

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10 15

Pro Lys Arg Asp Gly Tyr Met Phe

20

<210> 1063

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1063

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10 15

Lys Arg Asp Gly Tyr Met Phe Leu

20

<210> 1064

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1064

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10 15

Arg Asp Gly Tyr Met Phe Leu Lys

20

<210> 1065

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1065

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10 15

Asp Gly Tyr Met Phe Leu Lys Ala

20

<210> 1066

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1066

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10 15

Gly Tyr Met Phe Leu Lys Ala Glu

20

<210> 1067

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1067

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met Phe Leu Lys Ala Glu Ser

20

<210> 1068

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1068

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala Glu Ser Lys

20

<210> 1069

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1069

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10 15

Phe Leu Lys Ala Glu Ser Lys Ile

20

<210> 1070

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1070

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10 15

Leu Lys Ala Glu Ser Lys Ile Met

20

<210> 1071

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1071

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10 15

Lys Ala Glu Ser Lys Ile Met Phe

20

<210> 1072

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1072

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10 15

Ala Glu Ser Lys Ile Met Phe Ala

20

<210> 1073

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1073

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10 15

Glu Ser Lys Ile Met Phe Ala Thr

20

<210> 1074

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1074

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

1 5 10 15

Ser Lys Ile Met Phe Ala Thr Leu

20

<210> 1075

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1075

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

1 5 10 15

Lys Ile Met Phe Ala Thr Leu Gln

20

<210> 1076

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1076

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

1 5 10 15

Ile Met Phe Ala Thr Leu Gln Arg

20

<210> 1077

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1077

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg Ser

20

<210> 1078

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1078

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

1 5 10 15

Phe Ala Thr Leu Gln Arg Ser Ser

20

<210> 1079

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1079

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10 15

Ala Thr Leu Gln Arg Ser Ser Leu

20

<210> 1080

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1080

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

1 5 10 15

Thr Leu Gln Arg Ser Ser Leu Trp

20

<210> 1081

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1081

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

1 5 10 15

Leu Gln Arg Ser Ser Leu Trp Cys

20

<210> 1082

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1082

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

1 5 10 15

Gln Arg Ser Ser Leu Trp Cys Leu

20

<210> 1083

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1083

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

1 5 10 15

Arg Ser Ser Leu Trp Cys Leu Cys

20

<210> 1084

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1084

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

1 5 10 15

Ser Ser Leu Trp Cys Leu Cys Ser

20

<210> 1085

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1085

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

1 5 10 15

Ser Leu Trp Cys Leu Cys Ser Asn

20

<210> 1086

<211> 24

<212> PROTEIN

<213> Homo sapiens

<400> 1086

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

1 5 10 15

Leu Trp Cys Leu Cys Ser Asn His

20

<210> 1087

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1087

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His Phe Cys Arg Ser

20 25

<210> 1088

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1088

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10 15

Phe Asp Leu His Phe Cys Arg Ser Ser

20 25

<210> 1089

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1089

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10 15

Asp Leu His Phe Cys Arg Ser Ser Ile

20 25

<210> 1090

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1090

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His Phe Cys Arg Ser Ser Ile Met

20 25

<210> 1091

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1091

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10 15

His Phe Cys Arg Ser Ser Ile Met Lys

20 25

<210> 1092

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1092

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10 15

Phe Cys Arg Ser Ser Ile Met Lys Pro

20 25

<210> 1093

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1093

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10 15

Cys Arg Ser Ser Ile Met Lys Pro Lys

20 25

<210> 1094

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1094

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys Pro Lys Arg

20 25

<210> 1095

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1095

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

Ser Ser Ile Met Lys Pro Lys Arg Asp

20 25

<210> 1096

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1096

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10 15

Ser Ile Met Lys Pro Lys Arg Asp Gly

20 25

<210> 1097

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1097

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10 15

Ile Met Lys Pro Lys Arg Asp Gly Tyr

20 25

<210> 1098

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1098

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10 15

Met Lys Pro Lys Arg Asp Gly Tyr Met

20 25

<210> 1099

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1099

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10 15

Lys Pro Lys Arg Asp Gly Tyr Met Phe

20 25

<210> 1100

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1100

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10 15

Pro Lys Arg Asp Gly Tyr Met Phe Leu

20 25

<210> 1101

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1101

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10 15

Lys Arg Asp Gly Tyr Met Phe Leu Lys

20 25

<210> 1102

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1102

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10 15

Arg Asp Gly Tyr Met Phe Leu Lys Ala

20 25

<210> 1103

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1103

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10 15

Asp Gly Tyr Met Phe Leu Lys Ala Glu

20 25

<210> 1104

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1104

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10 15

Gly Tyr Met Phe Leu Lys Ala Glu Ser

20 25

<210> 1105

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1105

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met Phe Leu Lys Ala Glu Ser Lys

20 25

<210> 1106

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1106

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala Glu Ser Lys Ile

20 25

<210> 1107

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1107

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10 15

Phe Leu Lys Ala Glu Ser Lys Ile Met

20 25

<210> 1108

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1108

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10 15

Leu Lys Ala Glu Ser Lys Ile Met Phe

20 25

<210> 1109

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1109

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10 15

Lys Ala Glu Ser Lys Ile Met Phe Ala

20 25

<210> 1110

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1110

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10 15

Ala Glu Ser Lys Ile Met Phe Ala Thr

20 25

<210> 1111

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1111

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10 15

Glu Ser Lys Ile Met Phe Ala Thr Leu

20 25

<210> 1112

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1112

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

1 5 10 15

Ser Lys Ile Met Phe Ala Thr Leu Gln

20 25

<210> 1113

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1113

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

1 5 10 15

Lys Ile Met Phe Ala Thr Leu Gln Arg

20 25

<210> 1114

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1114

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

1 5 10 15

Ile Met Phe Ala Thr Leu Gln Arg Ser

20 25

<210> 1115

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1115

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg Ser Ser

20 25

<210> 1116

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1116

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

1 5 10 15

Phe Ala Thr Leu Gln Arg Ser Ser Leu

20 25

<210> 1117

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1117

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10 15

Ala Thr Leu Gln Arg Ser Ser Leu Trp

20 25

<210> 1118

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1118

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

1 5 10 15

Thr Leu Gln Arg Ser Ser Leu Trp Cys

20 25

<210> 1119

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1119

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

1 5 10 15

Leu Gln Arg Ser Ser Leu Trp Cys Leu

20 25

<210> 1120

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1120

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

1 5 10 15

Gln Arg Ser Ser Leu Trp Cys Leu Cys

20 25

<210> 1121

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1121

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

1 5 10 15

Arg Ser Ser Leu Trp Cys Leu Cys Ser

20 25

<210> 1122

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1122

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

1 5 10 15

Ser Ser Leu Trp Cys Leu Cys Ser Asn

20 25

<210> 1123

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 1123

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

1 5 10 15

Ser Leu Trp Cys Leu Cys Ser Asn His

20 25

<210> 1124

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1124

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His Phe Cys Arg Ser Ser

20 25

<210> 1125

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1125

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10 15

Phe Asp Leu His Phe Cys Arg Ser Ser Ile

20 25

<210> 1126

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1126

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10 15

Asp Leu His Phe Cys Arg Ser Ser Ile Met

20 25

<210> 1127

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1127

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His Phe Cys Arg Ser Ser Ile Met Lys

20 25

<210> 1128

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1128

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10 15

His Phe Cys Arg Ser Ser Ile Met Lys Pro

20 25

<210> 1129

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1129

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10 15

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

20 25

<210> 1130

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1130

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10 15

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

20 25

<210> 1131

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1131

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

20 25

<210> 1132

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1132

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

20 25

<210> 1133

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1133

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10 15

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

20 25

<210> 1134

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1134

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10 15

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

20 25

<210> 1135

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1135

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10 15

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

20 25

<210> 1136

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1136

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10 15

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

20 25

<210> 1137

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1137

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10 15

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

20 25

<210> 1138

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1138

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10 15

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

20 25

<210> 1139

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1139

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10 15

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

20 25

<210> 1140

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1140

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10 15

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

20 25

<210> 1141

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1141

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10 15

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

20 25

<210> 1142

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1142

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

20 25

<210> 1143

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1143

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala Glu Ser Lys Ile Met

20 25

<210> 1144

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1144

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10 15

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

20 25

<210> 1145

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1145

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10 15

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

20 25

<210> 1146

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1146

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10 15

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

20 25

<210> 1147

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1147

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10 15

Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

20 25

<210> 1148

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1148

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10 15

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

20 25

<210> 1149

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1149

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

1 5 10 15

Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

20 25

<210> 1150

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1150

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

1 5 10 15

Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

20 25

<210> 1151

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1151

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

1 5 10 15

Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

20 25

<210> 1152

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1152

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

20 25

<210> 1153

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1153

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

1 5 10 15

Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp

20 25

<210> 1154

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1154

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10 15

Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

20 25

<210> 1155

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1155

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

1 5 10 15

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

20 25

<210> 1156

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1156

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

1 5 10 15

Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys

20 25

<210> 1157

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1157

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

1 5 10 15

Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser

20 25

<210> 1158

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1158

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

1 5 10 15

Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

20 25

<210> 1159

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 1159

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

1 5 10 15

Ser Ser Leu Trp Cys Leu Cys Ser Asn His

20 25

<210> 1160

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1160

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

20 25

<210> 1161

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1161

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10 15

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

20 25

<210> 1162

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1162

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10 15

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

20 25

<210> 1163

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1163

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

20 25

<210> 1164

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1164

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10 15

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

20 25

<210> 1165

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1165

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10 15

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

20 25

<210> 1166

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1166

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10 15

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

20 25

<210> 1167

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1167

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

20 25

<210> 1168

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1168

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

20 25

<210> 1169

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1169

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10 15

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

20 25

<210> 1170

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1170

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10 15

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

20 25

<210> 1171

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1171

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10 15

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

20 25

<210> 1172

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1172

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10 15

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

20 25

<210> 1173

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1173

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10 15

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

20 25

<210> 1174

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1174

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10 15

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

20 25

<210> 1175

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1175

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10 15

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

20 25

<210> 1176

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1176

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10 15

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

20 25

<210> 1177

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1177

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10 15

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

20 25

<210> 1178

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1178

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

20 25

<210> 1179

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1179

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

20 25

<210> 1180

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1180

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10 15

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

20 25

<210> 1181

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1181

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10 15

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

20 25

<210> 1182

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1182

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10 15

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

20 25

<210> 1183

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1183

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10 15

Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

20 25

<210> 1184

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1184

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10 15

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

20 25

<210> 1185

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1185

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

1 5 10 15

Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

20 25

<210> 1186

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1186

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

1 5 10 15

Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

20 25

<210> 1187

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1187

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

1 5 10 15

Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

20 25

<210> 1188

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1188

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp

20 25

<210> 1189

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1189

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

1 5 10 15

Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

20 25

<210> 1190

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1190

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10 15

Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

20 25

<210> 1191

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1191

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

1 5 10 15

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys

20 25

<210> 1192

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1192

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

1 5 10 15

Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser

20 25

<210> 1193

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1193

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

1 5 10 15

Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

20 25

<210> 1194

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 1194

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

1 5 10 15

Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn His

20 25

<210> 1195

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1195

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

20 25

<210> 1196

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1196

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10 15

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

20 25

<210> 1197

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1197

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10 15

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

20 25

<210> 1198

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1198

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

20 25

<210> 1199

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1199

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10 15

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

20 25

<210> 1200

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1200

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10 15

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

20 25

<210> 1201

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1201

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10 15

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

20 25

<210> 1202

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1202

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

20 25

<210> 1203

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1203

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

20 25

<210> 1204

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1204

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10 15

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

20 25

<210> 1205

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1205

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10 15

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

20 25

<210> 1206

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1206

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10 15

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

20 25

<210> 1207

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1207

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10 15

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

20 25

<210> 1208

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1208

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10 15

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

20 25

<210> 1209

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1209

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10 15

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

20 25

<210> 1210

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1210

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10 15

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

20 25

<210> 1211

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1211

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10 15

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

20 25

<210> 1212

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1212

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10 15

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

20 25

<210> 1213

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1213

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

20 25

<210> 1214

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1214

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

20 25

<210> 1215

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1215

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10 15

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

20 25

<210> 1216

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1216

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10 15

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

20 25

<210> 1217

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1217

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10 15

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

20 25

<210> 1218

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1218

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10 15

Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

20 25

<210> 1219

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1219

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10 15

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

20 25

<210> 1220

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1220

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

1 5 10 15

Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

20 25

<210> 1221

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1221

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

1 5 10 15

Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

20 25

<210> 1222

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1222

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

1 5 10 15

Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp

20 25

<210> 1223

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1223

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

20 25

<210> 1224

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1224

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

1 5 10 15

Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

20 25

<210> 1225

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1225

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10 15

Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys

20 25

<210> 1226

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1226

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

1 5 10 15

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser

20 25

<210> 1227

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1227

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

1 5 10 15

Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

20 25

<210> 1228

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 1228

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

1 5 10 15

Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn His

20 25

<210> 1229

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1229

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

20 25

<210> 1230

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1230

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10 15

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

20 25

<210> 1231

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1231

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10 15

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

20 25

<210> 1232

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1232

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

20 25

<210> 1233

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1233

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10 15

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

20 25

<210> 1234

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1234

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10 15

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

20 25

<210> 1235

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1235

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10 15

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

20 25

<210> 1236

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1236

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

20 25

<210> 1237

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1237

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

20 25

<210> 1238

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1238

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10 15

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

20 25

<210> 1239

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1239

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10 15

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

20 25

<210> 1240

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1240

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10 15

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

20 25

<210> 1241

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1241

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10 15

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

20 25

<210> 1242

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1242

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10 15

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

20 25

<210> 1243

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1243

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10 15

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

20 25

<210> 1244

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1244

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10 15

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

20 25

<210> 1245

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1245

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10 15

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

20 25

<210> 1246

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1246

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10 15

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

20 25

<210> 1247

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1247

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

20 25

<210> 1248

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1248

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

20 25

<210> 1249

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1249

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10 15

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

20 25

<210> 1250

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1250

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10 15

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

20 25

<210> 1251

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1251

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10 15

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

20 25

<210> 1252

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1252

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10 15

Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

20 25

<210> 1253

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1253

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10 15

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

20 25

<210> 1254

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1254

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

1 5 10 15

Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

20 25

<210> 1255

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1255

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

1 5 10 15

Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp

20 25

<210> 1256

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1256

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

1 5 10 15

Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

20 25

<210> 1257

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1257

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

20 25

<210> 1258

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1258

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

1 5 10 15

Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys

20 25

<210> 1259

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1259

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10 15

Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser

20 25

<210> 1260

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1260

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

1 5 10 15

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

20 25

<210> 1261

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 1261

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

1 5 10 15

Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn His

20 25

<210> 1262

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1262

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

20 25 30

<210> 1263

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1263

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10 15

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

20 25 30

<210> 1264

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1264

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10 15

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

20 25 30

<210> 1265

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1265

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

20 25 30

<210> 1266

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1266

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10 15

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

20 25 30

<210> 1267

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1267

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10 15

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

20 25 30

<210> 1268

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1268

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10 15

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

20 25 30

<210> 1269

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1269

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

20 25 30

<210> 1270

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1270

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

20 25 30

<210> 1271

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1271

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10 15

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

20 25 30

<210> 1272

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1272

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10 15

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

20 25 30

<210> 1273

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1273

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10 15

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

20 25 30

<210> 1274

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1274

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10 15

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

20 25 30

<210> 1275

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1275

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10 15

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

20 25 30

<210> 1276

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1276

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10 15

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

20 25 30

<210> 1277

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1277

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10 15

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

20 25 30

<210> 1278

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1278

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10 15

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

20 25 30

<210> 1279

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1279

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10 15

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

20 25 30

<210> 1280

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1280

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

20 25 30

<210> 1281

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1281

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

20 25 30

<210> 1282

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1282

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10 15

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

20 25 30

<210> 1283

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1283

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10 15

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

20 25 30

<210> 1284

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1284

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10 15

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

20 25 30

<210> 1285

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1285

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10 15

Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

20 25 30

<210> 1286

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1286

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10 15

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

20 25 30

<210> 1287

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1287

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

1 5 10 15

Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp

20 25 30

<210> 1288

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1288

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

1 5 10 15

Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

20 25 30

<210> 1289

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1289

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

1 5 10 15

Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

20 25 30

<210> 1290

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1290

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys

20 25 30

<210> 1291

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1291

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

1 5 10 15

Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser

20 25 30

<210> 1292

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1292

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10 15

Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

20 25 30

<210> 1293

<211> 30

<212> PROTEIN

<213> Homo sapiens

<400> 1293

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

1 5 10 15

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn His

20 25 30

<210> 1294

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1294

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

20 25 30

<210> 1295

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1295

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10 15

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

20 25 30

<210> 1296

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1296

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10 15

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

20 25 30

<210> 1297

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1297

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

20 25 30

<210> 1298

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1298

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10 15

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

20 25 30

<210> 1299

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1299

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10 15

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

20 25 30

<210> 1300

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1300

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10 15

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

20 25 30

<210> 1301

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1301

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

20 25 30

<210> 1302

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1302

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

20 25 30

<210> 1303

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1303

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10 15

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

20 25 30

<210> 1304

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1304

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10 15

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

20 25 30

<210> 1305

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1305

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10 15

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

20 25 30

<210> 1306

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1306

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10 15

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

20 25 30

<210> 1307

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1307

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10 15

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

20 25 30

<210> 1308

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1308

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10 15

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

20 25 30

<210> 1309

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1309

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10 15

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

20 25 30

<210> 1310

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1310

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10 15

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

20 25 30

<210> 1311

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1311

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10 15

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

20 25 30

<210> 1312

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1312

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

20 25 30

<210> 1313

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1313

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

20 25 30

<210> 1314

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1314

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10 15

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

20 25 30

<210> 1315

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1315

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10 15

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

20 25 30

<210> 1316

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1316

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10 15

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

20 25 30

<210> 1317

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1317

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10 15

Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

20 25 30

<210> 1318

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1318

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10 15

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp

20 25 30

<210> 1319

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1319

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

1 5 10 15

Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

20 25 30

<210> 1320

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1320

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

1 5 10 15

Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

20 25 30

<210> 1321

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1321

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

1 5 10 15

Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys

20 25 30

<210> 1322

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1322

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser

20 25 30

<210> 1323

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1323

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

1 5 10 15

Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

20 25 30

<210> 1324

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 1324

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10 15

Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn His

20 25 30

<210> 1325

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1325

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

20 25 30

<210> 1326

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1326

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10 15

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

20 25 30

<210> 1327

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1327

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10 15

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

20 25 30

<210> 1328

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1328

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

20 25 30

<210> 1329

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1329

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10 15

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

20 25 30

<210> 1330

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1330

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10 15

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

20 25 30

<210> 1331

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1331

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10 15

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

20 25 30

<210> 1332

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1332

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

20 25 30

<210> 1333

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1333

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

20 25 30

<210> 1334

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1334

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10 15

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

20 25 30

<210> 1335

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1335

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10 15

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

20 25 30

<210> 1336

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1336

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10 15

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

20 25 30

<210> 1337

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1337

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10 15

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

20 25 30

<210> 1338

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1338

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10 15

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

20 25 30

<210> 1339

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1339

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10 15

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

20 25 30

<210> 1340

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1340

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10 15

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

20 25 30

<210> 1341

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1341

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10 15

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

20 25 30

<210> 1342

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1342

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10 15

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

20 25 30

<210> 1343

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1343

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

20 25 30

<210> 1344

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1344

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

20 25 30

<210> 1345

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1345

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10 15

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

20 25 30

<210> 1346

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1346

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10 15

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

20 25 30

<210> 1347

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1347

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10 15

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

20 25 30

<210> 1348

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1348

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10 15

Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp

20 25 30

<210> 1349

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1349

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10 15

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

20 25 30

<210> 1350

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1350

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

1 5 10 15

Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

20 25 30

<210> 1351

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1351

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

1 5 10 15

Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys

20 25 30

<210> 1352

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1352

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

1 5 10 15

Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser

20 25 30

<210> 1353

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1353

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

20 25 30

<210> 1354

<211> 32

<212> PROTEIN

<213> Homo sapiens

<400> 1354

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

1 5 10 15

Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn His

20 25 30

<210> 1355

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1355

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

20 25 30

Asp

<210> 1356

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1356

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10 15

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

20 25 30

Gly

<210> 1357

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1357

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10 15

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

20 25 30

Tyr

<210> 1358

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1358

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

20 25 30

Met

<210> 1359

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1359

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10 15

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

20 25 30

Phe

<210> 1360

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1360

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10 15

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

20 25 30

Leu

<210> 1361

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1361

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10 15

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

20 25 30

Lys

<210> 1362

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1362

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

20 25 30

Ala

<210> 1363

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1363

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

20 25 30

Glu

<210> 1364

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1364

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10 15

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

20 25 30

Ser

<210> 1365

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1365

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10 15

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

20 25 30

Lys

<210> 1366

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1366

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10 15

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

20 25 30

Ile

<210> 1367

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1367

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10 15

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

20 25 30

Met

<210> 1368

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1368

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10 15

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

20 25 30

Phe

<210> 1369

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1369

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10 15

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

20 25 30

Ala

<210> 1370

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1370

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10 15

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

20 25 30

Thr

<210> 1371

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1371

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10 15

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

20 25 30

Leu

<210> 1372

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1372

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10 15

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

20 25 30

Gln

<210> 1373

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1373

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

20 25 30

Arg

<210> 1374

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1374

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

20 25 30

Ser

<210> 1375

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1375

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10 15

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

20 25 30

Ser

<210> 1376

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1376

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10 15

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

20 25 30

Leu

<210> 1377

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1377

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10 15

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

20 25 30

Trp

<210> 1378

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1378

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10 15

Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp

20 25 30

Cys

<210> 1379

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1379

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10 15

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

20 25 30

Leu

<210> 1380

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1380

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

1 5 10 15

Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

20 25 30

Cys

<210> 1381

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1381

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

1 5 10 15

Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys

20 25 30

Ser

<210> 1382

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1382

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

1 5 10 15

Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser

20 25 30

Asn

<210> 1383

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 1383

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

20 25 30

His

<210> 1384

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1384

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

20 25 30

Asp Gly

<210> 1385

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1385

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10 15

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

20 25 30

Gly Tyr

<210> 1386

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1386

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10 15

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

20 25 30

Tyr Met

<210> 1387

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1387

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

20 25 30

Met Phe

<210> 1388

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1388

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10 15

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

20 25 30

Phe Leu

<210> 1389

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1389

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10 15

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

20 25 30

Leu Lys

<210> 1390

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1390

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10 15

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

20 25 30

Lys Ala

<210> 1391

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1391

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

20 25 30

Ala Glu

<210> 1392

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1392

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

20 25 30

Glu Ser

<210> 1393

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1393

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10 15

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

20 25 30

Ser Lys

<210> 1394

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1394

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10 15

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

20 25 30

Lys Ile

<210> 1395

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1395

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10 15

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

20 25 30

Ile Met

<210> 1396

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1396

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10 15

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

20 25 30

Met Phe

<210> 1397

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1397

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10 15

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

20 25 30

Phe Ala

<210> 1398

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1398

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10 15

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

20 25 30

Ala Thr

<210> 1399

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1399

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10 15

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

20 25 30

Thr Leu

<210> 1400

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1400

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10 15

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

20 25 30

Leu Gln

<210> 1401

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1401

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10 15

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

20 25 30

Gln Arg

<210> 1402

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1402

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

20 25 30

Arg Ser

<210> 1403

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1403

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

20 25 30

Ser Ser

<210> 1404

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1404

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10 15

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

20 25 30

Ser Leu

<210> 1405

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1405

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10 15

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

20 25 30

Leu Trp

<210> 1406

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1406

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10 15

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

20 25 30

Trp Cys

<210> 1407

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1407

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10 15

Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp

20 25 30

Cys Leu

<210> 1408

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1408

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10 15

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

20 25 30

Leu Cys

<210> 1409

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1409

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

1 5 10 15

Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

20 25 30

Cys Ser

<210> 1410

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1410

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

1 5 10 15

Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys

20 25 30

Ser Asn

<210> 1411

<211> 34

<212> PROTEIN

<213> Homo sapiens

<400> 1411

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

1 5 10 15

Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser

20 25 30

Asn His

<210> 1412

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1412

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

20 25 30

Asp Gly Tyr

35

<210> 1413

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1413

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10 15

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

20 25 30

Gly Tyr Met

35

<210> 1414

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1414

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10 15

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

20 25 30

Tyr Met Phe

35

<210> 1415

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1415

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

20 25 30

Met Phe Leu

35

<210> 1416

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1416

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10 15

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

20 25 30

Phe Leu Lys

35

<210> 1417

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1417

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10 15

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

20 25 30

Leu Lys Ala

35

<210> 1418

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1418

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10 15

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

20 25 30

Lys Ala Glu

35

<210> 1419

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1419

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

20 25 30

Ala Glu Ser

35

<210> 1420

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1420

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

20 25 30

Glu Ser Lys

35

<210> 1421

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1421

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10 15

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

20 25 30

Ser Lys Ile

35

<210> 1422

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1422

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10 15

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

20 25 30

Lys Ile Met

35

<210> 1423

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1423

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10 15

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

20 25 30

Ile Met Phe

35

<210> 1424

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1424

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10 15

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

20 25 30

Met Phe Ala

35

<210> 1425

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1425

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10 15

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

20 25 30

Phe Ala Thr

35

<210> 1426

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1426

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10 15

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

20 25 30

Ala Thr Leu

35

<210> 1427

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1427

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10 15

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

20 25 30

Thr Leu Gln

35

<210> 1428

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1428

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10 15

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

20 25 30

Leu Gln Arg

35

<210> 1429

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1429

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10 15

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

20 25 30

Gln Arg Ser

35

<210> 1430

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1430

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

20 25 30

Arg Ser Ser

35

<210> 1431

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1431

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

20 25 30

Ser Ser Leu

35

<210> 1432

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1432

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10 15

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

20 25 30

Ser Leu Trp

35

<210> 1433

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1433

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10 15

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

20 25 30

Leu Trp Cys

35

<210> 1434

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1434

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10 15

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

20 25 30

Trp CysLeu

35

<210> 1435

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1435

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10 15

Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp

20 25 30

Cys Leu Cys

35

<210> 1436

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1436

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10 15

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

20 25 30

Leu Cys Ser

35

<210> 1437

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1437

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

1 5 10 15

Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

20 25 30

Cys Ser Asn

35

<210> 1438

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1438

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

1 5 10 15

Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys

20 25 30

Ser Asn His

35

<210> 1439

<211> 36

<212> PROTEIN

<213> Homo sapiens

<400> 1439

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

20 25 30

Asp Gly Tyr Met

35

<210> 1440

<211> 36

<212> PROTEIN

<213> Homo sapiens

<400> 1440

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10 15

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

20 25 30

Gly Tyr Met Phe

35

<210> 1441

<211> 36

<212> PROTEIN

<213> Homo sapiens

<400> 1441

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10 15

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

20 25 30

Tyr Met Phe Leu

35

<210> 1442

<211> 36

<212> PROTEIN

<213> Homo sapiens

<400> 1442

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

20 25 30

Met Phe Leu Lys

35

<210> 1443

<211> 36

<212> PROTEIN

<213> Homo sapiens

<400> 1443

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10 15

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

20 25 30

Phe Leu Lys Ala

35

<210> 1444

<211> 36

<212> PROTEIN

<213> Homo sapiens

<400> 1444

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10 15

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

20 25 30

Leu Lys Ala Glu

35

<210> 1445

<211> 36

<212> PROTEIN

<213> Homo sapiens

<400> 1445

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10 15

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

20 25 30

Lys Ala Glu Ser

35

<210> 1446

<211> 36

<212> PROTEIN

<213> Homo sapiens

<400> 1446

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

20 25 30

Ala Glu Ser Lys

35

<210> 1447

<211> 36

<212> PROTEIN

<213> Homo sapiens

<400> 1447

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

20 25 30

Glu Ser Lys Ile

35

<210> 1448

<211> 36

<212> PROTEIN

<213> Homo sapiens

<400> 1448

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10 15

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

20 25 30

Ser Lys Ile Met

35

<210> 1449

<211> 36

<212> PROTEIN

<213> Homo sapiens

<400> 1449

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10 15

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

20 25 30

Lys Ile Met Phe

35

<210> 1450

<211> 36

<212> PROTEIN

<213> Homo sapiens

<400> 1450

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10 15

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

20 25 30

Ile Met Phe Ala

35

<210> 1451

<211> 36

<212> PROTEIN

<213> Homo sapiens

<400> 1451

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10 15

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

20 25 30

Met Phe Ala Thr

35

<210> 1452

<211> 36

<212> PROTEIN

<213> Homo sapiens

<400> 1452

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10 15

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

20 25 30

Phe Ala Thr Leu

35

<210> 1453

<211> 36

<212> PROTEIN

<213> Homo sapiens

<400> 1453

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10 15

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

20 25 30

Ala Thr Leu Gln

35

<210> 1454

<211> 36

<212> PROTEIN

<213> Homo sapiens

<400> 1454

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10 15

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

20 25 30

Thr Leu Gln Arg

35

<210> 1455

<211> 36

<212> PROTEIN

<213> Homo sapiens

<400> 1455

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10 15

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

20 25 30

Leu Gln Arg Ser

35

<210> 1456

<211> 36

<212> PROTEIN

<213> Homo sapiens

<400> 1456

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10 15

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

20 25 30

Gln Arg Ser Ser

35

<210> 1457

<211> 36

<212> PROTEIN

<213> Homo sapiens

<400> 1457

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

20 25 30

Arg Ser Ser Leu

35

<210> 1458

<211> 36

<212> PROTEIN

<213> Homo sapiens

<400> 1458

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

20 25 30

Ser Ser Leu Trp

35

<210> 1459

<211> 36

<212> PROTEIN

<213> Homo sapiens

<400> 1459

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10 15

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

20 25 30

Ser Leu Trp Cys

35

<210> 1460

<211> 36

<212> PROTEIN

<213> Homo sapiens

<400> 1460

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10 15

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

20 25 30

Leu Trp Cys Leu

35

<210> 1461

<211> 36

<212> PROTEIN

<213> Homo sapiens

<400> 1461

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10 15

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

20 25 30

Trp Cys Leu Cys

35

<210> 1462

<211> 36

<212> PROTEIN

<213> Homo sapiens

<400> 1462

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10 15

Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp

20 25 30

Cys Leu Cys Ser

35

<210> 1463

<211> 36

<212> PROTEIN

<213> Homo sapiens

<400> 1463

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10 15

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

20 25 30

Leu Cys Ser Asn

35

<210> 1464

<211> 36

<212> PROTEIN

<213> Homo sapiens

<400> 1464

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

1 5 10 15

Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

20 25 30

Cys Ser Asn His

35

<210> 1465

<211> 37

<212> PROTEIN

<213> Homo sapiens

<400> 1465

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

20 25 30

Asp Gly Tyr Met Phe

35

<210> 1466

<211> 37

<212> PROTEIN

<213> Homo sapiens

<400> 1466

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10 15

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

20 25 30

Gly Tyr Met Phe Leu

35

<210> 1467

<211> 37

<212> PROTEIN

<213> Homo sapiens

<400> 1467

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10 15

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

20 25 30

Tyr Met Phe Leu Lys

35

<210> 1468

<211> 37

<212> PROTEIN

<213> Homo sapiens

<400> 1468

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

20 25 30

Met Phe Leu Lys Ala

35

<210> 1469

<211> 37

<212> PROTEIN

<213> Homo sapiens

<400> 1469

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10 15

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

20 25 30

Phe Leu Lys Ala Glu

35

<210> 1470

<211> 37

<212> PROTEIN

<213> Homo sapiens

<400> 1470

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10 15

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

20 25 30

Leu Lys Ala Glu Ser

35

<210> 1471

<211> 37

<212> PROTEIN

<213> Homo sapiens

<400> 1471

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10 15

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

20 25 30

Lys Ala Glu Ser Lys

35

<210> 1472

<211> 37

<212> PROTEIN

<213> Homo sapiens

<400> 1472

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

20 25 30

Ala Glu Ser Lys Ile

35

<210> 1473

<211> 37

<212> PROTEIN

<213> Homo sapiens

<400> 1473

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

20 25 30

Glu Ser Lys Ile Met

35

<210> 1474

<211> 37

<212> PROTEIN

<213> Homo sapiens

<400> 1474

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10 15

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

20 25 30

Ser Lys Ile Met Phe

35

<210> 1475

<211> 37

<212> PROTEIN

<213> Homo sapiens

<400> 1475

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10 15

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

20 25 30

Lys Ile Met Phe Ala

35

<210> 1476

<211> 37

<212> PROTEIN

<213> Homo sapiens

<400> 1476

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10 15

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

20 25 30

Ile Met Phe Ala Thr

35

<210> 1477

<211> 37

<212> PROTEIN

<213> Homo sapiens

<400> 1477

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10 15

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

20 25 30

Met Phe Ala Thr Leu

35

<210> 1478

<211> 37

<212> PROTEIN

<213> Homo sapiens

<400> 1478

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10 15

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

20 25 30

Phe Ala Thr Leu Gln

35

<210> 1479

<211> 37

<212> PROTEIN

<213> Homo sapiens

<400> 1479

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10 15

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

20 25 30

Ala Thr Leu Gln Arg

35

<210> 1480

<211> 37

<212> PROTEIN

<213> Homo sapiens

<400> 1480

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10 15

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

20 25 30

Thr Leu Gln Arg Ser

35

<210> 1481

<211> 37

<212> PROTEIN

<213> Homo sapiens

<400> 1481

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10 15

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

20 25 30

Leu Gln Arg Ser Ser

35

<210> 1482

<211> 37

<212> PROTEIN

<213> Homo sapiens

<400> 1482

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10 15

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

20 25 30

Gln Arg Ser Ser Leu

35

<210> 1483

<211> 37

<212> PROTEIN

<213> Homo sapiens

<400> 1483

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

20 25 30

Arg Ser Ser Leu Trp

35

<210> 1484

<211> 37

<212> PROTEIN

<213> Homo sapiens

<400> 1484

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

20 25 30

Ser Ser Leu Trp Cys

35

<210> 1485

<211> 37

<212> PROTEIN

<213> Homo sapiens

<400> 1485

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10 15

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

20 25 30

Ser Leu Trp Cys Leu

35

<210> 1486

<211> 37

<212> PROTEIN

<213> Homo sapiens

<400> 1486

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10 15

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

20 25 30

Leu Trp Cys Leu Cys

35

<210> 1487

<211> 37

<212> PROTEIN

<213> Homo sapiens

<400> 1487

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10 15

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

20 25 30

Trp Cys Leu Cys Ser

35

<210> 1488

<211> 37

<212> PROTEIN

<213> Homo sapiens

<400> 1488

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10 15

Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp

20 25 30

Cys Leu Cys Ser Asn

35

<210> 1489

<211> 37

<212> PROTEIN

<213> Homo sapiens

<400> 1489

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10 15

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

20 25 30

Leu Cys Ser Asn His

35

<210> 1490

<211> 38

<212> PROTEIN

<213> Homo sapiens

<400> 1490

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

20 25 30

Asp Gly Tyr Met Phe Leu

35

<210> 1491

<211> 38

<212> PROTEIN

<213> Homo sapiens

<400> 1491

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10 15

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

20 25 30

Gly Tyr Met Phe Leu Lys

35

<210> 1492

<211> 38

<212> PROTEIN

<213> Homo sapiens

<400> 1492

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10 15

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

20 25 30

Tyr Met Phe Leu Lys Ala

35

<210> 1493

<211> 38

<212> PROTEIN

<213> Homo sapiens

<400> 1493

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

20 25 30

Met Phe Leu Lys Ala Glu

35

<210> 1494

<211> 38

<212> PROTEIN

<213> Homo sapiens

<400> 1494

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10 15

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

20 25 30

Phe Leu Lys Ala Glu Ser

35

<210> 1495

<211> 38

<212> PROTEIN

<213> Homo sapiens

<400> 1495

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10 15

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

20 25 30

Leu Lys Ala Glu Ser Lys

35

<210> 1496

<211> 38

<212> PROTEIN

<213> Homo sapiens

<400> 1496

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10 15

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

20 25 30

Lys Ala Glu Ser Lys Ile

35

<210> 1497

<211> 38

<212> PROTEIN

<213> Homo sapiens

<400> 1497

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

20 25 30

Ala Glu Ser Lys Ile Met

35

<210> 1498

<211> 38

<212> PROTEIN

<213> Homo sapiens

<400> 1498

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

20 25 30

Glu Ser Lys Ile Met Phe

35

<210> 1499

<211> 38

<212> PROTEIN

<213> Homo sapiens

<400> 1499

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10 15

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

20 25 30

Ser Lys Ile Met Phe Ala

35

<210> 1500

<211> 38

<212> PROTEIN

<213> Homo sapiens

<400> 1500

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10 15

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

20 25 30

Lys Ile Met Phe Ala Thr

35

<210> 1501

<211> 38

<212> PROTEIN

<213> Homo sapiens

<400> 1501

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10 15

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

20 25 30

Ile Met Phe Ala Thr Leu

35

<210> 1502

<211> 38

<212> PROTEIN

<213> Homo sapiens

<400> 1502

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10 15

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

20 25 30

Met Phe Ala Thr Leu Gln

35

<210> 1503

<211> 38

<212> PROTEIN

<213> Homo sapiens

<400> 1503

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10 15

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

20 25 30

Phe Ala Thr Leu Gln Arg

35

<210> 1504

<211> 38

<212> PROTEIN

<213> Homo sapiens

<400> 1504

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10 15

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

20 25 30

Ala Thr Leu Gln Arg Ser

35

<210> 1505

<211> 38

<212> PROTEIN

<213> Homo sapiens

<400> 1505

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10 15

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

20 25 30

Thr Leu Gln Arg Ser Ser

35

<210> 1506

<211> 38

<212> PROTEIN

<213> Homo sapiens

<400> 1506

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10 15

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

20 25 30

Leu Gln Arg Ser Ser Leu

35

<210> 1507

<211> 38

<212> PROTEIN

<213> Homo sapiens

<400> 1507

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10 15

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

20 25 30

Gln Arg Ser Ser Leu Trp

35

<210> 1508

<211> 38

<212> PROTEIN

<213> Homo sapiens

<400> 1508

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

20 25 30

Arg Ser Ser Leu Trp Cys

35

<210> 1509

<211> 38

<212> PROTEIN

<213> Homo sapiens

<400> 1509

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

20 25 30

Ser Ser Leu Trp Cys Leu

35

<210> 1510

<211> 38

<212> PROTEIN

<213> Homo sapiens

<400> 1510

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10 15

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

20 25 30

Ser Leu Trp Cys Leu Cys

35

<210> 1511

<211> 38

<212> PROTEIN

<213> Homo sapiens

<400> 1511

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10 15

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

20 25 30

Leu Trp Cys Leu Cys Ser

35

<210> 1512

<211> 38

<212> PROTEIN

<213> Homo sapiens

<400> 1512

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10 15

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

20 25 30

Trp Cys Leu Cys Ser Asn

35

<210> 1513

<211> 38

<212> PROTEIN

<213> Homo sapiens

<400> 1513

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

1 5 10 15

Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp

20 25 30

Cys Leu Cys Ser Asn His

35

<210> 1514

<211> 39

<212> PROTEIN

<213> Homo sapiens

<400> 1514

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

20 25 30

Asp Gly Tyr Met Phe Leu Lys

35

<210> 1515

<211> 39

<212> PROTEIN

<213> Homo sapiens

<400> 1515

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10 15

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

20 25 30

Gly Tyr Met Phe Leu Lys Ala

35

<210> 1516

<211> 39

<212> PROTEIN

<213> Homo sapiens

<400> 1516

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10 15

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

20 25 30

Tyr Met Phe Leu Lys Ala Glu

35

<210> 1517

<211> 39

<212> PROTEIN

<213> Homo sapiens

<400> 1517

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

20 25 30

Met Phe Leu Lys Ala Glu Ser

35

<210> 1518

<211> 39

<212> PROTEIN

<213> Homo sapiens

<400> 1518

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10 15

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

20 25 30

Phe Leu Lys Ala Glu Ser Lys

35

<210> 1519

<211> 39

<212> PROTEIN

<213> Homo sapiens

<400> 1519

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10 15

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

20 25 30

Leu Lys Ala Glu Ser Lys Ile

35

<210> 1520

<211> 39

<212> PROTEIN

<213> Homo sapiens

<400> 1520

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10 15

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

20 25 30

Lys Ala Glu Ser Lys Ile Met

35

<210> 1521

<211> 39

<212> PROTEIN

<213> Homo sapiens

<400> 1521

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

20 25 30

Ala Glu Ser Lys Ile Met Phe

35

<210> 1522

<211> 39

<212> PROTEIN

<213> Homo sapiens

<400> 1522

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

20 25 30

Glu Ser Lys Ile Met Phe Ala

35

<210> 1523

<211> 39

<212> PROTEIN

<213> Homo sapiens

<400> 1523

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10 15

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

20 25 30

Ser Lys Ile Met Phe Ala Thr

35

<210> 1524

<211> 39

<212> PROTEIN

<213> Homo sapiens

<400> 1524

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10 15

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

20 25 30

Lys Ile Met Phe Ala Thr Leu

35

<210> 1525

<211> 39

<212> PROTEIN

<213> Homo sapiens

<400> 1525

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10 15

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

20 25 30

Ile Met Phe Ala Thr Leu Gln

35

<210> 1526

<211> 39

<212> PROTEIN

<213> Homo sapiens

<400> 1526

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10 15

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

20 25 30

Met Phe Ala Thr Leu Gln Arg

35

<210> 1527

<211> 39

<212> PROTEIN

<213> Homo sapiens

<400> 1527

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10 15

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

20 25 30

Phe Ala Thr Leu Gln Arg Ser

35

<210> 1528

<211> 39

<212> PROTEIN

<213> Homo sapiens

<400> 1528

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10 15

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

20 25 30

Ala Thr Leu Gln Arg Ser Ser

35

<210> 1529

<211> 39

<212> PROTEIN

<213> Homo sapiens

<400> 1529

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10 15

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

20 25 30

Thr Leu Gln Arg Ser Ser Leu

35

<210> 1530

<211> 39

<212> PROTEIN

<213> Homo sapiens

<400> 1530

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10 15

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

20 25 30

Leu Gln Arg Ser Ser Leu Trp

35

<210> 1531

<211> 39

<212> PROTEIN

<213> Homo sapiens

<400> 1531

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10 15

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

20 25 30

Gln Arg Ser Ser Leu Trp Cys

35

<210> 1532

<211> 39

<212> PROTEIN

<213> Homo sapiens

<400> 1532

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

20 25 30

Arg Ser Ser Leu Trp Cys Leu

35

<210> 1533

<211> 39

<212> PROTEIN

<213> Homo sapiens

<400> 1533

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

20 25 30

Ser Ser Leu Trp Cys Leu Cys

35

<210> 1534

<211> 39

<212> PROTEIN

<213> Homo sapiens

<400> 1534

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10 15

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

20 25 30

Ser Leu Trp Cys Leu Cys Ser

35

<210> 1535

<211> 39

<212> PROTEIN

<213> Homo sapiens

<400> 1535

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10 15

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

20 25 30

Leu Trp Cys Leu Cys Ser Asn

35

<210> 1536

<211> 39

<212> PROTEIN

<213> Homo sapiens

<400> 1536

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10 15

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

20 25 30

Trp Cys Leu Cys Ser Asn His

35

<210> 1537

<211> 40

<212> PROTEIN

<213> Homo sapiens

<400> 1537

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

20 25 30

Asp Gly Tyr Met Phe Leu Lys Ala

35 40

<210> 1538

<211> 40

<212> PROTEIN

<213> Homo sapiens

<400> 1538

Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro

1 5 10 15

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

20 25 30

Gly Tyr Met Phe Leu Lys Ala Glu

35 40

<210> 1539

<211> 40

<212> PROTEIN

<213> Homo sapiens

<400> 1539

Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe

1 5 10 15

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

20 25 30

Tyr Met Phe Leu Lys Ala Glu Ser

35 40

<210> 1540

<211> 40

<212> PROTEIN

<213> Homo sapiens

<400> 1540

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

20 25 30

Met Phe Leu Lys Ala Glu Ser Lys

35 40

<210> 1541

<211> 40

<212> PROTEIN

<213> Homo sapiens

<400> 1541

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

1 5 10 15

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

20 25 30

Phe Leu Lys Ala Glu Ser Lys Ile

35 40

<210> 1542

<211> 40

<212> PROTEIN

<213> Homo sapiens

<400> 1542

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

1 5 10 15

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

20 25 30

Leu Lys Ala Glu Ser Lys Ile Met

35 40

<210> 1543

<211> 40

<212> PROTEIN

<213> Homo sapiens

<400> 1543

Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10 15

Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

20 25 30

Lys Ala Glu Ser Lys Ile Met Phe

35 40

<210> 1544

<211> 40

<212> PROTEIN

<213> Homo sapiens

<400> 1544

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys

20 25 30

Ala Glu Ser Lys Ile Met Phe Ala

35 40

<210> 1545

<211> 40

<212> PROTEIN

<213> Homo sapiens

<400> 1545

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

20 25 30

Glu Ser Lys Ile Met Phe Ala Thr

35 40

<210> 1546

<211> 40

<212> PROTEIN

<213> Homo sapiens

<400> 1546

Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser

1 5 10 15

Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu

20 25 30

Ser Lys Ile Met Phe Ala Thr Leu

35 40

<210> 1547

<211> 40

<212> PROTEIN

<213> Homo sapiens

<400> 1547

Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser

1 5 10 15

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser

20 25 30

Lys Ile Met Phe Ala Thr Leu Gln

35 40

<210> 1548

<211> 40

<212> PROTEIN

<213> Homo sapiens

<400> 1548

Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile

1 5 10 15

Met Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys

20 25 30

Ile Met Phe Ala Thr Leu Gln Arg

35 40

<210> 1549

<211> 40

<212> PROTEIN

<213> Homo sapiens

<400> 1549

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10 15

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

20 25 30

Met Phe Ala Thr Leu Gln Arg Ser

35 40

<210> 1550

<211> 40

<212> PROTEIN

<213> Homo sapiens

<400> 1550

Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys

1 5 10 15

Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met

20 25 30

Phe Ala Thr Leu Gln Arg Ser Ser

35 40

<210> 1551

<211> 40

<212> PROTEIN

<213> Homo sapiens

<400> 1551

Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro

1 5 10 15

Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

20 25 30

Ala Thr Leu Gln Arg Ser Ser Leu

35 40

<210> 1552

<211> 40

<212> PROTEIN

<213> Homo sapiens

<400> 1552

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

1 5 10 15

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

20 25 30

Thr Leu Gln Arg Ser Ser Leu Trp

35 40

<210> 1553

<211> 40

<212> PROTEIN

<213> Homo sapiens

<400> 1553

Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg

1 5 10 15

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

20 25 30

Leu Gln Arg Ser Ser Leu Trp Cys

35 40

<210> 1554

<211> 40

<212> PROTEIN

<213> Homo sapiens

<400> 1554

Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

1 5 10 15

Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu

20 25 30

Gln Arg Ser Ser Leu Trp Cys Leu

35 40

<210> 1555

<211> 40

<212> PROTEIN

<213> Homo sapiens

<400> 1555

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

20 25 30

Arg Ser Ser Leu Trp Cys Leu Cys

35 40

<210> 1556

<211> 40

<212> PROTEIN

<213> Homo sapiens

<400> 1556

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

20 25 30

Ser Ser Leu Trp Cys Leu Cys Ser

35 40

<210> 1557

<211> 40

<212> PROTEIN

<213> Homo sapiens

<400> 1557

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10 15

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

20 25 30

Ser Leu Trp Cys Leu Cys Ser Asn

35 40

<210> 1558

<211> 40

<212> PROTEIN

<213> Homo sapiens

<400> 1558

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

1 5 10 15

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

20 25 30

Leu Trp Cys Leu Cys Ser Asn His

35 40

<210> 1559

<211> 48

<212> PROTEIN

<213> Homo sapiens

<400> 1559

Ala Gln Ala Lys Ala Val Cys Ser Gln Glu Ser Arg Asp Val Leu Cys

1 5 10 15

Glu Leu Ser Asp His His Asn His Thr Leu Glu Glu Glu Cys Gln Trp

20 25 30

Gly Pro Cys Leu Gln Cys Leu Trp Ala Leu Leu Gln Ala Ser Gln Tyr

35 40 45

<210> 1560

<211> 113

<212> PROTEIN

<213> Homo sapiens

<400> 1560

Pro Gly Arg Pro Leu Gln Thr His Val Leu Pro Glu Pro His Leu Ala

1 5 10 15

Leu Gln Pro Leu Gln Pro His Ala Asp His Ala His Ala Asp Ala Pro

20 25 30

Ala Ile Gln Pro Val Leu Trp Thr Thr Pro Pro Leu Gln His Gly His

35 40 45

Arg His Gly Leu Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg

50 55 60

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

65 70 75 80

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

85 90 95

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

100 105 110

His

<210> 1561

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1561

Cys Leu Gln Cys Leu Trp Ala Leu Leu

15

<210> 1562

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1562

Cys Gln Trp Gly Pro Cys Leu Gln Cys Leu

1 5 10

<210> 1563

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1563

Gln Trp Gly Pro Cys Leu Gln Cys Leu

15

<210> 1564

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1564

Gln Trp Gly Pro Cys Leu Gln Cys Leu Trp

1 5 10

<210> 1565

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1565

Ala Ile Gln Pro Val Leu Trp Thr Thr

15

<210> 1566

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1566

Ala Leu Gln Pro Leu Gln Pro His Ala

15

<210> 1567

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1567

Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10

<210> 1568

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1568

Glu Pro His Leu Ala Leu Gln Pro Leu

15

<210> 1569

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1569

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 1570

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1570

Phe Ala Thr Leu Gln Arg Ser Ser Leu

15

<210> 1571

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1571

Phe Leu Lys Ala Glu Ser Lys Ile Met

15

<210> 1572

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1572

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10

<210> 1573

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1573

Gly Pro Pro Ala Arg Val Pro Ala Val

15

<210> 1574

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1574

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10

<210> 1575

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1575

Lys Ile Met Phe Ala Thr Leu Gln Arg

15

<210> 1576

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1576

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 1577

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1577

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 1578

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1578

Leu His Phe Cys Arg Ser Ser Ile Met

15

<210> 1579

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1579

Leu Gln His Gly His Arg His Gly Leu

15

<210> 1580

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1580

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 1581

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1581

Met Phe Leu Lys Ala Glu Ser Lys Ile

15

<210> 1582

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1582

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 1583

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1583

Gln Pro Val Leu Trp Thr Thr Pro Pro Leu

1 5 10

<210> 1584

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1584

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 1585

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1585

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

1 5 10

<210> 1586

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1586

Val Leu Pro Glu Pro His Leu Ala Leu

15

<210> 1587

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1587

Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10

<210> 1588

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1588

Tyr Met Phe Leu Lys Ala Glu Ser Lys

15

<210> 1589

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1589

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 1590

<211> 67

<212> PROTEIN

<213> Homo sapiens

<400> 1590

Met Ser Asp Val Ala Ile Val Lys Glu Gly Trp Leu His Lys Arg Gly

1 5 10 15

Lys Tyr Ile Lys Thr Trp Arg Pro Arg Tyr Phe Leu Leu Lys Asn Asp

20 25 30

Gly Thr Phe Ile Gly Tyr Lys Glu Arg Pro Gln Asp Val Asp Gln Arg

35 40 45

Glu Ala Pro Leu Asn Asn Phe Ser Val Ala Gln Cys Gln Leu Met Lys

50 55 60

Thr Glu Arg

65

<210> 1591

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1591

Thr Met Leu Val Leu Glu Gly Ser Gly Asn Leu Val Leu Tyr Thr Gly

1 5 10 15

Val Val Arg Val Gly Lys Val Phe Ile Pro Gly Leu Pro Ala Pro Ser

20 25 30

Leu Thr Met Ser Asn Thr Met Pro Arg Pro Ser Thr Pro Leu Asp Gly

35 40 45

Val Ser Ala Pro Lys Pro Leu Ser Lys Leu Leu Gly Ser Leu Asp Glu

50 55 60

Val Val Leu Leu Ser Pro Val Pro Glu Leu Arg Asp Ser Ser Lys Leu

65 70 75 80

His Asp Ser Leu Tyr Asn Glu Asp Cys Thr Phe Gln Gln Leu Gly Thr

85 90 95

Tyr Ile His Ser Ile

100

<210> 1592

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1592

His Arg Ile Gly Gly Ile Lys Leu Arg His Gln Gln Trp Ser Leu Val

1 5 10 15

Met Glu Ser Val Val Pro Ser Asp Arg Gly Asn Tyr Thr Cys Val Val

20 25 30

Glu Asn Lys Phe Gly Ser Ile Arg Gln Thr Tyr Thr Leu Asp Val Leu

35 40 45

Glu Arg Cys Pro His Arg Pro Ile Leu Gln Ala Gly Leu Pro Ala Asn

50 55 60

Gln Thr Ala Val Leu Gly Ser Asp Val Glu Phe His Cys Lys Val Tyr

65 70 75 80

Ser Asp Ala Gln Pro His Ile Gln Trp Leu Lys His Val Glu Val Asn

85 90 95

Gly Ser Lys Val Gly

100

<210> 1593

<211> 90

<212> PROTEIN

<213> Homo sapiens

<400> 1593

Met Arg Glu Pro Ile Tyr Met His Ser Thr Met Val Phe Leu Pro Trp

1 5 10 15

Glu Leu His Thr Lys Lys Gly Pro Ser Pro Pro Glu Gln Phe Met Ala

20 25 30

Val Lys Leu Ser Asp Ser Arg Thr Ala Leu Lys Ser Gly Tyr Gly Lys

35 40 45

Tyr Leu Gly Ile Asn Ser Asp Glu Leu Val Gly His Ser Asp Ala Ile

50 55 60

Gly Pro Arg Glu Gln Trp Glu Pro Val Phe Gln Asn Gly Lys Met Ala

65 70 75 80

Leu Leu Ala Ser Asn Ser Cys Phe Ile Arg

85 90

<210> 1594

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1594

Ala Val Lys Leu Ser Asp Ser Arg Ile Ala Leu Lys Ser Gly Tyr Gly

1 5 10 15

Lys Tyr Leu Gly Ile Asn Ser Asp Glu Leu Val Gly His Ser Asp Ala

20 25 30

Ile Gly Pro Arg Glu Gln Trp Glu Pro Val Phe Gln Asn Gly Lys Met

35 40 45

Ala Leu Ser Ala Ser Asn Ser Cys Phe Ile Arg Cys Asn Glu Ala Gly

50 55 60

Asp Ile Glu Ala Lys Ser Lys Thr Ala Gly Glu Glu Glu Met Ile Lys

65 70 75 80

Ile Arg Ser Cys Ala Glu Lys Glu Thr Lys Lys Lys Asp Asp Ile Pro

85 90 95

Glu Glu Asp Lys Gly

100

<210> 1595

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1595

Ala Met Pro Asn Gln Ala Gln Met Arg Ile Leu Lys Glu Thr Glu Leu

1 5 10 15

Arg Lys Val Lys Val Leu Gly Ser Gly Ala Phe Gly Thr Val Tyr Lys

20 25 30

Gly Ile Trp Ile Pro Asp Gly Glu Asn Val Lys Ile Pro Val Ala Ile

35 40 45

Lys Val Ser Arg Glu Asn Thr Ser Pro Lys Ala Asn Lys Glu Ile Leu

50 55 60

Asp Glu Ala Tyr Val Met Ala Gly Val Gly Ser Pro Tyr Val Ser Arg

65 70 75 80

Leu Leu Gly Ile Cys Leu Thr Ser Thr Val Gln Leu Val Thr Gln Leu

85 90 95

Met Pro Tyr Gly Cys

100

<210> 1596

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1596

Arg Val Glu Glu Phe Lys Leu Lys Gln Met Trp Lys Ser Pro Asn Gly

1 5 10 15

Thr Ile Arg Asn Ile Leu Gly Gly Thr Val Phe Arg Glu Ala Ile Ile

20 25 30

Cys Lys Asn Ile Pro Arg Leu Val Ser Gly Trp Val Lys Pro Ile Ile

35 40 45

Ile Gly Gly His Ala Tyr Gly Asp Gln Tyr Arg Ala Thr Asp Phe Val

50 55 60

Val Pro Gly Pro Gly Lys Val Glu Ile Thr Tyr Thr Pro Ser Asp Gly

65 70 75 80

Thr Gln Lys Val Thr Tyr Leu Val His Asn Phe Glu Glu Gly Gly Gly

85 90 95

Val Ala Met Gly Met

100

<210> 1597

<211> 62

<212> PROTEIN

<213> Homo sapiens

<400> 1597

Met Thr Glu Tyr Lys Leu Val Val Val Gly Ala Cys Gly Val Gly Lys

1 5 10 15

Ser Ala Leu Thr Ile Gln Leu Ile Gln Asn His Phe Val Asp Glu Tyr

20 25 30

Asp Pro Thr Ile Glu Asp Ser Tyr Arg Lys Gln Val Val Ile Asp Gly

35 40 45

Glu Thr Cys Leu Leu Asp Ile Leu Asp Thr Ala Gly Gln Glu

50 55 60

<210> 1598

<211> 62

<212> PROTEIN

<213> Homo sapiens

<400> 1598

Met Thr Glu Tyr Lys Leu Val Val Val Gly Ala Asp Gly Val Gly Lys

1 5 10 15

Ser Ala Leu Thr Ile Gln Leu Ile Gln Asn His Phe Val Asp Glu Tyr

20 25 30

Asp Pro Thr Ile Glu Asp Ser Tyr Arg Lys Gln Val Val Ile Asp Gly

35 40 45

Glu Thr Cys Leu Leu Asp Ile Leu Asp Thr Ala Gly Gln Glu

50 55 60

<210> 1599

<211> 62

<212> PROTEIN

<213> Homo sapiens

<400> 1599

Met Thr Glu Tyr Lys Leu Val Val Val Gly Ala Val Gly Val Gly Lys

1 5 10 15

Ser Ala Leu Thr Ile Gln Leu Ile Gln Asn His Phe Val Asp Glu Tyr

20 25 30

Asp Pro Thr Ile Glu Asp Ser Tyr Arg Lys Gln Val Val Ile Asp Gly

35 40 45

Glu Thr Cys Leu Leu Asp Ile Leu Asp Thr Ala Gly Gln Glu

50 55 60

<210> 1600

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1600

Ala Gly Gly Val Gly Lys Ser Ala Leu Thr Ile Gln Leu Ile Gln Asn

1 5 10 15

His Phe Val Asp Glu Tyr Asp Pro Thr Ile Glu Asp Ser Tyr Arg Lys

20 25 30

Gln Val Val Ile Asp Gly Glu Thr Cys Leu Leu Asp Ile Leu Asp Thr

35 40 45

Ala Gly His Glu Glu Tyr Ser Ala Met Arg Asp Gln Tyr Met Arg Thr

50 55 60

Gly Glu Gly Phe Leu Cys Val Phe Ala Ile Asn Asn Thr Lys Ser Phe

65 70 75 80

Glu Asp Ile His His Tyr Arg Glu Gln Ile Lys Arg Val Lys Asp Ser

85 90 95

Glu Asp Val Pro Met

100

<210> 1601

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1601

Ala Gly Gly Val Gly Lys Ser Ala Leu Thr Ile Gln Leu Ile Gln Asn

1 5 10 15

His Phe Val Asp Glu Tyr Asp Pro Thr Ile Glu Asp Ser Tyr Arg Lys

20 25 30

Gln Val Val Ile Asp Gly Glu Thr Cys Leu Leu Asp Ile Leu Asp Thr

35 40 45

Ala Gly Leu Glu Glu Tyr Ser Ala Met Arg Asp Gln Tyr Met Arg Thr

50 55 60

Gly Glu Gly Phe Leu Cys Val Phe Ala Ile Asn Asn Thr Lys Ser Phe

65 70 75 80

Glu Asp Ile His His Tyr Arg Glu Gln Ile Lys Arg Val Lys Asp Ser

85 90 95

Glu Asp Val Pro Met

100

<210> 1602

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1602

Ala Gly Gly Val Gly Lys Ser Ala Leu Thr Ile Gln Leu Ile Gln Asn

1 5 10 15

His Phe Val Asp Glu Tyr Asp Pro Thr Ile Glu Asp Ser Tyr Arg Lys

20 25 30

Gln Val Val Ile Asp Gly Glu Thr Cys Leu Leu Asp Ile Leu Asp Thr

35 40 45

Ala Gly Lys Glu Glu Tyr Ser Ala Met Arg Asp Gln Tyr Met Arg Thr

50 55 60

Gly Glu Gly Phe Leu Cys Val Phe Ala Ile Asn Asn Ser Lys Ser Phe

65 70 75 80

Ala Asp Ile Asn Leu Tyr Arg Glu Gln Ile Lys Arg Val Lys Asp Ser

85 90 95

Asp Asp Val Pro Met

100

<210> 1603

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1603

Ala Gly Gly Val Gly Lys Ser Ala Leu Thr Ile Gln Leu Ile Gln Asn

1 5 10 15

His Phe Val Asp Glu Tyr Asp Pro Thr Ile Glu Asp Ser Tyr Arg Lys

20 25 30

Gln Val Val Ile Asp Gly Glu Thr Cys Leu Leu Asp Ile Leu Asp Thr

35 40 45

Ala Gly Arg Glu Glu Tyr Ser Ala Met Arg Asp Gln Tyr Met Arg Thr

50 55 60

Gly Glu Gly Phe Leu Cys Val Phe Ala Ile Asn Asn Ser Lys Ser Phe

65 70 75 80

Ala Asp Ile Asn Leu Tyr Arg Glu Gln Ile Lys Arg Val Lys Asp Ser

85 90 95

Asp Asp Val Pro Met

100

<210> 1604

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1604

Ile Glu Glu His Ala Asn Trp Ser Val Ser Arg Glu Ala Gly Phe Ser

1 5 10 15

Tyr Ser His Ala Gly Leu Ser Asn Arg Leu Ala Arg Asp Asn Glu Leu

20 25 30

Arg Glu Asn Asp Lys Glu Gln Leu Lys Ala Ile Ser Thr Arg Asp Pro

35 40 45

Leu Ser Lys Ile Thr Glu Gln Glu Lys Asp Phe Leu Trp Ser His Arg

50 55 60

His Tyr Cys Val Thr Ile Pro Glu Ile Leu Pro Lys Leu Leu Leu Ser

65 70 75 80

Val Lys Trp Asn Ser Arg Asp Glu Val Ala Gln Met Tyr Cys Leu Val

85 90 95

Lys Asp Trp Pro Pro

100

<210> 1605

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1605

Lys Phe Asn Cys Arg Val Ala Gln Tyr Pro Phe Glu Asp His Asn Pro

1 5 10 15

Pro Gln Leu Glu Leu Ile Lys Pro Phe Cys Glu Asp Leu Asp Gln Trp

20 25 30

Leu Ser Glu Asp Asp Asn His Val Ala Ala Ile His Cys Lys Ala Gly

35 40 45

Lys Gly Gln Thr Gly Val Met Ile Cys Ala Tyr Leu Leu His Arg Gly

50 55 60

Lys Phe Leu Lys Ala Gln Glu Ala Leu Asp Phe Tyr Gly Glu Val Arg

65 70 75 80

Thr Arg Asp Lys Lys Gly Val Thr Ile Pro Ser Gln Arg Arg Tyr Val

85 90 95

Tyr Tyr Tyr Ser Tyr

100

<210> 1606

<211> 79

<212> PROTEIN

<213> Homo sapiens

<400> 1606

Met Gln Ala Ile Lys Cys Val Val Val Gly Asp Gly Ala Val Gly Lys

1 5 10 15

Thr Cys Leu Leu Ile Ser Tyr Thr Thr Asn Ala Phe Ser Gly Glu Tyr

20 25 30

Ile Pro Thr Val Phe Asp Asn Tyr Ser Ala Asn Val Met Val Asp Gly

35 40 45

Lys Pro Val Asn Leu Gly Leu Trp Asp Thr Ala Gly Gln Glu Asp Tyr

50 55 60

Asp Arg Leu Arg Pro Leu Ser Tyr Pro Gln Thr Val Gly Glu Thr

65 70 75

<210> 1607

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1607

Ala Val Cys Lys Ser Lys Lys Ser Trp Gln Ala Arg His Thr Gly Ile

1 5 10 15

Lys Ile Val Gln Gln Ile Ala Ile Leu Met Gly Cys Ala Ile Leu Pro

20 25 30

His Leu Arg Ser Leu Val Glu Ile Ile Glu His Gly Leu Val Asp Glu

35 40 45

Gln Gln Glu Val Arg Thr Ile Ser Ala Leu Ala Ile Ala Ala Leu Ala

50 55 60

Glu Ala Ala Thr Pro Tyr Gly Ile Glu Ser Phe Asp Ser Val Leu Lys

65 70 75 80

Pro Leu Trp Lys Gly Ile Arg Gln His Arg Gly Lys Gly Leu Ala Ala

85 90 95

Phe Leu Lys Ala Ile

100

<210> 1608

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1608

Tyr Leu Ser Leu Tyr Leu Leu Leu Val Ser Cys Pro Lys Ser Glu Val

1 5 10 15

Arg Ala Lys Phe Lys Phe Ser Ile Leu Asn Ala Lys Gly Glu Glu Thr

20 25 30

Lys Ala Met Glu Ser Gln Arg Ala Tyr Arg Phe Val Gln Gly Lys Asp

35 40 45

Trp Gly Leu Lys Lys Phe Ile Arg Arg Asp Phe Leu Leu Asp Glu Ala

50 55 60

Asn Gly Leu Leu Pro Asp Asp Lys Leu Thr Leu Phe Cys Glu Val Ser

65 70 75 80

Val Val Gln Asp Ser Val Asn Ile Ser Gly Gln Asn Thr Met Asn Met

85 90 95

Val Lys Val Pro Glu

100

<210> 1609

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1609

Tyr Leu Ser Leu Tyr Leu Leu Leu Val Ser Cys Pro Lys Ser Glu Val

1 5 10 15

Arg Ala Lys Phe Lys Phe Ser Ile Leu Asn Ala Lys Gly Glu Glu Thr

20 25 30

Lys Ala Met Glu Ser Gln Arg Ala Tyr Arg Phe Val Gln Gly Lys Asp

35 40 45

Trp Gly Val Lys Lys Phe Ile Arg Arg Asp Phe Leu Leu Asp Glu Ala

50 55 60

Asn Gly Leu Leu Pro Asp Asp Lys Leu Thr Leu Phe Cys Glu Val Ser

65 70 75 80

Val Val Gln Asp Ser Val Asn Ile Ser Gly Gln Asn Thr Met Asn Met

85 90 95

Val Lys Val Pro Glu

100

<210> 1610

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1610

Ile Arg Val Glu Gly Asn Leu Arg Val Glu Tyr Leu Asp Asp Arg Asn

1 5 10 15

Thr Phe Arg His Ser Val Val Val Pro Tyr Glu Pro Pro Glu Val Gly

20 25 30

Ser Asp Cys Thr Thr Ile His Tyr Asn Tyr Met Cys Asn Ser Ser Cys

35 40 45

Met Gly Ser Met Asn Arg Arg Pro Ile Leu Thr Ile Ile Thr Leu Glu

50 55 60

Asp Ser Ser Gly Asn Leu Leu Gly Arg Asn Ser Phe Glu Val Arg Val

65 70 75 80

Cys Ala Cys Pro Gly Arg Asp Arg Arg Thr Glu Glu Glu Asn Leu Arg

85 90 95

Lys Lys Gly Glu Pro

100

<210> 1611

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1611

Glu Gly Asn Leu Arg Val Glu Tyr Leu Asp Asp Arg Asn Thr Phe Arg

1 5 10 15

His Ser Val Val Val Pro Tyr Glu Pro Pro Glu Val Gly Ser Asp Cys

20 25 30

Thr Thr Ile His Tyr Asn Tyr Met Cys Asn Ser Ser Cys Met Gly Gly

35 40 45

Met Asn Gln Arg Pro Ile Leu Thr Ile Ile Thr Leu Glu Asp Ser Ser

50 55 60

Gly Asn Leu Leu Gly Arg Asn Ser Phe Glu Val Arg Val Cys Ala Cys

65 70 75 80

Pro Gly Arg Asp Arg Arg Thr Glu Glu Glu Asn Leu Arg Lys Lys Gly

85 90 95

Glu Pro His His Glu

100

<210> 1612

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1612

Glu Gly Asn Leu Arg Val Glu Tyr Leu Asp Asp Arg Asn Thr Phe Arg

1 5 10 15

His Ser Val Val Val Pro Tyr Glu Pro Pro Glu Val Gly Ser Asp Cys

20 25 30

Thr Thr Ile His Tyr Asn Tyr Met Cys Asn Ser Ser Cys Met Gly Gly

35 40 45

Met Asn Trp Arg Pro Ile Leu Thr Ile Ile Thr Leu Glu Asp Ser Ser

50 55 60

Gly Asn Leu Leu Gly Arg Asn Ser Phe Glu Val Arg Val Cys Ala Cys

65 70 75 80

Pro Gly Arg Asp Arg Arg Thr Glu Glu Glu Asn Leu Arg Lys Lys Gly

85 90 95

Glu Pro His His Glu

100

<210> 1613

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1613

Pro Glu Val Gly Ser Asp Cys Thr Thr Ile His Tyr Asn Tyr Met Cys

1 5 10 15

Asn Ser Ser Cys Met Gly Gly Met Asn Arg Arg Pro Ile Leu Thr Ile

20 25 30

Ile Thr Leu Glu Asp Ser Ser Gly Asn Leu Leu Gly Arg Asn Ser Phe

35 40 45

Glu Val Cys Val Cys Ala Cys Pro Gly Arg Asp Arg Arg Thr Glu Glu

50 55 60

Glu Asn Leu Arg Lys Lys Gly Glu Pro His His Glu Leu Pro Pro Gly

65 70 75 80

Ser Thr Lys Arg Ala Leu Pro Asn Asn Thr Ser Ser Ser Pro Gln Pro

85 90 95

Lys Lys Lys Pro Leu

100

<210> 1614

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1614

Pro Glu Val Gly Ser Asp Cys Thr Thr Ile His Tyr Asn Tyr Met Cys

1 5 10 15

Asn Ser Ser Cys Met Gly Gly Met Asn Arg Arg Pro Ile Leu Thr Ile

20 25 30

Ile Thr Leu Glu Asp Ser Ser Gly Asn Leu Leu Gly Arg Asn Ser Phe

35 40 45

Glu Val His Val Cys Ala Cys Pro Gly Arg Asp Arg Arg Thr Glu Glu

50 55 60

Glu Asn Leu Arg Lys Lys Gly Glu Pro His His Glu Leu Pro Pro Gly

65 70 75 80

Ser Thr Lys Arg Ala Leu Pro Asn Asn Thr Ser Ser Ser Pro Gln Pro

85 90 95

Lys Lys Lys Pro Leu

100

<210> 1615

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1615

Thr Glu Val Val Arg Arg Cys Pro His His Glu Arg Cys Ser Asp Ser

1 5 10 15

Asp Gly Leu Ala Pro Pro Gln His Leu Ile Arg Val Glu Gly Asn Leu

20 25 30

Arg Val Glu Tyr Leu Asp Asp Arg Asn Thr Phe Arg His Ser Val Val

35 40 45

Val Pro Cys Glu Pro Pro Glu Val Gly Ser Asp Cys Thr Thr Ile His

50 55 60

Tyr Asn Tyr Met Cys Asn Ser Ser Cys Met Gly Gly Met Asn Arg Arg

65 70 75 80

Pro Ile Leu Thr Ile Ile Thr Leu Glu Asp Ser Ser Gly Asn Leu Leu

85 90 95

Gly Arg Asn Ser Phe

100

<210> 1616

<211> 54

<212> PROTEIN

<213> Homo sapiens

<400> 1616

Tyr Asn Phe Asp Lys Asn Tyr Lys Asp Trp Gln Ser Ala Val Glu Cys

1 5 10 15

Ile Ala Val Leu Asp Val Leu Leu Cys Leu Ala Asn Tyr Ser Arg Gly

20 25 30

Gly Asp Gly Pro Met Cys Arg Pro Val Ile Leu Leu Pro Glu Asp Thr

35 40 45

Pro Pro Leu Leu Arg Ala

50

<210> 1617

<211> 93

<212> PROTEIN

<213> Homo sapiens

<400> 1617

Ala Lys Phe Gln Gln Cys His Ser Thr Leu Glu Pro Asn Pro Ala Asp

1 5 10 15

Cys Arg Val Leu Val Tyr Leu Gln Asn Gln Pro Gly Thr Lys Leu Leu

20 25 30

Asn Phe Leu Gln Glu Arg Asn Leu Pro Pro Lys Val Val Leu Arg His

35 40 45

Pro Lys Val His Leu Asn Thr Met Phe Arg Arg Pro His Ser Cys Leu

50 55 60

Ala Asp Val Leu Leu Ser Val His Leu Ile Val Leu Arg Val Val Arg

65 70 75 80

Leu Pro Ala Pro Phe Arg Val Asn His Ala Val Glu Trp

85 90

<210> 1618

<211> 179

<212> PROTEIN

<213> Homo sapiens

<400> 1618

Ala Leu Gly Pro His Ser Arg Ile Ser Cys Leu Pro Thr Gln Thr Arg

1 5 10 15

Gly Cys Ile Leu Leu Ala Ala Thr Pro Arg Ser Ser Ser Ser Ser Ser

20 25 30

Ser Asn Asp Met Ile Pro Met Ala Ile Ser Ser Pro Pro Lys Ala Pro

35 40 45

Leu Leu Ala Ala Pro Ser Pro Ala Ser Arg Leu Gln Cys Ile Asn Ser

50 55 60

Asn Ser Arg Ile Thr Ser Gly Gln Trp Met Ala His Met Ala Leu Leu

65 70 75 80

Pro Ser Gly Thr Lys Gly Arg Cys Thr Ala Cys His Thr Ala Leu Gly

85 90 95

Arg Gly Ser Leu Ser Ser Ser Ser Cys Pro Gln Pro Ser Pro Ser Leu

100 105 110

Pro Ala Ser Asn Lys Leu Pro Ser Leu Pro Leu Ser Lys Met Tyr Thr

115 120 125

Thr Ser Met Ala Met Pro Ile Leu Pro Leu Pro Gln Leu Leu Leu Ser

130 135 140

Ala Asp Gln Gln Ala Ala Pro Arg Thr Asn Phe His Ser Ser Leu Ala

145 150 155 160

Glu Thr Val Ser Leu His Pro Leu Ala Pro Met Pro Ser Lys Thr Cys

165 170 175

His His Lys

<210> 1619

<211> 67

<212> PROTEIN

<213> Homo sapiens

<400> 1619

Arg Ser Tyr Arg Arg Met Ile His Leu Trp Trp Thr Ala Gln Ile Ser

1 5 10 15

Leu Gly Val Cys Arg Ser Leu Thr Val Ala Cys Cys Thr Gly Gly Leu

20 25 30

Val Gly Gly Thr Pro Leu Ser Ile Ser Arg Pro Thr Ser Arg Ala Arg

35 40 45

Gln Ser Cys Cys Leu Pro Gly Leu Thr His Pro Ala His Gln Pro Leu

50 55 60

Gly Ser Met

65

<210> 1620

<211> 60

<212> PROTEIN

<213> Homo sapiens

<400> 1620

Gln His Ser Gly Arg Asp Val Ser Leu Arg Gly Leu Ser Cys Ala Arg

1 5 10 15

Ala Thr Leu Ser Phe Trp Pro Gly Gly Tyr Pro Ala Tyr Ser Lys Asp

20 25 30

Ser Gly Leu Leu Thr Ser Ser Ser Arg Glu Trp Lys Val Lys Phe Pro

35 40 45

Glu Leu Leu Cys Val Trp Val Ser Ser Ile Arg His

50 55 60

<210> 1621

<211> 48

<212> PROTEIN

<213> Homo sapiens

<400> 1621

Ala Gln Ala Lys Ala Val Cys Ser Gln Glu Ser Arg Asp Val Leu Cys

1 5 10 15

Glu Leu Ser Asp His His Asn His Thr Leu Glu Glu Glu Cys Gln Trp

20 25 30

Gly Pro Cys Leu Gln Cys Leu Trp Ala Leu Leu Gln Ala Ser Gln Tyr

35 40 45

<210> 1622

<211> 113

<212> PROTEIN

<213> Homo sapiens

<400> 1622

Pro Gly Arg Pro Leu Gln Thr His Val Leu Pro Glu Pro His Leu Ala

1 5 10 15

Leu Gln Pro Leu Gln Pro His Ala Asp His Ala His Ala Asp Ala Pro

20 25 30

Ala Ile Gln Pro Val Leu Trp Thr Thr Pro Pro Leu Gln His Gly His

35 40 45

Arg His Gly Leu Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg

50 55 60

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

65 70 75 80

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

85 90 95

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

100 105 110

His

<210> 1623

<211> 494

<212> PROTEIN

<213> Homo sapiens

<400> 1623

Thr Arg Arg Cys His Cys Cys Pro His Leu Arg Ser His Pro Cys Pro

1 5 10 15

His His Leu Arg Asn His Pro Arg Pro His His Leu Arg His His Ala

20 25 30

Cys His His His Leu Arg Asn Cys Pro His Pro His Phe Leu Arg His

35 40 45

Cys Thr Cys Pro Gly Arg Trp Arg Asn Arg Pro Ser Leu Arg Arg Leu

50 55 60

Arg Ser Leu Leu Cys Leu Pro His Leu Asn His His Leu Phe Leu His

65 70 75 80

Trp Arg Ser Arg Pro Cys Leu His Arg Lys Ser His Pro His Leu Leu

85 90 95

His Leu Arg Arg Leu Tyr Pro His His Leu Lys His Arg Pro Cys Pro

100 105 110

His His Leu Lys Asn Leu Leu Cys Pro Arg His Leu Arg Asn Cys Pro

115 120 125

Leu Pro Arg His Leu Lys His Leu Ala Cys Leu His His Leu Arg Ser

130 135 140

His Pro Cys Pro Leu His Leu Lys Ser His Pro Cys Leu His His Arg

145 150 155 160

Arg His Leu Val Cys Ser His His Leu Lys Ser Leu Leu Cys Pro Leu

165 170 175

His Leu Arg Ser Leu Pro Phe Pro His His Leu Arg His His Ala Cys

180 185 190

Pro His His Leu Arg Thr Arg Leu Cys Pro His His Leu Lys Asn His

195 200 205

Leu Cys Pro Pro His Leu Arg Tyr Arg Ala Tyr Pro Pro Cys Leu Trp

210 215 220

Cys His Ala Cys Leu His Arg Leu Arg Asn Leu Pro Cys Pro His Arg

225 230 235 240

Leu Arg Ser Leu Pro Arg Pro Leu His Leu Arg Leu His Ala Ser Pro

245 250 255

His His Leu Arg Thr Pro Pro His Pro His His Leu Arg Thr His Leu

260 265 270

Leu Pro His His Arg Arg Thr Arg Ser Cys Pro Cys Arg Trp Arg Ser

275 280 285

His Pro Cys Cys His Tyr Leu Arg Ser Arg Asn Ser Ala Pro Gly Pro

290 295 300

Arg Gly Arg Thr Cys His Pro Gly Leu Arg Ser Arg Thr Cys Pro Pro

305 310 315 320

Gly Leu Arg Ser His Thr Tyr Leu Arg Arg Leu Arg Ser His Thr Cys

325 330 335

Pro Pro Ser Leu Arg Ser His Ala Tyr Ala Leu Cys Leu Arg Ser His

340 345 350

Thr Cys Pro Pro Arg Leu Arg Asp His Ile Cys Pro Leu Ser Leu Arg

355 360 365

Asn Cys Thr Cys Pro Pro Arg Leu Arg Ser Arg Thr Cys Leu Leu Cys

370 375 380

Leu Arg Ser His Ala Cys Pro Pro Asn Leu Arg Asn His Thr Cys Pro

385 390 395 400

Pro Ser Leu Arg Ser His Ala Cys Pro Pro Gly Leu Arg Asn Arg Ile

405 410 415

Cys Pro Leu Ser Leu Arg Ser His Pro Cys Pro Leu Gly Leu Lys Ser

420 425 430

Pro Leu Arg Ser Gln Ala Asn Ala Leu His Leu Arg Ser Cys Pro Cys

435 440 445

Ser Leu Pro Leu Gly Asn His Pro Tyr Leu Pro Cys Leu Glu Ser Gln

450 455 460

Pro Cys Leu Ser Leu Gly Asn His Leu Cys Pro Leu Cys Pro Arg Ser

465 470 475 480

Cys Arg Cys Pro His Leu Gly Ser His Pro Cys Arg Leu Ser

485 490

<210> 1624

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 1624

Gly Pro Arg Ser His Pro Leu Pro Arg Leu Trp His Leu Leu Leu Gln

1 5 10 15

Val Thr Gln Thr Ser Phe Ala Leu Ala Pro Thr Leu Thr His Met Leu

20 25 30

Ser Pro His

35

<210> 1625

<211> 172

<212> PROTEIN

<213> Homo sapiens

<400> 1625

Pro Leu Gly Leu Val Pro Trp Thr Arg Trp Cys Pro Gln Gly Lys Pro

1 5 10 15

Arg Phe Pro Ala Met Ser Thr Thr Thr Ala Thr Gly Thr Thr Thr Thr

20 25 30

Lys Ser Gly Ser Ser Gly Met Ala Gly Ser Leu Ala Gln Lys Pro Glu

35 40 45

Ser Pro Ser Pro Gly Leu Leu Phe Leu Gly His Ser Pro Ser Gln Ser

50 55 60

His Leu Leu Leu Ile Ser Lys Ser Pro Asp Pro Thr Gln Gln Pro Leu

65 70 75 80

Arg Gly Gly Ser Leu Thr His Ser Ala Pro Gly Pro Ser Leu Ser Gln

85 90 95

Pro Leu Ala Gln Leu Thr Pro Pro Ala Ser Ala Pro Val Pro Ala Val

100 105 110

Cys Ser Thr Cys Lys Asn Pro Ala Ser Leu Pro Asp Thr His Arg Gly

115 120 125

Lys Gly Gly Gly Val Pro Pro Ser Pro Pro Leu Ala Leu Gly Pro Arg

130 135 140

Met Gln Leu Cys Thr Gln Leu Ala Arg Phe Phe Pro Ile Thr Pro Pro

145 150 155 160

Val Trp His Ile Leu Gly Pro Gln Arg His Thr Pro

165 170

<210> 1626

<211> 97

<212> PROTEIN

<213> Homo sapiens

<400> 1626

Lys Tyr Glu Lys Lys Lys Tyr Tyr Asp Lys Asn Ala Ile Ala Ile Thr

1 5 10 15

Asn Ile Ser Ser Ser Asp Ala Pro Leu Gln Pro Leu Val Ser Ser Pro

20 25 30

Ser Leu Gln Ala Ala Val Asp Lys Asn Lys Leu Glu Lys Glu Lys Glu

35 40 45

Lys Lys Arg Lys Arg Lys Arg Glu Lys Arg Ser Gln Lys Ser Arg Gln

50 55 60

Asn His Leu Gln Leu Lys Ser Cys Arg Arg Lys Ile Ser Asn Trp Ser

65 70 75 80

Leu Lys Lys Val Pro Ala Leu Lys Lys Leu Arg Ser Pro Leu Trp Ile

85 90 95

Phe

<210> 1627

<211> 78

<212> PROTEIN

<213> Homo sapiens

<400> 1627

Cys Cys Pro Arg Thr Ile Leu Asn Asn Gly Ser Leu Lys Thr Gln Val

1 5 10 15

Gln Met Lys Leu Pro Glu Cys Gln Arg Leu Leu Pro Pro Trp Pro Leu

20 25 30

His Gln Gln Leu Leu His Arg Arg Pro Leu His Gln Pro Pro Pro Gly

35 40 45

Pro Cys His Leu Leu Ser Leu Pro Arg Lys Pro Thr Arg Ala Ala Thr

50 55 60

Val Ser Val Trp Ala Ser Cys Ile Leu Gly Gln Pro Ser Leu

65 70 75

<210> 1628

<211> 46

<212> PROTEIN

<213> Homo sapiens

<400> 1628

Leu Ala Arg Thr Pro Leu Pro Ser Thr Arg Cys Phe Ala Asn Trp Pro

1 5 10 15

Arg Pro Ala Leu Cys Ser Cys Gly Leu Ile Pro His Pro Arg Pro Ala

20 25 30

Pro Ala Ser Ala Pro Trp Pro Ser Thr Ser Ser His Ser Thr

35 40 45

<210> 1629

<211> 77

<212> PROTEIN

<213> Homo sapiens

<400> 1629

Ser Gln Gly Leu Tyr Ser Ser Ser Ala Ser Ser Gly Lys Cys Leu Met

1 5 10 15

Glu Val Thr Val Asp Arg Asn Cys Leu Glu Val Leu Pro Thr Lys Met

20 25 30

Ser Tyr Ala Ala Asn Leu Lys Asn Val Met Asn Met Gln Asn Arg Gln

35 40 45

Lys Lys Lys Gly Lys Asn Ser Pro Cys Cys Gln Lys Lys Leu Arg Val

50 55 60

Gln Asn Gln Gly His Leu Leu Met Ile Leu Leu His Asn

65 70 75

<210> 1630

<211> 91

<212> PROTEIN

<213> Homo sapiens

<400> 1630

Thr Arg Ala Ser Pro Pro Arg Ser Ser Ser Ala Ile Ala Val Arg Ala

1 5 10 15

Ser Cys Cys Pro Tyr Gly Ser Thr Ser Thr Ala Ser Arg Ser Pro Thr

20 25 30

Gln Arg Cys Arg Leu Ala Arg Ala Ala Ala Ser Thr Ala Thr Glu Val

35 40 45

Thr Phe Gly Ser Ser Glu Met Gln Gly His Thr Met Gly Phe Trp Leu

50 55 60

Thr Lys Leu Asn Tyr Leu Cys His Leu Ser Met Leu Thr Asp Ser Leu

65 70 75 80

Phe Leu Pro Ile Ser His Cys Gln Cys Ile Leu

85 90

<210> 1631

<211> 104

<212> PROTEIN

<213> Homo sapiens

<400> 1631

Leu Gly Ser Gly Ala Phe Gly Thr Val Tyr Lys Gly Ile Trp Ile Pro

1 5 10 15

Asp Gly Glu Asn Val Lys Ile Pro Val Ala Ile Lys Val Leu Arg Glu

20 25 30

Asn Thr Ser Pro Lys Ala Asn Lys Glu Ile Leu Asp Glu Ala Tyr Val

35 40 45

Met Ala Tyr Val Met Ala Gly Val Gly Ser Pro Tyr Val Ser Arg Leu

50 55 60

Leu Gly Ile Cys Leu Thr Ser Thr Val Gln Leu Val Thr Gln Leu Met

65 70 75 80

Pro Tyr Gly Cys Leu Leu Asp His Val Arg Glu Asn Arg Gly Arg Leu

85 90 95

Gly Ser Gln Asp Leu Leu Asn Trp

100

<210> 1632

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1632

Lys Tyr Ile Lys Thr Trp Arg Pro Arg Tyr

1 5 10

<210> 1633

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1633

Trp Leu His Lys Arg Gly Lys Tyr Ile

15

<210> 1634

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1634

Trp Leu His Lys Arg Gly Lys Tyr Ile Lys

1 5 10

<210> 1635

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1635

Ala Pro Lys Pro Leu Ser Lys Leu Leu

15

<210> 1636

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1636

Gly Val Ser Ala Pro Lys Pro Leu Ser Lys

1 5 10

<210> 1637

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1637

Val Ser Ala Pro Lys Pro Leu Ser Lys

15

<210> 1638

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1638

Cys Pro His Arg Pro Ile Leu Gln Ala

15

<210> 1639

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1639

Lys Leu Ser Asp Ser Arg Thr Ala Leu

15

<210> 1640

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1640

Lys Leu Ser Asp Ser Arg Thr Ala Leu Lys

1 5 10

<210> 1641

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1641

Leu Ser Asp Ser Arg Thr Ala Leu Lys

15

<210> 1642

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1642

Arg Thr Ala Leu Lys Ser Gly Tyr Gly Lys

1 5 10

<210> 1643

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1643

Thr Ala Leu Lys Ser Gly Tyr Gly Lys

15

<210> 1644

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1644

Ala Leu Ser Ala Ser Asn Ser Cys Phe

15

<210> 1645

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1645

Ala Leu Ser Ala Ser Asn Ser Cys Phe Ile

1 5 10

<210> 1646

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1646

Phe Gln Asn Gly Lys Met Ala Leu Ser Ala

1 5 10

<210> 1647

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1647

Lys Val Ser Arg Glu Asn Thr Ser Pro Lys

1 5 10

<210> 1648

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1648

Lys Pro Ile Ile Ile Gly Gly His Ala Tyr

1 5 10

<210> 1649

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1649

Lys Leu Val Val Val Gly Ala Cys Gly Val

1 5 10

<210> 1650

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1650

Leu Val Val Val Gly Ala Cys Gly Val

15

<210> 1651

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1651

Val Val Gly Ala Cys Gly Val Gly Lys

15

<210> 1652

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1652

Val Val Val Gly Ala Cys Gly Val Gly Lys

1 5 10

<210> 1653

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1653

Val Val Gly Ala Asp Gly Val Gly Lys

15

<210> 1654

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1654

Val Val Val Gly Ala Asp Gly Val Gly Lys

1 5 10

<210> 1655

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1655

Lys Leu Val Val Val Gly Ala Asp Gly Val

1 5 10

<210> 1656

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1656

Leu Val Val Val Gly Ala Asp Gly Val

15

<210> 1657

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1657

Lys Leu Val Val Val Gly Ala Val Gly Val

1 5 10

<210> 1658

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1658

Leu Val Val Val Gly Ala Val Gly Val

15

<210> 1659

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1659

Val Val Gly Ala Val Gly Val Gly Lys

15

<210> 1660

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1660

Val Val Val Gly Ala Val Gly Val Gly Lys

1 5 10

<210> 1661

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1661

Ile Leu Asp Thr Ala Gly His Glu Glu Tyr

1 5 10

<210> 1662

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1662

Ile Leu Asp Thr Ala Gly Leu Glu Glu Tyr

1 5 10

<210> 1663

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1663

Leu Leu Asp Ile Leu Asp Thr Ala Gly Leu

1 5 10

<210> 1664

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1664

Ile Leu Asp Thr Ala Gly Lys Glu Glu Tyr

1 5 10

<210> 1665

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1665

Ile Leu Asp Thr Ala Gly Arg Glu Glu Tyr

1 5 10

<210> 1666

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1666

Ala Ile Ser Thr Arg Asp Pro Leu Ser Lys

1 5 10

<210> 1667

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1667

Gln Thr Gly Val Met Ile Cys Ala Tyr

15

<210> 1668

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1668

Phe Ser Gly Glu Tyr Ile Pro Thr Val

15

<210> 1669

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1669

Thr Thr Asn Ala Phe Ser Gly Glu Tyr

15

<210> 1670

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1670

Tyr Thr Thr Asn Ala Phe Ser Gly Glu Tyr

1 5 10

<210> 1671

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1671

Gly Leu Val Asp Glu Gln Gln Glu Val

15

<210> 1672

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1672

Phe Val Gln Gly Lys Asp Trp Gly Leu

15

<210> 1673

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1673

Phe Val Gln Gly Lys Asp Trp Gly Val

15

<210> 1674

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1674

Cys Met Gly Ser Met Asn Arg Arg Pro Ile

1 5 10

<210> 1675

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1675

Gly Ser Met Asn Arg Arg Pro Ile Leu

15

<210> 1676

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1676

Met Gly Ser Met Asn Arg Arg Pro Ile

15

<210> 1677

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1677

Met Gly Ser Met Asn Arg Arg Pro Ile Leu

1 5 10

<210> 1678

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1678

Ser Met Asn Arg Arg Pro Ile Leu Thr Ile

1 5 10

<210> 1679

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1679

Cys Met Gly Gly Met Asn Gln Arg Pro Ile

1 5 10

<210> 1680

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1680

Gly Met Asn Gln Arg Pro Ile Leu Thr Ile

1 5 10

<210> 1681

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1681

Asn Gln Arg Pro Ile Leu Thr Ile Ile

15

<210> 1682

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1682

Cys Met Gly Gly Met Asn Trp Arg Pro Ile

1 5 10

<210> 1683

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1683

Gly Met Asn Trp Arg Pro Ile Leu Thr Ile

1 5 10

<210> 1684

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1684

Met Asn Trp Arg Pro Ile Leu Thr Ile

15

<210> 1685

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1685

Met Asn Trp Arg Pro Ile Leu Thr Ile Ile

1 5 10

<210> 1686

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1686

Asn Ser Phe Glu Val Cys Val Cys Ala

15

<210> 1687

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1687

Asn Ser Phe Glu Val His Val Cys Ala

15

<210> 1688

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1688

Val Val Pro Cys Glu Pro Pro Glu Val

15

<210> 1689

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1689

Val Val Val Pro Cys Glu Pro Pro Glu Val

1 5 10

<210> 1690

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1690

Ile Leu Leu Pro Glu Asp Thr Pro Pro Leu

1 5 10

<210> 1691

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1691

Leu Leu Pro Glu Asp Thr Pro Pro Leu

15

<210> 1692

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1692

Ala Pro Phe Arg Val Asn His Ala Val

15

<210> 1693

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1693

Cys Leu Ala Asp Val Leu Leu Ser Val

15

<210> 1694

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1694

Phe Leu Gln Glu Arg Asn Leu Pro Pro Lys

1 5 10

<210> 1695

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1695

His Leu Ile Val Leu Arg Val Val Arg Leu

1 5 10

<210> 1696

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1696

His Pro Lys Val His Leu Asn Thr Met

15

<210> 1697

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1697

His Pro Lys Val His Leu Asn Thr Met Phe

1 5 10

<210> 1698

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1698

Lys Val His Leu Asn Thr Met Phe Arg

15

<210> 1699

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1699

Lys Val His Leu Asn Thr Met Phe Arg Arg

1 5 10

<210> 1700

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1700

Leu Pro Ala Pro Phe Arg Val Asn His Ala

1 5 10

<210> 1701

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1701

Met Phe Arg Arg Pro His Ser Cys Leu

15

<210> 1702

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1702

Met Phe Arg Arg Pro His Ser Cys Leu Ala

1 5 10

<210> 1703

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1703

Asn Thr Met Phe Arg Arg Pro His Ser Cys

1 5 10

<210> 1704

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1704

Arg Pro His Ser Cys Leu Ala Asp Val

15

<210> 1705

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1705

Arg Pro His Ser Cys Leu Ala Asp Val Leu

1 5 10

<210> 1706

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1706

Arg Val Val Arg Leu Pro Ala Pro Phe Arg

1 5 10

<210> 1707

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1707

Ser Val His Leu Ile Val Leu Arg Val

15

<210> 1708

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1708

Thr Met Phe Arg Arg Pro His Ser Cys

15

<210> 1709

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1709

Thr Met Phe Arg Arg Pro His Ser Cys Leu

1 5 10

<210> 1710

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1710

Val Leu Leu Ser Val His Leu Ile Val

15

<210> 1711

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1711

Val Leu Leu Ser Val His Leu Ile Val Leu

1 5 10

<210> 1712

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1712

Val Leu Arg Val Val Arg Leu Pro Ala

15

<210> 1713

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1713

Val Val Arg Leu Pro Ala Pro Phe Arg

15

<210> 1714

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1714

Ala Met Pro Ile Leu Pro Leu Pro Gln Leu

1 5 10

<210> 1715

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1715

Ala Pro Leu Leu Ala Ala Pro Ser Pro Ala

1 5 10

<210> 1716

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1716

Ala Pro Arg Thr Asn Phe His Ser Ser

15

<210> 1717

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1717

Ala Pro Arg Thr Asn Phe His Ser Ser Leu

1 5 10

<210> 1718

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1718

Cys Pro Gln Pro Ser Pro Ser Leu Pro Ala

1 5 10

<210> 1719

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1719

Gly Gln Trp Met Ala His Met Ala Leu

15

<210> 1720

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1720

Gly Gln Trp Met Ala His Met Ala Leu Leu

1 5 10

<210> 1721

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1721

His Met Ala Leu Leu Pro Ser Gly Thr Lys

1 5 10

<210> 1722

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1722

His Thr Ala Leu Gly Arg Gly Ser Leu

15

<210> 1723

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1723

Ile Pro Met Ala Ile Ser Ser Pro Pro

15

<210> 1724

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1724

Ile Pro Met Ala Ile Ser Ser Pro Pro Lys

1 5 10

<210> 1725

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1725

Lys Leu Pro Ser Leu Pro Leu Ser Lys

15

<210> 1726

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1726

Lys Leu Pro Ser Leu Pro Leu Ser Lys Met

1 5 10

<210> 1727

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1727

Lys Met Tyr Thr Thr Ser Met Ala Met

15

<210> 1728

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1728

Leu Leu Ala Ala Pro Ser Pro Ala Ser Arg

1 5 10

<210> 1729

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1729

Leu Leu Leu Ser Ala Asp Gln Gln Ala Ala

1 5 10

<210> 1730

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1730

Leu Leu Ser Ala Asp Gln Gln Ala Ala

15

<210> 1731

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1731

Leu Pro Ala Ser Asn Lys Leu Pro Ser

15

<210> 1732

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1732

Leu Pro Ala Ser Asn Lys Leu Pro Ser Leu

1 5 10

<210> 1733

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1733

Leu Pro Leu Pro Gln Leu Leu Leu Ser Ala

1 5 10

<210> 1734

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1734

Leu Pro Ser Leu Pro Leu Ser Lys Met

15

<210> 1735

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1735

Leu Ser Lys Met Tyr Thr Thr Ser Met

15

<210> 1736

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1736

Met Ala Leu Leu Pro Ser Gly Thr Lys

15

<210> 1737

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1737

Met Pro Ile Leu Pro Leu Pro Gln Leu

15

<210> 1738

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1738

Met Pro Ile Leu Pro Leu Pro Gln Leu Leu

1 5 10

<210> 1739

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1739

Met Tyr Thr Thr Ser Met Ala Met Pro Ile

1 5 10

<210> 1740

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1740

Pro Met Ala Ile Ser Ser Pro Pro Lys

15

<210> 1741

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1741

Gln Trp Met Ala His Met Ala Leu Leu

15

<210> 1742

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1742

Ser Lys Met Tyr Thr Thr Ser Met Ala Met

1 5 10

<210> 1743

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1743

Ser Met Ala Met Pro Ile Leu Pro Leu

15

<210> 1744

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1744

Ser Asn Lys Leu Pro Ser Leu Pro Leu

15

<210> 1745

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1745

Ser Pro Ala Ser Arg Leu Gln Cys Ile

15

<210> 1746

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1746

Ser Pro Pro Lys Ala Pro Leu Leu Ala Ala

1 5 10

<210> 1747

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1747

Ser Pro Ser Leu Pro Ala Ser Asn Lys Leu

1 5 10

<210> 1748

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1748

Tyr Thr Thr Ser Met Ala Met Pro Ile

15

<210> 1749

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1749

Tyr Thr Thr Ser Met Ala Met Pro Ile Leu

1 5 10

<210> 1750

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1750

Cys Leu Pro Gly Leu Thr His Pro Ala

15

<210> 1751

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1751

Gly Leu Thr His Pro Ala His Gln Pro Leu

1 5 10

<210> 1752

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1752

His Pro Ala His Gln Pro Leu Gly Ser Met

1 5 10

<210> 1753

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1753

Leu Thr His Pro Ala His Gln Pro Leu

15

<210> 1754

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1754

Arg Pro Thr Ser Arg Ala Arg Gln Ser Cys

1 5 10

<210> 1755

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1755

Arg Gln Ser Cys Cys Leu Pro Gly Leu

15

<210> 1756

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1756

Thr Ser Arg Ala Arg Gln Ser Cys Cys Leu

1 5 10

<210> 1757

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1757

Glu Leu Leu Cys Val Trp Val Ser Ser Ile

1 5 10

<210> 1758

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1758

Glu Trp Lys Val Lys Phe Pro Glu Leu

15

<210> 1759

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1759

Lys Phe Pro Glu Leu Leu Cys Val Trp

15

<210> 1760

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1760

Leu Leu Cys Val Trp Val Ser Ser Ile

15

<210> 1761

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1761

Leu Leu Thr Ser Ser Ser Arg Glu Trp Lys

1 5 10

<210> 1762

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1762

Leu Thr Ser Ser Ser Arg Glu Trp Lys

15

<210> 1763

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1763

Tyr Pro Ala Tyr Ser Lys Asp Ser Gly Leu

1 5 10

<210> 1764

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1764

Cys Leu Gln Cys Leu Trp Ala Leu Leu

15

<210> 1765

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1765

Cys Gln Trp Gly Pro Cys Leu Gln Cys Leu

1 5 10

<210> 1766

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1766

Gln Trp Gly Pro Cys Leu Gln Cys Leu

15

<210> 1767

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1767

Gln Trp Gly Pro Cys Leu Gln Cys Leu Trp

1 5 10

<210> 1768

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1768

Ala Ile Gln Pro Val Leu Trp Thr Thr

15

<210> 1769

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1769

Ala Leu Gln Pro Leu Gln Pro His Ala

15

<210> 1770

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1770

Asp Leu His Phe Cys Arg Ser Ser Ile Met

1 5 10

<210> 1771

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1771

Glu Pro His Leu Ala Leu Gln Pro Leu

15

<210> 1772

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1772

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 1773

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1773

Phe Ala Thr Leu Gln Arg Ser Ser Leu

15

<210> 1774

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1774

Phe Leu Lys Ala Glu Ser Lys Ile Met

15

<210> 1775

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1775

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10

<210> 1776

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1776

Gly Pro Pro Ala Arg Val Pro Ala Val

15

<210> 1777

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1777

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10

<210> 1778

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1778

Lys Ile Met Phe Ala Thr Leu Gln Arg

15

<210> 1779

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1779

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 1780

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1780

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 1781

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1781

Leu His Phe Cys Arg Ser Ser Ile Met

15

<210> 1782

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1782

Leu Gln His Gly His Arg His Gly Leu

15

<210> 1783

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1783

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 1784

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1784

Met Phe Leu Lys Ala Glu Ser Lys Ile

15

<210> 1785

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1785

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 1786

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1786

Gln Pro Val Leu Trp Thr Thr Pro Pro Leu

1 5 10

<210> 1787

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1787

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 1788

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1788

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

1 5 10

<210> 1789

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1789

Val Leu Pro Glu Pro His Leu Ala Leu

15

<210> 1790

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1790

Val Pro Ala Val Pro Phe Asp Leu His Phe

1 5 10

<210> 1791

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1791

Tyr Met Phe Leu Lys Ala Glu Ser Lys

15

<210> 1792

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1792

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 1793

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1793

Ala Pro Gly Pro Arg Gly Arg Thr Cys

15

<210> 1794

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1794

Cys Leu Arg Ser His Thr Cys Pro Pro Arg

1 5 10

<210> 1795

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1795

Cys Leu Trp Cys His Ala Cys Leu His Arg

1 5 10

<210> 1796

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1796

Cys Pro His Leu Gly Ser His Pro Cys

15

<210> 1797

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1797

Cys Pro Leu Gly Leu Lys Ser Pro Leu

15

<210> 1798

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1798

Cys Pro Arg Ser Cys Arg Cys Pro His

15

<210> 1799

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1799

Cys Pro Arg Ser Cys Arg Cys Pro His Leu

1 5 10

<210> 1800

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1800

Cys Ser Leu Pro Leu Gly Asn His Pro Tyr

1 5 10

<210> 1801

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1801

Gly Leu Arg Asn Arg Ile Cys Pro Leu

15

<210> 1802

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1802

Gly Leu Arg Ser His Thr Tyr Leu Arg

15

<210> 1803

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1803

Gly Leu Arg Ser His Thr Tyr Leu Arg Arg

1 5 10

<210> 1804

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1804

Gly Pro Arg Gly Arg Thr Cys His Pro Gly

1 5 10

<210> 1805

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1805

His Leu Gly Ser His Pro Cys Arg Leu

15

<210> 1806

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1806

His Leu Arg Leu His Ala Ser Pro His

15

<210> 1807

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1807

His Leu Arg Ser Cys Pro Cys Ser Leu

15

<210> 1808

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1808

His Leu Arg Thr His Leu Leu Pro His

15

<210> 1809

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1809

His Leu Arg Thr His Leu Leu Pro His His

1 5 10

<210> 1810

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1810

His Leu Arg Tyr Arg Ala Tyr Pro Pro

15

<210> 1811

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1811

His Leu Arg Tyr Arg Ala Tyr Pro Pro Cys

1 5 10

<210> 1812

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1812

His Pro His His Leu Arg Thr His Leu

15

<210> 1813

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1813

His Pro His His Leu Arg Thr His Leu Leu

1 5 10

<210> 1814

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1814

His Thr Tyr Leu Arg Arg Leu Arg Ser His

1 5 10

<210> 1815

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1815

Leu Pro Cys Pro His Arg Leu Arg Ser Leu

1 5 10

<210> 1816

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1816

Leu Pro His His Arg Arg Thr Arg Ser Cys

1 5 10

<210> 1817

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1817

Leu Pro Leu Gly Asn His Pro Tyr Leu

15

<210> 1818

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1818

Leu Pro Arg Pro Leu His Leu Arg Leu

15

<210> 1819

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1819

Asn Leu Arg Asn His Thr Cys Pro Pro

15

<210> 1820

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1820

Pro Pro Arg Leu Arg Ser Arg Thr Cys Leu

1 5 10

<210> 1821

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1821

Arg Leu His Ala Ser Pro His His Leu

15

<210> 1822

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1822

Arg Leu His Ala Ser Pro His His Leu Arg

1 5 10

<210> 1823

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1823

Arg Leu Arg Asp His Ile Cys Pro Leu

15

<210> 1824

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1824

Arg Leu Arg Asn Leu Pro Cys Pro His

15

<210> 1825

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1825

Arg Leu Arg Asn Leu Pro Cys Pro His Arg

1 5 10

<210> 1826

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1826

Arg Leu Arg Ser His Thr Cys Pro Pro

15

<210> 1827

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1827

Arg Leu Arg Ser Leu Pro Arg Pro Leu

15

<210> 1828

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1828

Arg Leu Arg Ser Leu Pro Arg Pro Leu His

1 5 10

<210> 1829

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1829

Arg Leu Arg Ser Arg Thr Cys Leu Leu

15

<210> 1830

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1830

Arg Asn Arg Ile Cys Pro Leu Ser Leu

15

<210> 1831

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1831

Arg Pro Leu His Leu Arg Leu His Ala

15

<210> 1832

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1832

Arg Pro Leu His Leu Arg Leu His Ala Ser

1 5 10

<210> 1833

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1833

Arg Ser His Ala Cys Pro Pro Gly Leu Arg

1 5 10

<210> 1834

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1834

Arg Ser His Ala Cys Pro Pro Asn Leu Arg

1 5 10

<210> 1835

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1835

Arg Ser His Ala Tyr Ala Leu Cys Leu Arg

1 5 10

<210> 1836

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1836

Arg Ser His Pro Cys Cys His Tyr Leu Arg

1 5 10

<210> 1837

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1837

Arg Ser His Pro Cys Pro Leu Gly Leu Lys

1 5 10

<210> 1838

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1838

Arg Ser His Thr Cys Pro Pro Ser Leu Arg

1 5 10

<210> 1839

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1839

Arg Ser Leu Pro Arg Pro Leu His Leu Arg

1 5 10

<210> 1840

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1840

Arg Ser Arg Thr Cys Leu Leu Cys Leu

15

<210> 1841

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1841

Arg Ser Arg Thr Cys Leu Leu Cys Leu Arg

1 5 10

<210> 1842

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1842

Arg Ser Arg Thr Cys Pro Pro Gly Leu

15

<210> 1843

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1843

Arg Ser Arg Thr Cys Pro Pro Gly Leu Arg

1 5 10

<210> 1844

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1844

Arg Thr His Leu Leu Pro His His Arg Arg

1 5 10

<210> 1845

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1845

Arg Thr Arg Ser Cys Pro Cys Arg Trp Arg

1 5 10

<210> 1846

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1846

Arg Tyr Arg Ala Tyr Pro Pro Cys Leu

15

<210> 1847

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1847

Arg Tyr Arg Ala Tyr Pro Pro Cys Leu Trp

1 5 10

<210> 1848

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1848

Ser Leu Gly Asn His Leu Cys Pro Leu

15

<210> 1849

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1849

Ser Leu Pro Leu Gly Asn His Pro Tyr Leu

1 5 10

<210> 1850

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1850

Ser Leu Pro Arg Pro Leu His Leu Arg Leu

1 5 10

<210> 1851

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1851

Ser Leu Arg Asn Cys Thr Cys Pro Pro Arg

1 5 10

<210> 1852

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1852

Ser Leu Arg Ser His Ala Tyr Ala Leu

15

<210> 1853

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1853

Ser Leu Arg Ser His Pro Cys Pro Leu

15

<210> 1854

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1854

Ser Pro His His Leu Arg Thr Pro Pro

15

<210> 1855

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1855

Ser Pro His His Leu Arg Thr Pro Pro His

1 5 10

<210> 1856

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1856

Ser Pro Leu Arg Ser Gln Ala Asn Ala Leu

1 5 10

<210> 1857

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1857

Tyr Leu Arg Arg Leu Arg Ser His Thr Cys

1 5 10

<210> 1858

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1858

Tyr Leu Arg Ser Arg Asn Ser Ala Pro

15

<210> 1859

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1859

Tyr Leu Arg Ser Arg Asn Ser Ala Pro Gly

1 5 10

<210> 1860

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1860

Ala Leu Ala Pro Thr Leu Thr His Met

15

<210> 1861

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1861

Ala Leu Ala Pro Thr Leu Thr His Met Leu

1 5 10

<210> 1862

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1862

Leu Leu Gln Val Thr Gln Thr Ser Phe Ala

1 5 10

<210> 1863

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1863

Leu Gln Val Thr Gln Thr Ser Phe Ala Leu

1 5 10

<210> 1864

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1864

Arg Leu Trp His Leu Leu Leu Gln Val

15

<210> 1865

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1865

Arg Leu Trp His Leu Leu Leu Gln Val Thr

1 5 10

<210> 1866

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1866

Cys Thr Gln Leu Ala Arg Phe Phe Pro Ile

1 5 10

<210> 1867

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1867

Phe Phe Pro Ile Thr Pro Pro Val Trp

15

<210> 1868

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1868

Phe Pro Ile Thr Pro Pro Val Trp His Ile

1 5 10

<210> 1869

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1869

Gly Pro Arg Met Gln Leu Cys Thr Gln Leu

1 5 10

<210> 1870

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1870

Ile Thr Pro Pro Val Trp His Ile Leu

15

<210> 1871

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1871

Leu Ala Leu Gly Pro Arg Met Gln Leu

15

<210> 1872

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1872

Met Gln Leu Cys Thr Gln Leu Ala Arg Phe

1 5 10

<210> 1873

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1873

Arg Phe Phe Pro Ile Thr Pro Pro Val

15

<210> 1874

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1874

Arg Phe Phe Pro Ile Thr Pro Pro Val Trp

1 5 10

<210> 1875

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1875

Arg Met Gln Leu Cys Thr Gln Leu Ala

15

<210> 1876

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1876

Arg Met Gln Leu Cys Thr Gln Leu Ala Arg

1 5 10

<210> 1877

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1877

Ser Pro Pro Leu Ala Leu Gly Pro Arg Met

1 5 10

<210> 1878

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1878

Thr Gln Leu Ala Arg Phe Phe Pro Ile

15

<210> 1879

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1879

Lys Ser Arg Gln Asn His Leu Gln Leu

15

<210> 1880

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1880

Ala Leu Lys Lys Leu Arg Ser Pro Leu

15

<210> 1881

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1881

His Leu Gln Leu Lys Ser Cys Arg Arg Lys

1 5 10

<210> 1882

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1882

Lys Ile Ser Asn Trp Ser Leu Lys Lys

15

<210> 1883

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1883

Lys Ile Ser Asn Trp Ser Leu Lys Lys Val

1 5 10

<210> 1884

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1884

Lys Leu Arg Ser Pro Leu Trp Ile Phe

15

<210> 1885

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1885

Lys Ser Arg Gln Asn His Leu Gln Leu Lys

1 5 10

<210> 1886

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1886

Asn Trp Ser Leu Lys Lys Val Pro Ala Leu

1 5 10

<210> 1887

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1887

Ser Leu Lys Lys Val Pro Ala Leu Lys

15

<210> 1888

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1888

Ser Leu Lys Lys Val Pro Ala Leu Lys Lys

1 5 10

<210> 1889

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1889

Ser Gln Lys Ser Arg Gln Asn His Leu

15

<210> 1890

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1890

Trp Ser Leu Lys Lys Val Pro Ala Leu

15

<210> 1891

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1891

Trp Ser Leu Lys Lys Val Pro Ala Leu Lys

1 5 10

<210> 1892

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1892

Lys Leu Pro Glu Cys Gln Arg Leu Leu

15

<210> 1893

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1893

Lys Pro Thr Arg Ala Ala Thr Val Ser Val

1 5 10

<210> 1894

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1894

Leu Pro Pro Trp Pro Leu His Gln Gln Leu

1 5 10

<210> 1895

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1895

Leu Pro Arg Lys Pro Thr Arg Ala Ala

15

<210> 1896

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1896

Leu Pro Arg Lys Pro Thr Arg Ala Ala Thr

1 5 10

<210> 1897

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1897

Gln Gln Leu Leu His Arg Arg Pro Leu

15

<210> 1898

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1898

Arg Leu Leu Pro Pro Trp Pro Leu His

15

<210> 1899

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1899

Ala Pro Ala Ser Ala Pro Trp Pro Ser Thr

1 5 10

<210> 1900

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1900

Ala Pro Trp Pro Ser Thr Ser Ser His

15

<210> 1901

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1901

Arg Pro Ala Pro Ala Ser Ala Pro Trp

15

<210> 1902

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1902

Trp Pro Ser Thr Ser Ser His Ser Thr

15

<210> 1903

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1903

Arg Val Gln Asn Gln Gly His Leu Leu

15

<210> 1904

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1904

Phe Leu Pro Ile Ser His Cys Gln Cys Ile

1 5 10

<210> 1905

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1905

Phe Trp Leu Thr Lys Leu Asn Tyr Leu

15

<210> 1906

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1906

His Leu Ser Met Leu Thr Asp Ser Leu

15

<210> 1907

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1907

His Thr Met Gly Phe Trp Leu Thr Lys

15

<210> 1908

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1908

His Thr Met Gly Phe Trp Leu Thr Lys Leu

1 5 10

<210> 1909

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1909

Lys Leu Asn Tyr Leu Cys His Leu Ser Met

1 5 10

<210> 1910

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1910

Leu Pro Ile Ser His Cys Gln Cys Ile

15

<210> 1911

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1911

Leu Pro Ile Ser His Cys Gln Cys Ile Leu

1 5 10

<210> 1912

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1912

Leu Thr Asp Ser Leu Phe Leu Pro Ile

15

<210> 1913

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1913

Leu Thr Lys Leu Asn Tyr Leu Cys His Leu

1 5 10

<210> 1914

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1914

Met Leu Thr Asp Ser Leu Phe Leu Pro Ile

1 5 10

<210> 1915

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1915

Met Gln Gly His Thr Met Gly Phe Trp Leu

1 5 10

<210> 1916

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1916

Asn Tyr Leu Cys His Leu Ser Met Leu

15

<210> 1917

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1917

Ser Met Leu Thr Asp Ser Leu Phe Leu

15

<210> 1918

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1918

Thr Met Gly Phe Trp Leu Thr Lys Leu

15

<210> 1919

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1919

Tyr Leu Cys His Leu Ser Met Leu Thr

15

<210> 1920

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1920

Ile Leu Asp Glu Ala Tyr Val Met Ala Tyr

1 5 10

<210> 1921

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1921

Val Met Ala Tyr Val Met Ala Gly Val

15

<210> 1922

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1922

Tyr Val Met Ala Tyr Val Met Ala Gly

15

<210> 1923

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1923

Tyr Val Met Ala Tyr Val Met Ala Gly Val

1 5 10

<210> 1924

<211> 23

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 1924

Ile Phe Ile Ile Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10 15

Leu Arg Glu Met Arg His Arg

20

<210> 1925

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 1925

Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 1926

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1926

Ala Asn Gly Ser Leu Leu Asn Tyr Leu

15

<210> 1927

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1927

Ala Asn Gly Ser Leu Leu Asn Tyr Leu Arg

1 5 10

<210> 1928

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 1928

Glu Tyr Met Ala Asn Gly Ser Leu

15

<210> 1929

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1929

Glu Tyr Met Ala Asn Gly Ser Leu Leu Asn

1 5 10

<210> 1930

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 1930

Glu Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 1931

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 1931

Gly Ser Leu Leu Asn Tyr Leu Arg

15

<210> 1932

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1932

Gly Ser Leu Leu Asn Tyr Leu Arg Glu Met

1 5 10

<210> 1933

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1933

Ile Thr Glu Tyr Met Ala Asn Gly Ser

15

<210> 1934

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1934

Ile Thr Glu Tyr Met Ala Asn Gly Ser Leu

1 5 10

<210> 1935

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 1935

Ile Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu

1 5 10

<210> 1936

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1936

Met Ala Asn Gly Ser Leu Leu Asn Tyr Leu

1 5 10

<210> 1937

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 1937

Met Ala Asn Gly Ser Leu Leu Asn Tyr Leu Arg

1 5 10

<210> 1938

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 1938

Asn Gly Ser Leu Leu Asn Tyr Leu

15

<210> 1939

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 1939

Asn Gly Ser Leu Leu Asn Tyr Leu

15

<210> 1940

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1940

Ser Leu Leu Asn Tyr Leu Arg Glu Met Arg

1 5 10

<210> 1941

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1941

Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu

1 5 10

<210> 1942

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 1942

Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 1943

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 1943

Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 1944

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1944

Tyr Met Ala Asn Gly Ser Leu Leu Asn

15

<210> 1945

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 1945

Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 1946

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1946

Ala Asn Gly Ser Leu Leu Asn Tyr Leu

15

<210> 1947

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1947

Ala Asn Gly Ser Leu Leu Asn Tyr Leu Arg

1 5 10

<210> 1948

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 1948

Glu Tyr Met Ala Asn Gly Ser Leu

15

<210> 1949

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1949

Glu Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 1950

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1950

Glu Tyr Met Ala Asn Gly Ser Leu Leu Asn

1 5 10

<210> 1951

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 1951

Glu Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 1952

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 1952

Gly Ser Leu Leu Asn Tyr Leu Arg

15

<210> 1953

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1953

Gly Ser Leu Leu Asn Tyr Leu Arg Glu Met

1 5 10

<210> 1954

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1954

Ile Thr Glu Tyr Met Ala Asn Gly Ser

15

<210> 1955

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1955

Ile Thr Glu Tyr Met Ala Asn Gly Ser Leu

1 5 10

<210> 1956

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 1956

Ile Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu

1 5 10

<210> 1957

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1957

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 1958

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1958

Met Ala Asn Gly Ser Leu Leu Asn Tyr Leu

1 5 10

<210> 1959

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 1959

Met Ala Asn Gly Ser Leu Leu Asn Tyr Leu Arg

1 5 10

<210> 1960

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 1960

Asn Gly Ser Leu Leu Asn Tyr Leu

15

<210> 1961

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1961

Asn Gly Ser Leu Leu Asn Tyr Leu Arg

15

<210> 1962

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1962

Ser Leu Leu Asn Tyr Leu Arg Glu Met

15

<210> 1963

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1963

Ser Leu Leu Asn Tyr Leu Arg Glu Met Arg

1 5 10

<210> 1964

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1964

Thr Glu Tyr Met Ala Asn Gly Ser Leu

15

<210> 1965

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1965

Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu

1 5 10

<210> 1966

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 1966

Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 1967

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 1967

Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 1968

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 1968

Tyr Met Ala Asn Gly Ser Leu Leu Asn

15

<210> 1969

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 1969

Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 1970

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1970

Val Ala Asp Gly Leu Ile Thr Thr Leu His Tyr Pro Ala Pro Lys Arg

1 5 10 15

Asn Lys Pro Thr Val Tyr Gly Val Ser Pro Asn Tyr Asp Lys Trp Glu

20 25 30

Met Glu Arg Thr Asp Ile Thr Met Lys His Lys Leu Gly Gly Gly Gln

35 40 45

Tyr Gly Lys Val Tyr Glu Gly Val Trp Lys Lys Tyr Ser Leu Thr Val

50 55 60

Ala Val Lys Thr Leu Lys Glu Asp Thr Met Glu Val Glu Glu Phe Leu

65 70 75 80

Lys Glu Ala Ala Val Met Lys Glu Ile Lys His Pro Asn Leu Val Gln

85 90 95

Leu Leu Gly Val Cys

100

<210> 1971

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1971

Val Ala Asp Gly Leu Ile Thr Thr Leu His Tyr Pro Ala Pro Lys Arg

1 5 10 15

Asn Lys Pro Thr Val Tyr Gly Val Ser Pro Asn Tyr Asp Lys Trp Glu

20 25 30

Met Glu Arg Thr Asp Ile Thr Met Lys His Lys Leu Gly Gly Gly Gln

35 40 45

Tyr Gly Val Val Tyr Glu Gly Val Trp Lys Lys Tyr Ser Leu Thr Val

50 55 60

Ala Val Lys Thr Leu Lys Glu Asp Thr Met Glu Val Glu Glu Phe Leu

65 70 75 80

Lys Glu Ala Ala Val Met Lys Glu Ile Lys His Pro Asn Leu Val Gln

85 90 95

Leu Leu Gly Val Cys

100

<210> 1972

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1972

Leu Leu Gly Val Cys Thr Arg Glu Pro Pro Phe Tyr Ile Ile Thr Glu

1 5 10 15

Phe Met Thr Tyr Gly Asn Leu Leu Asp Tyr Leu Arg Glu Cys Asn Arg

20 25 30

Gln Glu Val Asn Ala Val Val Leu Leu Tyr Met Ala Thr Gln Ile Ser

35 40 45

Ser Ala Thr Glu Tyr Leu Glu Lys Lys Asn Phe Ile His Arg Asp Leu

50 55 60

Ala Ala Arg Asn Cys Leu Val Gly Glu Asn His Leu Val Lys Val Ala

65 70 75 80

Asp Phe Gly Leu Ser Arg Leu Met Thr Gly Asp Thr Tyr Thr Ala His

85 90 95

Ala Gly Ala Lys Phe

100

<210> 1973

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1973

Ser Leu Thr Val Ala Val Lys Thr Leu Lys Glu Asp Thr Met Glu Val

1 5 10 15

Glu Glu Phe Leu Lys Glu Ala Ala Val Met Lys Glu Ile Lys His Pro

20 25 30

Asn Leu Val Gln Leu Leu Gly Val Cys Thr Arg Glu Pro Pro Phe Tyr

35 40 45

Ile Ile Ile Glu Phe Met Thr Tyr Gly Asn Leu Leu Asp Tyr Leu Arg

50 55 60

Glu Cys Asn Arg Gln Glu Val Asn Ala Val Val Leu Leu Tyr Met Ala

65 70 75 80

Thr Gln Ile Ser Ser Ala Met Glu Tyr Leu Glu Lys Lys Asn Phe Ile

85 90 95

His Arg Asp Leu Ala

100

<210> 1974

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1974

Ser Thr Val Ala Asp Gly Leu Ile Thr Thr Leu His Tyr Pro Ala Pro

1 5 10 15

Lys Arg Asn Lys Pro Thr Val Tyr Gly Val Ser Pro Asn Tyr Asp Lys

20 25 30

Trp Glu Met Glu Arg Thr Asp Ile Thr Met Lys His Lys Leu Gly Gly

35 40 45

Gly Gln His Gly Glu Val Tyr Glu Gly Val Trp Lys Lys Tyr Ser Leu

50 55 60

Thr Val Ala Val Lys Thr Leu Lys Glu Asp Thr Met Glu Val Glu Glu

65 70 75 80

Phe Leu Lys Glu Ala Ala Val Met Lys Glu Ile Lys His Pro Asn Leu

85 90 95

Val Gln Leu Leu Gly

100

<210> 1975

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1975

Ser Ser Leu Ala Met Leu Asp Leu Leu His Val Ala Arg Asp Ile Ala

1 5 10 15

Cys Gly Cys Gln Tyr Leu Glu Glu Asn His Phe Ile His Arg Asp Ile

20 25 30

Ala Ala Arg Asn Cys Leu Leu Thr Cys Pro Gly Pro Gly Arg Val Ala

35 40 45

Lys Ile Ala Asp Phe Gly Met Ala Arg Asp Ile Tyr Arg Ala Ser Tyr

50 55 60

Tyr Arg Lys Gly Gly Cys Ala Met Leu Pro Val Lys Trp Met Pro Pro

65 70 75 80

Glu Ala Phe Met Glu Gly Ile Phe Thr Ser Lys Thr Asp Thr Trp Ser

85 90 95

Phe Gly Val Leu Leu

100

<210> 1976

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1976

Gln Val Ala Val Lys Thr Leu Pro Glu Val Cys Ser Glu Gln Asp Glu

1 5 10 15

Leu Asp Phe Leu Met Glu Ala Leu Ile Ile Ser Lys Phe Asn His Gln

20 25 30

Asn Ile Val Arg Cys Ile Gly Val Ser Leu Gln Ser Leu Pro Arg Phe

35 40 45

Ile Leu Met Glu Leu Met Ala Gly Gly Asp Leu Lys Ser Phe Leu Arg

50 55 60

Glu Thr Arg Pro Arg Pro Ser Gln Pro Ser Ser Leu Ala Met Leu Asp

65 70 75 80

Leu Leu His Val Ala Arg Asp Ile Ala Cys Gly Cys Gln Tyr Leu Glu

85 90 95

Glu Asn His Phe Ile

100

<210> 1977

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1977

Met Ile Lys Leu Ile Asp Ile Ala Arg Gln Thr Ala Gln Gly Met Asp

1 5 10 15

Tyr Leu His Ala Lys Ser Ile Ile His Arg Asp Leu Lys Ser Asn Asn

20 25 30

Ile Phe Leu His Glu Asp Leu Thr Val Lys Ile Gly Asp Phe Gly Leu

35 40 45

Ala Thr Glu Lys Ser Arg Trp Ser Gly Ser His Gln Phe Glu Gln Leu

50 55 60

Ser Gly Ser Ile Leu Trp Met Ala Pro Glu Val Ile Arg Met Gln Asp

65 70 75 80

Lys Asn Pro Tyr Ser Phe Gln Ser Asp Val Tyr Ala Phe Gly Ile Val

85 90 95

Leu Tyr Glu Leu Met

100

<210> 1978

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1978

Met Ile Lys Glu Gly Ser Met Ser Glu Asp Glu Phe Ile Glu Glu Ala

1 5 10 15

Lys Val Met Met Asn Leu Ser His Glu Lys Leu Val Gln Leu Tyr Gly

20 25 30

Val Cys Thr Lys Gln Arg Pro Ile Phe Ile Ile Thr Glu Tyr Met Ala

35 40 45

Asn Gly Ser Leu Leu Asn Tyr Leu Arg Glu Met Arg His Arg Phe Gln

50 55 60

Thr Gln Gln Leu Leu Glu Met Cys Lys Asp Val Cys Glu Ala Met Glu

65 70 75 80

Tyr Leu Glu Ser Lys Gln Phe Leu His Arg Asp Leu Ala Ala Arg Asn

85 90 95

Cys Leu Val Asn Asp

100

<210> 1979

<211> 93

<212> PROTEIN

<213> Homo sapiens

<400> 1979

Met Gly Phe Gly Asp Leu Lys Ser Pro Ala Gly Leu Gln Val Leu Asn

1 5 10 15

Asp Tyr Leu Ala Asp Lys Ser Tyr Ile Glu Gly Tyr Val Pro Ser Gln

20 25 30

Ala Asp Val Ala Val Phe Glu Ala Val Ser Gly Pro Pro Pro Ala Asp

35 40 45

Leu Cys His Ala Leu Arg Trp Tyr Asn His Ile Lys Ser Tyr Glu Lys

50 55 60

Glu Lys Ala Ser Leu Pro Gly Val Lys Lys Ala Leu Gly Lys Tyr Gly

65 70 75 80

Pro Ala Asp Val Glu Asp Thr Thr Gly Ser Gly Ala Thr

85 90

<210> 1980

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1980

Glu Arg Cys Glu Val Val Met Gly Asn Leu Glu Ile Val Leu Thr Gly

1 5 10 15

His Asn Ala Asp Leu Ser Phe Leu Gln Trp Ile Arg Glu Val Thr Gly

20 25 30

Tyr Val Leu Val Ala Met Asn Glu Phe Ser Thr Leu Pro Leu Pro Asn

35 40 45

Leu Arg Met Val Arg Gly Thr Gln Val Tyr Asp Gly Lys Phe Ala Ile

50 55 60

Phe Val Met Leu Asn Tyr Asn Thr Asn Ser Ser His Ala Leu Arg Gln

65 70 75 80

Leu Arg Leu Thr Gln Leu Thr Glu Ile Leu Ser Gly Gly Val Tyr Ile

85 90 95

Glu Lys Asn Asp Lys

100

<210> 1981

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1981

His Leu Met Ala Lys Ala Gly Leu Thr Leu Gln Gln Gln His Gln Arg

1 5 10 15

Leu Ala Gln Leu Leu Leu Ile Leu Ser His Ile Arg His Met Ser Asn

20 25 30

Lys Gly Met Glu His Leu Tyr Ser Met Lys Cys Lys Asn Val Val Pro

35 40 45

Leu Tyr Gly Leu Leu Leu Glu Met Leu Asp Ala His Arg Leu His Ala

50 55 60

Pro Thr Ser Arg Gly Gly Ala Ser Val Glu Glu Thr Asp Gln Ser His

65 70 75 80

Leu Ala Thr Ala Gly Ser Thr Ser Ser His Ser Leu Gln Lys Tyr Tyr

85 90 95

Ile Thr Gly Glu Ala

100

<210> 1982

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1982

Asn Gln Gly Lys Cys Val Glu Gly Met Val Glu Ile Phe Asp Met Leu

1 5 10 15

Leu Ala Thr Ser Ser Arg Phe Arg Met Met Asn Leu Gln Gly Glu Glu

20 25 30

Phe Val Cys Leu Lys Ser Ile Ile Leu Leu Asn Ser Gly Val Tyr Thr

35 40 45

Phe Leu Pro Ser Thr Leu Lys Ser Leu Glu Glu Lys Asp His Ile His

50 55 60

Arg Val Leu Asp Lys Ile Thr Asp Thr Leu Ile His Leu Met Ala Lys

65 70 75 80

Ala Gly Leu Thr Leu Gln Gln Gln His Gln Arg Leu Ala Gln Leu Leu

85 90 95

Leu Ile Leu Ser His

100

<210> 1983

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1983

Ile His Leu Met Ala Lys Ala Gly Leu Thr Leu Gln Gln Gln His Gln

1 5 10 15

Arg Leu Ala Gln Leu Leu Leu Ile Leu Ser His Ile Arg His Met Ser

20 25 30

Asn Lys Gly Met Glu His Leu Tyr Ser Met Lys Cys Lys Asn Val Val

35 40 45

Pro Leu Cys Asp Leu Leu Leu Glu Met Leu Asp Ala His Arg Leu His

50 55 60

Ala Pro Thr Ser Arg Gly Gly Ala Ser Val Glu Glu Thr Asp Gln Ser

65 70 75 80

His Leu Ala Thr Ala Gly Ser Thr Ser Ser His Ser Leu Gln Lys Tyr

85 90 95

Tyr Ile Thr Gly Glu

100

<210> 1984

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1984

Ile His Leu Met Ala Lys Ala Gly Leu Thr Leu Gln Gln Gln His Gln

1 5 10 15

Arg Leu Ala Gln Leu Leu Leu Ile Leu Ser His Ile Arg His Met Ser

20 25 30

Asn Lys Gly Met Glu His Leu Tyr Ser Met Lys Cys Lys Asn Val Val

35 40 45

Pro Leu Asn Asp Leu Leu Leu Glu Met Leu Asp Ala His Arg Leu His

50 55 60

Ala Pro Thr Ser Arg Gly Gly Ala Ser Val Glu Glu Thr Asp Gln Ser

65 70 75 80

His Leu Ala Thr Ala Gly Ser Thr Ser Ser His Ser Leu Gln Lys Tyr

85 90 95

Tyr Ile Thr Gly Glu

100

<210> 1985

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1985

Ile His Leu Met Ala Lys Ala Gly Leu Thr Leu Gln Gln Gln His Gln

1 5 10 15

Arg Leu Ala Gln Leu Leu Leu Ile Leu Ser His Ile Arg His Met Ser

20 25 30

Asn Lys Gly Met Glu His Leu Tyr Ser Met Lys Cys Lys Asn Val Val

35 40 45

Pro Leu Ser Asp Leu Leu Leu Glu Met Leu Asp Ala His Arg Leu His

50 55 60

Ala Pro Thr Ser Arg Gly Gly Ala Ser Val Glu Glu Thr Asp Gln Ser

65 70 75 80

His Leu Ala Thr Ala Gly Ser Thr Ser Ser His Ser Leu Gln Lys Tyr

85 90 95

Tyr Ile Thr Gly Glu

100

<210> 1986

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1986

His Arg Ile Gly Gly Ile Lys Leu Arg His Gln Gln Trp Ser Leu Val

1 5 10 15

Met Glu Ser Val Val Pro Ser Asp Arg Gly Asn Tyr Thr Cys Val Val

20 25 30

Glu Asn Lys Phe Gly Ser Ile Arg Gln Thr Tyr Thr Leu Asp Val Leu

35 40 45

Glu Arg Cys Pro His Arg Pro Ile Leu Gln Ala Gly Leu Pro Ala Asn

50 55 60

Gln Thr Ala Val Leu Gly Ser Asp Val Glu Phe His Cys Lys Val Tyr

65 70 75 80

Ser Asp Ala Gln Pro His Ile Gln Trp Leu Lys His Val Glu Val Asn

85 90 95

Gly Ser Lys Val Gly

100

<210> 1987

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1987

Ala Val Lys Leu Ser Asp Ser Arg Ile Ala Leu Lys Ser Gly Tyr Gly

1 5 10 15

Lys Tyr Leu Gly Ile Asn Ser Asp Glu Leu Val Gly His Ser Asp Ala

20 25 30

Ile Gly Pro Arg Glu Gln Trp Glu Pro Val Phe Gln Asn Gly Lys Met

35 40 45

Ala Leu Ser Ala Ser Asn Ser Cys Phe Ile Arg Cys Asn Glu Ala Gly

50 55 60

Asp Ile Glu Ala Lys Ser Lys Thr Ala Gly Glu Glu Glu Met Ile Lys

65 70 75 80

Ile Arg Ser Cys Ala Glu Lys Glu Thr Lys Lys Lys Asp Asp Ile Pro

85 90 95

Glu Glu Asp Lys Gly

100

<210> 1988

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1988

Gly Ser Gly Ala Phe Gly Thr Val Tyr Lys Gly Ile Trp Ile Pro Asp

1 5 10 15

Gly Glu Asn Val Lys Ile Pro Val Ala Ile Lys Val Leu Arg Glu Asn

20 25 30

Thr Ser Pro Lys Ala Asn Lys Glu Ile Leu Asp Glu Ala Tyr Val Met

35 40 45

Ala Gly Leu Gly Ser Pro Tyr Val Ser Arg Leu Leu Gly Ile Cys Leu

50 55 60

Thr Ser Thr Val Gln Leu Val Thr Gln Leu Met Pro Tyr Gly Cys Leu

65 70 75 80

Leu Asp His Val Arg Glu Asn Arg Gly Arg Leu Gly Ser Gln Asp Leu

85 90 95

Leu Asn Trp Cys Met

100

<210> 1989

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1989

Arg Val Glu Glu Phe Lys Leu Lys Gln Met Trp Lys Ser Pro Asn Gly

1 5 10 15

Thr Ile Arg Asn Ile Leu Gly Gly Thr Val Phe Arg Glu Ala Ile Ile

20 25 30

Cys Lys Asn Ile Pro Arg Leu Val Ser Gly Trp Val Lys Pro Ile Ile

35 40 45

Ile Gly His His Ala Tyr Gly Asp Gln Tyr Arg Ala Thr Asp Phe Val

50 55 60

Val Pro Gly Pro Gly Lys Val Glu Ile Thr Tyr Thr Pro Ser Asp Gly

65 70 75 80

Thr Gln Lys Val Thr Tyr Leu Val His Asn Phe Glu Glu Gly Gly Gly

85 90 95

Val Ala Met Gly Met

100

<210> 1990

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1990

Arg Val Glu Glu Phe Lys Leu Lys Gln Met Trp Lys Ser Pro Asn Gly

1 5 10 15

Thr Ile Arg Asn Ile Leu Gly Gly Thr Val Phe Arg Glu Ala Ile Ile

20 25 30

Cys Lys Asn Ile Pro Arg Leu Val Ser Gly Trp Val Lys Pro Ile Ile

35 40 45

Ile Gly Cys His Ala Tyr Gly Asp Gln Tyr Arg Ala Thr Asp Phe Val

50 55 60

Val Pro Gly Pro Gly Lys Val Glu Ile Thr Tyr Thr Pro Ser Asp Gly

65 70 75 80

Thr Gln Lys Val Thr Tyr Leu Val His Asn Phe Glu Glu Gly Gly Gly

85 90 95

Val Ala Met Gly Met

100

<210> 1991

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1991

Arg Val Glu Glu Phe Lys Leu Lys Gln Met Trp Lys Ser Pro Asn Gly

1 5 10 15

Thr Ile Arg Asn Ile Leu Gly Gly Thr Val Phe Arg Glu Ala Ile Ile

20 25 30

Cys Lys Asn Ile Pro Arg Leu Val Ser Gly Trp Val Lys Pro Ile Ile

35 40 45

Ile Gly Gly His Ala Tyr Gly Asp Gln Tyr Arg Ala Thr Asp Phe Val

50 55 60

Val Pro Gly Pro Gly Lys Val Glu Ile Thr Tyr Thr Pro Ser Asp Gly

65 70 75 80

Thr Gln Lys Val Thr Tyr Leu Val His Asn Phe Glu Glu Gly Gly Gly

85 90 95

Val Ala Met Gly Met

100

<210> 1992

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1992

Arg Val Glu Glu Phe Lys Leu Lys Gln Met Trp Lys Ser Pro Asn Gly

1 5 10 15

Thr Ile Arg Asn Ile Leu Gly Gly Thr Val Phe Arg Glu Ala Ile Ile

20 25 30

Cys Lys Asn Ile Pro Arg Leu Val Ser Gly Trp Val Lys Pro Ile Ile

35 40 45

Ile Gly Ser His Ala Tyr Gly Asp Gln Tyr Arg Ala Thr Asp Phe Val

50 55 60

Val Pro Gly Pro Gly Lys Val Glu Ile Thr Tyr Thr Pro Ser Asp Gly

65 70 75 80

Thr Gln Lys Val Thr Tyr Leu Val His Asn Phe Glu Glu Gly Gly Gly

85 90 95

Val Ala Met Gly Met

100

<210> 1993

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1993

Val Ala Val Lys Met Leu Lys Pro Ser Ala His Leu Thr Glu Arg Glu

1 5 10 15

Ala Leu Met Ser Glu Leu Lys Val Leu Ser Tyr Leu Gly Asn His Met

20 25 30

Asn Ile Val Asn Leu Leu Gly Ala Cys Thr Ile Gly Gly Pro Thr Leu

35 40 45

Val Ile Ile Glu Tyr Cys Cys Tyr Gly Asp Leu Leu Asn Phe Leu Arg

50 55 60

Arg Lys Arg Asp Ser Phe Ile Cys Ser Lys Gln Glu Asp His Ala Glu

65 70 75 80

Ala Ala Leu Tyr Lys Asn Leu Leu His Ser Lys Glu Ser Ser Cys Ser

85 90 95

Asp Ser Thr Asn Glu

100

<210> 1994

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1994

Val Glu Ala Thr Ala Tyr Gly Leu Ile Lys Ser Asp Ala Ala Met Thr

1 5 10 15

Val Ala Val Lys Met Leu Lys Pro Ser Ala His Leu Thr Glu Arg Glu

20 25 30

Ala Leu Met Ser Glu Leu Lys Val Leu Ser Tyr Leu Gly Asn His Met

35 40 45

Asn Ile Ala Asn Leu Leu Gly Ala Cys Thr Ile Gly Gly Pro Thr Leu

50 55 60

Val Ile Thr Glu Tyr Cys Cys Tyr Gly Asp Leu Leu Asn Phe Leu Arg

65 70 75 80

Arg Lys Arg Asp Ser Phe Ile Cys Ser Lys Gln Glu Asp His Ala Glu

85 90 95

Ala Ala Leu Tyr Lys

100

<210> 1995

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1995

Ile Ser Glu Leu Gly Ala Gly Asn Gly Gly Val Val Phe Lys Val Ser

1 5 10 15

His Lys Pro Ser Gly Leu Val Met Ala Arg Lys Leu Ile His Leu Glu

20 25 30

Ile Lys Pro Ala Ile Arg Asn Gln Ile Ile Arg Glu Leu Gln Val Leu

35 40 45

His Glu Ser Asn Ser Pro Tyr Ile Val Gly Phe Tyr Gly Ala Phe Tyr

50 55 60

Ser Asp Gly Glu Ile Ser Ile Cys Met Glu His Met Asp Gly Gly Ser

65 70 75 80

Leu Asp Gln Val Leu Lys Lys Ala Gly Arg Ile Pro Glu Gln Ile Leu

85 90 95

Gly Lys Val Ser Ile

100

<210> 1996

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1996

Leu Gly Ala Gly Asn Gly Gly Val Val Phe Lys Val Ser His Lys Pro

1 5 10 15

Ser Gly Leu Val Met Ala Arg Lys Leu Ile His Leu Glu Ile Lys Pro

20 25 30

Ala Ile Arg Asn Gln Ile Ile Arg Glu Leu Gln Val Leu His Glu Cys

35 40 45

Asn Ser Leu Tyr Ile Val Gly Phe Tyr Gly Ala Phe Tyr Ser Asp Gly

50 55 60

Glu Ile Ser Ile Cys Met Glu His Met Asp Gly Gly Ser Leu Asp Gln

65 70 75 80

Val Leu Lys Lys Ala Gly Arg Ile Pro Glu Gln Ile Leu Gly Lys Val

85 90 95

Ser Ile Ala Val Ile

100

<210> 1997

<211> 89

<212> PROTEIN

<213> Homo sapiens

<400> 1997

Met Pro Leu Asn Val Ser Phe Thr Asn Arg Asn Tyr Asp Leu Asp Tyr

1 5 10 15

Asp Ser Val Gln Pro Tyr Phe Tyr Cys Asp Glu Glu Glu Asn Phe Tyr

20 25 30

Gln Gln Gln Gln Gln Ser Asp Leu Gln Pro Pro Ala Pro Ser Glu Asp

35 40 45

Ile Trp Lys Lys Phe Glu Leu Leu Pro Thr Pro Pro Leu Ser Pro Ser

50 55 60

Arg Arg Ser Gly Leu Cys Ser Pro Ser Tyr Val Ala Val Thr Pro Phe

65 70 75 80

Ser Leu Arg Gly Asp Asn Asp Gly Gly

85

<210> 1998

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1998

Phe Thr Asn Arg Asn Tyr Asp Leu Asp Tyr Asp Ser Val Gln Pro Tyr

1 5 10 15

Phe Tyr Cys Asp Glu Glu Glu Asn Phe Tyr Gln Gln Gln Gln Gln Ser

20 25 30

Glu Leu Gln Pro Pro Ala Pro Ser Glu Asp Ile Trp Lys Lys Phe Glu

35 40 45

Leu Leu Ser Thr Pro Pro Leu Ser Pro Ser Arg Arg Ser Gly Leu Cys

50 55 60

Ser Pro Ser Tyr Val Ala Val Thr Pro Phe Ser Leu Arg Gly Asp Asn

65 70 75 80

Asp Gly Gly Gly Gly Ser Phe Ser Thr Ala Asp Gln Leu Glu Met Val

85 90 95

Thr Glu Leu Leu Gly

100

<210> 1999

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 1999

Thr Asn Arg Asn Tyr Asp Leu Asp Tyr Asp Ser Val Gln Pro Tyr Phe

1 5 10 15

Tyr Cys Asp Glu Glu Glu Asn Phe Tyr Gln Gln Gln Gln Gln Ser Glu

20 25 30

Leu Gln Pro Pro Ala Pro Ser Glu Asp Ile Trp Lys Lys Phe Glu Leu

35 40 45

Leu Pro Ile Pro Pro Leu Ser Pro Ser Arg Arg Ser Gly Leu Cys Ser

50 55 60

Pro Ser Tyr Val Ala Val Thr Pro Phe Ser Leu Arg Gly Asp Asn Asp

65 70 75 80

Gly Gly Gly Gly Ser Phe Ser Thr Ala Asp Gln Leu Glu Met Val Thr

85 90 95

Glu Leu Leu Gly Gly

100

<210> 2000

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 2000

Val Ala Val Lys Met Leu Lys Pro Thr Ala Arg Ser Ser Glu Lys Gln

1 5 10 15

Ala Leu Met Ser Glu Leu Lys Ile Met Thr His Leu Gly Pro His Leu

20 25 30

Asn Ile Val Asn Leu Leu Gly Ala Cys Thr Lys Ser Gly Pro Ile Tyr

35 40 45

Ile Ile Ile Glu Tyr Cys Phe Tyr Gly Asp Leu Val Asn Tyr Leu His

50 55 60

Lys Asn Arg Asp Ser Phe Leu Ser His His Pro Glu Lys Pro Lys Lys

65 70 75 80

Glu Leu Asp Ile Phe Gly Leu Asn Pro Ala Asp Glu Ser Thr Arg Ser

85 90 95

Tyr Val Ile Leu Ser

100

<210> 2001

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 2001

Ile Glu Glu His Ala Asn Trp Ser Val Ser Arg Glu Ala Gly Phe Ser

1 5 10 15

Tyr Ser His Ala Gly Leu Ser Asn Arg Leu Ala Arg Asp Asn Glu Leu

20 25 30

Arg Glu Asn Asp Lys Glu Gln Leu Lys Ala Ile Ser Thr Arg Asp Pro

35 40 45

Leu Ser Lys Ile Thr Glu Gln Glu Lys Asp Phe Leu Trp Ser His Arg

50 55 60

His Tyr Cys Val Thr Ile Pro Glu Ile Leu Pro Lys Leu Leu Leu Ser

65 70 75 80

Val Lys Trp Asn Ser Arg Asp Glu Val Ala Gln Met Tyr Cys Leu Val

85 90 95

Lys Asp Trp Pro Pro

100

<210> 2002

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 2002

His Ala Asn Trp Ser Val Ser Arg Glu Ala Gly Phe Ser Tyr Ser His

1 5 10 15

Ala Gly Leu Ser Asn Arg Leu Ala Arg Asp Asn Glu Leu Arg Glu Asn

20 25 30

Asp Lys Glu Gln Leu Lys Ala Ile Ser Thr Arg Asp Pro Leu Ser Glu

35 40 45

Ile Thr Lys Gln Glu Lys Asp Phe Leu Trp Ser His Arg His Tyr Cys

50 55 60

Val Thr Ile Pro Glu Ile Leu Pro Lys Leu Leu Leu Ser Val Lys Trp

65 70 75 80

Asn Ser Arg Asp Glu Val Ala Gln Met Tyr Cys Leu Val Lys Asp Trp

85 90 95

Pro Pro Ile Lys Pro

100

<210> 2003

<211> 72

<212> PROTEIN

<213> Homo sapiens

<400> 2003

Leu Phe Ile Asn Leu Phe Ser Met Met Leu Gly Ser Gly Met Pro Glu

1 5 10 15

Leu Gln Ser Phe Asp Asp Ile Ala Tyr Ile Arg Lys Thr Leu Ala Leu

20 25 30

Asp Lys Thr Glu Gln Glu Ala Leu Glu Tyr Phe Met Lys Gln Met Asn

35 40 45

Asp Ala Arg His Gly Gly Trp Thr Thr Lys Met Asp Trp Ile Phe His

50 55 60

Thr Ile Lys Gln His Ala Leu Asn

65 70

<210> 2004

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 2004

Gln Arg Gly Gly Val Ile Thr Asp Glu Glu Glu Thr Ser Lys Lys Ile

1 5 10 15

Ala Asp Gln Leu Asp Asn Ile Val Asp Met Arg Glu Tyr Asp Val Pro

20 25 30

Tyr His Ile Arg Leu Ser Ile Asp Ile Glu Thr Thr Lys Leu Pro Leu

35 40 45

Lys Phe Arg Asp Ala Glu Thr Asp Gln Ile Met Met Ile Ser Tyr Met

50 55 60

Ile Asp Gly Gln Gly Tyr Leu Ile Thr Asn Arg Glu Ile Val Ser Glu

65 70 75 80

Asp Ile Glu Asp Phe Glu Phe Thr Pro Lys Pro Glu Tyr Glu Gly Pro

85 90 95

Phe Cys Val Phe Asn

100

<210> 2005

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 2005

Lys Phe Asn Cys Arg Val Ala Gln Tyr Pro Phe Glu Asp His Asn Pro

1 5 10 15

Pro Gln Leu Glu Leu Ile Lys Pro Phe Cys Glu Asp Leu Asp Gln Trp

20 25 30

Leu Ser Glu Asp Asp Asn His Val Ala Ala Ile His Cys Lys Ala Gly

35 40 45

Lys Gly Gln Thr Gly Val Met Ile Cys Ala Tyr Leu Leu His Arg Gly

50 55 60

Lys Phe Leu Lys Ala Gln Glu Ala Leu Asp Phe Tyr Gly Glu Val Arg

65 70 75 80

Thr Arg Asp Lys Lys Gly Val Thr Ile Pro Ser Gln Arg Arg Tyr Val

85 90 95

Tyr Tyr Tyr Ser Tyr

100

<210> 2006

<211> 79

<212> PROTEIN

<213> Homo sapiens

<400> 2006

Met Gln Ala Ile Lys Cys Val Val Val Gly Asp Gly Ala Val Gly Lys

1 5 10 15

Thr Cys Leu Leu Ile Ser Tyr Thr Thr Asn Ala Phe Ser Gly Glu Tyr

20 25 30

Ile Pro Thr Val Phe Asp Asn Tyr Ser Ala Asn Val Met Val Asp Gly

35 40 45

Lys Pro Val Asn Leu Gly Leu Trp Asp Thr Ala Gly Gln Glu Asp Tyr

50 55 60

Asp Arg Leu Arg Pro Leu Ser Tyr Pro Gln Thr Val Gly Glu Thr

65 70 75

<210> 2007

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 2007

Ile Arg Val Glu Gly Asn Leu Arg Val Glu Tyr Leu Asp Asp Arg Asn

1 5 10 15

Thr Phe Arg His Ser Val Val Val Pro Tyr Glu Pro Pro Glu Val Gly

20 25 30

Ser Asp Cys Thr Thr Ile His Tyr Asn Tyr Met Cys Asn Ser Ser Cys

35 40 45

Met Gly Ser Met Asn Arg Arg Pro Ile Leu Thr Ile Ile Thr Leu Glu

50 55 60

Asp Ser Ser Gly Asn Leu Leu Gly Arg Asn Ser Phe Glu Val Arg Val

65 70 75 80

Cys Ala Cys Pro Gly Arg Asp Arg Arg Thr Glu Glu Glu Asn Leu Arg

85 90 95

Lys Lys Gly Glu Pro

100

<210> 2008

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 2008

Thr Tyr Ser Pro Ala Leu Asn Lys Met Phe Cys Gln Leu Ala Lys Thr

1 5 10 15

Cys Pro Val Gln Leu Trp Val Asp Ser Thr Pro Pro Pro Gly Thr Arg

20 25 30

Val Arg Ala Met Ala Ile Tyr Lys Gln Ser Gln His Met Thr Glu Val

35 40 45

Val Arg His Cys Pro His His Glu Arg Cys Ser Asp Ser Asp Gly Leu

50 55 60

Ala Pro Pro Gln His Leu Ile Arg Val Glu Gly Asn Leu Arg Val Glu

65 70 75 80

Tyr Leu Asp Asp Arg Asn Thr Phe Arg His Ser Val Val Val Pro Tyr

85 90 95

Glu Pro Pro Glu Val

100

<210> 2009

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 2009

Glu Gly Asn Leu Arg Val Glu Tyr Leu Asp Asp Arg Asn Thr Phe Arg

1 5 10 15

His Ser Val Val Val Pro Tyr Glu Pro Pro Glu Val Gly Ser Asp Cys

20 25 30

Thr Thr Ile His Tyr Asn Tyr Met Cys Asn Ser Ser Cys Met Gly Gly

35 40 45

Met Asn Gln Arg Pro Ile Leu Thr Ile Ile Thr Leu Glu Asp Ser Ser

50 55 60

Gly Asn Leu Leu Gly Arg Asn Ser Phe Glu Val Arg Val Cys Ala Cys

65 70 75 80

Pro Gly Arg Asp Arg Arg Thr Glu Glu Glu Asn Leu Arg Lys Lys Gly

85 90 95

Glu Pro His His Glu

100

<210> 2010

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 2010

Glu Gly Asn Leu Arg Val Glu Tyr Leu Asp Asp Arg Asn Thr Phe Arg

1 5 10 15

His Ser Val Val Val Pro Tyr Glu Pro Pro Glu Val Gly Ser Asp Cys

20 25 30

Thr Thr Ile His Tyr Asn Tyr Met Cys Asn Ser Ser Cys Met Gly Gly

35 40 45

Met Asn Trp Arg Pro Ile Leu Thr Ile Ile Thr Leu Glu Asp Ser Ser

50 55 60

Gly Asn Leu Leu Gly Arg Asn Ser Phe Glu Val Arg Val Cys Ala Cys

65 70 75 80

Pro Gly Arg Asp Arg Arg Thr Glu Glu Glu Asn Leu Arg Lys Lys Gly

85 90 95

Glu Pro His His Glu

100

<210> 2011

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 2011

Pro Glu Val Gly Ser Asp Cys Thr Thr Ile His Tyr Asn Tyr Met Cys

1 5 10 15

Asn Ser Ser Cys Met Gly Gly Met Asn Arg Arg Pro Ile Leu Thr Ile

20 25 30

Ile Thr Leu Glu Asp Ser Ser Gly Asn Leu Leu Gly Arg Asn Ser Phe

35 40 45

Glu Val Cys Val Cys Ala Cys Pro Gly Arg Asp Arg Arg Thr Glu Glu

50 55 60

Glu Asn Leu Arg Lys Lys Gly Glu Pro His His Glu Leu Pro Pro Gly

65 70 75 80

Ser Thr Lys Arg Ala Leu Pro Asn Asn Thr Ser Ser Ser Pro Gln Pro

85 90 95

Lys Lys Lys Pro Leu

100

<210> 2012

<211> 53

<212> PROTEIN

<213> Homo sapiens

<400> 2012

Gly Val Glu Pro Cys Tyr Gly Asp Lys Asp Lys Arg Arg His Cys Phe

1 5 10 15

Ala Thr Trp Lys Asn Ile Ser Gly Ser Ile Glu Ile Val Lys Gln Gly

20 25 30

Cys Trp Leu Asp Asp Ile Asn Cys Tyr Asp Arg Thr Asp Cys Val Glu

35 40 45

Lys Lys Arg Gln Pro

50

<210> 2013

<211> 103

<212> PROTEIN

<213> Homo sapiens

<400> 2013

Gly Val Glu Pro Cys Tyr Gly Asp Lys Asp Lys Arg Arg His Cys Phe

1 5 10 15

Ala Thr Trp Lys Asn Ile Ser Gly Ser Ile Glu Ile Val Lys Gln Gly

20 25 30

Cys Trp Leu Asp Asp Ile Asn Cys Tyr Asp Arg Thr Asp Cys Val Glu

35 40 45

Lys Lys Thr Ala Leu Lys Tyr Ile Phe Val Ala Val Arg Ala Ile Cys

50 55 60

Val Met Lys Ser Phe Leu Ile Phe Arg Arg Trp Lys Ser His Ser Pro

65 70 75 80

Leu Gln Ile Gln Leu His Leu Ser His Pro Ile Thr Thr Ser Cys Ser

85 90 95

Ile Pro Trp Cys His Leu Cys

100

<210> 2014

<211> 118

<212> PROTEIN

<213> Homo sapiens

<400> 2014

Thr Ala Glu Ala Val Asn Val Ala Ile Ala Ala Pro Pro Ser Glu Gly

1 5 10 15

Glu Ala Asn Ala Glu Leu Cys Arg Tyr Leu Ser Lys Val Leu Glu Leu

20 25 30

Arg Lys Ser Asp Val Val Leu Asp Lys Val Gly Leu Ala Leu Phe Phe

35 40 45

Phe Phe Phe Glu Thr Lys Ser Cys Ser Val Ala Gln Ala Gly Val Gln

50 55 60

Trp Arg Ser Leu Gly Ser Leu Gln Pro Pro Pro Pro Gly Phe Lys Leu

65 70 75 80

Phe Ser Cys Leu Ser Phe Leu Ser Ser Trp Asp Tyr Arg Arg Met Pro

85 90 95

Pro Cys Leu Ala Asn Phe Cys Ile Phe Asn Arg Asp Gly Val Ser Pro

100 105 110

Cys Trp Ser Gly Trp Ser

115

<210> 2015

<211> 71

<212> PROTEIN

<213> Homo sapiens

<400> 2015

Leu Ser Val Ile Ile Phe Phe Phe Val Tyr Ile Trp His Trp Ala Leu

1 5 10 15

Pro Leu Ile Leu Asn Asn His His Ile Cys Leu Met Ser Ser Ile Ile

20 25 30

Leu Asp Cys Asn Ser Val Arg Gln Ser Ile Met Ser Val Cys Phe Phe

35 40 45

Phe Phe Ser Val Ile Phe Ser Thr Arg Cys Leu Thr Asp Ser Arg Tyr

50 55 60

Pro Asn Ile Cys Trp Phe Lys

65 70

<210> 2016

<211> 60

<212> PROTEIN

<213> Homo sapiens

<400> 2016

Leu Ser Val Ile Ile Phe Phe Phe Val Tyr Ile Trp His Trp Ala Leu

1 5 10 15

Pro Leu Ile Leu Asn Asn His His Ile Cys Leu Met Ser Ser Ile Ile

20 25 30

Leu Asp Cys Asn Ser Val Arg Gln Ser Ile Met Ser Val Cys Phe Phe

35 40 45

Phe Phe Cys Tyr Ile Leu Asn Thr Met Phe Asp Arg

50 55 60

<210> 2017

<211> 106

<212> PROTEIN

<213> Homo sapiens

<400> 2017

Val Leu Val Leu Ser Cys Asp Leu Ile Thr Asp Val Ala Leu His Glu

1 5 10 15

Val Val Asp Leu Phe Arg Ala Tyr Asp Ala Ser Leu Ala Met Leu Met

20 25 30

Arg Lys Gly Gln Asp Ser Ile Glu Pro Val Pro Gly Gln Lys Gly Lys

35 40 45

Lys Lys Gln Trp Ser Ser Val Thr Ser Leu Glu Trp Thr Ala Gln Glu

50 55 60

Arg Gly Cys Ser Ser Trp Leu Met Lys Gln Thr Trp Met Lys Ser Trp

65 70 75 80

Ser Leu Arg Asp Pro Ser Tyr Arg Ser Ile Leu Glu Tyr Val Ser Thr

85 90 95

Arg Val Leu Trp Met Pro Thr Ser Thr Val

100 105

<210> 2018

<211> 112

<212> PROTEIN

<213> Homo sapiens

<400> 2018

Ser Ile Gln Val Met Arg Ala Gln Met Asn Gln Ile Gln Ser Val Glu

1 5 10 15

Gly Gln Pro Leu Ala Arg Arg Pro Arg Ala Thr Gly Arg Thr Lys Arg

20 25 30

Cys Gln Pro Arg Asp Val Thr Lys Lys Thr Cys Asn Ser Asn Asp Gly

35 40 45

Lys Lys Arg Glu Trp Glu Lys Arg Lys Gln Ile Leu Gly Gly Gly Gly

50 55 60

Lys Tyr Lys Glu Tyr Phe Leu Lys Arg Ile Leu Ile Arg Lys Ala Met

65 70 75 80

Thr Val Leu Ala Gly Asp Lys Lys Gly Leu Gly Arg Phe Met Arg Cys

85 90 95

Val Gln Ser Glu Thr Lys Ala Val Ser Leu Gln Leu Pro Leu Gly Arg

100 105 110

<210> 2019

<211> 57

<212> PROTEIN

<213> Homo sapiens

<400> 2019

Leu Asp Phe Leu Gly Glu Phe Ala Thr Asp Ile Arg Thr His Gly Val

1 5 10 15

His Met Val Leu Asn His Gln Gly Arg Pro Ser Gly Asp Ala Phe Ile

20 25 30

Gln Met Lys Ser Ala Asp Arg Ala Phe Met Ala Ala Gln Lys Cys His

35 40 45

Lys Lys Lys His Glu Gly Gln Ile Cys

50 55

<210> 2020

<211> 51

<212> PROTEIN

<213> Homo sapiens

<400> 2020

Leu Asp Phe Leu Gly Glu Phe Ala Thr Asp Ile Arg Thr His Gly Val

1 5 10 15

His Met Val Leu Asn His Gln Gly Arg Pro Ser Gly Asp Ala Phe Ile

20 25 30

Gln Met Lys Ser Ala Asp Arg Ala Phe Met Ala Ala Gln Lys Cys His

35 40 45

Lys Lys Thr

50

<210> 2021

<211> 75

<212> PROTEIN

<213> Homo sapiens

<400> 2021

Gly Ala Leu Cys Lys Asp Gly Arg Phe Arg Ser Asp Ile Gly Glu Phe

1 5 10 15

Glu Trp Lys Leu Lys Glu Gly His Lys Lys Ile Tyr Gly Lys Gln Ser

20 25 30

Met Val Asp Glu Val Ser Gly Lys Val Leu Glu Met Asp Ile Ser Lys

35 40 45

Lys Lys His Tyr Asn Arg Lys Ile Ser Ile Lys Lys Leu Asn Arg Met

50 55 60

Lys Val Pro Leu Met Lys Leu Ile Thr Arg Val

65 70 75

<210> 2022

<211> 58

<212> PROTEIN

<213> Homo sapiens

<400> 2022

Arg Glu Arg Ala Gln Leu Leu Glu Glu Gln Glu Lys Thr Leu Thr Ser

1 5 10 15

Lys Leu Gln Glu Gln Ala Arg Val Leu Lys Glu Arg Cys Gln Gly Glu

20 25 30

Ser Thr Gln Leu Gln Asn Glu Ile Gln Lys Leu Gln Lys Thr Leu Lys

35 40 45

Lys Lys Pro Arg Asp Ile Cys Arg Ile Ser

50 55

<210> 2023

<211> 53

<212> PROTEIN

<213> Homo sapiens

<400> 2023

Val Asn Thr Leu Lys Glu Gly Lys Arg Leu Pro Cys Pro Pro Asn Cys

1 5 10 15

Pro Asp Glu Val Tyr Gln Leu Met Arg Lys Cys Trp Glu Phe Gln Pro

20 25 30

Ser Asn Arg Thr Ser Phe Gln Asn Leu Ile Glu Gly Phe Glu Ala Leu

35 40 45

Leu Lys Thr Ser Asn

50

<210> 2024

<211> 65

<212> PROTEIN

<213> Homo sapiens

<400> 2024

Cys Arg Pro Val Thr Pro Ser Cys Lys Glu Leu Ala Asp Leu Met Thr

1 5 10 15

Arg Cys Met Asn Tyr Asp Pro Asn Gln Arg Pro Phe Phe Arg Ala Ile

20 25 30

Met Arg Asp Ile Asn Lys Leu Glu Glu Gln Asn Pro Asp Ile Val Ser

35 40 45

Glu Lys Asn Gln Gln Leu Lys Trp Thr Pro His Ile Leu Lys Ser Ala

50 55 60

Ser

65

<210> 2025

<211> 69

<212> PROTEIN

<213> Homo sapiens

<400> 2025

Asp Asp His Asp Val Leu Ser Phe Leu Thr Phe Gln Leu Thr Glu Pro

1 5 10 15

Gly Lys Glu Pro Pro Thr Pro Asp Lys Glu Ile Ser Glu Lys Glu Lys

20 25 30

Glu Lys Tyr Gln Glu Glu Phe Glu His Phe Gln Gln Glu Leu Asp Lys

35 40 45

Lys Lys Arg Gly Ile Pro Glu Gly Pro Pro Arg Pro Pro Arg Ala Ala

50 55 60

Cys Gly Gly Asn Ile

65

<210> 2026

<211> 71

<212> PROTEIN

<213> Homo sapiens

<400> 2026

Asp Asp His Asp Val Leu Ser Phe Leu Thr Phe Gln Leu Thr Glu Pro

1 5 10 15

Gly Lys Glu Pro Pro Thr Pro Asp Lys Glu Ile Ser Glu Lys Glu Lys

20 25 30

Glu Lys Tyr Gln Glu Glu Phe Glu His Phe Gln Gln Glu Leu Asp Lys

35 40 45

Lys Lys Arg Asn Ser Arg Arg Ala Thr Pro Thr Ser Lys Gly Ser Leu

50 55 60

Arg Arg Lys Tyr Leu Arg Val

65 70

<210> 2027

<211> 68

<212> PROTEIN

<213> Homo sapiens

<400> 2027

Thr Lys Ser Thr Leu Ile Gly Glu Asp Val Asn Pro Leu Ile Lys Leu

1 5 10 15

Asp Asp Ala Val Asn Val Asp Glu Ile Met Thr Asp Thr Ser Thr Ser

20 25 30

Tyr Leu Leu Cys Ile Ser Glu Asn Lys Glu Asn Val Arg Asp Lys Lys

35 40 45

Lys Gly Gln His Phe Tyr Trp His Cys Gly Ser Ala Ala Cys His Arg

50 55 60

Arg Gly Cys Val

65

<210> 2028

<211> 81

<212> PROTEIN

<213> Homo sapiens

<400> 2028

Leu Tyr Thr Lys Ser Thr Leu Ile Gly Glu Asp Val Asn Pro Leu Ile

1 5 10 15

Lys Leu Asp Asp Ala Val Asn Val Asp Glu Ile Met Thr Asp Thr Ser

20 25 30

Thr Ser Tyr Leu Leu Cys Ile Ser Glu Asn Lys Glu Asn Val Arg Asp

35 40 45

Lys Lys Arg Ala Thr Phe Leu Leu Ala Leu Trp Glu Cys Ser Leu Pro

50 55 60

Gln Ala Arg Leu Cys Leu Ile Val Ser Arg Thr Leu Leu Leu Val Gln

65 70 75 80

Ser

<210> 2029

<211> 58

<212> PROTEIN

<213> Homo sapiens

<400> 2029

Leu Pro Pro Pro Lys Leu Thr Asp Pro Arg Leu Leu Tyr Ile Gly Phe

1 5 10 15

Leu Gly Tyr Cys Ser Gly Leu Ile Asp Asn Leu Ile Arg Arg Arg Pro

20 25 30

Ile Ala Thr Ala Gly Leu His Arg Gln Leu Leu Tyr Ile Thr Ala Phe

35 40 45

Phe Phe Cys Trp Ile Leu Ser Cys Lys Thr

50 55

<210> 2030

<211> 56

<212> PROTEIN

<213> Homo sapiens

<400> 2030

Ser Leu Pro Pro Pro Lys Leu Thr Asp Pro Arg Leu Leu Tyr Ile Gly

1 5 10 15

Phe Leu Gly Tyr Cys Ser Gly Leu Ile Asp Asn Leu Ile Arg Arg Arg

20 25 30

Pro Ile Ala Thr Ala Gly Leu His Arg Gln Leu Leu Tyr Ile Thr Ala

35 40 45

Phe Phe Leu Leu Asp Ile Ile Leu

50 55

<210> 2031

<211> 112

<212> PROTEIN

<213> Homo sapiens

<400> 2031

Asn Gln Ser Gly Gly Ala Gly Glu Asp Cys Gln Ile Phe Ser Thr Pro

1 5 10 15

Gly His Pro Lys Met Ile Tyr Ser Ser Ser Asn Leu Lys Thr Pro Ser

20 25 30

Lys Leu Cys Ser Gly Ser Lys Ser His Asp Val Gln Glu Val Leu Lys

35 40 45

Lys Lys Thr Gly Ser Asn Glu Val Thr Thr Arg Tyr Glu Glu Lys Lys

50 55 60

Thr Gly Ser Val Arg Lys Ala Asn Arg Met Pro Lys Asp Val Asn Ile

65 70 75 80

Gln Val Arg Lys Lys Gln Lys His Glu Thr Arg Arg Lys Ser Lys Tyr

85 90 95

Asn Glu Asp Phe Glu Arg Ala Trp Arg Glu Asp Leu Thr Ile Lys Arg

100 105 110

<210> 2032

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 2032

Met Ala Pro Val Lys Lys Leu Val Val Lys Gly Gly Lys Lys Lys Glu

1 5 10 15

Ala Ser Ser Glu Val His Ser

20

<210> 2033

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 2033

Met Ala Pro Val Lys Lys Leu Val Val Lys Gly Gly Lys Lys Arg Ser

1 5 10 15

Lys Phe

<210> 2034

<211> 51

<212> PROTEIN

<213> Homo sapiens

<400> 2034

Met Pro Ser His Gln Gly Ala Glu Gln Gln Gln Gln Gln His His Val

1 5 10 15

Phe Ile Ser Gln Val Val Thr Glu Lys Glu Phe Leu Ser Arg Ser Asp

20 25 30

Gln Leu Gln Gln Ala Val Gln Ser Gln Gly Phe Ile Asn Tyr Cys Gln

35 40 45

Lys Lys Asn

50

<210> 2035

<211> 65

<212> PROTEIN

<213> Homo sapiens

<400> 2035

Met Pro Ser His Gln Gly Ala Glu Gln Gln Gln Gln Gln His His Val

1 5 10 15

Phe Ile Ser Gln Val Val Thr Glu Lys Glu Phe Leu Ser Arg Ser Asp

20 25 30

Gln Leu Gln Gln Ala Val Gln Ser Gln Gly Phe Ile Asn Tyr Cys Gln

35 40 45

Lys Lys Leu Met Leu Leu Arg Leu Asn Leu Arg Lys Met Cys Gly Pro

50 55 60

Phe

65

<210> 2036

<211> 79

<212> PROTEIN

<213> Homo sapiens

<400> 2036

Ala Glu Val Phe Glu Lys Glu Gln Ser Ile Cys Ala Ala Glu Glu Gln

1 5 10 15

Pro Ala Glu Asp Gly Gln Gly Glu Thr Asn Lys Asn Arg Thr Lys Gly

20 25 30

Gly Trp Gln Gln Lys Ser Lys Gly Pro Lys Lys Thr Ala Lys Ser Lys

35 40 45

Lys Lys Glu Thr Phe Lys Lys Lys Thr Tyr Thr Cys Ala Ile Thr Thr

50 55 60

Val Lys Ala Thr Glu Thr Lys Ala Gly Lys Trp Ser Arg Trp Glu

65 70 75

<210> 2037

<211> 53

<212> PROTEIN

<213> Homo sapiens

<400> 2037

Met Ala Glu Val Phe Glu Lys Glu Gln Ser Ile Cys Ala Ala Glu Glu

1 5 10 15

Gln Pro Ala Glu Asp Gly Gln Gly Glu Thr Asn Lys Asn Arg Thr Lys

20 25 30

Gly Gly Trp Gln Gln Lys Ser Lys Gly Pro Lys Lys Thr Ala Lys Ser

35 40 45

Lys Lys Arg Asn Leu

50

<210> 2038

<211> 71

<212> PROTEIN

<213> Homo sapiens

<400> 2038

Asn Ile Met Glu Ile Arg Gln Leu Pro Ser Ser His Ala Leu Glu Ala

1 5 10 15

Lys Leu Ser Arg Met Ser Tyr Pro Val Lys Glu Gln Glu Ser Ile Leu

20 25 30

Lys Thr Val Gly Lys Leu Thr Ala Thr Gln Val Ala Lys Ile Ser Phe

35 40 45

Phe Phe Ala Leu Cys Gly Phe Trp Gln Ile Cys His Ile Lys Lys His

50 55 60

Phe Gln Thr His Lys Leu Leu

65 70

<210> 2039

<211> 68

<212> PROTEIN

<213> Homo sapiens

<400> 2039

Tyr Glu Lys Lys Lys Tyr Tyr Asp Lys Asn Ala Ile Ala Ile Thr Asn

1 5 10 15

Ile Ser Ser Ser Asp Ala Pro Leu Gln Pro Leu Val Ser Ser Pro Ser

20 25 30

Leu Gln Ala Ala Val Asp Lys Asn Lys Leu Glu Lys Glu Lys Glu Lys

35 40 45

Lys Lys Gly Arg Glu Lys Glu Arg Lys Gly Ala Arg Lys Ala Gly Lys

50 55 60

Thr Thr Tyr Ser

65

<210> 2040

<211> 97

<212> PROTEIN

<213> Homo sapiens

<400> 2040

Lys Tyr Glu Lys Lys Lys Tyr Tyr Asp Lys Asn Ala Ile Ala Ile Thr

1 5 10 15

Asn Ile Ser Ser Ser Asp Ala Pro Leu Gln Pro Leu Val Ser Ser Pro

20 25 30

Ser Leu Gln Ala Ala Val Asp Lys Asn Lys Leu Glu Lys Glu Lys Glu

35 40 45

Lys Lys Arg Lys Arg Lys Arg Glu Lys Arg Ser Gln Lys Ser Arg Gln

50 55 60

Asn His Leu Gln Leu Lys Ser Cys Arg Arg Lys Ile Ser Asn Trp Ser

65 70 75 80

Leu Lys Lys Val Pro Ala Leu Lys Lys Leu Arg Ser Pro Leu Trp Ile

85 90 95

Phe

<210> 2041

<211> 65

<212> PROTEIN

<213> Homo sapiens

<400> 2041

Ile Tyr Gln Asp Ala Tyr Arg Ala Glu Trp Gln Val Tyr Lys Glu Glu

1 5 10 15

Ile Ser Arg Phe Lys Glu Gln Leu Thr Pro Ser Gln Ile Met Ser Leu

20 25 30

Glu Lys Glu Ile Met Asp Lys His Leu Lys Arg Lys Ala Met Thr Lys

35 40 45

Lys Lys Arg Val Asn Thr Ala Trp Lys Thr Lys Lys Thr Ser Phe Ser

50 55 60

Leu

65

<210> 2042

<211> 51

<212> PROTEIN

<213> Homo sapiens

<400> 2042

Ile Tyr Gln Asp Ala Tyr Arg Ala Glu Trp Gln Val Tyr Lys Glu Glu

1 5 10 15

Ile Ser Arg Phe Lys Glu Gln Leu Thr Pro Ser Gln Ile Met Ser Leu

20 25 30

Glu Lys Glu Ile Met Asp Lys His Leu Lys Arg Lys Ala Met Thr Lys

35 40 45

Lys Lys Ser

50

<210> 2043

<211> 52

<212> PROTEIN

<213> Homo sapiens

<400> 2043

Lys Pro Gln Glu Val Cys Val Ala Val Trp Arg Lys Asn Asp Glu Asn

1 5 10 15

Ile Thr Leu Glu Thr Val Cys His Asp Pro Lys Leu Pro Tyr His Asp

20 25 30

Phe Ile Leu Glu Asp Ala Ala Ser Pro Lys Cys Ile Met Lys Glu Lys

35 40 45

Lys Lys Ala Trp

50

<210> 2044

<211> 84

<212> PROTEIN

<213> Homo sapiens

<400> 2044

Glu Lys Pro Gln Glu Val Cys Val Ala Val Trp Arg Lys Asn Asp Glu

1 5 10 15

Asn Ile Thr Leu Glu Thr Val Cys His Asp Pro Lys Leu Pro Tyr His

20 25 30

Asp Phe Ile Leu Glu Asp Ala Ala Ser Pro Lys Cys Ile Met Lys Glu

35 40 45

Lys Lys Ser Leu Val Arg Leu Ser Ser Cys Val Pro Val Ala Leu Met

50 55 60

Ser Ala Met Thr Thr Ser Ser Ser Gln Lys Asn Ile Thr Pro Ala Ile

65 70 75 80

Leu Thr Cys Cys

<210> 2045

<211> 74

<212> PROTEIN

<213> Homo sapiens

<400> 2045

Val Pro Ser Lys Tyr Gln Phe Leu Cys Ser Asp His Phe Thr Pro Asp

1 5 10 15

Ser Leu Asp Ile Arg Trp Gly Ile Arg Tyr Leu Lys Gln Thr Ala Val

20 25 30

Pro Thr Ile Phe Ser Leu Pro Glu Asp Asn Gln Gly Lys Asp Pro Ser

35 40 45

Lys Lys Asn Pro Arg Arg Lys Thr Trp Lys Met Arg Lys Lys Tyr Ala

50 55 60

Gln Lys Pro Ser Gln Lys Asn His Leu Tyr

65 70

<210> 2046

<211> 88

<212> PROTEIN

<213> Homo sapiens

<400> 2046

Gly Thr Thr Glu Glu Met Lys Tyr Val Leu Gly Gln Leu Val Gly Leu

1 5 10 15

Asn Ser Pro Asn Ser Ile Leu Lys Ala Ala Lys Thr Leu Tyr Glu His

20 25 30

Tyr Ser Gly Gly Glu Ser His Asn Ser Ser Ser Ser Lys Thr Phe Glu

35 40 45

Lys Lys Gly Glu Lys Asn Asp Leu Gln Leu Phe Val Met Ser Asp Thr

50 55 60

Thr Tyr Lys Ile Tyr Trp Thr Val Ile Leu Leu Asn Pro Cys Gly Asn

65 70 75 80

Leu His Leu Lys Thr Thr Ser Leu

85

<210> 2047

<211> 55

<212> PROTEIN

<213> Homo sapiens

<400> 2047

Gln Gln Leu Ile Arg Glu Thr Leu Ile Ser Trp Leu Gln Ala Gln Met

1 5 10 15

Leu Asn Pro Gln Pro Glu Lys Thr Phe Ile Arg Asn Lys Ala Ala Gln

20 25 30

Val Phe Ala Leu Leu Phe Val Thr Glu Tyr Leu Thr Lys Trp Pro Lys

35 40 45

Phe Phe Leu Thr Phe Ser Gln

50 55

<210> 2048

<211> 93

<212> PROTEIN

<213> Homo sapiens

<400> 2048

Ala Lys Phe Gln Gln Cys His Ser Thr Leu Glu Pro Asn Pro Ala Asp

1 5 10 15

Cys Arg Val Leu Val Tyr Leu Gln Asn Gln Pro Gly Thr Lys Leu Leu

20 25 30

Asn Phe Leu Gln Glu Arg Asn Leu Pro Pro Lys Val Val Leu Arg His

35 40 45

Pro Lys Val His Leu Asn Thr Met Phe Arg Arg Pro His Ser Cys Leu

50 55 60

Ala Asp Val Leu Leu Ser Val His Leu Ile Val Leu Arg Val Val Arg

65 70 75 80

Leu Pro Ala Pro Phe Arg Val Asn His Ala Val Glu Trp

85 90

<210> 2049

<211> 53

<212> PROTEIN

<213> Homo sapiens

<400> 2049

Ala Pro Val Ile Phe Gln Ile Ala Leu Asp Lys Pro Cys His Gln Ala

1 5 10 15

Glu Val Lys His Leu His His Leu Leu Lys Gln Leu Lys Pro Ser Glu

20 25 30

Lys Tyr Leu Lys Ile Lys His Leu Leu Leu Lys Arg Glu Arg Val Asp

35 40 45

Leu Ser Lys Leu Gln

50

<210> 2050

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 2050

Met Leu Gln Phe Arg Gly Ser Arg Phe Phe Gln Met Leu Ile Leu Tyr

1 5 10 15

Tyr Ile Leu Pro Arg Lys Val Leu Gln Met Asp Phe Leu Val His Pro

20 25 30

Ala

<210> 2051

<211> 179

<212> PROTEIN

<213> Homo sapiens

<400> 2051

Ala Leu Gly Pro His Ser Arg Ile Ser Cys Leu Pro Thr Gln Thr Arg

1 5 10 15

Gly Cys Ile Leu Leu Ala Ala Thr Pro Arg Ser Ser Ser Ser Ser Ser

20 25 30

Ser Asn Asp Met Ile Pro Met Ala Ile Ser Ser Pro Pro Lys Ala Pro

35 40 45

Leu Leu Ala Ala Pro Ser Pro Ala Ser Arg Leu Gln Cys Ile Asn Ser

50 55 60

Asn Ser Arg Ile Thr Ser Gly Gln Trp Met Ala His Met Ala Leu Leu

65 70 75 80

Pro Ser Gly Thr Lys Gly Arg Cys Thr Ala Cys His Thr Ala Leu Gly

85 90 95

Arg Gly Ser Leu Ser Ser Ser Ser Cys Pro Gln Pro Ser Pro Ser Leu

100 105 110

Pro Ala Ser Asn Lys Leu Pro Ser Leu Pro Leu Ser Lys Met Tyr Thr

115 120 125

Thr Ser Met Ala Met Pro Ile Leu Pro Leu Pro Gln Leu Leu Leu Ser

130 135 140

Ala Asp Gln Gln Ala Ala Pro Arg Thr Asn Phe His Ser Ser Leu Ala

145 150 155 160

Glu Thr Val Ser Leu His Pro Leu Ala Pro Met Pro Ser Lys Thr Cys

165 170 175

His His Lys

<210> 2052

<211> 79

<212> PROTEIN

<213> Homo sapiens

<400> 2052

Ala His Gln Gly Phe Pro Ala Ala Lys Glu Ser Arg Val Ile Gln Leu

1 5 10 15

Ser Leu Leu Ser Leu Leu Ile Pro Pro Leu Thr Cys Leu Ala Ser Glu

20 25 30

Ala Leu Pro Arg Pro Leu Leu Ala Leu Pro Pro Val Leu Leu Ser Leu

35 40 45

Ala Gln Asp His Ser Arg Leu Leu Gln Cys Gln Ala Thr Arg Cys His

50 55 60

Leu Gly His Pro Val Ala Ser Arg Thr Ala Ser Cys Ile Leu Pro

65 70 75

<210> 2053

<211> 222

<212> PROTEIN

<213> Homo sapiens

<400> 2053

Pro Ile Leu Ala Ala Thr Gly Thr Ser Val Arg Thr Ala Ala Arg Thr

1 5 10 15

Trp Val Pro Arg Ala Ala Ile Arg Val Pro Asp Pro Ala Ala Val Pro

20 25 30

Asp Asp His Ala Gly Pro Gly Ala Glu Cys His Gly Arg Pro Leu Leu

35 40 45

Tyr Thr Ala Asp Ser Ser Leu Trp Thr Thr Arg Pro Gln Arg Val Trp

50 55 60

Ser Thr Gly Pro Asp Ser Ile Leu Gln Pro Ala Lys Ser Ser Pro Ser

65 70 75 80

Ala Ala Ala Ala Thr Leu Leu Pro Ala Thr Thr Val Pro Asp Pro Ser

85 90 95

Cys Pro Thr Phe Val Ser Ala Ala Ala Thr Val Ser Thr Thr Thr Ala

100 105 110

Pro Val Leu Ser Ala Ser Ile Leu Pro Ala Ala Ile Pro Ala Ser Thr

115 120 125

Ser Ala Val Pro Gly Ser Ile Pro Leu Pro Ala Val Asp Asp Thr Ala

130 135 140

Ala Pro Pro Glu Pro Ala Pro Leu Leu Thr Ala Thr Gly Ser Val Ser

145 150 155 160

Leu Pro Ala Ala Ala Thr Ser Ala Ala Ser Thr Leu Asp Ala Leu Pro

165 170 175

Ala Gly Cys Val Ser Ser Ala Pro Val Ser Ala Val Pro Ala Asn Cys

180 185 190

Leu Phe Pro Ala Ala Leu Pro Ser Thr Ala Gly Ala Ile Ser Arg Phe

195 200 205

Ile Trp Val Ser Gly Ile Leu Ser Pro Leu Asn Asp Leu Gln

210 215 220

<210> 2054

<211> 185

<212> PROTEIN

<213> Homo sapiens

<400> 2054

Pro Cys Arg Ala Gly Arg Arg Val Pro Trp Ala Ala Ser Leu Ile His

1 5 10 15

Ser Arg Phe Leu Leu Met Asp Asn Lys Ala Pro Ala Gly Met Val Asn

20 25 30

Arg Ala Arg Leu His Ile Thr Thr Ser Lys Val Leu Thr Leu Ser Ser

35 40 45

Ser Ser His Pro Thr Pro Ser Asn His Arg Pro Arg Pro Leu Met Pro

50 55 60

Asn Leu Arg Ile Ser Ser Ser His Ser Leu Asn His His Ser Ser Ser

65 70 75 80

Pro Leu Ser Leu His Thr Pro Ser Ser His Pro Ser Leu His Ile Ser

85 90 95

Ser Pro Arg Leu His Thr Pro Pro Ser Ser Arg Arg His Ser Ser Thr

100 105 110

Pro Arg Ala Ser Pro Pro Thr His Ser His Arg Leu Ser Leu Leu Thr

115 120 125

Ser Ser Ser Asn Leu Ser Ser Gln His Pro Arg Arg Ser Pro Ser Arg

130 135 140

Leu Arg Ile Leu Ser Pro Ser Leu Ser Ser Pro Ser Lys Leu Pro Ile

145 150 155 160

Pro Ser Ser Ala Ser Leu His Arg Arg Ser Tyr Leu Lys Ile His Leu

165 170 175

Gly Leu Arg His Pro Gln Pro Pro Gln

180 185

<210> 2055

<211> 58

<212> PROTEIN

<213> Homo sapiens

<400> 2055

Arg Thr Asn Pro Thr Val Arg Met Arg Pro His Cys Val Pro Phe Trp

1 5 10 15

Thr Gly Arg Ile Leu Leu Pro Ser Ala Ala Ser Val Cys Pro Ile Pro

20 25 30

Phe Glu Ala Cys His Leu Cys Gln Ala Met Thr Leu Arg Cys Pro Asn

35 40 45

Thr Gln Gly Cys Cys Ser Ser Trp Ala Ser

50 55

<210> 2056

<211> 90

<212> PROTEIN

<213> Homo sapiens

<400> 2056

Thr Asn Gln Ala Leu Pro Lys Ile Glu Val Ile Cys Arg Gly Thr Pro

1 5 10 15

Arg Cys Pro Ser Thr Val Pro Pro Ser Pro Ala Gln Pro Tyr Leu Arg

20 25 30

Val Ser Leu Pro Glu Asp Arg Tyr Thr Gln Ala Trp Ala Pro Thr Ser

35 40 45

Arg Thr Pro Trp Gly Ala Met Val Pro Arg Gly Val Ser Met Ala His

50 55 60

Lys Val Ala Thr Pro Gly Ser Gln Thr Ile Met Pro Cys Pro Met Pro

65 70 75 80

Thr Thr Pro Val Gln Ala Trp Leu Glu Ala

85 90

<210> 2057

<211> 41

<212> PROTEIN

<213> Homo sapiens

<400> 2057

Arg Met Glu Arg Glu Leu Lys Lys Trp Ser Ile Gln Thr Cys Leu Ser

1 5 10 15

Ala Arg Thr Gly Leu Ser Ile Ser Cys Thr Thr Leu Asn Ser Pro Pro

20 25 30

Leu Lys Lys Met Ser Met Pro Ala Val

35 40

<210> 2058

<211> 35

<212> PROTEIN

<213> Homo sapiens

<400> 2058

Leu Cys Ser Arg Tyr Ser Leu Phe Leu Ala Trp Arg Leu Ser Ser Val

1 5 10 15

Leu Gln Arg Phe Arg Phe Thr His Val Ile Gln Gln Arg Met Glu Ser

20 25 30

Gln Ile Ser

35

<210> 2059

<211> 39

<212> PROTEIN

<213> Homo sapiens

<400> 2059

Arg Ser Ala Cys Val Thr Val Lys Gly Pro Leu Ala Ser Val Gly Arg

1 5 10 15

His Ser Leu Ser Lys Gln Asp Cys Lys Phe Leu Pro Phe Trp Gly Phe

20 25 30

Leu Glu Glu Phe Leu Leu Cys

35

<210> 2060

<211> 97

<212> PROTEIN

<213> Homo sapiens

<400> 2060

Ile Gln Trp Gly Thr Thr Thr Ala Pro Arg Pro Ile Arg Pro Pro Phe

1 5 10 15

Leu Glu Ser Lys Gln Asn Cys Ser His Phe Pro Thr Pro Leu Leu Ala

20 25 30

Ser Glu Asp Arg Arg Glu Thr Gly Leu Phe Leu Pro Ser Ala Ala Gln

35 40 45

Lys Met Lys Lys Ala His Phe Leu Lys Thr Trp Phe Arg Ser Asn Pro

50 55 60

Thr Lys Thr Lys Lys Ala Arg Phe Ser Thr Ala Ser Leu Ala Lys Glu

65 70 75 80

Leu Thr His Pro Leu Leu Val Ser Leu Leu Leu Lys Glu Lys Gln Asp

85 90 95

Gly

<210> 2061

<211> 73

<212> PROTEIN

<213> Homo sapiens

<400> 2061

Pro Thr Asp Pro Phe Leu Gly Leu Arg Leu Gly Leu His Leu Gln Lys

1 5 10 15

Val Phe His Gln Ser His Ala Glu Tyr Ser Gly Ala Pro Pro Pro Pro

20 25 30

Pro Ala Pro Ser Gly Leu Arg Phe Trp Asn Pro Ser Arg Ile Ala His

35 40 45

Ile Ser Gln Leu Leu Ser Trp Pro Gln Lys Thr Glu Glu Arg Leu Gly

50 55 60

Tyr Ser Ser His Gln Leu Pro Arg Lys

65 70

<210> 2062

<211> 45

<212> PROTEIN

<213> Homo sapiens

<400> 2062

Phe Cys Cys Ser Cys Cys Phe Phe Gly Gly Glu Arg Trp Ser Lys Ser

1 5 10 15

Pro Tyr Cys Pro Gln Arg Met Thr Pro Gly Thr Thr Phe Ile Thr Met

20 25 30

Met Lys Lys Glu Ala Glu Lys Arg Thr Arg Thr Leu Thr

35 40 45

<210> 2063

<211> 95

<212> PROTEIN

<213> Homo sapiens

<400> 2063

Trp Arg Arg Asn Cys Lys Ala Pro Val Ser Leu Arg Lys Ser Val Gln

1 5 10 15

Thr Pro Ala Arg Ser Ser Pro Ala Arg Pro Asp Arg Thr Arg Arg Leu

20 25 30

Pro Ser Leu Gly Val Pro Gly Gln Pro Trp Ala Leu Gly Ala Ala Ala

35 40 45

Ser Arg Arg Cys Cys Cys Cys Cys Arg Ser Pro Leu Gly Ser Ala Arg

50 55 60

Ser Arg Ser Pro Ala Thr Leu Ala Leu Thr Pro Arg Ala Thr Arg Ser

65 70 75 80

Arg Cys Pro Gly Ala Thr Trp Arg Glu Ala Ala Ser Trp Ala Glu

85 90 95

<210> 2064

<211> 113

<212> PROTEIN

<213> Homo sapiens

<400> 2064

Pro Gly Arg Pro Leu Gln Thr His Val Leu Pro Glu Pro His Leu Ala

1 5 10 15

Leu Gln Pro Leu Gln Pro His Ala Asp His Ala His Ala Asp Ala Pro

20 25 30

Ala Ile Gln Pro Val Leu Trp Thr Thr Pro Pro Leu Gln His Gly His

35 40 45

Arg His Gly Leu Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg

50 55 60

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

65 70 75 80

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

85 90 95

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

100 105 110

His

<210> 2065

<211> 57

<212> PROTEIN

<213> Homo sapiens

<400> 2065

Pro Arg Pro Arg Arg Cys Thr Arg His Pro Ala Cys Pro Leu Asp His

1 5 10 15

Thr Thr Pro Pro Ala Trp Ser Pro Pro Trp Val Arg Ala Leu Leu Asp

20 25 30

Ala His Arg Ala Pro Ser Glu Ser Pro Cys Ser Pro Phe Arg Leu Ala

35 40 45

Phe Leu Gln Glu Gln Tyr His Glu Ala

50 55

<210> 2066

<211> 494

<212> PROTEIN

<213> Homo sapiens

<400> 2066

Thr Arg Arg Cys His Cys Cys Pro His Leu Arg Ser His Pro Cys Pro

1 5 10 15

His His Leu Arg Asn His Pro Arg Pro His His Leu Arg His His Ala

20 25 30

Cys His His His Leu Arg Asn Cys Pro His Pro His Phe Leu Arg His

35 40 45

Cys Thr Cys Pro Gly Arg Trp Arg Asn Arg Pro Ser Leu Arg Arg Leu

50 55 60

Arg Ser Leu Leu Cys Leu Pro His Leu Asn His His Leu Phe Leu His

65 70 75 80

Trp Arg Ser Arg Pro Cys Leu His Arg Lys Ser His Pro His Leu Leu

85 90 95

His Leu Arg Arg Leu Tyr Pro His His Leu Lys His Arg Pro Cys Pro

100 105 110

His His Leu Lys Asn Leu Leu Cys Pro Arg His Leu Arg Asn Cys Pro

115 120 125

Leu Pro Arg His Leu Lys His Leu Ala Cys Leu His His Leu Arg Ser

130 135 140

His Pro Cys Pro Leu His Leu Lys Ser His Pro Cys Leu His His Arg

145 150 155 160

Arg His Leu Val Cys Ser His His Leu Lys Ser Leu Leu Cys Pro Leu

165 170 175

His Leu Arg Ser Leu Pro Phe Pro His His Leu Arg His His Ala Cys

180 185 190

Pro His His Leu Arg Thr Arg Leu Cys Pro His His Leu Lys Asn His

195 200 205

Leu Cys Pro Pro His Leu Arg Tyr Arg Ala Tyr Pro Pro Cys Leu Trp

210 215 220

Cys His Ala Cys Leu His Arg Leu Arg Asn Leu Pro Cys Pro His Arg

225 230 235 240

Leu Arg Ser Leu Pro Arg Pro Leu His Leu Arg Leu His Ala Ser Pro

245 250 255

His His Leu Arg Thr Pro Pro His Pro His His Leu Arg Thr His Leu

260 265 270

Leu Pro His His Arg Arg Thr Arg Ser Cys Pro Cys Arg Trp Arg Ser

275 280 285

His Pro Cys Cys His Tyr Leu Arg Ser Arg Asn Ser Ala Pro Gly Pro

290 295 300

Arg Gly Arg Thr Cys His Pro Gly Leu Arg Ser Arg Thr Cys Pro Pro

305 310 315 320

Gly Leu Arg Ser His Thr Tyr Leu Arg Arg Leu Arg Ser His Thr Cys

325 330 335

Pro Pro Ser Leu Arg Ser His Ala Tyr Ala Leu Cys Leu Arg Ser His

340 345 350

Thr Cys Pro Pro Arg Leu Arg Asp His Ile Cys Pro Leu Ser Leu Arg

355 360 365

Asn Cys Thr Cys Pro Pro Arg Leu Arg Ser Arg Thr Cys Leu Leu Cys

370 375 380

Leu Arg Ser His Ala Cys Pro Pro Asn Leu Arg Asn His Thr Cys Pro

385 390 395 400

Pro Ser Leu Arg Ser His Ala Cys Pro Pro Gly Leu Arg Asn Arg Ile

405 410 415

Cys Pro Leu Ser Leu Arg Ser His Pro Cys Pro Leu Gly Leu Lys Ser

420 425 430

Pro Leu Arg Ser Gln Ala Asn Ala Leu His Leu Arg Ser Cys Pro Cys

435 440 445

Ser Leu Pro Leu Gly Asn His Pro Tyr Leu Pro Cys Leu Glu Ser Gln

450 455 460

Pro Cys Leu Ser Leu Gly Asn His Leu Cys Pro Leu Cys Pro Arg Ser

465 470 475 480

Cys Arg Cys Pro His Leu Gly Ser His Pro Cys Arg Leu Ser

485 490

<210> 2067

<211> 53

<212> PROTEIN

<213> Homo sapiens

<400> 2067

Ser Trp Lys Gly Thr Asn Trp Cys Asn Asp Met Cys Ile Phe Ile Thr

1 5 10 15

Ser Gly Gln Ile Phe Lys Gly Thr Arg Gly Pro Arg Phe Leu Trp Gly

20 25 30

Ser Lys Asp Gln Arg Gln Lys Gly Ser Asn Tyr Ser Gln Ser Glu Ala

35 40 45

Leu Cys Val Leu Leu

50

<210> 2068

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2068

Lys Arg Thr Lys Cys Phe Thr Phe Gly

15

<210> 2069

<211> 27

<212> PROTEIN

<213> Homo sapiens

<400> 2069

Pro Ile Phe Ile Gln Thr Leu Leu Leu Trp Asp Phe Leu Gln Lys Asp

1 5 10 15

Leu Lys Ala Tyr Thr Gly Thr Ile Leu Met Met

20 25

<210> 2070

<211> 22

<212> PROTEIN

<213> Homo sapiens

<400> 2070

Gln Lys Met Ile Leu Thr Lys Gln Ile Lys Thr Lys Pro Thr Asp Thr

1 5 10 15

Phe Leu Gln Ile Leu Arg

20

<210> 2071

<211> 43

<212> PROTEIN

<213> Homo sapiens

<400> 2071

Gly Phe Trp Ile Gln Ser Ile Lys Thr Ile Thr Arg Tyr Thr Ile Phe

1 5 10 15

Val Leu Lys Asp Ile Met Thr Pro Pro Asn Leu Ile Ala Glu Leu His

20 25 30

Asn Ile Leu Leu Lys Thr Ile Thr His His Ser

35 40

<210> 2072

<211> 40

<212> PROTEIN

<213> Homo sapiens

<400> 2072

Asn Tyr Ser Asn Val Gln Trp Arg Asn Leu Gln Ser Ser Val Cys Gly

1 5 10 15

Leu Pro Ala Lys Gly Glu Asp Ile Phe Leu Gln Phe Arg Thr His Thr

20 25 30

Thr Gly Arg Gln Val His Val Leu

35 40

<210> 2073

<211> 44

<212> PROTEIN

<213> Homo sapiens

<400> 2073

Tyr Gln Ser Arg Val Leu Pro Gln Thr Glu Gln Asp Ala Lys Lys Gly

1 5 10 15

Gln Asn Val Ser Leu Leu Gly Lys Tyr Ile Leu His Thr Arg Thr Arg

20 25 30

Gly Asn Leu Arg Lys Ser Arg Lys Trp Lys Ser Met

35 40

<210> 2074

<211> 85

<212> PROTEIN

<213> Homo sapiens

<400> 2074

Ser Ser Gln Asn Ala Arg Gly Cys Ser Pro Arg Gly Pro Cys Thr Ser

1 5 10 15

Ser Ser Tyr Thr Gly Gly Pro Cys Thr Ser Pro Leu Leu Ala Pro Val

20 25 30

Ile Phe Cys Pro Phe Pro Glu Asn Leu Pro Gly Gln Leu Arg Phe Pro

35 40 45

Ser Gly Leu Leu Ala Phe Trp Asp Ser Gln Val Cys Asp Leu His Val

50 55 60

Leu Pro Cys Pro Gln Gln Asp Val Leu Pro Thr Gly Gln Asp Leu Pro

65 70 75 80

Cys Ala Ala Val Gly

85

<210> 2075

<211> 72

<212> PROTEIN

<213> Homo sapiens

<400> 2075

Gly Ala Ala Pro Thr Met Ser Ala Ala Gln Ile Ala Met Val Trp Pro

1 5 10 15

Leu Leu Ser Ile Leu Ser Glu Trp Lys Glu Ile Cys Val Trp Ser Ile

20 25 30

Trp Met Thr Glu Thr Leu Phe Asp Ile Val Trp Trp Cys Pro Met Ser

35 40 45

Arg Leu Arg Leu Ala Leu Thr Val Pro Pro Ser Thr Thr Thr Thr Cys

50 55 60

Val Thr Val Pro Ala Trp Ala Ala

65 70

<210> 2076

<211> 97

<212> PROTEIN

<213> Homo sapiens

<400> 2076

Thr Gly Gly Pro Ser Ser Pro Ser Ser His Trp Lys Thr Pro Val Val

1 5 10 15

Ile Tyr Trp Asp Gly Thr Ala Leu Arg Cys Val Phe Val Pro Val Leu

20 25 30

Gly Glu Thr Gly Ala Gln Arg Lys Arg Ile Ser Ala Arg Lys Gly Ser

35 40 45

Leu Thr Thr Ser Cys Pro Gln Gly Ala Leu Ser Glu His Cys Pro Thr

50 55 60

Thr Pro Ala Pro Leu Pro Ser Gln Arg Arg Asn His Trp Met Glu Asn

65 70 75 80

Ile Ser Pro Phe Arg Ser Val Gly Val Ser Ala Ser Arg Cys Ser Glu

85 90 95

Ser

<210> 2077

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 2077

Phe His Thr Pro Ala Arg His Pro Arg Pro Arg His Gly His Leu Gln

1 5 10 15

Ala Val Thr Ala His Asp Gly Gly Cys Glu Ala Leu Pro Pro Pro

20 25 30

<210> 2078

<211> 78

<212> PROTEIN

<213> Homo sapiens

<400> 2078

Cys Cys Pro Arg Thr Ile Leu Asn Asn Gly Ser Leu Lys Thr Gln Val

1 5 10 15

Gln Met Lys Leu Pro Glu Cys Gln Arg Leu Leu Pro Pro Trp Pro Leu

20 25 30

His Gln Gln Leu Leu His Arg Arg Pro Leu His Gln Pro Pro Pro Gly

35 40 45

Pro Cys His Leu Leu Ser Leu Pro Arg Lys Pro Thr Arg Ala Ala Thr

50 55 60

Val Ser Val Trp Ala Ser Cys Ile Leu Gly Gln Pro Ser Leu

65 70 75

<210> 2079

<211> 28

<212> PROTEIN

<213> Homo sapiens

<400> 2079

Val Arg Lys His Phe Gln Thr Tyr Gly Asn Tyr Phe Leu Lys Thr Thr

1 5 10 15

Phe Cys Pro Pro Cys Arg Pro Lys Gln Trp Met Ile

20 25

<210> 2080

<211> 46

<212> PROTEIN

<213> Homo sapiens

<400> 2080

Leu Ala Arg Thr Pro Leu Pro Ser Thr Arg Cys Phe Ala Asn Trp Pro

1 5 10 15

Arg Pro Ala Leu Cys Ser Cys Gly Leu Ile Pro His Pro Arg Pro Ala

20 25 30

Pro Ala Ser Ala Pro Trp Pro Ser Thr Ser Ser His Ser Thr

35 40 45

<210> 2081

<211> 81

<212> PROTEIN

<213> Homo sapiens

<400> 2081

Glu Leu Gln Glu Thr Gly His Arg Gln Val Ala Leu Arg Arg Ser Gly

1 5 10 15

Arg Pro Pro Lys Cys Ala Glu Arg Pro Gly Ala Ala Asp Thr Gly Ala

20 25 30

His Cys Thr Ser Thr Asp Gly Arg Leu Lys Ile Ser Val Glu Thr Tyr

35 40 45

Thr Val Ser Ser Gln Leu Leu Met Val Leu Met Ser Leu Asp Leu Asp

50 55 60

Thr Gly Leu Val Pro Ser Leu Val Ser Lys Cys Leu Ile Leu Arg Val

65 70 75 80

Lys

<210> 2082

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2082

Lys Ser Asp Ala Ser Arg Leu Ser Gly Ala

1 5 10

<210> 2083

<211> 29

<212> PROTEIN

<213> Homo sapiens

<400> 2083

Arg Thr Ala Tyr Phe Cys Gln Tyr His Thr Ala Ser Val Tyr Ser Glu

1 5 10 15

Arg Ala Met Pro Pro Gly Cys Pro Glu Pro Ser Gln Ala

20 25

<210> 2084

<211> 91

<212> PROTEIN

<213> Homo sapiens

<400> 2084

Thr Arg Ala Ser Pro Pro Arg Ser Ser Ser Ala Ile Ala Val Arg Ala

1 5 10 15

Ser Cys Cys Pro Tyr Gly Ser Thr Ser Thr Ala Ser Arg Ser Pro Thr

20 25 30

Gln Arg Cys Arg Leu Ala Arg Ala Ala Ala Ser Thr Ala Thr Glu Val

35 40 45

Thr Phe Gly Ser Ser Glu Met Gln Gly His Thr Met Gly Phe Trp Leu

50 55 60

Thr Lys Leu Asn Tyr Leu Cys His Leu Ser Met Leu Thr Asp Ser Leu

65 70 75 80

Phe Leu Pro Ile Ser His Cys Gln Cys Ile Leu

85 90

<210> 2085

<211> 31

<212> PROTEIN

<213> Homo sapiens

<400> 2085

Ser Ser Leu Arg Ile Thr Gly Asp Trp Thr Ser Ser Gly Arg Ser Thr

1 5 10 15

Lys Ile Trp Lys Thr Thr Gln Met Cys Arg Lys Thr Trp Ser Gly

20 25 30

<210> 2086

<211> 104

<212> PROTEIN

<213> Homo sapiens

<400> 2086

Arg Arg Arg Arg Gly Gly Val Gly Arg Arg Gly Val Arg Pro Gly Arg

1 5 10 15

Val Arg Pro Gly Gly Thr Gly Arg Arg Gly Gly Asp Gly Gly Arg Ala

20 25 30

Ala Ala Ala Arg Ala Ala Leu Gly Glu Leu Ala Arg Ala Leu Pro Gly

35 40 45

His Leu Leu Gln Ser Gln Ser Ala Arg Arg Ala Ala Arg Met Ala Gln

50 55 60

Leu Arg Arg Arg Ala Ala Ala Leu Pro Asn Ala Ala Ala Trp His Gly

65 70 75 80

Pro Pro His Pro Gln Leu Pro Arg Ser Pro Leu Ala Leu Gln Arg Cys

85 90 95

Arg Asp Thr Arg Trp Ala Ser Gly

100

<210> 2087

<211> 66

<212> PROTEIN

<213> Homo sapiens

<400> 2087

Ser Cys Lys Val Phe Phe Lys Arg Ala Ala Glu Gly Lys Gln Lys Tyr

1 5 10 15

Leu Cys Ala Ser Arg Asn Asp Cys Thr Ile Asp Lys Phe Arg Arg Lys

20 25 30

Asn Cys Pro Ser Cys Arg Leu Arg Lys Cys Tyr Glu Ala Gly Met Thr

35 40 45

Leu Gly Glu Lys Phe Arg Val Gly Asn Cys Lys His Leu Lys Met Thr

50 55 60

Arg Pro

65

<210> 2088

<211> 49

<212> PROTEIN

<213> Homo sapiens

<400> 2088

Met Ala Gly Ala Pro Pro Pro Ala Ser Leu Pro Pro Cys Ser Leu Ile

1 5 10 15

Ser Asp Cys Cys Ala Ser Asn Gln Arg Asp Ser Val Gly Val Gly Pro

20 25 30

Ser Glu Pro Gly Asn Asn Ile Lys Ile Cys Asn Glu Ser Ala Ser Arg

35 40 45

Lys

<210> 2089

<211> 61

<212> PROTEIN

<213> Homo sapiens

<400> 2089

His Gly Trp Arg Pro Phe Leu Pro Val Arg Ala Arg Ser Arg Trp Asn

1 5 10 15

Arg Arg Leu Asp Val Thr Val Ala Asn Gly Arg Ser Trp Lys Tyr Gly

20 25 30

Trp Ser Leu Leu Arg Val Pro Gln Val Asn Gly Ile Gln Val Leu Asn

35 40 45

Val Ser Leu Lys Ser Ser Ser Asn Val Ile Ser Tyr Glu

50 55 60

<210> 2090

<211> 65

<212> PROTEIN

<213> Homo sapiens

<400> 2090

Arg Leu Lys Glu Val Phe Gln Thr Lys Ile Gln Glu Phe Arg Lys Ala

1 5 10 15

Cys Tyr Thr Leu Thr Gly Tyr Gln Ile Asp Ile Thr Thr Glu Asn Gln

20 25 30

Tyr Arg Leu Thr Ser Leu Tyr Ala Glu His Pro Gly Asp Cys Leu Ile

35 40 45

Phe Lys Leu Arg Val Pro Gly Ser Ser Val Leu Val Thr Val Pro Gly

50 55 60

Leu

65

<210> 2091

<211> 107

<212> PROTEIN

<213> Homo sapiens

<400> 2091

Ala Glu Val Leu Lys Val Ile Arg Gln Ser Ala Gly Gln Lys Thr Thr

1 5 10 15

Cys Gly Gln Gly Leu Glu Gly Pro Trp Glu Arg Pro Pro Pro Leu Asp

20 25 30

Glu Ser Glu Arg Asp Gly Gly Ser Glu Asp Gln Val Glu Asp Pro Ala

35 40 45

Leu Ser Ala Leu Leu Leu Arg Pro Arg Pro Pro Arg Pro Glu Val Gly

50 55 60

Ala His Gln Asp Glu Gln Ala Ala Gln Gly Ala Asp Pro Arg Leu Gly

65 70 75 80

Ala Gln Pro Ala Cys Arg Gly Leu Pro Gly Leu Leu Thr Val Pro Gln

85 90 95

Pro Glu Pro Leu Leu Ala Pro Pro Ser Ala Ala

100 105

<210> 2092

<211> 100

<212> PROTEIN

<213> Homo sapiens

<400> 2092

Glu Arg Ala Glu Trp Arg Glu Asn Ile Arg Glu Gln Gln Lys Lys Cys

1 5 10 15

Phe Arg Ser Phe Ser Leu Thr Ser Val Glu Leu Gln Met Leu Thr Asn

20 25 30

Ser Cys Val Lys Leu Gln Thr Val His Ser Ile Pro Leu Thr Ile Asn

35 40 45

Lys Glu Glu Ala Leu Gln Arg Pro Val Ala Ser Asp Phe Glu Pro Gln

50 55 60

Gly Leu Ser Glu Ala Ala Arg Trp Asn Ser Lys Glu Asn Leu Leu Ala

65 70 75 80

Gly Pro Ser Glu Asn Asp Pro Asn Leu Phe Val Ala Leu Tyr Asp Phe

85 90 95

Val Ala Ser Gly

100

<210> 2093

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 2093

Glu Leu Gln Met Leu Thr Asn Ser Cys Val Lys Leu Gln Thr Val His

1 5 10 15

Ser Ile Pro Leu Thr Ile Asn Lys Glu Asp Asp Glu Ser Pro Gly Leu

20 25 30

Tyr Gly Phe Leu Asn Val Ile Val His Ser Ala Thr Gly Phe Lys Gln

35 40 45

Ser Ser Lys Ala Leu Gln Arg Pro Val Ala Ser Asp Phe Glu Pro Gln

50 55 60

Gly Leu Ser Glu Ala Ala Arg Trp Asn Ser Lys Glu Asn Leu Leu Ala

65 70 75 80

Gly Pro Ser Glu Asn Asp Pro Asn Leu Phe Val Ala Leu Tyr Asp Phe

85 90 95

Val Ala Ser Gly Asp

100

<210> 2094

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 2094

Ile Ser Asn Ser Trp Asp Ala His Leu Gly Leu Gly Ala Cys Gly Glu

1 5 10 15

Ala Glu Gly Leu Gly Val Gln Gly Ala Glu Glu Glu Glu Glu Glu Glu

20 25 30

Glu Glu Glu Glu Glu Glu Gly Ala Gly Val Pro Ala Cys Pro Pro Lys

35 40 45

Gly Pro Glu Leu Phe Pro Leu Ile Phe Pro Ala Glu Pro Ala Gln Ala

50 55 60

Ser Gly Pro Tyr Val Glu Ile Ile Glu Gln Pro Lys Gln Arg Gly Met

65 70 75 80

Arg Phe Arg Tyr Lys Cys Glu Gly Arg Ser Ala Gly Ser Ile Pro Gly

85 90 95

Glu Arg Ser Thr Asp

100

<210> 2095

<211> 100

<212> PROTEIN

<213> Homo sapiens

<400> 2095

Leu Gln Arg Leu Asp Gly Met Gly Cys Leu Glu Phe Asp Glu Glu Arg

1 5 10 15

Ala Gln Gln Glu Asp Ala Leu Ala Gln Gln Ala Phe Glu Glu Ala Arg

20 25 30

Arg Arg Thr Arg Glu Phe Glu Asp Arg Asp Arg Ser His Arg Glu Glu

35 40 45

Met Glu Val His Glu Leu Glu Lys Ser Lys Arg Ala Leu Glu Thr Gln

50 55 60

Met Glu Glu Met Lys Thr Gln Leu Glu Glu Leu Glu Asp Glu Leu Gln

65 70 75 80

Ala Thr Glu Asp Ala Lys Leu Arg Leu Glu Val Asn Met Gln Ala Leu

85 90 95

Lys Gly Gln Phe

100

<210> 2096

<211> 100

<212> PROTEIN

<213> Homo sapiens

<400> 2096

Lys Gly Ser Phe Pro Glu Asn Leu Arg His Leu Lys Asn Thr Met Glu

1 5 10 15

Thr Ile Asp Trp Lys Val Phe Glu Ser Trp Met His His Trp Leu Leu

20 25 30

Phe Glu Met Ser Arg His Ser Leu Glu Gln Lys Pro Thr Asp Ala Pro

35 40 45

Pro Lys Ala Gly Val Pro Asn Lys Pro Gly Ile Pro Lys Leu Leu Glu

50 55 60

Gly Ser Lys Asn Ser Ile Gln Trp Glu Lys Ala Glu Asp Asn Gly Cys

65 70 75 80

Arg Ile Thr Tyr Tyr Ile Leu Glu Ile Arg Lys Ser Thr Ser Asn Asn

85 90 95

Leu Gln Asn Gln

100

<210> 2097

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 2097

Ser Trp Glu Asn Ser Asp Asp Ser Arg Asn Lys Leu Ser Lys Ile Pro

1 5 10 15

Ser Thr Pro Lys Leu Ile Pro Lys Val Thr Lys Thr Ala Asp Lys His

20 25 30

Lys Asp Val Ile Ile Asn Gln Ala Lys Met Ser Thr Arg Glu Lys Asn

35 40 45

Ser Gln Val Tyr Arg Arg Lys His Gln Glu Leu Gln Ala Met Gln Met

50 55 60

Glu Leu Gln Ser Pro Glu Tyr Lys Leu Ser Lys Leu Arg Thr Ser Thr

65 70 75 80

Ile Met Thr Asp Tyr Asn Pro Asn Tyr Cys Phe Ala Gly Lys Thr Ser

85 90 95

Ser Ile Ser Asp Leu

100

<210> 2098

<211> 100

<212> PROTEIN

<213> Homo sapiens

<400> 2098

Glu Gly His Arg Met Asp Lys Pro Ala Asn Cys Thr His Asp Leu Tyr

1 5 10 15

Met Ile Met Arg Glu Cys Trp His Ala Ala Pro Ser Gln Arg Pro Thr

20 25 30

Phe Lys Gln Leu Val Glu Asp Leu Asp Arg Val Leu Thr Val Thr Ser

35 40 45

Thr Asp Val Lys Ala Thr Gln Glu Glu Asn Arg Glu Leu Arg Ser Arg

50 55 60

Cys Glu Glu Leu His Gly Lys Asn Leu Glu Leu Gly Lys Ile Met Asp

65 70 75 80

Arg Phe Glu Glu Val Val Tyr Gln Ala Met Glu Glu Val Gln Lys Gln

85 90 95

Lys Glu Leu Ser

100

<210> 2099

<211> 107

<212> PROTEIN

<213> Homo sapiens

<400> 2099

Arg Asp Asn Thr Leu Leu Leu Arg Arg Val Glu Leu Phe Ser Leu Ser

1 5 10 15

Arg Gln Val Ala Arg Glu Ser Thr Tyr Leu Ser Ser Leu Lys Gly Ser

20 25 30

Arg Leu His Pro Glu Glu Leu Gly Gly Pro Pro Leu Lys Lys Leu Lys

35 40 45

Gln Glu Ala Thr Ser Lys Ser Gln Ile Met Ser Leu Trp Gly Leu Val

50 55 60

Ser Lys Met Pro Pro Glu Lys Val Gln Arg Leu Tyr Val Asp Phe Pro

65 70 75 80

Gln His Leu Arg His Leu Leu Gly Asp Trp Leu Glu Ser Gln Pro Trp

85 90 95

Glu Phe Leu Val Gly Ser Asp Ala Phe Cys Cys

100 105

<210> 2100

<211> 83

<212> PROTEIN

<213> Homo sapiens

<400> 2100

Met Ser Arg Glu Met Gln Asp Val Asp Leu Ala Glu Val Lys Pro Leu

1 5 10 15

Val Glu Lys Gly Glu Thr Ile Thr Gly Leu Leu Gln Glu Phe Asp Val

20 25 30

Gln Glu Ala Leu Ser Val Val Ser Glu Asp Gln Ser Leu Phe Glu Cys

35 40 45

Ala Tyr Gly Thr Pro His Leu Ala Lys Thr Glu Met Thr Ala Ser Ser

50 55 60

Ser Ser Asp Tyr Gly Gln Thr Ser Lys Met Ser Pro Arg Val Pro Gln

65 70 75 80

Gln Asp Trp

<210> 2101

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 2101

Val Leu Asp Met His Gly Phe Leu Arg Gln Ala Leu Cys Arg Leu Arg

1 5 10 15

Gln Glu Glu Pro Gln Ser Leu Gln Ala Ala Val Arg Thr Asp Gly Phe

20 25 30

Asp Glu Phe Lys Val Arg Leu Gln Asp Leu Ser Ser Cys Ile Thr Gln

35 40 45

Gly Lys Ala Ile Glu Thr Gln Ser Ser Ser Ser Glu Glu Ile Val Pro

50 55 60

Ser Pro Pro Ser Pro Pro Pro Leu Pro Arg Ile Tyr Lys Pro Cys Phe

65 70 75 80

Val Cys Gln Asp Lys Ser Ser Gly Tyr His Tyr Gly Val Ser Ala Cys

85 90 95

Glu Gly Cys Lys Gly

100

<210> 2102

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 2102

Arg Ser Ser Pro Glu Gln Pro Arg Pro Ser Thr Ser Lys Ala Val Ser

1 5 10 15

Pro Pro His Leu Asp Gly Pro Pro Ser Pro Arg Ser Pro Val Ile Gly

20 25 30

Ser Glu Val Phe Leu Pro Asn Ser Asn His Val Ala Ser Gly Ala Gly

35 40 45

Glu Ala Ala Ile Glu Thr Gln Ser Ser Ser Ser Glu Glu Ile Val Pro

50 55 60

Ser Pro Pro Ser Pro Pro Pro Leu Pro Arg Ile Tyr Lys Pro Cys Phe

65 70 75 80

Val Cys Gln Asp Lys Ser Ser Gly Tyr His Tyr Gly Val Ser Ala Cys

85 90 95

Glu Gly Cys Lys Gly

100

<210> 2103

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 2103

Val Ala Arg Phe Asn Asp Leu Arg Phe Val Gly Arg Ser Gly Arg Gly

1 5 10 15

Lys Ser Phe Thr Leu Thr Ile Thr Val Phe Thr Asn Pro Pro Gln Val

20 25 30

Ala Thr Tyr His Arg Ala Ile Lys Ile Thr Val Asp Gly Pro Arg Glu

35 40 45

Pro Arg Asn Arg Thr Glu Lys His Ser Thr Met Pro Asp Ser Pro Val

50 55 60

Asp Val Lys Thr Gln Ser Arg Leu Thr Pro Pro Thr Met Pro Pro Pro

65 70 75 80

Pro Thr Thr Gln Gly Ala Pro Arg Thr Ser Ser Phe Thr Pro Thr Thr

85 90 95

Leu Thr Asn Gly Thr

100

<210> 2104

<211> 55

<212> PROTEIN

<213> Homo sapiens

<400> 2104

Met Ala Leu Asn Ser Glu Ala Leu Ser Val Val Ser Glu Asp Gln Ser

1 5 10 15

Leu Phe Glu Cys Ala Tyr Gly Thr Pro His Leu Ala Lys Thr Glu Met

20 25 30

Thr Ala Ser Ser Ser Ser Asp Tyr Gly Gln Thr Ser Lys Met Ser Pro

35 40 45

Arg Val Pro Gln Gln Asp Trp

50 55

<210> 2105

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2105

Gly Gln Tyr Gly Lys Val Tyr Glu Gly

15

<210> 2106

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2106

Gly Gln Tyr Gly Lys Val Tyr Glu Gly Val

1 5 10

<210> 2107

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2107

Lys Leu Gly Gly Gly Gln Tyr Gly Lys

15

<210> 2108

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2108

Lys Leu Gly Gly Gly Gln Tyr Gly Lys Val

1 5 10

<210> 2109

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2109

Lys Val Tyr Glu Gly Val Trp Lys Lys

15

<210> 2110

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2110

Lys Val Tyr Glu Gly Val Trp Lys Lys Tyr

1 5 10

<210> 2111

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2111

Gln Tyr Gly Lys Val Tyr Glu Gly Val

15

<210> 2112

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2112

Gln Tyr Gly Lys Val Tyr Glu Gly Val Trp

1 5 10

<210> 2113

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2113

Gly Gln Tyr Gly Val Val Tyr Glu Gly

15

<210> 2114

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2114

Gly Gln Tyr Gly Val Val Tyr Glu Gly Val

1 5 10

<210> 2115

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2115

Lys Leu Gly Gly Gly Gln Tyr Gly Val

15

<210> 2116

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2116

Lys Leu Gly Gly Gly Gln Tyr Gly Val Val

1 5 10

<210> 2117

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2117

Gln Tyr Gly Val Val Tyr Glu Gly Val

15

<210> 2118

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2118

Gln Tyr Gly Val Val Tyr Glu Gly Val Trp

1 5 10

<210> 2119

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2119

Val Val Tyr Glu Gly Val Trp Lys Lys

15

<210> 2120

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2120

Val Val Tyr Glu Gly Val Trp Lys Lys Tyr

1 5 10

<210> 2121

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2121

Ala Thr Gln Ile Ser Ser Ala Thr Glu Tyr

1 5 10

<210> 2122

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2122

Ile Ser Ser Ala Thr Glu Tyr Leu Glu Lys

1 5 10

<210> 2123

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2123

Ser Ser Ala Thr Glu Tyr Leu Glu Lys

15

<210> 2124

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2124

Thr Gln Ile Ser Ser Ala Thr Glu Tyr Leu

1 5 10

<210> 2125

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2125

Tyr Met Ala Thr Gln Ile Ser Ser Ala Thr

1 5 10

<210> 2126

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2126

Phe Tyr Ile Ile Ile Glu Phe Met Thr Tyr

1 5 10

<210> 2127

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2127

Ile Ile Glu Phe Met Thr Tyr Gly Asn Leu

1 5 10

<210> 2128

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2128

Ile Ile Ile Glu Phe Met Thr Tyr Gly

15

<210> 2129

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2129

Ile Ile Ile Glu Phe Met Thr Tyr Gly Asn

1 5 10

<210> 2130

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2130

Tyr Ile Ile Ile Glu Phe Met Thr Tyr Gly

1 5 10

<210> 2131

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2131

Gly Gln His Gly Glu Val Tyr Glu Gly Val

1 5 10

<210> 2132

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2132

Lys Leu Gly Gly Gly Gln His Gly Glu Val

1 5 10

<210> 2133

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2133

Lys Ile Ala Asp Phe Gly Met Ala Arg

15

<210> 2134

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2134

Arg Val Ala Lys Ile Ala Asp Phe Gly Met

1 5 10

<210> 2135

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2135

Phe Ile Leu Met Glu Leu Met Ala Gly Gly

1 5 10

<210> 2136

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2136

Ile Leu Met Glu Leu Met Ala Gly Gly

15

<210> 2137

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2137

Ile Leu Met Glu Leu Met Ala Gly Gly Asp

1 5 10

<210> 2138

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2138

Leu Met Glu Leu Met Ala Gly Gly Asp Leu

1 5 10

<210> 2139

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2139

Leu Pro Arg Phe Ile Leu Met Glu Leu

15

<210> 2140

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2140

Leu Pro Arg Phe Ile Leu Met Glu Leu Met

1 5 10

<210> 2141

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2141

Leu Gln Ser Leu Pro Arg Phe Ile Leu Met

1 5 10

<210> 2142

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2142

Ser Leu Pro Arg Phe Ile Leu Met Glu Leu

1 5 10

<210> 2143

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2143

Leu Ala Thr Glu Lys Ser Arg Trp Ser

15

<210> 2144

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2144

Leu Ala Thr Glu Lys Ser Arg Trp Ser Gly

1 5 10

<210> 2145

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2145

Glu Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 2146

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 2146

Gly Pro Pro Pro Ala Asp Leu Cys His Ala Leu

1 5 10

<210> 2147

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2147

Gly Leu Leu Leu Glu Met Leu Asp Ala

15

<210> 2148

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2148

Leu Tyr Gly Leu Leu Leu Glu Met Leu

15

<210> 2149

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2149

Asn Val Val Pro Leu Tyr Gly Leu Leu

15

<210> 2150

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2150

Pro Leu Tyr Gly Leu Leu Leu Glu Met

15

<210> 2151

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2151

Pro Leu Tyr Gly Leu Leu Leu Glu Met Leu

1 5 10

<210> 2152

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2152

Val Pro Leu Tyr Gly Leu Leu Leu Glu Met

1 5 10

<210> 2153

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2153

Val Val Pro Leu Tyr Gly Leu Leu Leu

15

<210> 2154

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2154

Phe Leu Pro Ser Thr Leu Lys Ser Leu

15

<210> 2155

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2155

Gly Val Tyr Thr Phe Leu Pro Ser Thr

15

<210> 2156

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2156

Gly Val Tyr Thr Phe Leu Pro Ser Thr Leu

1 5 10

<210> 2157

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2157

Thr Phe Leu Pro Ser Thr Leu Lys Ser Leu

1 5 10

<210> 2158

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2158

Val Tyr Thr Phe Leu Pro Ser Thr Leu

15

<210> 2159

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2159

Tyr Thr Phe Leu Pro Ser Thr Leu Lys

15

<210> 2160

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2160

Asn Val Val Pro Leu Cys Asp Leu Leu

15

<210> 2161

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2161

Asn Val Val Pro Leu Cys Asp Leu Leu Leu

1 5 10

<210> 2162

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2162

Pro Leu Cys Asp Leu Leu Leu Glu Met

15

<210> 2163

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2163

Pro Leu Cys Asp Leu Leu Leu Glu Met Leu

1 5 10

<210> 2164

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2164

Val Pro Leu Cys Asp Leu Leu Leu Glu Met

1 5 10

<210> 2165

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2165

Val Val Pro Leu Cys Asp Leu Leu Leu

15

<210> 2166

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2166

Asn Val Val Pro Leu Asn Asp Leu Leu

15

<210> 2167

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2167

Asn Val Val Pro Leu Asn Asp Leu Leu Leu

1 5 10

<210> 2168

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2168

Pro Leu Asn Asp Leu Leu Leu Glu Met

15

<210> 2169

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2169

Pro Leu Asn Asp Leu Leu Leu Glu Met Leu

1 5 10

<210> 2170

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2170

Val Pro Leu Asn Asp Leu Leu Leu Glu Met

1 5 10

<210> 2171

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2171

Asn Val Val Pro Leu Ser Asp Leu Leu

15

<210> 2172

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2172

Asn Val Val Pro Leu Ser Asp Leu Leu Leu

1 5 10

<210> 2173

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2173

Pro Leu Ser Asp Leu Leu Leu Glu Met

15

<210> 2174

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2174

Pro Leu Ser Asp Leu Leu Leu Glu Met Leu

1 5 10

<210> 2175

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2175

Val Pro Leu Ser Asp Leu Leu Leu Glu Met

1 5 10

<210> 2176

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2176

Val Val Pro Leu Ser Asp Leu Leu Leu

15

<210> 2177

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2177

Val Leu Glu Arg Cys Pro His Arg Pro Ile

1 5 10

<210> 2178

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2178

Tyr Thr Leu Asp Val Leu Glu Arg Cys

15

<210> 2179

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2179

Phe Gln Asn Gly Lys Met Ala Leu Ser

15

<210> 2180

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2180

Val Met Ala Gly Leu Gly Ser Pro Tyr Val

1 5 10

<210> 2181

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2181

Lys Pro Ile Ile Ile Gly His His Ala

15

<210> 2182

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2182

Lys Pro Ile Ile Ile Gly Cys His Ala

15

<210> 2183

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2183

Lys Pro Ile Ile Ile Gly Gly His Ala

15

<210> 2184

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2184

Lys Pro Ile Ile Ile Gly Ser His Ala

15

<210> 2185

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2185

Ile Ile Glu Tyr Cys Cys Tyr Gly Asp Leu

1 5 10

<210> 2186

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2186

Thr Ile Gly Gly Pro Thr Leu Val Ile Ile

1 5 10

<210> 2187

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2187

Val Ile Ile Glu Tyr Cys Cys Tyr Gly

15

<210> 2188

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2188

His Met Asn Ile Ala Asn Leu Leu Gly Ala

1 5 10

<210> 2189

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2189

Ile Ala Asn Leu Leu Gly Ala Cys Thr Ile

1 5 10

<210> 2190

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2190

Met Asn Ile Ala Asn Leu Leu Gly Ala

15

<210> 2191

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2191

Tyr Leu Gly Asn His Met Asn Ile Ala

15

<210> 2192

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2192

Tyr Leu Gly Asn His Met Asn Ile Ala Asn

1 5 10

<210> 2193

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2193

Val Leu His Glu Ser Asn Ser Pro Tyr

15

<210> 2194

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2194

Val Leu His Glu Ser Asn Ser Pro Tyr Ile

1 5 10

<210> 2195

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2195

Leu Gln Val Leu His Glu Cys Asn Ser Leu

1 5 10

<210> 2196

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2196

Leu Tyr Ile Val Gly Phe Tyr Gly Ala Phe

1 5 10

<210> 2197

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2197

Asn Ser Leu Tyr Ile Val Gly Phe Tyr

15

<210> 2198

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2198

Gln Val Leu His Glu Cys Asn Ser Leu

15

<210> 2199

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2199

Ser Leu Tyr Ile Val Gly Phe Tyr Gly

15

<210> 2200

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2200

Ser Leu Tyr Ile Val Gly Phe Tyr Gly Ala

1 5 10

<210> 2201

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2201

Val Leu His Glu Cys Asn Ser Leu Tyr

15

<210> 2202

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2202

Val Leu His Glu Cys Asn Ser Leu Tyr Ile

1 5 10

<210> 2203

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2203

Phe Tyr Gln Gln Gln Gln Gln Ser Asp Leu

1 5 10

<210> 2204

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2204

Gln Gln Gln Ser Asp Leu Gln Pro Pro Ala

1 5 10

<210> 2205

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2205

Gln Gln Ser Asp Leu Gln Pro Pro Ala

15

<210> 2206

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2206

Tyr Gln Gln Gln Gln Gln Ser Asp Leu

15

<210> 2207

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2207

Phe Glu Leu Leu Ser Thr Pro Pro Leu

15

<210> 2208

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2208

Leu Leu Ser Thr Pro Pro Leu Ser Pro Ser

1 5 10

<210> 2209

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2209

Phe Glu Leu Leu Pro Ile Pro Pro Leu

15

<210> 2210

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2210

Ile Trp Lys Lys Phe Glu Leu Leu Pro Ile

1 5 10

<210> 2211

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2211

Leu Leu Pro Ile Pro Pro Leu Ser Pro Ser

1 5 10

<210> 2212

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2212

Leu Pro Ile Pro Pro Leu Ser Pro Ser

15

<210> 2213

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2213

Ile Ile Glu Tyr Cys Phe Tyr Gly Asp Leu

1 5 10

<210> 2214

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2214

Ile Ile Ile Glu Tyr Cys Phe Tyr Gly

15

<210> 2215

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2215

Ile Tyr Ile Ile Ile Glu Tyr Cys Phe

15

<210> 2216

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2216

Ile Tyr Ile Ile Ile Glu Tyr Cys Phe Tyr

1 5 10

<210> 2217

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2217

Tyr Ile Ile Ile Glu Tyr Cys Phe Tyr Gly

1 5 10

<210> 2218

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2218

Lys Ile Thr Glu Gln Glu Lys Asp Phe Leu

1 5 10

<210> 2219

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 2219

Ser Thr Arg Asp Pro Leu Ser Glu Ile Thr Lys

1 5 10

<210> 2220

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 2220

Asp Pro Leu Ser Glu Ile Thr Lys

15

<210> 2221

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2221

Leu Pro Leu Lys Phe Arg Asp Ala Glu Thr

1 5 10

<210> 2222

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2222

Gln Thr Gly Val Met Ile Cys Ala Tyr Leu

1 5 10

<210> 2223

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2223

Ala Phe Ser Gly Glu Tyr Ile Pro Thr Val

1 5 10

<210> 2224

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2224

Ser Met Asn Arg Arg Pro Ile Leu Thr

15

<210> 2225

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2225

Tyr Met Cys Asn Ser Ser Cys Met Gly Ser

1 5 10

<210> 2226

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2226

Gly Met Asn Gln Arg Pro Ile Leu Thr

15

<210> 2227

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2227

Gly Met Asn Trp Arg Pro Ile Leu Thr

15

<210> 2228

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2228

Leu Leu Gly Arg Asn Ser Phe Glu Val Cys

1 5 10

<210> 2229

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2229

Ala Leu Lys Tyr Ile Phe Val Ala Val

15

<210> 2230

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2230

Ala Leu Lys Tyr Ile Phe Val Ala Val Arg

1 5 10

<210> 2231

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2231

Ala Val Arg Ala Ile Cys Val Met Lys

15

<210> 2232

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2232

Ala Val Arg Ala Ile Cys Val Met Lys Ser

1 5 10

<210> 2233

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2233

Cys Val Glu Lys Lys Thr Ala Leu Lys

15

<210> 2234

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2234

Cys Val Glu Lys Lys Thr Ala Leu Lys Tyr

1 5 10

<210> 2235

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2235

Cys Val Met Lys Ser Phe Leu Ile Phe

15

<210> 2236

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2236

Cys Val Met Lys Ser Phe Leu Ile Phe Arg

1 5 10

<210> 2237

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2237

Phe Leu Ile Phe Arg Arg Trp Lys Ser

15

<210> 2238

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2238

Phe Arg Arg Trp Lys Ser His Ser Pro Leu

1 5 10

<210> 2239

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2239

Phe Val Ala Val Arg Ala Ile Cys Val

15

<210> 2240

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2240

Phe Val Ala Val Arg Ala Ile Cys Val Met

1 5 10

<210> 2241

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2241

Ile Gln Leu His Leu Ser His Pro Ile

15

<210> 2242

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2242

Lys Ser Phe Leu Ile Phe Arg Arg Trp Lys

1 5 10

<210> 2243

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2243

Lys Thr Ala Leu Lys Tyr Ile Phe Val

15

<210> 2244

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2244

Lys Tyr Ile Phe Val Ala Val Arg Ala Ile

1 5 10

<210> 2245

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2245

Arg Trp Lys Ser His Ser Pro Leu Gln Ile

1 5 10

<210> 2246

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2246

Thr Ala Leu Lys Tyr Ile Phe Val Ala Val

1 5 10

<210> 2247

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2247

Val Ala Val Arg Ala Ile Cys Val Met Lys

1 5 10

<210> 2248

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2248

Val Met Lys Ser Phe Leu Ile Phe Arg

15

<210> 2249

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2249

Val Met Lys Ser Phe Leu Ile Phe Arg Arg

1 5 10

<210> 2250

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2250

Tyr Ile Phe Val Ala Val Arg Ala Ile

15

<210> 2251

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2251

Ala Leu Phe Phe Phe Phe Phe Glu Thr

15

<210> 2252

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2252

Ala Leu Phe Phe Phe Phe Glu Thr Lys

1 5 10

<210> 2253

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2253

Ala Gln Ala Gly Val Gln Trp Arg Ser Leu

1 5 10

<210> 2254

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2254

Cys Leu Ala Asn Phe Cys Ile Phe Asn Arg

1 5 10

<210> 2255

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2255

Cys Leu Ser Phe Leu Ser Ser Trp Asp Tyr

1 5 10

<210> 2256

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2256

Phe Phe Glu Thr Lys Ser Cys Ser Val

15

<210> 2257

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2257

Phe Phe Phe Glu Thr Lys Ser Cys Ser Val

1 5 10

<210> 2258

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2258

Phe Lys Leu Phe Ser Cys Leu Ser Phe Leu

1 5 10

<210> 2259

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2259

Phe Leu Ser Ser Trp Asp Tyr Arg Arg Met

1 5 10

<210> 2260

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2260

Gly Phe Lys Leu Phe Ser Cys Leu Ser Phe

1 5 10

<210> 2261

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2261

Lys Leu Phe Ser Cys Leu Ser Phe Leu

15

<210> 2262

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2262

Lys Leu Phe Ser Cys Leu Ser Phe Leu Ser

1 5 10

<210> 2263

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2263

Leu Ala Leu Phe Phe Phe Phe Phe Glu Thr

1 5 10

<210> 2264

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2264

Leu Phe Phe Phe Phe Glu Thr Lys

15

<210> 2265

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2265

Leu Ser Phe Leu Ser Ser Trp Asp Tyr

15

<210> 2266

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2266

Leu Ser Phe Leu Ser Ser Trp Asp Tyr Arg

1 5 10

<210> 2267

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2267

Arg Met Pro Pro Cys Leu Ala Asn Phe

15

<210> 2268

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2268

Arg Arg Met Pro Pro Cys Leu Ala Asn Phe

1 5 10

<210> 2269

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2269

Ser Leu Gln Pro Pro Pro Pro Gly Phe Lys

1 5 10

<210> 2270

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2270

Val Gln Trp Arg Ser Leu Gly Ser Leu

15

<210> 2271

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2271

Phe Phe Phe Ser Val Ile Phe Ser Thr

15

<210> 2272

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2272

Met Ser Val Cys Phe Phe Phe Phe Ser Val

1 5 10

<210> 2273

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2273

Ser Val Cys Phe Phe Phe Phe Ser Val

15

<210> 2274

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2274

Ser Val Cys Phe Phe Phe Phe Ser Val Ile

1 5 10

<210> 2275

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2275

Phe Phe Cys Tyr Ile Leu Asn Thr Met Phe

1 5 10

<210> 2276

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2276

Met Ser Val Cys Phe Phe Phe Phe Cys Tyr

1 5 10

<210> 2277

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2277

Ser Val Cys Phe Phe Phe Phe Cys Tyr Ile

1 5 10

<210> 2278

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2278

Lys Gln Trp Ser Ser Val Thr Ser Leu

15

<210> 2279

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2279

Val Leu Trp Met Pro Thr Ser Thr Val

15

<210> 2280

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2280

Ile Leu Ile Arg Lys Ala Met Thr Val

15

<210> 2281

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 2281

Arg Met Lys Val Pro Leu Met Lys

15

<210> 2282

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2282

Thr Leu Lys Lys Lys Pro Arg Asp Ile

15

<210> 2283

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2283

Leu Ile Glu Gly Phe Glu Ala Leu Leu Lys

1 5 10

<210> 2284

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2284

Gln Gln Leu Lys Trp Thr Pro His Ile

15

<210> 2285

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2285

Gln Leu Lys Trp Thr Pro His Ile Leu Lys

1 5 10

<210> 2286

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2286

Ile Val Ser Glu Lys Asn Gln Gln Leu Lys

1 5 10

<210> 2287

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2287

Gln Leu Lys Trp Thr Pro His Ile Leu Lys

1 5 10

<210> 2288

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2288

Gln Gln Leu Lys Trp Thr Pro His Ile

15

<210> 2289

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 2289

Asn Gln Gln Leu Lys Trp Thr Pro His Ile Leu

1 5 10

<210> 2290

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2290

Asn Gln Gln Leu Lys Trp Thr Pro His Ile

1 5 10

<210> 2291

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2291

Gln Leu Lys Trp Thr Pro His Ile Leu

15

<210> 2292

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2292

Gly Pro Pro Arg Pro Pro Arg Ala Ala Cys

1 5 10

<210> 2293

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2293

Pro Pro Arg Pro Pro Arg Ala Ala Cys

15

<210> 2294

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2294

Ser Leu Arg Arg Lys Tyr Leu Arg Val

15

<210> 2295

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2295

Ser Ala Ala Cys His Arg Arg Gly Cys Val

1 5 10

<210> 2296

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2296

Ala Leu Trp Glu Cys Ser Leu Pro Gln Ala

1 5 10

<210> 2297

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2297

Cys Leu Ile Val Ser Arg Thr Leu Leu

15

<210> 2298

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2298

Cys Leu Ile Val Ser Arg Thr Leu Leu Leu

1 5 10

<210> 2299

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2299

Phe Leu Leu Ala Leu Trp Glu Cys Ser

15

<210> 2300

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2300

Phe Leu Leu Ala Leu Trp Glu Cys Ser Leu

1 5 10

<210> 2301

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2301

Ile Val Ser Arg Thr Leu Leu Leu Val

15

<210> 2302

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2302

Leu Ile Val Ser Arg Thr Leu Leu Leu

15

<210> 2303

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2303

Leu Ile Val Ser Arg Thr Leu Leu Leu Val

1 5 10

<210> 2304

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2304

Leu Leu Ala Leu Trp Glu Cys Ser Leu

15

<210> 2305

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2305

Leu Pro Gln Ala Arg Leu Cys Leu Ile

15

<210> 2306

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2306

Leu Pro Gln Ala Arg Leu Cys Leu Ile Val

1 5 10

<210> 2307

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2307

Asn Val Arg Asp Lys Lys Arg Ala Thr Phe

1 5 10

<210> 2308

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2308

Ser Leu Pro Gln Ala Arg Leu Cys Leu Ile

1 5 10

<210> 2309

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2309

Phe Phe Cys Trp Ile Leu Ser Cys Lys

15

<210> 2310

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2310

Phe Phe Phe Cys Trp Ile Leu Ser Cys Lys

1 5 10

<210> 2311

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2311

Ile Thr Ala Phe Phe Phe Cys Trp Ile

15

<210> 2312

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2312

Leu Tyr Ile Thr Ala Phe Phe Phe Cys Trp

1 5 10

<210> 2313

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2313

Tyr Ile Thr Ala Phe Phe Phe Cys Trp Ile

1 5 10

<210> 2314

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2314

Ile Thr Ala Phe Phe Leu Leu Asp Ile

15

<210> 2315

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2315

Leu Leu Tyr Ile Thr Ala Phe Phe Leu

15

<210> 2316

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2316

Leu Leu Tyr Ile Thr Ala Phe Phe Leu Leu

1 5 10

<210> 2317

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2317

Leu Tyr Ile Thr Ala Phe Phe Leu Leu

15

<210> 2318

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2318

Leu Tyr Ile Thr Ala Phe Phe Leu Leu Asp

1 5 10

<210> 2319

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2319

Tyr Ile Thr Ala Phe Phe Leu Leu Asp Ile

1 5 10

<210> 2320

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2320

Gly Ser Asn Glu Val Thr Thr Arg Tyr

15

<210> 2321

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2321

Met Pro Lys Asp Val Asn Ile Gln Val

15

<210> 2322

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2322

Thr Gly Ser Asn Glu Val Thr Thr Arg Tyr

1 5 10

<210> 2323

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2323

Lys Lys Leu Met Leu Leu Arg Leu Asn Leu

1 5 10

<210> 2324

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2324

Lys Leu Met Leu Leu Arg Leu Asn Leu

15

<210> 2325

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2325

Lys Leu Met Leu Leu Arg Leu Asn Leu Arg

1 5 10

<210> 2326

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2326

Leu Leu Arg Leu Asn Leu Arg Lys Met

15

<210> 2327

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 2327

Leu Met Leu Leu Arg Leu Asn Leu

15

<210> 2328

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2328

Leu Met Leu Leu Arg Leu Asn Leu Arg Lys

1 5 10

<210> 2329

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2329

Leu Asn Leu Arg Lys Met Cys Gly Pro Phe

1 5 10

<210> 2330

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2330

Met Leu Leu Arg Leu Asn Leu Arg Lys

15

<210> 2331

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2331

Met Leu Leu Arg Leu Asn Leu Arg Lys Met

1 5 10

<210> 2332

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2332

Asn Leu Arg Lys Met Cys Gly Pro Phe

15

<210> 2333

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2333

Asn Tyr Cys Gln Lys Lys Leu Met Leu Leu

1 5 10

<210> 2334

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2334

Tyr Cys Gln Lys Lys Leu Met Leu Leu

15

<210> 2335

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2335

Phe Lys Lys Lys Thr Tyr Thr Cys Ala Ile

1 5 10

<210> 2336

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2336

Ile Thr Thr Val Lys Ala Thr Glu Thr Lys

1 5 10

<210> 2337

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2337

Lys Ser Lys Lys Lys Glu Thr Phe Lys

15

<210> 2338

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2338

Lys Ser Lys Lys Lys Glu Thr Phe Lys Lys

1 5 10

<210> 2339

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2339

Lys Thr Tyr Thr Cys Ala Ile Thr Thr Val

1 5 10

<210> 2340

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2340

Thr Phe Lys Lys Lys Thr Tyr Thr Cys

15

<210> 2341

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2341

Thr Tyr Thr Cys Ala Ile Thr Thr Val

15

<210> 2342

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2342

Thr Tyr Thr Cys Ala Ile Thr Thr Val Lys

1 5 10

<210> 2343

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2343

Tyr Thr Cys Ala Ile Thr Thr Val Lys

15

<210> 2344

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2344

Thr Ala Lys Ser Lys Lys Arg Asn Leu

15

<210> 2345

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2345

Phe Ala Leu Cys Gly Phe Trp Gln Ile

15

<210> 2346

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 2346

Leu Lys Lys Leu Arg Ser Pro Leu

15

<210> 2347

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 2347

Ser Leu Lys Lys Val Pro Ala Leu

15

<210> 2348

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2348

Arg Lys Ile Ser Asn Trp Ser Leu Lys Lys

1 5 10

<210> 2349

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 2349

Val Pro Ala Leu Lys Lys Leu Arg Ser Pro Leu

1 5 10

<210> 2350

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2350

Lys Arg Val Asn Thr Ala Trp Lys Thr Lys

1 5 10

<210> 2351

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2351

Met Thr Lys Lys Lys Arg Val Asn Thr Ala

1 5 10

<210> 2352

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2352

Arg Val Asn Thr Ala Trp Lys Thr Lys

15

<210> 2353

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2353

Arg Val Asn Thr Ala Trp Lys Thr Lys Lys

1 5 10

<210> 2354

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2354

Thr Lys Lys Lys Arg Val Asn Thr Ala

15

<210> 2355

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2355

Trp Lys Thr Lys Lys Thr Ser Phe Ser Leu

1 5 10

<210> 2356

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2356

Ala Leu Met Ser Ala Met Thr Thr Ser

15

<210> 2357

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2357

Ala Met Thr Thr Ser Ser Ser Gln Lys

15

<210> 2358

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2358

Ala Met Thr Thr Ser Ser Ser Gln Lys Asn

1 5 10

<210> 2359

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2359

Cys Ile Met Lys Glu Lys Lys Ser Leu

15

<210> 2360

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2360

Cys Ile Met Lys Glu Lys Lys Ser Leu Val

1 5 10

<210> 2361

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 2361

Ile Met Lys Glu Lys Lys Ser Leu

15

<210> 2362

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2362

Ile Met Lys Glu Lys Lys Ser Leu Val

15

<210> 2363

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2363

Lys Ser Leu Val Arg Leu Ser Ser Cys Val

1 5 10

<210> 2364

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2364

Leu Val Arg Leu Ser Ser Cys Val Pro Val

1 5 10

<210> 2365

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2365

Arg Leu Ser Ser Cys Val Pro Val Ala

15

<210> 2366

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2366

Arg Leu Ser Ser Cys Val Pro Val Ala Leu

1 5 10

<210> 2367

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2367

Ser Ala Met Thr Thr Ser Ser Ser Gln Lys

1 5 10

<210> 2368

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2368

Ser Leu Val Arg Leu Ser Ser Cys Val

15

<210> 2369

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2369

Val Pro Val Ala Leu Met Ser Ala Met

15

<210> 2370

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2370

Val Arg Leu Ser Ser Cys Val Pro Val Ala

1 5 10

<210> 2371

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2371

Lys Met Arg Lys Lys Tyr Ala Gln Lys

15

<210> 2372

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2372

Phe Val Met Ser Asp Thr Thr Tyr Lys

15

<210> 2373

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2373

Phe Val Met Ser Asp Thr Thr Tyr Lys Ile

1 5 10

<210> 2374

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2374

Lys Thr Phe Glu Lys Lys Gly Glu Lys

15

<210> 2375

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2375

Leu Phe Val Met Ser Asp Thr Thr Tyr Lys

1 5 10

<210> 2376

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2376

Met Ser Asp Thr Thr Tyr Lys Ile Tyr

15

<210> 2377

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2377

Val Met Ser Asp Thr Thr Tyr Lys Ile

15

<210> 2378

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2378

Val Met Ser Asp Thr Thr Tyr Lys Ile Tyr

1 5 10

<210> 2379

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2379

Tyr Leu Thr Lys Trp Pro Lys Phe Phe Leu

1 5 10

<210> 2380

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2380

Phe Leu Gln Glu Arg Asn Leu Pro Pro

15

<210> 2381

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2381

Phe Arg Arg Pro His Ser Cys Leu Ala

15

<210> 2382

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2382

Leu Ile Val Leu Arg Val Val Arg Leu

15

<210> 2383

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2383

Leu Leu Ser Val His Leu Ile Val Leu

15

<210> 2384

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2384

Glu Val Lys His Leu His His Leu Leu

15

<210> 2385

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2385

His Leu His His Leu Leu Lys Gln Leu Lys

1 5 10

<210> 2386

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2386

His Leu Leu Leu Lys Arg Glu Arg Val

15

<210> 2387

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2387

Lys Ile Lys His Leu Leu Leu Lys Arg

15

<210> 2388

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2388

Lys Pro Ser Glu Lys Tyr Leu Lys Ile

15

<210> 2389

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2389

Lys Tyr Leu Lys Ile Lys His Leu Leu

15

<210> 2390

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2390

Lys Tyr Leu Lys Ile Lys His Leu Leu Leu

1 5 10

<210> 2391

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2391

Leu Leu Lys Gln Leu Lys Pro Ser Glu Lys

1 5 10

<210> 2392

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2392

Leu Leu Lys Arg Glu Arg Val Asp Leu

15

<210> 2393

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2393

Leu Leu Leu Lys Arg Glu Arg Val Asp Leu

1 5 10

<210> 2394

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2394

Gln Leu Lys Pro Ser Glu Lys Tyr Leu Lys

1 5 10

<210> 2395

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2395

Tyr Leu Lys Ile Lys His Leu Leu Leu

15

<210> 2396

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2396

Tyr Leu Lys Ile Lys His Leu Leu Leu Lys

1 5 10

<210> 2397

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2397

Ile Leu Pro Arg Lys Val Leu Gln Met

15

<210> 2398

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2398

Lys Val Leu Gln Met Asp Phe Leu Val

15

<210> 2399

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2399

Leu Pro Arg Lys Val Leu Gln Met Asp Phe

1 5 10

<210> 2400

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2400

Leu Gln Met Asp Phe Leu Val His Pro Ala

1 5 10

<210> 2401

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2401

Gln Met Asp Phe Leu Val His Pro Ala

15

<210> 2402

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2402

Tyr Ile Leu Pro Arg Lys Val Leu Gln Met

1 5 10

<210> 2403

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2403

Ala Pro Ser Pro Ala Ser Arg Leu Gln Cys

1 5 10

<210> 2404

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2404

His Pro Leu Ala Pro Met Pro Ser Lys Thr

1 5 10

<210> 2405

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2405

Ile Leu Pro Leu Pro Gln Leu Leu Leu

15

<210> 2406

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2406

Leu Leu Leu Ser Ala Asp Gln Gln Ala

15

<210> 2407

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2407

Leu Pro Thr Gln Thr Arg Gly Cys Ile

15

<210> 2408

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2408

Leu Pro Thr Gln Thr Arg Gly Cys Ile Leu

1 5 10

<210> 2409

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2409

Arg Ile Ser Cys Leu Pro Thr Gln Thr Arg

1 5 10

<210> 2410

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2410

Ser Leu Ala Glu Thr Val Ser Leu His

15

<210> 2411

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2411

Thr Pro Arg Ser Ser Ser Ser Ser Ser

15

<210> 2412

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2412

Thr Pro Arg Ser Ser Ser Ser Ser Ser Ser

1 5 10

<210> 2413

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2413

Ala Leu Pro Pro Val Leu Leu Ser Leu

15

<210> 2414

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2414

Ala Leu Pro Pro Val Leu Leu Ser Leu Ala

1 5 10

<210> 2415

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2415

Ala Leu Pro Arg Pro Leu Leu Ala Leu

15

<210> 2416

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2416

Ala Ser Arg Thr Ala Ser Cys Ile Leu

15

<210> 2417

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2417

Glu Ala Leu Pro Arg Pro Leu Leu Ala Leu

1 5 10

<210> 2418

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2418

His Leu Gly His Pro Val Ala Ser Arg

15

<210> 2419

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2419

His Pro Val Ala Ser Arg Thr Ala Ser

15

<210> 2420

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2420

His Pro Val Ala Ser Arg Thr Ala Ser Cys

1 5 10

<210> 2421

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2421

Ile Ile Gln Leu Ser Leu Leu Ser Leu Leu

1 5 10

<210> 2422

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2422

Ile Gln Leu Ser Leu Leu Ser Leu Leu

15

<210> 2423

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2423

Ile Gln Leu Ser Leu Leu Ser Leu Leu Ile

1 5 10

<210> 2424

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2424

Leu Leu Ala Leu Pro Pro Val Leu Leu

15

<210> 2425

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2425

Leu Leu Ile Pro Pro Leu Thr Cys Leu

15

<210> 2426

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2426

Leu Leu Ile Pro Pro Leu Thr Cys Leu Ala

1 5 10

<210> 2427

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2427

Leu Leu Ser Leu Leu Ile Pro Pro Leu

15

<210> 2428

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2428

Leu Leu Ser Leu Leu Ile Pro Pro Leu Thr

1 5 10

<210> 2429

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2429

Leu Pro Arg Pro Leu Leu Ala Leu Pro Pro

1 5 10

<210> 2430

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2430

Gln Leu Ser Leu Leu Ser Leu Leu Ile

15

<210> 2431

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2431

Arg Leu Leu Gln Cys Gln Ala Thr Arg

15

<210> 2432

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2432

Arg Pro Leu Leu Ala Leu Pro Pro Val

15

<210> 2433

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2433

Arg Pro Leu Leu Ala Leu Pro Pro Val Leu

1 5 10

<210> 2434

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2434

Ser Leu Ala Gln Asp His Ser Arg Leu

15

<210> 2435

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2435

Ser Leu Ala Gln Asp His Ser Arg Leu Leu

1 5 10

<210> 2436

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2436

Ser Leu Leu Ile Pro Pro Leu Thr Cys Leu

1 5 10

<210> 2437

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2437

Ser Leu Leu Ser Leu Leu Ile Pro Pro

15

<210> 2438

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2438

Ser Leu Leu Ser Leu Leu Ile Pro Pro Leu

1 5 10

<210> 2439

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2439

Ala Ala Ala Thr Ser Ala Ala Ser Thr Leu

1 5 10

<210> 2440

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2440

Ala Ala Ile Pro Ala Ser Thr Ser Ala Val

1 5 10

<210> 2441

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2441

Ala Ile Pro Ala Ser Thr Ser Ala Val

15

<210> 2442

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2442

Ala Leu Pro Ala Gly Cys Val Ser Ser Ala

1 5 10

<210> 2443

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2443

Ala Pro Leu Leu Thr Ala Thr Gly Ser Val

1 5 10

<210> 2444

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2444

Ala Pro Val Leu Ser Ala Ser Ile Leu

15

<210> 2445

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2445

Ala Thr Leu Leu Pro Ala Thr Thr Val

15

<210> 2446

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2446

Ala Thr Val Ser Thr Thr Thr Ala Pro Val

1 5 10

<210> 2447

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2447

Ala Val Pro Ala Asn Cys Leu Phe Pro Ala

1 5 10

<210> 2448

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2448

Cys Leu Phe Pro Ala Ala Leu Pro Ser Thr

1 5 10

<210> 2449

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2449

Cys Pro Thr Phe Val Ser Ala Ala Ala

15

<210> 2450

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2450

Phe Pro Ala Ala Leu Pro Ser Thr Ala

15

<210> 2451

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2451

Phe Pro Ala Ala Leu Pro Ser Thr Ala Gly

1 5 10

<210> 2452

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2452

Gly Ala Glu Cys His Gly Arg Pro Leu

15

<210> 2453

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2453

Gly Ala Ile Ser Arg Phe Ile Trp Val

15

<210> 2454

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2454

Ile Leu Pro Ala Ala Ile Pro Ala Ser Thr

1 5 10

<210> 2455

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2455

Ile Trp Val Ser Gly Ile Leu Ser Pro Leu

1 5 10

<210> 2456

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2456

Leu Leu Thr Ala Thr Gly Ser Val Ser Leu

1 5 10

<210> 2457

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2457

Leu Leu Tyr Thr Ala Asp Ser Ser Leu

15

<210> 2458

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2458

Leu Pro Ala Ala Ala Thr Ser Ala Ala

15

<210> 2459

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2459

Leu Pro Ala Ala Ala Thr Ser Ala Ala Ser

1 5 10

<210> 2460

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2460

Leu Pro Ala Ala Ile Pro Ala Ser Thr

15

<210> 2461

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2461

Leu Pro Ala Gly Cys Val Ser Ser Ala

15

<210> 2462

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2462

Leu Pro Ala Gly Cys Val Ser Ser Ala Pro

1 5 10

<210> 2463

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2463

Leu Tyr Thr Ala Asp Ser Ser Leu Trp

15

<210> 2464

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2464

Gln Pro Ala Lys Ser Ser Pro Ser Ala

15

<210> 2465

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2465

Gln Pro Ala Lys Ser Ser Pro Ser Ala Ala

1 5 10

<210> 2466

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2466

Arg Phe Ile Trp Val Ser Gly Ile Leu

15

<210> 2467

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2467

Arg Pro Gln Arg Val Trp Ser Thr Gly

15

<210> 2468

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2468

Arg Val Trp Ser Thr Gly Pro Asp Ser Ile

1 5 10

<210> 2469

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2469

Ser Ala Val Pro Gly Ser Ile Pro Leu

15

<210> 2470

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2470

Ser Ile Leu Pro Ala Ala Ile Pro Ala

15

<210> 2471

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2471

Ser Leu Pro Ala Ala Ala Thr Ser Ala

15

<210> 2472

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2472

Ser Leu Pro Ala Ala Ala Thr Ser Ala Ala

1 5 10

<210> 2473

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2473

Ser Leu Trp Thr Thr Arg Pro Gln Arg

15

<210> 2474

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2474

Ser Leu Trp Thr Thr Arg Pro Gln Arg Val

1 5 10

<210> 2475

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2475

Ser Pro Ser Ala Ala Ala Ala Thr Leu

15

<210> 2476

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2476

Ser Pro Ser Ala Ala Ala Ala Thr Leu Leu

1 5 10

<210> 2477

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2477

Thr Leu Asp Ala Leu Pro Ala Gly Cys Val

1 5 10

<210> 2478

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2478

Thr Val Ser Thr Thr Thr Ala Pro Val

15

<210> 2479

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2479

Val Leu Ser Ala Ser Ile Leu Pro Ala

15

<210> 2480

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2480

Val Leu Ser Ala Ser Ile Leu Pro Ala Ala

1 5 10

<210> 2481

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2481

Val Pro Ala Asn Cys Leu Phe Pro Ala

15

<210> 2482

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2482

Val Pro Ala Asn Cys Leu Phe Pro Ala Ala

1 5 10

<210> 2483

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2483

Val Pro Asp Pro Ser Cys Pro Thr Phe

15

<210> 2484

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2484

Val Pro Gly Ser Ile Pro Leu Pro Ala

15

<210> 2485

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2485

Val Pro Gly Ser Ile Pro Leu Pro Ala Val

1 5 10

<210> 2486

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2486

Trp Val Ser Gly Ile Leu Ser Pro Leu

15

<210> 2487

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2487

Tyr Thr Ala Asp Ser Ser Leu Trp Thr Thr

1 5 10

<210> 2488

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2488

Ala Pro Ala Gly Met Val Asn Arg Ala

15

<210> 2489

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2489

Ala Ser Leu His Arg Arg Ser Tyr Leu

15

<210> 2490

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2490

Ala Ser Leu His Arg Arg Ser Tyr Leu Lys

1 5 10

<210> 2491

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2491

Phe Leu Leu Met Asp Asn Lys Ala Pro Ala

1 5 10

<210> 2492

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2492

His Pro Arg Arg Ser Pro Ser Arg Leu

15

<210> 2493

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2493

His Pro Ser Leu His Ile Ser Ser Pro

15

<210> 2494

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2494

His Arg Arg Ser Tyr Leu Lys Ile His Leu

1 5 10

<210> 2495

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2495

His Ser Arg Phe Leu Leu Met Asp Asn Lys

1 5 10

<210> 2496

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2496

Lys Leu Pro Ile Pro Ser Ser Ala Ser Leu

1 5 10

<210> 2497

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2497

Lys Val Leu Thr Leu Ser Ser Ser Ser His

1 5 10

<210> 2498

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2498

Leu Ile His Ser Arg Phe Leu Leu Met

15

<210> 2499

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2499

Leu Leu Met Asp Asn Lys Ala Pro Ala

15

<210> 2500

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2500

Leu Met Asp Asn Lys Ala Pro Ala Gly Met

1 5 10

<210> 2501

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2501

Leu Pro Ile Pro Ser Ser Ala Ser Leu

15

<210> 2502

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2502

Met Pro Asn Leu Arg Ile Ser Ser Ser

15

<210> 2503

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2503

Met Pro Asn Leu Arg Ile Ser Ser Ser His

1 5 10

<210> 2504

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2504

Asn Leu Arg Ile Ser Ser Ser His Ser Leu

1 5 10

<210> 2505

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2505

Pro Pro Thr His Ser His Arg Leu Ser Leu

1 5 10

<210> 2506

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2506

Arg Ala Gly Arg Arg Val Pro Trp Ala Ala

1 5 10

<210> 2507

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2507

Arg Ala Arg Leu His Ile Thr Thr Ser Lys

1 5 10

<210> 2508

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2508

Arg Ile Ser Ser Ser His Ser Leu Asn His

1 5 10

<210> 2509

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2509

Arg Leu His Thr Pro Pro Ser Ser Arg

15

<210> 2510

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2510

Arg Leu His Thr Pro Pro Ser Ser Arg Arg

1 5 10

<210> 2511

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2511

Arg Leu Arg Ile Leu Ser Pro Ser Leu

15

<210> 2512

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2512

Arg Pro Leu Met Pro Asn Leu Arg Ile

15

<210> 2513

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2513

Arg Pro Arg Pro Leu Met Pro Asn Leu

15

<210> 2514

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2514

Ser Ala Ser Leu His Arg Arg Ser Tyr Leu

1 5 10

<210> 2515

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2515

Ser Leu His Ile Ser Ser Pro Arg Leu

15

<210> 2516

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2516

Ser Leu His Arg Arg Ser Tyr Leu Lys

15

<210> 2517

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2517

Ser Leu His Arg Arg Ser Tyr Leu Lys Ile

1 5 10

<210> 2518

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2518

Ser Leu Ile His Ser Arg Phe Leu Leu

15

<210> 2519

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2519

Ser Leu Ile His Ser Arg Phe Leu Leu Met

1 5 10

<210> 2520

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2520

Ser Leu Leu Thr Ser Ser Ser Asn Leu

15

<210> 2521

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2521

Ser Leu Asn His His Ser Ser Ser Pro Leu

1 5 10

<210> 2522

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2522

Ser Leu Ser Ser Pro Ser Lys Leu Pro Ile

1 5 10

<210> 2523

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2523

Ser Pro Leu Ser Leu His Thr Pro Ser

15

<210> 2524

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2524

Ser Pro Leu Ser Leu His Thr Pro Ser Ser

1 5 10

<210> 2525

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2525

Ser Pro Pro Thr His Ser His Arg Leu

15

<210> 2526

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2526

Ser Pro Arg Leu His Thr Pro Pro Ser

15

<210> 2527

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2527

Ser Pro Arg Leu His Thr Pro Pro Ser Ser

1 5 10

<210> 2528

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2528

Ser Pro Ser Leu Ser Ser Pro Ser Lys Leu

1 5 10

<210> 2529

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2529

Ser Tyr Leu Lys Ile His Leu Gly Leu

15

<210> 2530

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2530

Thr Pro Ser Asn His Arg Pro Arg Pro Leu

1 5 10

<210> 2531

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2531

Thr Pro Ser Ser His Pro Ser Leu His Ile

1 5 10

<210> 2532

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2532

Cys Val Pro Phe Trp Thr Gly Arg Ile Leu

1 5 10

<210> 2533

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 2533

His Cys Val Pro Phe Trp Thr Gly Arg Ile Leu

1 5 10

<210> 2534

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2534

Ile Leu Leu Pro Ser Ala Ala Ser Val

15

<210> 2535

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2535

Ile Leu Leu Pro Ser Ala Ala Ser Val Cys

1 5 10

<210> 2536

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 2536

Leu Leu Pro Ser Ala Ala Ser Val Cys Pro Ile

1 5 10

<210> 2537

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2537

Leu Pro Ser Ala Ala Ser Val Cys Pro Ile

1 5 10

<210> 2538

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 2538

Met Arg Pro His Cys Val Pro Phe

15

<210> 2539

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2539

Arg Ile Leu Leu Pro Ser Ala Ala Ser Val

1 5 10

<210> 2540

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2540

Arg Met Arg Pro His Cys Val Pro Phe

15

<210> 2541

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2541

Arg Met Arg Pro His Cys Val Pro Phe Trp

1 5 10

<210> 2542

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2542

Arg Thr Asn Pro Thr Val Arg Met Arg

15

<210> 2543

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2543

Ser Val Cys Pro Ile Pro Phe Glu Ala

15

<210> 2544

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2544

Thr Val Arg Met Arg Pro His Cys Val

15

<210> 2545

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 2545

Thr Val Arg Met Arg Pro His Cys Val Pro Phe

1 5 10

<210> 2546

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2546

Val Pro Phe Trp Thr Gly Arg Ile Leu

15

<210> 2547

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2547

Val Pro Phe Trp Thr Gly Arg Ile Leu Leu

1 5 10

<210> 2548

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2548

Val Arg Met Arg Pro His Cys Val Pro Phe

1 5 10

<210> 2549

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2549

Ala Met Val Pro Arg Gly Val Ser Met

15

<210> 2550

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2550

Ala Met Val Pro Arg Gly Val Ser Met Ala

1 5 10

<210> 2551

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2551

Ala Trp Ala Pro Thr Ser Arg Thr Pro Trp

1 5 10

<210> 2552

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2552

Cys Pro Met Pro Thr Thr Pro Val Gln Ala

1 5 10

<210> 2553

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2553

Cys Pro Ser Thr Val Pro Pro Ser Pro Ala

1 5 10

<210> 2554

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2554

Gly Ala Met Val Pro Arg Gly Val Ser Met

1 5 10

<210> 2555

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2555

Met Pro Cys Pro Met Pro Thr Thr Pro Val

1 5 10

<210> 2556

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2556

Met Pro Thr Thr Pro Val Gln Ala Trp

15

<210> 2557

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2557

Met Pro Thr Thr Pro Val Gln Ala Trp Leu

1 5 10

<210> 2558

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2558

Ser Leu Pro Glu Asp Arg Tyr Thr Gln Ala

1 5 10

<210> 2559

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2559

Ser Pro Ala Gln Pro Tyr Leu Arg Val

15

<210> 2560

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2560

Ser Pro Ala Gln Pro Tyr Leu Arg Val Ser

1 5 10

<210> 2561

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2561

Thr Ile Met Pro Cys Pro Met Pro Thr

15

<210> 2562

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2562

Thr Pro Val Gln Ala Trp Leu Glu Ala

15

<210> 2563

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2563

Thr Ser Arg Thr Pro Trp Gly Ala Met

15

<210> 2564

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2564

Val Pro Pro Ser Pro Ala Gln Pro Tyr Leu

1 5 10

<210> 2565

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2565

Val Pro Arg Gly Val Ser Met Ala His

15

<210> 2566

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2566

Cys Leu Ser Ala Arg Thr Gly Leu Ser Ile

1 5 10

<210> 2567

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2567

Cys Thr Thr Leu Asn Ser Pro Pro Leu Lys

1 5 10

<210> 2568

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2568

Gly Leu Ser Ile Ser Cys Thr Thr Leu

15

<210> 2569

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2569

Ser Pro Pro Leu Lys Lys Met Ser Met

15

<210> 2570

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2570

Thr Leu Asn Ser Pro Pro Leu Lys Lys

15

<210> 2571

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2571

Thr Thr Leu Asn Ser Pro Pro Leu Lys

15

<210> 2572

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2572

Thr Thr Leu Asn Ser Pro Pro Leu Lys Lys

1 5 10

<210> 2573

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2573

Leu Gln Arg Phe Arg Phe Thr His Val

15

<210> 2574

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2574

Leu Gln Arg Phe Arg Phe Thr His Val Ile

1 5 10

<210> 2575

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2575

Arg Leu Ser Ser Val Leu Gln Arg Phe

15

<210> 2576

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2576

Arg Leu Ser Ser Val Leu Gln Arg Phe Arg

1 5 10

<210> 2577

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2577

Val Leu Gln Arg Phe Arg Phe Thr His Val

1 5 10

<210> 2578

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2578

Ala Ser Val Gly Arg His Ser Leu Ser Lys

1 5 10

<210> 2579

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2579

Lys Phe Leu Pro Phe Trp Gly Phe Leu

15

<210> 2580

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2580

Leu Ala Ser Val Gly Arg His Ser Leu

15

<210> 2581

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2581

Leu Pro Phe Trp Gly Phe Leu Glu Glu Phe

1 5 10

<210> 2582

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2582

Pro Phe Trp Gly Phe Leu Glu Glu Phe

15

<210> 2583

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2583

Ser Val Gly Arg His Ser Leu Ser Lys

15

<210> 2584

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2584

Ala Pro Arg Pro Ile Arg Pro Pro Phe

15

<210> 2585

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2585

Ala Pro Arg Pro Ile Arg Pro Pro Phe Leu

1 5 10

<210> 2586

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2586

Ala Gln Lys Met Lys Lys Ala His Phe Leu

1 5 10

<210> 2587

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2587

Phe Leu Pro Ser Ala Ala Gln Lys Met

15

<210> 2588

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2588

Gly Leu Phe Leu Pro Ser Ala Ala Gln Lys

1 5 10

<210> 2589

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2589

His Pro Leu Leu Val Ser Leu Leu Leu

15

<210> 2590

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2590

Lys Ala His Phe Leu Lys Thr Trp Phe Arg

1 5 10

<210> 2591

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2591

Lys Ala Arg Phe Ser Thr Ala Ser Leu

15

<210> 2592

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2592

Lys Met Lys Lys Ala His Phe Leu Lys

15

<210> 2593

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2593

Lys Thr Trp Phe Arg Ser Asn Pro Thr Lys

1 5 10

<210> 2594

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2594

Leu Ala Lys Glu Leu Thr His Pro Leu

15

<210> 2595

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2595

Leu Ala Lys Glu Leu Thr His Pro Leu Leu

1 5 10

<210> 2596

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2596

Asn Pro Thr Lys Thr Lys Lys Ala Arg Phe

1 5 10

<210> 2597

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2597

Gln Lys Met Lys Lys Ala His Phe Leu

15

<210> 2598

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2598

Arg Phe Ser Thr Ala Ser Leu Ala Lys

15

<210> 2599

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2599

Arg Pro Ile Arg Pro Pro Phe Leu Glu Ser

1 5 10

<210> 2600

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2600

Arg Ser Asn Pro Thr Lys Thr Lys Lys

15

<210> 2601

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2601

Ser Leu Ala Lys Glu Leu Thr His Pro Leu

1 5 10

<210> 2602

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2602

Thr Lys Lys Ala Arg Phe Ser Thr Ala

15

<210> 2603

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2603

Gly Leu Arg Phe Trp Asn Pro Ser Arg

15

<210> 2604

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2604

Ile Ser Gln Leu Leu Ser Trp Pro Gln Lys

1 5 10

<210> 2605

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2605

Arg Ile Ala His Ile Ser Gln Leu Leu

15

<210> 2606

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2606

Arg Leu Gly Tyr Ser Ser His Gln Leu

15

<210> 2607

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2607

Ser Gln Leu Leu Ser Trp Pro Gln Lys

15

<210> 2608

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2608

Ser Arg Ile Ala His Ile Ser Gln Leu

15

<210> 2609

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2609

Trp Pro Gln Lys Thr Glu Glu Arg Leu

15

<210> 2610

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2610

Tyr Ser Ser His Gln Leu Pro Arg Lys

15

<210> 2611

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2611

Cys Pro Gln Arg Met Thr Pro Gly Thr Thr

1 5 10

<210> 2612

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2612

Glu Ala Glu Lys Arg Thr Arg Thr Leu

15

<210> 2613

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2613

Gly Thr Thr Phe Ile Thr Met Met Lys

15

<210> 2614

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2614

Gly Thr Thr Phe Ile Thr Met Met Lys Lys

1 5 10

<210> 2615

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2615

Ile Thr Met Met Lys Lys Glu Ala Glu Lys

1 5 10

<210> 2616

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2616

Arg Met Thr Pro Gly Thr Thr Phe Ile

15

<210> 2617

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2617

Ser Pro Tyr Cys Pro Gln Arg Met Thr

15

<210> 2618

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2618

Thr Met Met Lys Lys Glu Ala Glu Lys

15

<210> 2619

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2619

Thr Pro Gly Thr Thr Phe Ile Thr Met

15

<210> 2620

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2620

Thr Pro Gly Thr Thr Phe Ile Thr Met Met

1 5 10

<210> 2621

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2621

Thr Thr Phe Ile Thr Met Met Lys Lys

15

<210> 2622

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2622

Cys Pro Gly Ala Thr Trp Arg Glu Ala

15

<210> 2623

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2623

Cys Pro Gly Ala Thr Trp Arg Glu Ala Ala

1 5 10

<210> 2624

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2624

Arg Ser Arg Cys Pro Gly Ala Thr Trp Arg

1 5 10

<210> 2625

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2625

Thr Pro Arg Ala Thr Arg Ser Arg Cys

15

<210> 2626

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2626

His Val Leu Pro Glu Pro His Leu Ala Leu

1 5 10

<210> 2627

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2627

Arg Pro Leu Gln Thr His Val Leu Pro Glu

1 5 10

<210> 2628

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2628

Val Leu Trp Thr Thr Pro Pro Leu Gln His

1 5 10

<210> 2629

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2629

Ala Pro Ser Glu Ser Pro Cys Ser Pro Phe

1 5 10

<210> 2630

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2630

Cys Pro Leu Asp His Thr Thr Pro Pro Ala

1 5 10

<210> 2631

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2631

Phe Leu Gln Glu Gln Tyr His Glu Ala

15

<210> 2632

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2632

Arg Leu Ala Phe Leu Gln Glu Gln Tyr His

1 5 10

<210> 2633

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2633

Ser Pro Cys Ser Pro Phe Arg Leu Ala Phe

1 5 10

<210> 2634

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2634

Ser Pro Pro Trp Val Arg Ala Leu Leu

15

<210> 2635

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2635

Tyr Pro Ala Cys Pro Leu Asp His Thr Thr

1 5 10

<210> 2636

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2636

Ala Leu His Leu Arg Ser Cys Pro Cys

15

<210> 2637

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2637

Cys Leu His His Arg Arg His Leu Val

15

<210> 2638

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2638

Cys Leu His His Arg Arg His Leu Val Cys

1 5 10

<210> 2639

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2639

Cys Leu His Arg Lys Ser His Pro His Leu

1 5 10

<210> 2640

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2640

Cys Leu Arg Ser His Ala Cys Pro Pro

15

<210> 2641

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2641

Cys Leu Arg Ser His Thr Cys Pro Pro

15

<210> 2642

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2642

Cys Leu Trp Cys His Ala Cys Leu His

15

<210> 2643

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2643

Cys Pro His His Leu Lys Asn His Leu

15

<210> 2644

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2644

Cys Pro His His Leu Lys Asn Leu Leu

15

<210> 2645

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2645

Cys Pro His His Leu Arg Thr Arg Leu

15

<210> 2646

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2646

Cys Pro Leu His Leu Arg Ser Leu Pro Phe

1 5 10

<210> 2647

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2647

Cys Pro Leu Pro Arg His Leu Lys His Leu

1 5 10

<210> 2648

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2648

Cys Pro Leu Ser Leu Arg Ser His Pro Cys

1 5 10

<210> 2649

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2649

Cys Pro Arg His Leu Arg Asn Cys Pro Leu

1 5 10

<210> 2650

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2650

Phe Pro His His Leu Arg His His Ala

15

<210> 2651

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2651

Phe Pro His His Leu Arg His His Ala Cys

1 5 10

<210> 2652

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2652

Gly Leu Arg Ser Arg Thr Cys Pro Pro

15

<210> 2653

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2653

His Ala Cys Leu His Arg Leu Arg Asn Leu

1 5 10

<210> 2654

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2654

His Leu Ala Cys Leu His His Leu Arg

15

<210> 2655

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2655

His Leu Cys Pro Pro His Leu Arg Tyr

15

<210> 2656

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2656

His Leu Cys Pro Pro His Leu Arg Tyr Arg

1 5 10

<210> 2657

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2657

His Leu Lys His Leu Ala Cys Leu His

15

<210> 2658

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2658

His Leu Lys His Arg Pro Cys Pro His

15

<210> 2659

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2659

His Leu Lys Asn His Leu Cys Pro Pro

15

<210> 2660

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2660

His Leu Lys Ser His Pro Cys Leu His

15

<210> 2661

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2661

His Leu Lys Ser Leu Leu Cys Pro Leu

15

<210> 2662

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2662

His Leu Leu His Leu Arg Arg Leu Tyr

15

<210> 2663

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2663

His Leu Arg Asn Cys Pro Leu Pro Arg

15

<210> 2664

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2664

His Leu Arg Asn Cys Pro Leu Pro Arg His

1 5 10

<210> 2665

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2665

His Leu Arg Arg Leu Tyr Pro His His Leu

1 5 10

<210> 2666

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2666

His Leu Arg Ser His Pro Cys Pro Leu

15

<210> 2667

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2667

His Leu Arg Ser His Pro Cys Pro Leu His

1 5 10

<210> 2668

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2668

His Leu Arg Ser Leu Pro Phe Pro His

15

<210> 2669

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2669

His Leu Arg Thr Arg Leu Cys Pro His

15

<210> 2670

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2670

His Leu Val Cys Ser His His Leu Lys

15

<210> 2671

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2671

His Pro Cys Leu His His Arg Arg His Leu

1 5 10

<210> 2672

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2672

His Pro Gly Leu Arg Ser Arg Thr Cys

15

<210> 2673

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2673

His Pro His Leu Leu His Leu Arg Arg Leu

1 5 10

<210> 2674

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2674

His Arg Lys Ser His Pro His Leu Leu

15

<210> 2675

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2675

His Arg Arg Thr Arg Ser Cys Pro Cys

15

<210> 2676

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2676

Lys Ser His Pro His Leu Leu His Leu Arg

1 5 10

<210> 2677

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2677

Lys Ser Leu Leu Cys Pro Leu His Leu Arg

1 5 10

<210> 2678

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2678

Leu Leu Cys Pro Leu His Leu Arg Ser Leu

1 5 10

<210> 2679

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2679

Leu Leu His Leu Arg Arg Leu Tyr Pro His

1 5 10

<210> 2680

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2680

Leu Pro Arg His Leu Lys His Leu Ala

15

<210> 2681

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2681

Leu Pro Arg His Leu Lys His Leu Ala Cys

1 5 10

<210> 2682

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2682

Leu Arg Arg Leu Arg Ser His Thr Cys

15

<210> 2683

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2683

Leu Arg Arg Leu Tyr Pro His His Leu

15

<210> 2684

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2684

Leu Val Cys Ser His His Leu Lys Ser Leu

1 5 10

<210> 2685

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2685

Asn Leu Arg Asn His Thr Cys Pro Pro Ser

1 5 10

<210> 2686

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2686

Pro Leu His Leu Arg Ser Leu Pro Phe

15

<210> 2687

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2687

Arg Leu Cys Pro His His Leu Lys Asn His

1 5 10

<210> 2688

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2688

Arg Leu Tyr Pro His His Leu Lys His

15

<210> 2689

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2689

Arg Leu Tyr Pro His His Leu Lys His Arg

1 5 10

<210> 2690

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2690

Arg Pro Cys Pro His His Leu Lys Asn Leu

1 5 10

<210> 2691

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2691

Arg Ser His Pro Cys Pro Leu His Leu Lys

1 5 10

<210> 2692

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2692

Arg Ser Leu Pro Phe Pro His His Leu Arg

1 5 10

<210> 2693

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2693

Arg Thr Arg Leu Cys Pro His His Leu

15

<210> 2694

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2694

Arg Thr Arg Leu Cys Pro His His Leu Lys

1 5 10

<210> 2695

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2695

Ser Leu Leu Cys Pro Leu His Leu Arg

15

<210> 2696

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2696

Ser Leu Arg Ser His Ala Cys Pro Pro

15

<210> 2697

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2697

Ser Pro Leu Arg Ser Gln Ala Asn Ala

15

<210> 2698

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2698

Tyr Leu Arg Arg Leu Arg Ser His Thr

15

<210> 2699

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2699

Tyr Pro His His Leu Lys His Arg Pro Cys

1 5 10

<210> 2700

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2700

Phe Ile Thr Ser Gly Gln Ile Phe Lys

15

<210> 2701

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2701

Ile Phe Ile Thr Ser Gly Gln Ile Phe

15

<210> 2702

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2702

Ser Gln Ser Glu Ala Leu Cys Val Leu

15

<210> 2703

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2703

Ser Gln Ser Glu Ala Leu Cys Val Leu Leu

1 5 10

<210> 2704

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2704

Ala Tyr Thr Gly Thr Ile Leu Met Met

15

<210> 2705

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2705

Asp Leu Lys Ala Tyr Thr Gly Thr Ile Leu

1 5 10

<210> 2706

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2706

Ile Leu Thr Lys Gln Ile Lys Thr Lys

15

<210> 2707

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2707

Lys Met Ile Leu Thr Lys Gln Ile Lys

15

<210> 2708

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2708

Lys Pro Thr Asp Thr Phe Leu Gln Ile

15

<210> 2709

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2709

Lys Pro Thr Asp Thr Phe Leu Gln Ile Leu

1 5 10

<210> 2710

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2710

Met Ile Leu Thr Lys Gln Ile Lys Thr Lys

1 5 10

<210> 2711

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2711

Ile Thr Arg Tyr Thr Ile Phe Val Leu Lys

1 5 10

<210> 2712

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2712

Leu Ile Ala Glu Leu His Asn Ile Leu

15

<210> 2713

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2713

Leu Ile Ala Glu Leu His Asn Ile Leu Leu

1 5 10

<210> 2714

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2714

Met Thr Pro Pro Asn Leu Ile Ala Glu Leu

1 5 10

<210> 2715

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2715

Asn Leu Ile Ala Glu Leu His Asn Ile

15

<210> 2716

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2716

Asn Leu Ile Ala Glu Leu His Asn Ile Leu

1 5 10

<210> 2717

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2717

Arg Tyr Thr Ile Phe Val Leu Lys Asp Ile

1 5 10

<210> 2718

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2718

Thr Ile Thr Arg Tyr Thr Ile Phe Val Leu

1 5 10

<210> 2719

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2719

Thr Pro Pro Asn Leu Ile Ala Glu Leu

15

<210> 2720

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2720

Phe Leu Gln Phe Arg Thr His Thr Thr

15

<210> 2721

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2721

Leu Pro Ala Lys Gly Glu Asp Ile Phe Leu

1 5 10

<210> 2722

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2722

Leu Gln Phe Arg Thr His Thr Thr Gly Arg

1 5 10

<210> 2723

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2723

Asn Leu Gln Ser Ser Val Cys Gly Leu

15

<210> 2724

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2724

Ser Ser Val Cys Gly Leu Pro Ala Lys

15

<210> 2725

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2725

Val Gln Trp Arg Asn Leu Gln Ser Ser Val

1 5 10

<210> 2726

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2726

Gly Gln Asn Val Ser Leu Leu Gly Lys

15

<210> 2727

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2727

His Thr Arg Thr Arg Gly Asn Leu Arg Lys

1 5 10

<210> 2728

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2728

Ile Leu His Thr Arg Thr Arg Gly Asn Leu

1 5 10

<210> 2729

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2729

Lys Gly Gln Asn Val Ser Leu Leu Gly Lys

1 5 10

<210> 2730

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2730

Leu Leu Gly Lys Tyr Ile Leu His Thr

15

<210> 2731

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2731

Leu Arg Lys Ser Arg Lys Trp Lys Ser Met

1 5 10

<210> 2732

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2732

Ser Leu Leu Gly Lys Tyr Ile Leu His

15

<210> 2733

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2733

Ser Leu Leu Gly Lys Tyr Ile Leu His Thr

1 5 10

<210> 2734

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2734

Cys Thr Ser Pro Leu Leu Ala Pro Val

15

<210> 2735

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2735

Phe Pro Glu Asn Leu Pro Gly Gln Leu

15

<210> 2736

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2736

Gly Leu Leu Ala Phe Trp Asp Ser Gln Val

1 5 10

<210> 2737

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2737

Ile Phe Cys Pro Phe Pro Glu Asn Leu

15

<210> 2738

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2738

Leu Leu Ala Phe Trp Asp Ser Gln Val

15

<210> 2739

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2739

Leu Leu Ala Pro Val Ile Phe Cys Pro

15

<210> 2740

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2740

Leu Leu Ala Pro Val Ile Phe Cys Pro Phe

1 5 10

<210> 2741

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2741

Leu Pro Cys Pro Gln Gln Asp Val Leu

15

<210> 2742

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2742

Arg Phe Pro Ser Gly Leu Leu Ala Phe

15

<210> 2743

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2743

Arg Phe Pro Ser Gly Leu Leu Ala Phe Trp

1 5 10

<210> 2744

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2744

Ser Pro Leu Leu Ala Pro Val Ile Phe

15

<210> 2745

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2745

Ser Pro Arg Gly Pro Cys Thr Ser Ser

15

<210> 2746

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2746

Ser Pro Arg Gly Pro Cys Thr Ser Ser Ser

1 5 10

<210> 2747

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2747

Ser Gln Val Cys Asp Leu His Val Leu

15

<210> 2748

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2748

Val Ile Phe Cys Pro Phe Pro Glu Asn Leu

1 5 10

<210> 2749

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2749

Ala Met Val Trp Pro Leu Leu Ser Ile

15

<210> 2750

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2750

Ala Met Val Trp Pro Leu Leu Ser Ile Leu

1 5 10

<210> 2751

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2751

Ala Gln Ile Ala Met Val Trp Pro Leu

15

<210> 2752

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2752

Ala Gln Ile Ala Met Val Trp Pro Leu Leu

1 5 10

<210> 2753

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2753

Cys Pro Met Ser Arg Leu Arg Leu Ala

15

<210> 2754

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2754

Cys Pro Met Ser Arg Leu Arg Leu Ala Leu

1 5 10

<210> 2755

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2755

Ile Ala Met Val Trp Pro Leu Leu Ser Ile

1 5 10

<210> 2756

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2756

Ile Leu Ser Glu Trp Lys Glu Ile Cys Val

1 5 10

<210> 2757

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2757

Ile Val Trp Trp Cys Pro Met Ser Arg

15

<210> 2758

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2758

Ile Val Trp Trp Cys Pro Met Ser Arg Leu

1 5 10

<210> 2759

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2759

Ile Trp Met Thr Glu Thr Leu Phe Asp Ile

1 5 10

<210> 2760

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2760

Leu Leu Ser Ile Leu Ser Glu Trp Lys

15

<210> 2761

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2761

Met Ser Ala Ala Gln Ile Ala Met Val

15

<210> 2762

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2762

Met Ser Arg Leu Arg Leu Ala Leu Thr

15

<210> 2763

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2763

Met Ser Arg Leu Arg Leu Ala Leu Thr Val

1 5 10

<210> 2764

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2764

Met Val Trp Pro Leu Leu Ser Ile Leu

15

<210> 2765

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2765

Arg Leu Ala Leu Thr Val Pro Pro Ser Thr

1 5 10

<210> 2766

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2766

Thr Leu Phe Asp Ile Val Trp Trp Cys

15

<210> 2767

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2767

Thr Leu Phe Asp Ile Val Trp Trp Cys Pro

1 5 10

<210> 2768

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2768

Thr Met Ser Ala Ala Gln Ile Ala Met Val

1 5 10

<210> 2769

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2769

Val Trp Ser Ile Trp Met Thr Glu Thr Leu

1 5 10

<210> 2770

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2770

Trp Met Thr Glu Thr Leu Phe Asp Ile

15

<210> 2771

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2771

Trp Met Thr Glu Thr Leu Phe Asp Ile Val

1 5 10

<210> 2772

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2772

Ala Leu Arg Cys Val Phe Val Pro Val

15

<210> 2773

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2773

Ala Leu Arg Cys Val Phe Val Pro Val Leu

1 5 10

<210> 2774

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2774

Ala Leu Ser Glu His Cys Pro Thr Thr

15

<210> 2775

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2775

Ala Gln Arg Lys Arg Ile Ser Ala Arg Lys

1 5 10

<210> 2776

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2776

Gly Ala Gln Arg Lys Arg Ile Ser Ala

15

<210> 2777

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2777

His Trp Met Glu Asn Ile Ser Pro Phe

15

<210> 2778

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2778

Leu Pro Ser Gln Arg Arg Asn His Trp

15

<210> 2779

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2779

Leu Pro Ser Gln Arg Arg Asn His Trp Met

1 5 10

<210> 2780

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2780

Asn Ile Ser Pro Phe Arg Ser Val Gly Val

1 5 10

<210> 2781

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2781

Arg Ile Ser Ala Arg Lys Gly Ser Leu

15

<210> 2782

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2782

Ser Pro Phe Arg Ser Val Gly Val Ser Ala

1 5 10

<210> 2783

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2783

Ser Pro Ser Ser His Trp Lys Thr Pro Val

1 5 10

<210> 2784

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2784

Thr Ala Leu Arg Cys Val Phe Val Pro Val

1 5 10

<210> 2785

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2785

Val Ile Tyr Trp Asp Gly Thr Ala Leu

15

<210> 2786

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2786

Val Ile Tyr Trp Asp Gly Thr Ala Leu Arg

1 5 10

<210> 2787

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2787

Val Leu Gly Glu Thr Gly Ala Gln Arg Lys

1 5 10

<210> 2788

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2788

His Pro Arg Pro Arg His Gly His Leu

15

<210> 2789

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2789

His Pro Arg Pro Arg His Gly His Leu Gln

1 5 10

<210> 2790

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2790

Arg Pro Arg His Gly His Leu Gln Ala

15

<210> 2791

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2791

Arg Pro Arg His Gly His Leu Gln Ala Val

1 5 10

<210> 2792

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2792

Gly Ser Leu Lys Thr Gln Val Gln Met Lys

1 5 10

<210> 2793

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2793

Pro Pro Gly Pro Cys His Leu Leu Ser Leu

1 5 10

<210> 2794

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2794

Arg Thr Ile Leu Asn Asn Gly Ser Leu Lys

1 5 10

<210> 2795

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2795

Ser Leu Lys Thr Gln Val Gln Met Lys

15

<210> 2796

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2796

Ser Leu Lys Thr Gln Val Gln Met Lys Leu

1 5 10

<210> 2797

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2797

Thr Ile Leu Asn Asn Gly Ser Leu Lys

15

<210> 2798

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2798

Cys Pro Pro Cys Arg Pro Lys Gln Trp Met

1 5 10

<210> 2799

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2799

Thr Thr Phe Cys Pro Pro Cys Arg Pro Lys

1 5 10

<210> 2800

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2800

Cys Phe Ala Asn Trp Pro Arg Pro Ala Leu

1 5 10

<210> 2801

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2801

Phe Ala Asn Trp Pro Arg Pro Ala Leu

15

<210> 2802

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2802

Gly Leu Ile Pro His Pro Arg Pro Ala

15

<210> 2803

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2803

His Pro Arg Pro Ala Pro Ala Ser Ala

15

<210> 2804

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2804

His Pro Arg Pro Ala Pro Ala Ser Ala Pro

1 5 10

<210> 2805

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2805

Ile Pro His Pro Arg Pro Ala Pro Ala

15

<210> 2806

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2806

Ile Pro His Pro Arg Pro Ala Pro Ala Ser

1 5 10

<210> 2807

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2807

Arg Pro Ala Leu Cys Ser Cys Gly Leu

15

<210> 2808

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2808

Arg Pro Ala Leu Cys Ser Cys Gly Leu Ile

1 5 10

<210> 2809

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2809

Thr Pro Leu Pro Ser Thr Arg Cys Phe

15

<210> 2810

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2810

Trp Pro Arg Pro Ala Leu Cys Ser Cys

15

<210> 2811

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2811

Trp Pro Arg Pro Ala Leu Cys Ser Cys Gly

1 5 10

<210> 2812

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2812

Ala Leu Arg Arg Ser Gly Arg Pro Pro Lys

1 5 10

<210> 2813

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2813

Gly Leu Val Pro Ser Leu Val Ser Lys

15

<210> 2814

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2814

Lys Ile Ser Val Glu Thr Tyr Thr Val

15

<210> 2815

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2815

Leu Leu Met Val Leu Met Ser Leu Asp Leu

1 5 10

<210> 2816

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2816

Leu Met Ser Leu Asp Leu Asp Thr Gly Leu

1 5 10

<210> 2817

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2817

Leu Met Val Leu Met Ser Leu Asp Leu

15

<210> 2818

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2818

Leu Val Ser Lys Cys Leu Ile Leu Arg Val

1 5 10

<210> 2819

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2819

Gln Leu Leu Met Val Leu Met Ser Leu

15

<210> 2820

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2820

Arg Pro Gly Ala Ala Asp Thr Gly Ala

15

<210> 2821

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2821

Arg Pro Gly Ala Ala Asp Thr Gly Ala His

1 5 10

<210> 2822

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2822

Ser Leu Asp Leu Asp Thr Gly Leu Val

15

<210> 2823

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2823

Ser Leu Val Ser Lys Cys Leu Ile Leu

15

<210> 2824

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2824

Ser Gln Leu Leu Met Val Leu Met Ser Leu

1 5 10

<210> 2825

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2825

Thr Val Ser Ser Gln Leu Leu Met Val

15

<210> 2826

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2826

Thr Tyr Thr Val Ser Ser Gln Leu Leu

15

<210> 2827

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2827

Thr Tyr Thr Val Ser Ser Gln Leu Leu Met

1 5 10

<210> 2828

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2828

Val Leu Met Ser Leu Asp Leu Asp Thr

15

<210> 2829

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2829

Val Pro Ser Leu Val Ser Lys Cys Leu

15

<210> 2830

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2830

Val Ser Lys Cys Leu Ile Leu Arg Val Lys

1 5 10

<210> 2831

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2831

Tyr Thr Val Ser Ser Gln Leu Leu Met

15

<210> 2832

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2832

Tyr Thr Val Ser Ser Gln Leu Leu Met Val

1 5 10

<210> 2833

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2833

Phe Cys Gln Tyr His Thr Ala Ser Val

15

<210> 2834

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2834

Cys Pro Tyr Gly Ser Thr Ser Thr Ala

15

<210> 2835

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2835

Cys Pro Tyr Gly Ser Thr Ser Thr Ala Ser

1 5 10

<210> 2836

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2836

Leu Ala Arg Ala Ala Ala Ser Thr Ala Thr

1 5 10

<210> 2837

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2837

Met Leu Thr Asp Ser Leu Phe Leu Pro

15

<210> 2838

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2838

Pro Pro Arg Ser Ser Ser Ala Ile Ala Val

1 5 10

<210> 2839

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2839

Arg Ala Ala Ala Ser Thr Ala Thr Glu Val

1 5 10

<210> 2840

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2840

Ser Pro Pro Arg Ser Ser Ser Ala Ile

15

<210> 2841

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2841

Ser Pro Pro Arg Ser Ser Ser Ala Ile Ala

1 5 10

<210> 2842

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2842

Ser Pro Thr Gln Arg Cys Arg Leu Ala

15

<210> 2843

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2843

Thr Gln Arg Cys Arg Leu Ala Arg Ala

15

<210> 2844

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2844

Thr Gln Arg Cys Arg Leu Ala Arg Ala Ala

1 5 10

<210> 2845

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2845

Lys Ile Trp Lys Thr Thr Gln Met Cys Arg

1 5 10

<210> 2846

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2846

Trp Thr Ser Ser Gly Arg Ser Thr Lys

15

<210> 2847

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2847

Ala Leu Gly Glu Leu Ala Arg Ala Leu

15

<210> 2848

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2848

Ala Gln Leu Arg Arg Arg Ala Ala Ala

15

<210> 2849

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2849

Ala Gln Leu Arg Arg Arg Ala Ala Ala Leu

1 5 10

<210> 2850

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2850

Ala Arg Arg Ala Ala Arg Met Ala Gln Leu

1 5 10

<210> 2851

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2851

His Pro Gln Leu Pro Arg Ser Pro Leu

15

<210> 2852

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2852

His Pro Gln Leu Pro Arg Ser Pro Leu Ala

1 5 10

<210> 2853

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2853

Leu Ala Arg Ala Leu Pro Gly His Leu

15

<210> 2854

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2854

Leu Ala Arg Ala Leu Pro Gly His Leu Leu

1 5 10

<210> 2855

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2855

Met Ala Gln Leu Arg Arg Arg Ala Ala

15

<210> 2856

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2856

Met Ala Gln Leu Arg Arg Arg Ala Ala Ala

1 5 10

<210> 2857

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2857

Gln Leu Arg Arg Arg Ala Ala Ala Leu

15

<210> 2858

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2858

Arg Ala Ala Ala Leu Pro Asn Ala Ala Ala

1 5 10

<210> 2859

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2859

Arg Met Ala Gln Leu Arg Arg Arg Ala Ala

1 5 10

<210> 2860

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2860

Ser Gln Ser Ala Arg Arg Ala Ala Arg Met

1 5 10

<210> 2861

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2861

Gly Met Thr Leu Gly Glu Lys Phe Arg Val

1 5 10

<210> 2862

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2862

Arg Val Gly Asn Cys Lys His Leu Lys

15

<210> 2863

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2863

Gly Pro Ser Glu Pro Gly Asn Asn Ile

15

<210> 2864

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2864

Lys Ile Cys Asn Glu Ser Ala Ser Arg Lys

1 5 10

<210> 2865

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2865

Gly Ile Gln Val Leu Asn Val Ser Leu Lys

1 5 10

<210> 2866

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2866

Ile Gln Val Leu Asn Val Ser Leu Lys

15

<210> 2867

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2867

Lys Ser Ser Ser Asn Val Ile Ser Tyr

15

<210> 2868

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2868

Lys Tyr Gly Trp Ser Leu Leu Arg Val

15

<210> 2869

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2869

Arg Ser Trp Lys Tyr Gly Trp Ser Leu

15

<210> 2870

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2870

Ser Leu Lys Ser Ser Ser Asn Val Ile

15

<210> 2871

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2871

Ser Trp Lys Tyr Gly Trp Ser Leu Leu

15

<210> 2872

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2872

Thr Val Ala Asn Gly Arg Ser Trp Lys

15

<210> 2873

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2873

Val Pro Gln Val Asn Gly Ile Gln Val

15

<210> 2874

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2874

Val Pro Gln Val Asn Gly Ile Gln Val Leu

1 5 10

<210> 2875

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2875

Val Thr Val Ala Asn Gly Arg Ser Trp Lys

1 5 10

<210> 2876

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2876

Trp Ser Leu Leu Arg Val Pro Gln Val

15

<210> 2877

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2877

His Pro Gly Asp Cys Leu Ile Phe Lys Leu

1 5 10

<210> 2878

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2878

Lys Leu Arg Val Pro Gly Ser Ser Val

15

<210> 2879

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2879

Lys Leu Arg Val Pro Gly Ser Ser Val Leu

1 5 10

<210> 2880

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2880

Arg Val Pro Gly Ser Ser Val Leu Val

15

<210> 2881

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2881

Ser Val Leu Val Thr Val Pro Gly Leu

15

<210> 2882

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2882

Val Pro Gly Ser Ser Val Leu Val Thr Val

1 5 10

<210> 2883

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2883

Ala Leu Leu Leu Arg Pro Arg Pro Pro Arg

1 5 10

<210> 2884

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2884

Ala Leu Ser Ala Leu Leu Leu Arg Pro Arg

1 5 10

<210> 2885

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2885

Leu Thr Ile Asn Lys Glu Glu Ala Leu

15

<210> 2886

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2886

Ile Val His Ser Ala Thr Gly Phe Lys

15

<210> 2887

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2887

Ala Thr Gly Phe Lys Gln Ser Ser Lys

15

<210> 2888

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2888

Glu Leu Phe Pro Leu Ile Phe Pro Ala

15

<210> 2889

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2889

Lys Gly Pro Glu Leu Phe Pro Leu Ile

15

<210> 2890

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2890

Lys Gly Pro Glu Leu Phe Pro Leu Ile Phe

1 5 10

<210> 2891

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 2891

Lys Pro Thr Asp Ala Pro Pro Lys Ala Gly Val

1 5 10

<210> 2892

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2892

Gln Val Tyr Arg Arg Lys His Gln Glu Leu

1 5 10

<210> 2893

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2893

Ser Thr Arg Glu Lys Asn Ser Gln Val

15

<210> 2894

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2894

Val Tyr Arg Arg Lys His Gln Glu Leu

15

<210> 2895

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2895

Val Leu Thr Val Thr Ser Thr Asp Val

15

<210> 2896

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2896

Val Leu Thr Val Thr Ser Thr Asp Val Lys

1 5 10

<210> 2897

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2897

Ile Met Ser Leu Trp Gly Leu Val Ser

15

<210> 2898

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2898

Ile Met Ser Leu Trp Gly Leu Val Ser Lys

1 5 10

<210> 2899

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2899

Lys Leu Lys Gln Glu Ala Thr Ser Lys

15

<210> 2900

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2900

Gln Ile Met Ser Leu Trp Gly Leu Val

15

<210> 2901

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2901

Ser Gln Ile Met Ser Leu Trp Gly Leu

15

<210> 2902

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2902

Ser Gln Ile Met Ser Leu Trp Gly Leu Val

1 5 10

<210> 2903

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2903

Thr Ser Lys Ser Gln Ile Met Ser Leu

15

<210> 2904

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2904

Leu Leu Gln Glu Phe Asp Val Gln Glu Ala

1 5 10

<210> 2905

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2905

Leu Gln Glu Phe Asp Val Gln Glu Ala Leu

1 5 10

<210> 2906

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2906

Gly Pro Arg Glu Pro Arg Asn Arg Thr

15

<210> 2907

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2907

Arg Asn Arg Thr Glu Lys His Ser Thr Met

1 5 10

<210> 2908

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2908

Ala Leu Asn Ser Glu Ala Leu Ser Val

15

<210> 2909

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2909

Ala Leu Asn Ser Glu Ala Leu Ser Val Val

1 5 10

<210> 2910

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2910

Met Ala Leu Asn Ser Glu Ala Leu Ser Val

1 5 10

<210> 2911

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2911

Ser Leu Leu Asn Tyr Leu Arg Glu Met

15

<210> 2912

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2912

Glu Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 2913

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2913

Thr Glu Tyr Met Ala Asn Gly Ser Leu

15

<210> 2914

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2914

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 2915

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2915

Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 2916

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 2916

Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 2917

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2917

Ala Asn Gly Ser Leu Leu Asn Tyr Leu

15

<210> 2918

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2918

Ala Asn Gly Ser Leu Leu Asn Tyr Leu Arg

1 5 10

<210> 2919

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 2919

Glu Tyr Met Ala Asn Gly Ser Leu

15

<210> 2920

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2920

Glu Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 2921

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2921

Glu Tyr Met Ala Asn Gly Ser Leu Leu Asn

1 5 10

<210> 2922

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 2922

Glu Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 2923

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 2923

Gly Ser Leu Leu Asn Tyr Leu Arg

15

<210> 2924

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2924

Gly Ser Leu Leu Asn Tyr Leu Arg Glu Met

1 5 10

<210> 2925

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2925

Ile Thr Glu Tyr Met Ala Asn Gly Ser

15

<210> 2926

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2926

Ile Thr Glu Tyr Met Ala Asn Gly Ser Leu

1 5 10

<210> 2927

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 2927

Ile Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu

1 5 10

<210> 2928

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2928

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 2929

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2929

Met Ala Asn Gly Ser Leu Leu Asn Tyr Leu

1 5 10

<210> 2930

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 2930

Met Ala Asn Gly Ser Leu Leu Asn Tyr Leu Arg

1 5 10

<210> 2931

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 2931

Asn Gly Ser Leu Leu Asn Tyr Leu

15

<210> 2932

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2932

Asn Gly Ser Leu Leu Asn Tyr Leu Arg

15

<210> 2933

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2933

Ser Leu Leu Asn Tyr Leu Arg Glu Met

15

<210> 2934

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2934

Ser Leu Leu Asn Tyr Leu Arg Glu Met Arg

1 5 10

<210> 2935

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2935

Thr Glu Tyr Met Ala Asn Gly Ser Leu

15

<210> 2936

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2936

Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu

1 5 10

<210> 2937

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 2937

Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 2938

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 2938

Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 2939

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2939

Tyr Met Ala Asn Gly Ser Leu Leu Asn

15

<210> 2940

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2940

Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 2941

<211> 51

<212> PROTEIN

<213> Homo sapiens

<400> 2941

Cys Thr Gly Arg Gly Pro Asp Asn Cys Ile Gln Cys Ala His Tyr Ile

1 5 10 15

Asp Gly Pro Arg Cys Val Arg Thr Cys Ser Ala Gly Val Met Gly Glu

20 25 30

Asn Asn Thr Leu Val Trp Lys Tyr Ala Asp Ala Gly His Val Cys His

35 40 45

Leu Cys His

50

<210> 2942

<211> 51

<212> PROTEIN

<213> Homo sapiens

<400> 2942

Cys Thr Gly Arg Cys Pro Asp Asn Cys Ile Gln Cys Ala His Tyr Ile

1 5 10 15

Asp Gly Pro His Cys Val Lys Thr Cys Leu Ala Gly Val Met Gly Glu

20 25 30

Asn Asn Thr Leu Val Trp Lys Tyr Ala Asp Ala Gly His Val Cys His

35 40 45

Leu Cys His

50

<210> 2943

<211> 51

<212> PROTEIN

<213> Homo sapiens

<400> 2943

Gly Arg Gly Pro Asp Asn Cys Ile Gln Cys Ala His Tyr Ile Asp Gly

1 5 10 15

Pro His Cys Val Lys Thr Cys Pro Ala Ala Val Met Gly Glu Asn Asn

20 25 30

Thr Leu Val Trp Lys Tyr Ala Asp Ala Gly His Val Cys His Leu Cys

35 40 45

His Pro Asn

50

<210> 2944

<211> 51

<212> PROTEIN

<213> Homo sapiens

<400> 2944

Gly Arg Gly Pro Asp Asn Cys Ile Gln Cys Ala His Tyr Ile Asp Gly

1 5 10 15

Pro His Cys Val Lys Thr Cys Pro Ala Val Val Met Gly Glu Asn Asn

20 25 30

Thr Leu Val Trp Lys Tyr Ala Asp Ala Gly His Val Cys His Leu Cys

35 40 45

His Pro Asn

50

<210> 2945

<211> 50

<212> PROTEIN

<213> Homo sapiens

<400> 2945

Lys Leu Thr Gln Leu Gly Thr Phe Glu Asp His Phe Leu Ser Leu Gln

1 5 10 15

Arg Met Phe Asn Asn Cys Leu Val Val Arg Gly Asn Leu Glu Ile Thr

20 25 30

Tyr Val Gln Arg Asn Tyr Asp Leu Ser Phe Leu Lys Thr Gln Glu Val

35 40 45

Ala Gly

50

<210> 2946

<211> 50

<212> PROTEIN

<213> Homo sapiens

<400> 2946

Gln Glu Arg Glu Leu Val Glu Pro Leu Thr Pro Ser Gly Glu Ala Pro

1 5 10 15

Asn Gln Ala Leu Leu Arg Ile Leu Lys Lys Thr Glu Phe Lys Lys Ile

20 25 30

Lys Val Leu Gly Ser Gly Ala Phe Gly Thr Val Tyr Lys Gly Leu Trp

35 40 45

Ile Pro

50

<210> 2947

<211> 51

<212> PROTEIN

<213> Homo sapiens

<400> 2947

Pro Ser Gly Glu Ala Pro Asn Gln Ala Leu Leu Arg Ile Leu Lys Glu

1 5 10 15

Thr Glu Phe Lys Lys Ile Lys Val Leu Ala Ser Gly Ala Phe Gly Thr

20 25 30

Val Tyr Lys Gly Leu Trp Ile Pro Glu Gly Glu Lys Val Lys Ile Pro

35 40 45

Val Ala Ile

50

<210> 2948

<211> 65

<212> PROTEIN

<213> Homo sapiens

<400> 2948

Gly Ala Phe Gly Thr Val Tyr Lys Gly Leu Trp Ile Pro Glu Gly Glu

1 5 10 15

Lys Val Lys Ile Pro Val Ala Ile Lys Thr Ser Pro Lys Ala Asn Lys

20 25 30

Glu Ile Leu Asp Glu Ala Tyr Val Met Ala Ser Val Asp Asn Pro His

35 40 45

Val Cys Arg Leu Leu Gly Ile Cys Leu Thr Ser Thr Val Gln Leu Ile

50 55 60

Thr

65

<210> 2949

<211> 52

<212> PROTEIN

<213> Homo sapiens

<400> 2949

Ala Ile Lys Glu Leu Arg Glu Gln Ala Thr Ser Pro Lys Ala Asn Lys

1 5 10 15

Glu Ile Leu Asp Glu Ala Tyr Val Met Ala Ile Val Asp Asn Pro His

20 25 30

Val Cys Arg Leu Leu Gly Ile Cys Leu Thr Ser Thr Val Gln Leu Ile

35 40 45

Thr Gln Leu Met

50

<210> 2950

<211> 52

<212> PROTEIN

<213> Homo sapiens

<400> 2950

Tyr Leu Leu Asn Val Val Cys Val Gln Leu Ala Lys Gly Met Asn Tyr

1 5 10 15

Leu Glu Asp Arg Arg Leu Val His Arg Asp Met Ala Ala Arg Asn Val

20 25 30

Leu Val Lys Thr Pro Gln His Val Lys Ile Thr Asp Phe Gly Leu Ala

35 40 45

Lys Leu Leu Gly

50

<210> 2951

<211> 51

<212> PROTEIN

<213> Homo sapiens

<400> 2951

Leu Val His Arg Asp Leu Ala Ala Arg Asn Val Leu Val Lys Thr Pro

1 5 10 15

Gln His Ile Val Lys Ile Thr Asp Glu Gly Arg Ala Lys Leu Gly Ala

20 25 30

Glu Glu Lys Glu Tyr His Ala Phe Gly Gly Arg Val Pro Ile Lys Trp

35 40 45

Met Ala Leu

50

<210> 2952

<211> 50

<212> PROTEIN

<213> Homo sapiens

<400> 2952

Arg Asp Leu Ala Ala Arg Asn Val Leu Val Lys Thr Pro Gln His Val

1 5 10 15

Arg Ile Thr Asp Phe Gly Leu Ala Lys Gln Leu Gly Ala Glu Glu Lys

20 25 30

Glu Tyr His Ala Glu Gly Gly Lys Val Pro Ile Lys Trp Met Ala Leu

35 40 45

Glu Ser

50

<210> 2953

<211> 51

<212> PROTEIN

<213> Homo sapiens

<400> 2953

Gln Glu Val Ala Gly Tyr Val Leu Ile Ala Leu Asn Thr Val Glu Arg

1 5 10 15

Ile Pro Leu Glu Asn Leu Gln Ala Ile Glu Lys Gly Asn Met Tyr Tyr

20 25 30

Glu Asn Ser Tyr Ala Leu Val Leu Ser Asn Tyr Asp Ala Asn Lys Thr

35 40 45

Gly Leu Lys

50

<210> 2954

<211> 51

<212> PROTEIN

<213> Homo sapiens

<400> 2954

Ser Pro Ser Asp Glu Cys Leu Met Asn Gln Cys Ala Ala Gly Glu Ile

1 5 10 15

Gly Pro Asn Glu Ser Asp Leu Val Cys Cys Lys Phe Arg Asp Glu Ala

20 25 30

Thr Cys Lys Asp Thr Cys Pro Pro Leu Met Leu Tyr Asn Pro Thr Thr

35 40 45

Tyr Gln Met

50

<210> 2955

<211> 51

<212> PROTEIN

<213> Homo sapiens

<400> 2955

Cys Pro Pro Leu Met Leu Tyr Asn Pro Thr Thr Tyr Gln Met Asp Val

1 5 10 15

Asn Pro Glu Gly Lys Tyr Ser Phe Gly Thr Thr Cys Val Lys Lys Cys

20 25 30

Pro Arg Asn Tyr Val Val Thr Asp His Gly Ser Cys Val Arg Ala Cys

35 40 45

Gly Ala Asp

50

<210> 2956

<211> 51

<212> PROTEIN

<213> Homo sapiens

<400> 2956

Cys Pro Pro Leu Met Leu Tyr Asn Pro Thr Thr Tyr Gln Met Asp Val

1 5 10 15

Asn Pro Glu Gly Lys Tyr Ser Phe Gly Asp Thr Cys Val Lys Lys Cys

20 25 30

Pro Arg Asn Tyr Val Val Thr Asp His Gly Ser Cys Val Arg Ala Cys

35 40 45

Gly Ala Asp

50

<210> 2957

<211> 51

<212> PROTEIN

<213> Homo sapiens

<400> 2957

Cys Pro Pro Leu Met Leu Tyr Asn Pro Thr Thr Tyr Gln Met Asp Val

1 5 10 15

Asn Pro Glu Gly Lys Tyr Ser Phe Gly Val Thr Cys Val Lys Lys Cys

20 25 30

Pro Arg Asn Tyr Val Val Thr Asp His Gly Ser Cys Val Arg Ala Cys

35 40 45

Gly Ala Asp

50

<210> 2958

<211> 52

<212> PROTEIN

<213> Homo sapiens

<400> 2958

Val Asn Pro Glu Gly Lys Tyr Ser Phe Gly Ala Thr Cys Val Lys Lys

1 5 10 15

Ile Cys Pro Arg Asn Tyr Val Val Thr Asp Tyr Gly Ser Cys Val Arg

20 25 30

Ala Cys Gly Ala Asp Ser Tyr Glu Met Glu Glu Asp Gly Val Arg Lys

35 40 45

Cys Lys Lys Cys

50

<210> 2959

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2959

Cys Val Lys Thr Cys Ser Ala Gly Val

15

<210> 2960

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2960

Val Lys Thr Cys Ser Ala Gly Val Met

15

<210> 2961

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2961

Cys Val Lys Thr Cys Ser Ala Gly Val Met

1 5 10

<210> 2962

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2962

Cys Val Lys Thr Cys Leu Ala Gly Val

15

<210> 2963

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2963

Gly Pro His Cys Val Lys Thr Cys Leu

15

<210> 2964

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2964

Val Lys Thr Cys Leu Ala Gly Val Met

15

<210> 2965

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2965

Cys Val Lys Thr Cys Pro Ala Ala Val

15

<210> 2966

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2966

Val Lys Thr Cys Pro Ala Ala Val Met

15

<210> 2967

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2967

Ala Val Met Gly Glu Asn Asn Thr Leu

15

<210> 2968

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2968

Ala Val Met Gly Glu Asn Asn Thr Leu Val

1 5 10

<210> 2969

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2969

Cys Val Lys Thr Cys Pro Ala Ala Val Met

1 5 10

<210> 2970

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2970

Ala Ala Val Met Gly Glu Asn Asn Thr Leu

1 5 10

<210> 2971

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 2971

Cys Val Lys Cys Pro Ala Val Val

15

<210> 2972

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2972

Val Lys Thr Cys Pro Ala Val Val Met

15

<210> 2973

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2973

Val Val Met Gly Glu Asn Asn Thr Leu Val

1 5 10

<210> 2974

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2974

Cys Val Lys Thr Cys Pro Ala Val Val Met

1 5 10

<210> 2975

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2975

Met Phe Asn Asn Cys Glu Val Val Arg

15

<210> 2976

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2976

Glu Val Val Arg Gly Asn Leu Glu Ile

15

<210> 2977

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2977

Val Arg Gly Asn Leu Glu Thr Thr Tyr

15

<210> 2978

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2978

Arg Met Phe Asn Asn Cys Glu Val Val Arg

1 5 10

<210> 2979

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2979

Val Val Arg Gly Asn Leu Glu Ile Thr Tyr

1 5 10

<210> 2980

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2980

Cys Glu Val Val Arg Gly Asn Ile Glu

15

<210> 2981

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2981

Arg Ile Leu Lys Lys Thr Glu Phe Lys

15

<210> 2982

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2982

Ile Leu Lys Lys Thr Glu Phe Lys Lys

15

<210> 2983

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2983

Gln Ala Leu Leu Arg Ile Leu Lys Lys

15

<210> 2984

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 2984

Leu Arg Ile Leu Lys Thr Glu Phe

15

<210> 2985

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2985

Arg Ile Leu Lys Lys Thr Glu Phe Lys Lys

1 5 10

<210> 2986

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2986

Asn Gln Ala Leu Leu Arg Ile Leu Lys Lys

1 5 10

<210> 2987

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2987

Leu Leu Arg Leu Lys Lys Thr Glu Phe

15

<210> 2988

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2988

Ala Ser Gly Ala Phe Gly Thr Val Tyr

15

<210> 2989

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2989

Val Leu Ala Ser Gly Ala Phe Gly Thr

15

<210> 2990

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 2990

Leu Ala Ser Ala Phe Gly Thr Tyr

15

<210> 2991

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2991

Lys Ile Lys Val Leu Ala Ser Gly Ala

15

<210> 2992

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2992

Lys Val Leu Ala Ser Gly Ala Phe Gly

15

<210> 2993

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2993

Ile Lys Val Leu Ala Ser Gly Ala Phe

15

<210> 2994

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 2994

Lys Lys Ile Lys Val Leu Ala Ser Gly

15

<210> 2995

<211> 5

<212> PROTEIN

<213> Homo sapiens

<400> 2995

Val Leu Ala Ser Gly

15

<210> 2996

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2996

Val Leu Ala Ser Gly Ala Phe Gly Thr Val

1 5 10

<210> 2997

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2997

Ala Ser Gly Ala Phe Gly Thr Val Tyr Lys

1 5 10

<210> 2998

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2998

Lys Ile Lys Val Leu Ala Ser Gly Ala Phe

1 5 10

<210> 2999

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 2999

Leu Ala Ser Gly Ala Phe Gly Thr Val Tyr

1 5 10

<210> 3000

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3000

Lys Lys Ile Lys Val Leu Ala Ser Gly Ala

1 5 10

<210> 3001

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3001

Thr Glu Phe Lys Lys Ile Lys Val Ile Ala

1 5 10

<210> 3002

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3002

Ala Ile Lys Thr Ser Pro Lys Ala Asn Lys

1 5 10

<210> 3003

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3003

Lys Val Lys Ile Pro Val Ala Ile Lys Thr

1 5 10

<210> 3004

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3004

Lys Thr Ser Pro Lys Ala Asn Lys Glu Ile

1 5 10

<210> 3005

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3005

Met Ala Ile Val Asp Asn Pro His Val

15

<210> 3006

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3006

Val Met Ala Ile Val Asp Asn Pro His

15

<210> 3007

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3007

Asp Glu Ala Tyr Val Met Ala Ile Val

15

<210> 3008

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3008

Leu Asp Glu Ala Tyr Tyr Met Ala Ile

15

<210> 3009

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3009

Arg Asp Glu Ala Tyr Val Met Ala Ile

15

<210> 3010

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3010

Val Met Ala Ile Val Asp Asn Pro His Val

1 5 10

<210> 3011

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3011

Ala Ile Val Asp Asn Pro His Val Cys Arg

1 5 10

<210> 3012

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3012

Tyr Val Met Ala Ile Val Asp Asn Pro His

1 5 10

<210> 3013

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3013

Asp Glu Ala Tyr Val Met Ala Ile Val Asp

1 5 10

<210> 3014

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3014

Arg Leu Val His Arg Asp Met Ala Ala

15

<210> 3015

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3015

Asp Met Ala Ala Arg Asn Val Leu Val

15

<210> 3016

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3016

Met Ala Ala Arg Asn Val Leu Val Lys

15

<210> 3017

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3017

Leu Val His Arg Asp Met Ala Arg Arg

15

<210> 3018

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3018

Arg Asp Met Ala Ala Arg Asn Val Leu

15

<210> 3019

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3019

Arg Leu Val His Arg Asp Met Ala Ala Arg

1 5 10

<210> 3020

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3020

Asp Met Ala Ala Arg Asn Val Leu Val Lys

1 5 10

<210> 3021

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3021

His Arg Asp Met Ala Ala Arg Asn Val Leu

1 5 10

<210> 3022

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3022

Arg Asp Met Ala Ala Arg Asn Val Leu Val

1 5 10

<210> 3023

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3023

Lys Ile Thr Asp Gly Arg Ala Lys

15

<210> 3024

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3024

His Val Lys Ile Thr Asp Phe Gly Arg

15

<210> 3025

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3025

Phe Gly Arg Ala Lys Leu Leu Gly Ala

15

<210> 3026

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3026

His Val Lys Ile Thr Asp Phe Gly Arg Ala

1 5 10

<210> 3027

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3027

Arg Ala Lys Leu Ile Gly Ala Glu Glu Lys

1 5 10

<210> 3028

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3028

Leu Ala Lys Gln Leu Gly Ala Glu Glu Lys

1 5 10

<210> 3029

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3029

Lys Gln Leu Gly Ala Glu Glu Lys Glu Tyr

1 5 10

<210> 3030

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3030

Gln His Lys Gly Asn Met Tyr Tyr

15

<210> 3031

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3031

Leu Gln His Lys Gly Asn Met Tyr

15

<210> 3032

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3032

Leu Gln His Lys Gly Asn Met Tyr Tyr

15

<210> 3033

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3033

Lys Gly Asn Met Tyr Tyr Glu Asn Ser Tyr

1 5 10

<210> 3034

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3034

Arg Glu Ser Asp Cys Leu Val Cys Cys

15

<210> 3035

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3035

Tyr Ser Phe Gly Thr Thr Cys Val Lys

15

<210> 3036

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3036

Thr Thr Cys Val Lys Lys Cys Pro Arg

15

<210> 3037

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3037

Gly Lys Tyr Ser Phe Gly Thr Thr Cys

15

<210> 3038

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3038

Tyr Ser Phe Gly Thr Thr Cys Val Lys Lys

1 5 10

<210> 3039

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3039

Lys Tyr Ser Phe Gly Thr Thr Cys Val Lys

1 5 10

<210> 3040

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3040

Gly Thr Thr Cys Val Lys Lys Cys Pro Arg

1 5 10

<210> 3041

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3041

Gly Lys Tyr Ser Phe Gly Thr Thr Cys Val

1 5 10

<210> 3042

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3042

Tyr Ser Phe Gly Asp Thr Cys Val Lys

15

<210> 3043

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3043

Asp Thr Cys Val Lys Lys Cys Pro Arg

15

<210> 3044

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3044

Gly Lys Tyr Ser Phe Gly Asp Thr Cys

15

<210> 3045

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3045

Tyr Ser Phe Gly Asp Thr Cys Val Lys Lys

1 5 10

<210> 3046

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3046

Lys Tyr Ser Phe Gly Thr Cys Val Lys

15

<210> 3047

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3047

Gly Lys Tyr Ser Phe Gly Asp Thr Cys Val

1 5 10

<210> 3048

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3048

Tyr Ser Phe Gly Val Thr Cys Val Lys

15

<210> 3049

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3049

Lys Tyr Ser Phe Gly Val Thr Cys Val

15

<210> 3050

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3050

Val Thr Cys Val Lys Lys Cys Pro Arg

15

<210> 3051

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3051

Gly Lys Tyr Ser Phe Gly Val Thr Cys

15

<210> 3052

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3052

Tyr Ser Phe Gly Val Thr Cys Val Lys Lys

1 5 10

<210> 3053

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3053

Lys Tyr Ser Phe Gly Val Thr Cys Val Lys

1 5 10

<210> 3054

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3054

Gly Val Thr Cys Val Lys Lys Cys Pro Arg

1 5 10

<210> 3055

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3055

Gly Lys Tyr Ser Phe Gly Val Thr Cys Val

1 5 10

<210> 3056

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3056

Val Val Thr Asp Tyr Gly Ser Cys Val

15

<210> 3057

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3057

Tyr Val Val Thr Asp Tyr Gly Ser Cys Val

1 5 10

<210> 3058

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3058

Val Val Thr Asp Tyr Gly Ser Cys Val Arg

1 5 10

<210> 3059

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3059

Cys Pro Arg Asn Tyr Val Val Thr Asp Tyr

1 5 10

<210> 3060

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3060

Phe Gly Arg Ala Lys Leu Leu Gly Ala

15

<210> 3061

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3061

Lys Ile Thr Asp Phe Gly Arg Ala Lys

15

<210> 3062

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 3062

Gly Ile Cys Leu Thr Ser Thr Val Gln Leu Ile Met Gln Leu Met Pro

1 5 10 15

Phe Gly Cys Leu Leu Asp Tyr

20

<210> 3063

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 3063

Ser Leu Asn Ile Thr Ser Leu Gly Leu Arg Ser Leu Lys Glu Ile Ser

1 5 10 15

Asp Gly Asp Val Ile Ile Ser Gly Asn Lys Asn Leu Cys Tyr Ala Asn

20 25 30

Thr Ile Asn Trp Lys Lys Leu Phe Gly Thr Ser Gly Gln Lys Thr Lys

35 40 45

Ile Ile Arg Asn Arg Gly Glu Asn Ser Cys Lys Ala Thr Gly Gln Val

50 55 60

Cys His Ala Leu Cys Ser Pro Glu Gly Cys Trp Gly Pro Glu Pro Arg

65 70 75 80

Asp Cys Val Ser Cys Arg Asn Val Ser Arg Gly Arg Glu Cys Val Asp

85 90 95

Lys Cys Asn Leu Leu

100

<210> 3064

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3064

Val Gln Leu Ile Met Gln Leu Met Pro Phe

1 5 10

<210> 3065

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3065

Ser Thr Val Gln Leu Ile Met Gln Leu Met

1 5 10

<210> 3066

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3066

Gln Leu Ile Met Gln Leu Met Pro Phe

15

<210> 3067

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3067

Met Gln Leu Met Pro Phe Gly Cys Leu Leu

1 5 10

<210> 3068

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3068

Leu Ile Met Gln Leu Met Pro Phe

15

<210> 3069

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3069

Leu Thr Ser Thr Val Gln Leu Ile Met

15

<210> 3070

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3070

Ser Thr Val Gln Leu Ile Met Gln Leu

15

<210> 3071

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3071

Thr Ser Thr Val Gln Leu Ile Met Gln Leu

1 5 10

<210> 3072

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3072

Thr Val Gln Leu Ile Met Gln Leu

15

<210> 3073

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3073

Thr Val Gln Leu Ile Met Gln Leu Met

15

<210> 3074

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3074

Val Gln Leu Ile Met Gln Leu Met

15

<210> 3075

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3075

Cys Leu Thr Ser Thr Val Gln Leu Ile Met

1 5 10

<210> 3076

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3076

Ile Met Gln Leu Met Pro Phe Gly Cys

15

<210> 3077

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3077

Ile Met Gln Leu Met Pro Phe Gly Cys Leu

1 5 10

<210> 3078

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3078

Leu Ile Met Gln Leu Met Pro Phe Gly

15

<210> 3079

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3079

Leu Ile Met Gln Leu Met Pro Phe Gly Cys

1 5 10

<210> 3080

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3080

Gln Leu Ile Met Gln Leu Met Pro Phe Gly

1 5 10

<210> 3081

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 3081

Ile Ile Arg Asn Arg Gly Glu Asn Ser Cys Lys

1 5 10

<210> 3082

<211> 80

<212> PROTEIN

<213> Homo sapiens

<400> 3082

Met Arg Pro Ser Gly Thr Ala Gly Ala Ala Leu Leu Ala Leu Leu Ala

1 5 10 15

Ala Leu Cys Pro Ala Ser Arg Ala Leu Glu Glu Lys Lys Gly Asn Tyr

20 25 30

Val Val Thr Asp His Gly Ser Cys Val Arg Ala Cys Gly Ala Asp Ser

35 40 45

Tyr Glu Met Glu Glu Asp Gly Val Arg Lys Cys Lys Lys Cys Glu Gly

50 55 60

Pro Cys Arg Lys Val Cys Asn Gly Ile Gly Ile Gly Glu Phe Lys Asp

65 70 75 80

<210> 3083

<211> 100

<212> PROTEIN

<213> Homo sapiens

<400> 3083

Leu Pro Gln Pro Pro Ile Cys Thr Ile Asp Val Tyr Met Ile Met Val

1 5 10 15

Lys Cys Trp Met Ile Asp Ala Asp Ser Arg Pro Lys Phe Arg Glu Leu

20 25 30

Ile Ile Glu Phe Ser Lys Met Ala Arg Asp Pro Gln Arg Tyr Leu Val

35 40 45

Ile Gln Leu Gln Asp Lys Phe Glu His Leu Lys Met Ile Gln Gln Glu

50 55 60

Glu Ile Arg Lys Leu Glu Glu Glu Lys Lys Gln Leu Glu Gly Glu Ile

65 70 75 80

Ile Asp Phe Tyr Lys Met Lys Ala Ala Ser Glu Ala Leu Gln Thr Gln

85 90 95

Leu Ser Thr Asp

100

<210> 3084

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3084

Ala Leu Glu Glu Lys Lys Gly Asn Tyr Val

1 5 10

<210> 3085

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3085

Ile Gln Leu Gln Asp Lys Phe Glu His Leu

1 5 10

<210> 3086

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3086

Gln Leu Gln Asp Lys Phe Glu His Leu

15

<210> 3087

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3087

Gln Leu Gln Asp Lys Phe Glu His Leu Lys

1 5 10

<210> 3088

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3088

Tyr Leu Val Ile Gln Leu Gln Asp Lys Phe

1 5 10

<210> 3089

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 3089

Met Ile Lys Glu Gly Ser Met Ser Glu Asp Glu Phe Ile Glu Glu Ala

1 5 10 15

Lys Val Met Met Asn Leu Ser His Glu Lys Leu Val Gln Leu Tyr Gly

20 25 30

Val Cys Thr Lys Gln Arg Pro Ile Phe Ile Ile Thr Glu Tyr Met Ala

35 40 45

Asn Gly Ser Leu Leu Asn Tyr Leu Arg Glu Met Arg His Arg Phe Gln

50 55 60

Thr Gln Gln Leu Leu Glu Met Cys Lys Asp Val Cys Glu Ala Met Glu

65 70 75 80

Tyr Leu Glu Ser Lys Gln Phe Leu His Arg Asp Leu Ala Ala Arg Asn

85 90 95

Cys Leu Val Asn Asp

100

<210> 3090

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3090

Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 3091

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3091

Ala Asn Gly Ser Leu Leu Asn Tyr Leu

15

<210> 3092

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3092

Ala Asn Gly Ser Leu Leu Asn Tyr Leu Arg

1 5 10

<210> 3093

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3093

Glu Tyr Met Ala Asn Gly Ser Leu

15

<210> 3094

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3094

Glu Tyr Met Ala Asn Gly Ser Leu Leu Asn

1 5 10

<210> 3095

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 3095

Glu Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 3096

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3096

Gly Ser Leu Leu Asn Tyr Leu Arg

15

<210> 3097

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3097

Gly Ser Leu Leu Asn Tyr Leu Arg Glu Met

1 5 10

<210> 3098

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3098

Ile Thr Glu Tyr Met Ala Asn Gly Ser

15

<210> 3099

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3099

Ile Thr Glu Tyr Met Ala Asn Gly Ser Leu

1 5 10

<210> 3100

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 3100

Ile Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu

1 5 10

<210> 3101

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3101

Met Ala Asn Gly Ser Leu Leu Asn Tyr Leu

1 5 10

<210> 3102

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 3102

Met Ala Asn Gly Ser Leu Leu Asn Tyr Leu Arg

1 5 10

<210> 3103

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3103

Asn Gly Ser Leu Leu Asn Tyr Leu

15

<210> 3104

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3104

Asn Gly Ser Leu Leu Asn Tyr Leu

15

<210> 3105

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3105

Ser Leu Leu Asn Tyr Leu Arg Glu Met Arg

1 5 10

<210> 3106

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3106

Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu

1 5 10

<210> 3107

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 3107

Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 3108

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3108

Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 3109

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 3109

Gly Ile Cys Leu Thr Ser Thr Val Gln Leu Ile Met Gln Leu Met Pro

1 5 10 15

Phe Gly Cys Leu Leu Asp Tyr

20

<210> 3110

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3110

Val Gln Leu Ile Met Gln Leu Met Pro Phe

1 5 10

<210> 3111

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3111

Ser Thr Val Gln Leu Ile Met Gln Leu Met

1 5 10

<210> 3112

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3112

Gln Leu Ile Met Gln Leu Met Pro Phe

15

<210> 3113

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3113

Met Gln Leu Met Pro Phe Gly Cys Leu Leu

1 5 10

<210> 3114

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3114

Leu Ile Met Gln Leu Met Pro Phe

15

<210> 3115

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3115

Leu Thr Ser Thr Val Gln Leu Ile Met

15

<210> 3116

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3116

Ser Thr Val Gln Leu Ile Met Gln Leu

15

<210> 3117

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3117

Thr Ser Thr Val Gln Leu Ile Met Gln Leu

1 5 10

<210> 3118

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3118

Thr Val Gln Leu Ile Met Gln Leu

15

<210> 3119

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3119

Thr Val Gln Leu Ile Met Gln Leu Met

15

<210> 3120

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3120

Val Gln Leu Ile Met Gln Leu Met

15

<210> 3121

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3121

Cys Leu Thr Ser Thr Val Gln Leu Ile Met

1 5 10

<210> 3122

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3122

Ile Met Gln Leu Met Pro Phe Gly Cys

15

<210> 3123

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3123

Ile Met Gln Leu Met Pro Phe Gly Cys

15

<210> 3124

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3124

Ile Met Gln Leu Met Pro Phe Gly Cys Leu

1 5 10

<210> 3125

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3125

Leu Ile Met Gln Leu Met Pro Phe Gly

15

<210> 3126

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3126

Leu Ile Met Gln Leu Met Pro Phe Gly Cys

1 5 10

<210> 3127

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3127

Gln Leu Ile Met Gln Leu Met Pro Phe Gly

1 5 10

<210> 3128

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 3128

Ser Leu Asn Ile Thr Ser Leu Gly Leu Arg Ser Leu Lys Glu Ile Ser

1 5 10 15

Asp Gly Asp Val Ile Ile Ser Gly Asn Lys Asn Leu Cys Tyr Ala Asn

20 25 30

Thr Ile Asn Trp Lys Lys Leu Phe Gly Thr Ser Gly Gln Lys Thr Lys

35 40 45

Ile Ile Arg Asn Arg Gly Glu Asn Ser Cys Lys Ala Thr Gly Gln Val

50 55 60

Cys His Ala Leu Cys Ser Pro Glu Gly Cys Trp Gly Pro Glu Pro Arg

65 70 75 80

Asp Cys Val Ser Cys Arg Asn Val Ser Arg Gly Arg Glu Cys Val Asp

85 90 95

Lys Cys Asn Leu Leu

100

<210> 3129

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 3129

Ile Ile Arg Asn Arg Gly Glu Asn Ser Cys Lys

1 5 10

<210> 3130

<211> 80

<212> PROTEIN

<213> Homo sapiens

<400> 3130

Met Arg Pro Ser Gly Thr Ala Gly Ala Ala Leu Leu Ala Leu Leu Ala

1 5 10 15

Ala Leu Cys Pro Ala Ser Arg Ala Leu Glu Glu Lys Lys Gly Asn Tyr

20 25 30

Val Val Thr Asp His Gly Ser Cys Val Arg Ala Cys Gly Ala Asp Ser

35 40 45

Tyr Glu Met Glu Glu Asp Gly Val Arg Lys Cys Lys Lys Cys Glu Gly

50 55 60

Pro Cys Arg Lys Val Cys Asn Gly Ile Gly Ile Gly Glu Phe Lys Asp

65 70 75 80

<210> 3131

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3131

Ala Leu Glu Glu Lys Lys Gly Asn Tyr Val

1 5 10

<210> 3132

<211> 100

<212> PROTEIN

<213> Homo sapiens

<400> 3132

Leu Pro Gln Pro Pro Ile Cys Thr Ile Asp Val Tyr Met Ile Met Val

1 5 10 15

Lys Cys Trp Met Ile Asp Ala Asp Ser Arg Pro Lys Phe Arg Glu Leu

20 25 30

Ile Ile Glu Phe Ser Lys Met Ala Arg Asp Pro Gln Arg Tyr Leu Val

35 40 45

Ile Gln Leu Gln Asp Lys Phe Glu His Leu Lys Met Ile Gln Gln Glu

50 55 60

Glu Ile Arg Lys Leu Glu Glu Glu Lys Lys Gln Leu Glu Gly Glu Ile

65 70 75 80

Ile Asp Phe Tyr Lys Met Lys Ala Ala Ser Glu Ala Leu Gln Thr Gln

85 90 95

Leu Ser Thr Asp

100

<210> 3133

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3133

Ile Gln Leu Gln Asp Lys Phe Glu His Leu

1 5 10

<210> 3134

<211> 100

<212> PROTEIN

<213> Homo sapiens

<400> 3134

Leu Pro Gln Pro Pro Ile Cys Thr Ile Asp Val Tyr Met Ile Met Val

1 5 10 15

Lys Cys Trp Met Ile Asp Ala Asp Ser Arg Pro Lys Phe Arg Glu Leu

20 25 30

Ile Ile Glu Phe Ser Lys Met Ala Arg Asp Pro Gln Arg Tyr Leu Val

35 40 45

Ile Gln Leu Gln Asp Lys Phe Glu His Leu Lys Met Ile Gln Gln Glu

50 55 60

Glu Ile Arg Lys Leu Glu Glu Glu Lys Lys Gln Leu Glu Gly Glu Ile

65 70 75 80

Ile Asp Phe Tyr Lys Met Lys Ala Ala Ser Glu Ala Leu Gln Thr Gln

85 90 95

Leu Ser Thr Asp

100

<210> 3135

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3135

Gln Leu Gln Asp Lys Phe Glu His Leu

15

<210> 3136

<211> 100

<212> PROTEIN

<213> Homo sapiens

<400> 3136

Leu Pro Gln Pro Pro Ile Cys Thr Ile Asp Val Tyr Met Ile Met Val

1 5 10 15

Lys Cys Trp Met Ile Asp Ala Asp Ser Arg Pro Lys Phe Arg Glu Leu

20 25 30

Ile Ile Glu Phe Ser Lys Met Ala Arg Asp Pro Gln Arg Tyr Leu Val

35 40 45

Ile Gln Leu Gln Asp Lys Phe Glu His Leu Lys Met Ile Gln Gln Glu

50 55 60

Glu Ile Arg Lys Leu Glu Glu Glu Lys Lys Gln Leu Glu Gly Glu Ile

65 70 75 80

Ile Asp Phe Tyr Lys Met Lys Ala Ala Ser Glu Ala Leu Gln Thr Gln

85 90 95

Leu Ser Thr Asp

100

<210> 3137

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3137

Gln Leu Gln Asp Lys Phe Glu His Leu Lys

1 5 10

<210> 3138

<211> 100

<212> PROTEIN

<213> Homo sapiens

<400> 3138

Leu Pro Gln Pro Pro Ile Cys Thr Ile Asp Val Tyr Met Ile Met Val

1 5 10 15

Lys Cys Trp Met Ile Asp Ala Asp Ser Arg Pro Lys Phe Arg Glu Leu

20 25 30

Ile Ile Glu Phe Ser Lys Met Ala Arg Asp Pro Gln Arg Tyr Leu Val

35 40 45

Ile Gln Leu Gln Asp Lys Phe Glu His Leu Lys Met Ile Gln Gln Glu

50 55 60

Glu Ile Arg Lys Leu Glu Glu Glu Lys Lys Gln Leu Glu Gly Glu Ile

65 70 75 80

Ile Asp Phe Tyr Lys Met Lys Ala Ala Ser Glu Ala Leu Gln Thr Gln

85 90 95

Leu Ser Thr Asp

100

<210> 3139

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3139

Ser Thr Val Gln Leu Ile Met Gln Leu

15

<210> 3140

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3140

Leu Ile Met Gln Leu Met Pro Phe

15

<210> 3141

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3141

Leu Thr Ser Thr Val Gln Leu Ile Met

15

<210> 3142

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3142

Thr Val Gln Leu Ile Met Gln Leu

15

<210> 3143

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3143

Thr Ser Thr Val Gln Leu Ile Met Gln Leu

1 5 10

<210> 3144

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3144

Thr Val Gln Leu Ile Met Gln Leu Met

15

<210> 3145

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3145

Val Gln Leu Ile Met Gln Leu Met

15

<210> 3146

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3146

Ser Thr Val Gln Leu Ile Met Gln Leu

15

<210> 3147

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3147

Leu Ile Met Gln Leu Met Pro Phe

15

<210> 3148

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3148

Leu Thr Ser Thr Val Gln Leu Ile Met

15

<210> 3149

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3149

Thr Val Gln Leu Ile Met Gln Leu

15

<210> 3150

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3150

Thr Ser Thr Val Gln Leu Ile Met Gln Leu

1 5 10

<210> 3151

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3151

Thr Val Gln Leu Ile Met Gln Leu Met

15

<210> 3152

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3152

Val Gln Leu Ile Met Gln Leu Met

15

<210> 3153

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 3153

Ser Leu Asn Ile Thr Ser Leu Gly Leu Arg Ser Leu Lys Glu Ile Ser

1 5 10 15

Asp Gly Asp Val Ile Ile Ser Gly Asn Lys Asn Leu Cys Tyr Ala Asn

20 25 30

Thr Ile Asn Trp Lys Lys Leu Phe Gly Thr Ser Gly Gln Lys Thr Lys

35 40 45

Ile Ile Arg Asn Arg Gly Glu Asn Ser Cys Lys Ala Thr Gly Gln Val

50 55 60

Cys His Ala Leu Cys Ser Pro Glu Gly Cys Trp Gly Pro Glu Pro Arg

65 70 75 80

Asp Cys Val Ser Cys Arg Asn Val Ser Arg Gly Arg Glu Cys Val Asp

85 90 95

Lys Cys Asn Leu Leu

100

<210> 3154

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 3154

Ile Ile Arg Asn Arg Gly Glu Asn Ser Cys Lys

1 5 10

<210> 3155

<211> 101

<212> PROTEIN

<213> Homo sapiens

<400> 3155

Ile Pro Val Ala Ile Lys Glu Leu Arg Glu Ala Thr Ser Pro Lys Ala

1 5 10 15

Asn Lys Glu Ile Leu Asp Glu Ala Tyr Val Met Ala Ser Val Asp Asn

20 25 30

Pro His Val Cys Arg Leu Leu Gly Ile Cys Leu Thr Ser Thr Val Gln

35 40 45

Leu Ile Met Gln Leu Met Pro Phe Gly Cys Leu Leu Asp Tyr Val Arg

50 55 60

Glu His Lys Asp Asn Ile Gly Ser Gln Tyr Leu Leu Asn Trp Cys Val

65 70 75 80

Gln Ile Ala Lys Gly Met Asn Tyr Leu Glu Asp Arg Arg Leu Val His

85 90 95

Arg Asp Leu Ala Ala

100

<210> 3156

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3156

Cys Leu Thr Ser Thr Val Gln Leu Ile Met

1 5 10

<210> 3157

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3157

Ile Met Gln Leu Met Pro Phe Gly Cys

15

<210> 3158

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3158

Ile Met Gln Leu Met Pro Phe Gly Cys Leu

1 5 10

<210> 3159

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3159

Leu Ile Met Gln Leu Met Pro Phe Gly

15

<210> 3160

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3160

Leu Ile Met Gln Leu Met Pro Phe Gly Cys

1 5 10

<210> 3161

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3161

Leu Thr Ser Thr Val Gln Leu Ile Met

15

<210> 3162

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3162

Met Gln Leu Met Pro Phe Gly Cys Leu

15

<210> 3163

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3163

Met Gln Leu Met Pro Phe Gly Cys Leu Leu

1 5 10

<210> 3164

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3164

Val Gln Leu Ile Met Gln Leu Met Pro Phe

1 5 10

<210> 3165

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3165

Leu Ile Met Gln Leu Met Pro Phe

15

<210> 3166

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3166

Leu Thr Ser Thr Val Gln Leu Ile Met

15

<210> 3167

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3167

Gln Leu Ile Met Gln Leu Met Pro Phe

15

<210> 3168

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3168

Ser Thr Val Gln Leu Ile Met Gln Leu

15

<210> 3169

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3169

Ser Thr Val Gln Leu Ile Met Gln Leu Met

1 5 10

<210> 3170

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3170

Thr Ser Thr Val Gln Leu Ile Met Gln Leu

1 5 10

<210> 3171

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3171

Thr Val Gln Leu Ile Met Gln Leu

15

<210> 3172

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3172

Thr Val Gln Leu Ile Met Gln Leu Met

15

<210> 3173

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3173

Val Gln Leu Ile Met Gln Leu Met

15

<210> 3174

<211> 80

<212> PROTEIN

<213> Homo sapiens

<400> 3174

Met Arg Pro Ser Gly Thr Ala Gly Ala Ala Leu Leu Ala Leu Leu Ala

1 5 10 15

Ala Leu Cys Pro Ala Ser Arg Ala Leu Glu Glu Lys Lys Gly Asn Tyr

20 25 30

Val Val Thr Asp His Gly Ser Cys Val Arg Ala Cys Gly Ala Asp Ser

35 40 45

Tyr Glu Met Glu Glu Asp Gly Val Arg Lys Cys Lys Lys Cys Glu Gly

50 55 60

Pro Cys Arg Lys Val Cys Asn Gly Ile Gly Ile Gly Glu Phe Lys Asp

65 70 75 80

<210> 3175

<211> 100

<212> PROTEIN

<213> Homo sapiens

<400> 3175

Leu Pro Gln Pro Pro Ile Cys Thr Ile Asp Val Tyr Met Ile Met Val

1 5 10 15

Lys Cys Trp Met Ile Asp Ala Asp Ser Arg Pro Lys Phe Arg Glu Leu

20 25 30

Ile Ile Glu Phe Ser Lys Met Ala Arg Asp Pro Gln Arg Tyr Leu Val

35 40 45

Ile Gln Leu Gln Asp Lys Phe Glu His Leu Lys Met Ile Gln Gln Glu

50 55 60

Glu Ile Arg Lys Leu Glu Glu Glu Lys Lys Gln Leu Glu Gly Glu Ile

65 70 75 80

Ile Asp Phe Tyr Lys Met Lys Ala Ala Ser Glu Ala Leu Gln Thr Gln

85 90 95

Leu Ser Thr Asp

100

<210> 3176

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3176

Ala Leu Glu Glu Lys Lys Gly Asn Tyr Val

1 5 10

<210> 3177

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3177

Ile Gln Leu Gln Asp Lys Phe Glu His Leu

1 5 10

<210> 3178

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3178

Gln Leu Gln Asp Lys Phe Glu His Leu

15

<210> 3179

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3179

Gln Leu Gln Asp Lys Phe Glu His Leu Lys

1 5 10

<210> 3180

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3180

Tyr Leu Val Ile Gln Leu Gln Asp Lys Phe

1 5 10

<210> 3181

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3181

Val Gln Leu Ile Met Gln Leu Met Pro Phe

1 5 10

<210> 3182

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3182

Ser Thr Val Gln Leu Ile Met Gln Leu Met

1 5 10

<210> 3183

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3183

Gln Leu Ile Met Gln Leu Met Pro Phe

15

<210> 3184

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3184

Met Gln Leu Met Pro Phe Gly Cys Leu Leu

1 5 10

<210> 3185

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3185

Leu Ile Met Gln Leu Met Pro Phe

15

<210> 3186

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3186

Leu Thr Ser Thr Val Gln Leu Ile Met

15

<210> 3187

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3187

Ser Thr Val Gln Leu Ile Met Gln Leu

15

<210> 3188

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3188

Thr Ser Thr Val Gln Leu Ile Met Gln Leu

1 5 10

<210> 3189

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3189

Thr Val Gln Leu Ile Met Gln Leu

15

<210> 3190

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3190

Thr Val Gln Leu Ile Met Gln Leu Met

15

<210> 3191

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3191

Val Gln Leu Ile Met Gln Leu Met

15

<210> 3192

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3192

Cys Leu Thr Ser Thr Val Gln Leu Ile Met

1 5 10

<210> 3193

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3193

Ile Met Gln Leu Met Pro Phe Gly Cys

15

<210> 3194

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3194

Ile Met Gln Leu Met Pro Phe Gly Cys

15

<210> 3195

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3195

Ile Met Gln Leu Met Pro Phe Gly Cys Leu

1 5 10

<210> 3196

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3196

Leu Ile Met Gln Leu Met Pro Phe Gly

15

<210> 3197

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3197

Leu Ile Met Gln Leu Met Pro Phe Gly Cys

1 5 10

<210> 3198

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3198

Gln Leu Ile Met Gln Leu Met Pro Phe Gly

1 5 10

<210> 3199

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 3199

Ile Ile Arg Asn Arg Gly Glu Asn Ser Cys Lys

1 5 10

<210> 3200

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3200

Ala Leu Glu Glu Lys Lys Gly Asn Tyr Val

1 5 10

<210> 3201

<211> 100

<212> PROTEIN

<213> Homo sapiens

<400> 3201

Leu Pro Gln Pro Pro Ile Cys Thr Ile Asp Val Tyr Met Ile Met Val

1 5 10 15

Lys Cys Trp Met Ile Asp Ala Asp Ser Arg Pro Lys Phe Arg Glu Leu

20 25 30

Ile Ile Glu Phe Ser Lys Met Ala Arg Asp Pro Gln Arg Tyr Leu Val

35 40 45

Ile Gln Leu Gln Asp Lys Phe Glu His Leu Lys Met Ile Gln Gln Glu

50 55 60

Glu Ile Arg Lys Leu Glu Glu Glu Lys Lys Gln Leu Glu Gly Glu Ile

65 70 75 80

Ile Asp Phe Tyr Lys Met Lys Ala Ala Ser Glu Ala Leu Gln Thr Gln

85 90 95

Leu Ser Thr Asp

100

<210> 3202

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3202

Ile Gln Leu Gln Asp Lys Phe Glu His Leu

1 5 10

<210> 3203

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3203

Gln Leu Gln Asp Lys Phe Glu His Leu

15

<210> 3204

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3204

Gln Leu Gln Asp Lys Phe Glu His Leu Lys

1 5 10

<210> 3205

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3205

Tyr Leu Val Ile Gln Leu Gln Asp Lys Phe

1 5 10

<210> 3206

<211> 6

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

6xHis tag

<400> 3206

His His His His His

15

<210> 3207

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3207

Glu Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 3208

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3208

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 3209

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3209

Ser Leu Leu Asn Tyr Leu Arg Glu Met

15

<210> 3210

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3210

Thr Glu Tyr Met Ala Asn Gly Ser Leu

15

<210> 3211

<211> 6

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

6xHis label

<400> 3211

His His His His His

15

<210> 3212

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3212

Val Leu Pro Glu Pro His Leu Ala Leu

15

<210> 3213

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3213

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 3214

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3214

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3215

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3215

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 3216

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3216

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 3217

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3217

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 3218

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3218

Ala Ile Gln Pro Val Leu Trp Thr Thr

15

<210> 3219

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3219

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3220

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3220

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 3221

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3221

Val Leu Pro Glu Pro His Leu Ala Leu

15

<210> 3222

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3222

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

1 5 10

<210> 3223

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3223

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 3224

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3224

Ala Leu Gln Pro Leu Gln Pro His Ala

15

<210> 3225

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3225

Lys Ile Met Phe Ala Thr Leu Gln Arg

15

<210> 3226

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3226

Val Leu Trp Thr Thr Pro Pro Leu Gln His

1 5 10

<210> 3227

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3227

Tyr Met Phe Leu Lys Ala Glu Ser Lys

15

<210> 3228

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3228

Lys Ile Met Phe Ala Thr Leu Gln Arg

15

<210> 3229

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3229

Val Leu Trp Thr Thr Pro Pro Leu Gln His

1 5 10

<210> 3230

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3230

Tyr Met Phe Leu Lys Ala Glu Ser Lys

15

<210> 3231

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3231

Met Phe Leu Lys Ala Glu Ser Lys Ile

15

<210> 3232

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3232

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 3233

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3233

Phe Ala Thr Leu Gln Arg Ser Ser Leu

15

<210> 3234

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3234

Glu Pro His Leu Ala Leu Gln Pro Leu

15

<210> 3235

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3235

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 3236

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3236

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 3237

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3237

Gln Pro Val Leu Trp Thr Thr Pro Pro Leu

1 5 10

<210> 3238

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3238

Gly Pro Pro Ala Arg Val Pro Ala Val

15

<210> 3239

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3239

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 3240

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3240

Glu Pro His Leu Ala Leu Gln Pro Leu

15

<210> 3241

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3241

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 3242

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3242

Phe Leu Lys Ala Glu Ser Lys Ile Met

15

<210> 3243

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3243

Phe Ala Thr Leu Gln Arg Ser Ser Leu

15

<210> 3244

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3244

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 3245

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3245

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10

<210> 3246

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3246

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 3247

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3247

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10

<210> 3248

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3248

Leu His Phe Cys Arg Ser Ser Ile Met

15

<210> 3249

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3249

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 3250

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3250

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3251

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3251

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3252

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3252

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 3253

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3253

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3254

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3254

Val Leu Pro Glu Pro His Leu Ala Leu

15

<210> 3255

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3255

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 3256

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3256

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3257

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3257

Lys Ile Met Phe Ala Thr Leu Gln Arg

15

<210> 3258

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3258

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 3259

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3259

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 3260

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3260

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 3261

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 3261

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

20 25 30

His

<210> 3262

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3262

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 3263

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3263

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 3264

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 3264

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His

<210> 3265

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3265

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 3266

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3266

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3267

<211> 21

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3267

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His

20

<210> 3268

<211> 26

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3268

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

20 25

<210> 3269

<211> 25

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3269

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala Glu Ser Lys Ile

20 25

<210> 3270

<211> 23

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3270

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg

20

<210> 3271

<211> 20

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3271

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr

20

<210> 3272

<211> 24

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3272

Lys Lys Lys Lys Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10 15

Glu Ser Lys Ile Met Phe Ala Thr

20

<210> 3273

<211> 16

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3273

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

<210> 3274

<211> 21

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3274

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

1 5 10 15

Ser Leu Trp Cys Leu

20

<210> 3275

<211> 23

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3275

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

1 5 10 15

Arg Ser Ser Leu Trp Cys Leu

20

<210> 3276

<211> 19

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3276

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

1 5 10 15

Arg Ser Ser

<210> 3277

<211> 23

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3277

Lys Lys Lys Lys Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10 15

Ala Thr Leu Gln Arg Ser Ser

20

<210> 3278

<211> 19

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3278

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10 15

Trp CysLeu

<210> 3279

<211> 23

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3279

Lys Lys Lys Lys Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

1 5 10 15

Arg Ser Ser Leu Trp Cys Leu

20

<210> 3280

<211> 16

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3280

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

1 5 10 15

<210> 3281

<211> 16

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3281

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

1 5 10 15

<210> 3282

<211> 16

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3282

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

1 5 10 15

<210> 3283

<211> 15

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3283

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

1 5 10 15

<210> 3284

<211> 14

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3284

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 3285

<211> 19

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3285

Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys

1 5 10 15

Ser Asn His

<210> 3286

<211> 23

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3286

Lys Lys Lys Lys Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10 15

Trp Cys Leu Cys Ser Asn His

20

<210> 3287

<211> 17

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3287

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

1 5 10 15

His

<210> 3288

<211> 21

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3288

Lys Lys Lys Lys Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

1 5 10 15

Leu Cys Ser Asn His

20

<210> 3289

<211> 14

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3289

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys

1 5 10

<210> 3290

<211> 14

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3290

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn His

1 5 10

<210> 3291

<211> 18

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3291

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His

<210> 3292

<211> 33

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<400> 3292

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

20 25 30

His

<210> 3293

<211> 29

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3293

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

20 25

<210> 3294

<211> 39

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<400> 3294

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

20 25 30

Arg Ser Ser Leu Trp Cys Leu

35

<210> 3295

<211> 21

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3295

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His

20

<210> 3296

<211> 18

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3296

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His

<210> 3297

<211> 26

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3297

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

20 25

<210> 3298

<211> 25

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3298

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala Glu Ser Lys Ile

20 25

<210> 3299

<211> 23

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3299

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg

20

<210> 3300

<211> 21

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3300

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

1 5 10 15

Ser Leu Trp Cys Leu

20

<210> 3301

<211> 19

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3301

Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys

1 5 10 15

Ser Asn His

<210> 3302

<211> 20

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3302

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr

20

<210> 3303

<211> 23

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3303

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

1 5 10 15

Arg Ser Ser Leu Trp Cys Leu

20

<210> 3304

<211> 19

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3304

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

1 5 10 15

Arg Ser Ser

<210> 3305

<211> 19

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3305

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10 15

Trp CysLeu

<210> 3306

<211> 17

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3306

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

1 5 10 15

His

<210> 3307

<211> 24

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3307

Lys Lys Lys Lys Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10 15

Glu Ser Lys Ile Met Phe Ala Thr

20

<210> 3308

<211> 23

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3308

Lys Lys Lys Lys Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10 15

Ala Thr Leu Gln Arg Ser Ser

20

<210> 3309

<211> 23

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3309

Lys Lys Lys Lys Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

1 5 10 15

Arg Ser Ser Leu Trp Cys Leu

20

<210> 3310

<211> 21

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3310

Lys Lys Lys Lys Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

1 5 10 15

Leu Cys Ser Asn His

20

<210> 3311

<211> 23

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3311

Lys Lys Lys Lys Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10 15

Trp Cys Leu Cys Ser Asn His

20

<210> 3312

<211> 16

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3312

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

<210> 3313

<211> 16

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3313

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

1 5 10 15

<210> 3314

<211> 16

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3314

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

1 5 10 15

<210> 3315

<211> 16

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3315

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

1 5 10 15

<210> 3316

<211> 15

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3316

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

1 5 10 15

<210> 3317

<211> 14

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3317

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 3318

<211> 14

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3318

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys

1 5 10

<210> 3319

<211> 14

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3319

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn His

1 5 10

<210> 3320

<211> 33

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<400> 3320

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

20 25 30

His

<210> 3321

<211> 29

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3321

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

20 25

<210> 3322

<211> 39

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<400> 3322

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

20 25 30

Arg Ser Ser Leu Trp Cys Leu

35

<210> 3323

<211> 24

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3323

Lys Lys Lys Lys Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala

1 5 10 15

Glu Ser Lys Ile Met Phe Ala Thr

20

<210> 3324

<211> 23

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3324

Lys Lys Lys Lys Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10 15

Ala Thr Leu Gln Arg Ser Ser

20

<210> 3325

<211> 23

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3325

Lys Lys Lys Lys Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

1 5 10 15

Arg Ser Ser Leu Trp Cys Leu

20

<210> 3326

<211> 21

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3326

Lys Lys Lys Lys Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

1 5 10 15

Leu Cys Ser Asn His

20

<210> 3327

<211> 23

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3327

Lys Lys Lys Lys Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10 15

Trp Cys Leu Cys Ser Asn His

20

<210> 3328

<211> 21

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3328

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His

20

<210> 3329

<211> 18

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3329

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His

<210> 3330

<211> 26

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3330

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

20 25

<210> 3331

<211> 16

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3331

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

<210> 3332

<211> 15

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3332

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg

1 5 10 15

<210> 3333

<211> 14

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3333

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 3334

<211> 33

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<400> 3334

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

20 25 30

His

<210> 3335

<211> 25

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3335

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala Glu Ser Lys Ile

20 25

<210> 3336

<211> 21

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3336

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His

20

<210> 3337

<211> 26

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3337

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

20 25

<210> 3338

<211> 25

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3338

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala Glu Ser Lys Ile

20 25

<210> 3339

<211> 20

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3339

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr

20

<210> 3340

<211> 19

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3340

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln

1 5 10 15

Arg Ser Ser

<210> 3341

<211> 19

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3341

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10 15

Trp CysLeu

<210> 3342

<211> 17

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3342

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

1 5 10 15

His

<210> 3343

<211> 23

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3343

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg

20

<210> 3344

<211> 16

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3344

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

<210> 3345

<211> 21

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3345

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

1 5 10 15

Ser Leu Trp Cys Leu

20

<210> 3346

<211> 16

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3346

Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr

1 5 10 15

<210> 3347

<211> 16

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3347

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

1 5 10 15

<210> 3348

<211> 16

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3348

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys

1 5 10 15

<210> 3349

<211> 14

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3349

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys

1 5 10

<210> 3350

<211> 14

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3350

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn His

1 5 10

<210> 3351

<211> 33

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<400> 3351

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

20 25 30

His

<210> 3352

<211> 18

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3352

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His

<210> 3353

<211> 14

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3353

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 3354

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 3354

His Gly Leu Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg

1 5 10 15

<210> 3355

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3355

Arg Asp Gly Tyr Met Phe Leu Lys

15

<210> 3356

<211> 7

<212> PROTEIN

<213> Homo sapiens

<400> 3356

Ser Ser Ile Met Lys Pro Lys

15

<210> 3357

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 3357

Ala Gly Thr Ser Cys Ala Asn Cys Gln Thr Thr Thr Thr Thr Leu Trp

1 5 10 15

Arg

<210> 3358

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 3358

Ala Leu Gly Ser His His Thr Ala Ser Pro Trp Asn Leu Ser Pro Phe

1 5 10 15

Ser Lys

<210> 3359

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 3359

Asp Gly Thr Gly His Tyr Leu Cys Asn Ala Cys Gly Leu Tyr His Lys

1 5 10 15

<210> 3360

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 3360

Asp Val Ser Pro Asp Pro Ser Leu Ser Thr Pro Gly Ser Ala Gly Ser

1 5 10 15

Ala Arg

<210> 3361

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 3361

Glu Cys Val Asn Cys Gly Ala Thr Ser Thr Pro Leu Trp Arg

1 5 10

<210> 3362

<211> 6

<212> PROTEIN

<213> Homo sapiens

<400> 3362

Glu Gly Ile Gln Thr Arg

15

<210> 3363

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3363

Glu Gly Ile Gln Thr Arg Asn Arg

15

<210> 3364

<211> 7

<212> PROTEIN

<213> Homo sapiens

<400> 3364

Lys Glu Gly Ile Gln Thr Arg

15

<210> 3365

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 3365

Lys Val His Asp Ser Leu Glu Asp Phe Pro Lys

1 5 10

<210> 3366

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 3366

Leu His Asn Ile Asn Arg Pro Leu Thr Met Lys

1 5 10

<210> 3367

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 3367

Leu His Asn Ile Asn Arg Pro Leu Thr Met Lys Lys

1 5 10

<210> 3368

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 3368

Met Asn Gly Gln Asn Arg Pro Leu Ile Lys Pro Lys

1 5 10

<210> 3369

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 3369

Asn Ala Asn Gly Asp Pro Val Cys Asn Ala Cys Gly Leu Tyr Tyr Lys

1 5 10 15

<210> 3370

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 3370

Asn Ser Ser Phe Asn Pro Ala Ala Leu Ser Arg

1 5 10

<210> 3371

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 3371

Arg Ala Gly Thr Ser Cys Ala Asn Cys Gln Thr Thr Thr Thr Thr Leu

1 5 10 15

Trp Arg

<210> 3372

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 3372

Arg Asp Gly Thr Gly His Tyr Leu Cys Asn Ala Cys Gly Leu Tyr His

1 5 10 15

Lys

<210> 3373

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 3373

Ser Ser Thr Glu Gly Arg Glu Cys Val Asn Cys Gly Ala Thr Ser Thr

1 5 10 15

Pro Leu Trp Arg

20

<210> 3374

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3374

Val His Asp Ser Leu Glu Asp Phe Pro Lys

1 5 10

<210> 3375

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3375

Tyr Gln Val Pro Leu Pro Asp Ser Met Lys

1 5 10

<210> 3376

<211> 8

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3376

Arg Ala Lys Phe Lys Gln Leu Leu

15

<210> 3377

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3377

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3378

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3378

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 3379

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3379

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

1 5 10

<210> 3380

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3380

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 3381

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3381

Phe Ala Thr Leu Gln Arg Ser Ser Leu

15

<210> 3382

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3382

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 3383

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3383

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 3384

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3384

Gly Pro Pro Ala Arg Val Pro Ala Val

15

<210> 3385

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3385

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 3386

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3386

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 3387

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3387

Phe Leu Lys Ala Glu Ser Lys Ile Met

15

<210> 3388

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3388

Phe Ala Thr Leu Gln Arg Ser Ser Leu

15

<210> 3389

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3389

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 3390

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3390

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10

<210> 3391

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3391

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 3392

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3392

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10

<210> 3393

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3393

Leu His Phe Cys Arg Ser Ser Ile Met

15

<210> 3394

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3394

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

1 5 10

<210> 3395

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3395

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3396

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3396

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 3397

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3397

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 3398

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3398

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 3399

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3399

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 3400

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3400

Phe Ala Thr Leu Gln Arg Ser Ser Leu

15

<210> 3401

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3401

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 3402

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3402

Gly Pro Pro Ala Arg Val Pro Ala Val

15

<210> 3403

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3403

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10

<210> 3404

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3404

Phe Ala Thr Leu Gln Arg Ser Ser Leu

15

<210> 3405

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3405

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 3406

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3406

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 3407

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3407

Phe Leu Lys Ala Glu Ser Lys Ile Met

15

<210> 3408

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3408

Leu His Phe Cys Arg Ser Ser Ile Met

15

<210> 3409

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3409

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10

<210> 3410

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3410

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 3411

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3411

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 3412

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3412

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3413

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3413

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 3414

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3414

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 3415

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3415

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 3416

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3416

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 3417

<211> 9

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3417

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3418

<211> 9

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3418

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 3419

<211> 10

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3419

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 3420

<211> 9

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3420

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 3421

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3421

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3422

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3422

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3423

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3423

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 3424

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3424

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 3425

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3425

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

1 5 10

<210> 3426

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3426

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

1 5 10

<210> 3427

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3427

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

1 5 10

<210> 3428

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3428

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

1 5 10

<210> 3429

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3429

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

1 5 10

<210> 3430

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3430

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

1 5 10

<210> 3431

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3431

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 3432

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3432

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 3433

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3433

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 3434

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3434

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 3435

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3435

Phe Ala Thr Leu Gln Arg Ser Ser Leu

15

<210> 3436

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3436

Gly Pro Pro Ala Arg Val Pro Ala Val

15

<210> 3437

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3437

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 3438

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3438

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 3439

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3439

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 3440

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3440

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 3441

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3441

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 3442

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3442

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 3443

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3443

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 3444

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3444

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 3445

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3445

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 3446

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3446

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 3447

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3447

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 3448

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3448

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 3449

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3449

Phe Ala Thr Leu Gln Arg Ser Ser Leu

15

<210> 3450

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3450

Phe Leu Lys Ala Glu Ser Lys Ile Met

15

<210> 3451

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3451

Phe Leu Lys Ala Glu Ser Lys Ile Met

15

<210> 3452

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3452

Phe Leu Lys Ala Glu Ser Lys Ile Met

15

<210> 3453

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3453

Phe Leu Lys Ala Glu Ser Lys Ile Met

15

<210> 3454

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3454

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10

<210> 3455

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3455

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10

<210> 3456

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3456

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10

<210> 3457

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3457

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10

<210> 3458

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3458

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10

<210> 3459

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3459

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10

<210> 3460

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3460

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10

<210> 3461

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3461

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10

<210> 3462

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3462

Leu His Phe Cys Arg Ser Ser Ile Met

15

<210> 3463

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3463

Leu His Phe Cys Arg Ser Ser Ile Met

15

<210> 3464

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3464

Leu His Phe Cys Arg Ser Ser Ile Met

15

<210> 3465

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3465

Leu His Phe Cys Arg Ser Ser Ile Met

15

<210> 3466

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3466

Leu His Phe Cys Arg Ser Ser Ile Met

15

<210> 3467

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3467

Leu His Phe Cys Arg Ser Ser Ile Met

15

<210> 3468

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3468

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 3469

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3469

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 3470

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3470

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 3471

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3471

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 3472

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3472

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 3473

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3473

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 3474

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3474

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 3475

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3475

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3476

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3476

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 3477

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3477

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3478

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3478

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 3479

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3479

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 3480

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3480

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 3481

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3481

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 3482

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3482

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3483

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3483

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 3484

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3484

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 3485

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3485

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 3486

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3486

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 3487

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3487

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3488

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3488

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 3489

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3489

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 3490

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3490

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 3491

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3491

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 3492

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3492

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 3493

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3493

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 3494

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3494

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 3495

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3495

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 3496

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3496

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3497

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3497

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 3498

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3498

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 3499

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3499

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 3500

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3500

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 3501

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3501

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 3502

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3502

Val Leu Pro Glu Pro His Leu Ala Leu

15

<210> 3503

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3503

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

1 5 10

<210> 3504

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3504

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3505

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3505

Tyr Met Phe Leu Lys Ala Glu Ser Lys

15

<210> 3506

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3506

Lys Ile Met Phe Ala Thr Leu Gln Arg

15

<210> 3507

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3507

Val Leu Trp Thr Thr Pro Pro Leu Gln His

1 5 10

<210> 3508

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3508

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 3509

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3509

Met Phe Leu Lys Ala Glu Ser Lys Ile

15

<210> 3510

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3510

Tyr Met Phe Leu Lys Ala Glu Ser Lys

15

<210> 3511

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3511

Lys Ile Met Phe Ala Thr Leu Gln Arg

15

<210> 3512

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3512

Val Leu Trp Thr Thr Pro Pro Leu Gln His

1 5 10

<210> 3513

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3513

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 3514

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3514

Phe Ala Thr Leu Gln Arg Ser Ser Leu

15

<210> 3515

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3515

Glu Pro His Leu Ala Leu Gln Pro Leu

15

<210> 3516

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3516

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 3517

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3517

Gly Pro Pro Ala Arg Val Pro Ala Val

15

<210> 3518

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3518

Phe Ala Thr Leu Gln Arg Ser Ser Leu

15

<210> 3519

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3519

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 3520

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3520

Phe Leu Lys Ala Glu Ser Lys Ile Met

15

<210> 3521

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3521

Glu Pro His Leu Ala Leu Gln Pro Leu

15

<210> 3522

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3522

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 3523

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3523

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 3524

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3524

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10

<210> 3525

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3525

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10

<210> 3526

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3526

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3527

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3527

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 3528

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3528

Gly Pro Pro Ala Arg Val Pro Ala Val

15

<210> 3529

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3529

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 3530

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3530

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 3531

<211> 27

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3531

Pro Gly Arg Pro Leu Gln Thr His Val Leu Pro Glu Pro His Leu Ala

1 5 10 15

Leu Gln Pro Leu Gln Pro His Ala Asp His Ala

20 25

<210> 3532

<211> 26

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3532

Ala Pro Ala Ile Gln Pro Val Leu Trp Thr Thr Pro Pro Leu Gln His

1 5 10 15

Gly His Arg His Gly Leu Glu Pro Cys Ser

20 25

<210> 3533

<211> 25

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3533

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

Ser Ser Ile Met Lys Pro Lys Arg Asp

20 25

<210> 3534

<211> 26

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3534

Glu Pro His Leu Ala Leu Gln Pro Leu Gln Pro His Ala Asp His Ala

1 5 10 15

His Ala Asp Ala Pro Ala Ile Gln Pro Val

20 25

<210> 3535

<211> 27

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3535

Thr Pro Pro Leu Gln His Gly His Arg His Gly Leu Glu Pro Cys Ser

1 5 10 15

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala

20 25

<210> 3536

<211> 25

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3536

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met Phe Leu Lys Ala Glu Ser Lys

20 25

<210> 3537

<211> 23

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3537

Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10 15

Trp Cys Leu Cys Ser Asn His

20

<210> 3538

<211> 24

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3538

His Ala Asp His Ala His Ala Asp Ala Pro Ala Ile Gln Pro Val Leu

1 5 10 15

Trp Thr Thr Pro Pro Leu Gln His

20

<210> 3539

<211> 24

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3539

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His Phe Cys Arg

20

<210> 3540

<211> 24

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3540

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg Ser

20

<210> 3541

<211> 26

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3541

Glu Pro His Leu Ala Leu Gln Pro Leu Gln Pro His Ala Asp His Ala

1 5 10 15

His Ala Asp Ala Pro Ala Ile Gln Pro Val

20 25

<210> 3542

<211> 26

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3542

Ala Pro Ala Ile Gln Pro Val Leu Trp Thr Thr Pro Pro Leu Gln His

1 5 10 15

Gly His Arg His Gly Leu Glu Pro Cys Ser

20 25

<210> 3543

<211> 25

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3543

Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg

1 5 10 15

Ser Ser Ile Met Lys Pro Lys Arg Asp

20 25

<210> 3544

<211> 25

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3544

Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly

1 5 10 15

Tyr Met Phe Leu Lys Ala Glu Ser Lys

20 25

<210> 3545

<211> 24

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3545

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg Ser

20

<210> 3546

<211> 24

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

peptide

<400> 3546

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

1 5 10 15

Leu Trp Cys Leu Cys Ser Asn His

20

<210> 3547

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3547

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3548

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3548

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3549

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3549

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3550

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3550

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3551

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 3551

Cys Ala Leu Asp Ile Tyr Gly Asn Asn Arg Leu Ala Phe

1 5 10

<210> 3552

<211> 19

<212> PROTEIN

<213> Homo sapiens

<400> 3552

Cys Ala Ser Ser Leu Asp Phe Val Leu Ala Gly Ser Tyr Ser Tyr Glu

1 5 10 15

Gln Phe Phe

<210> 3553

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 3553

Cys Ala Leu Asp Ile Tyr Gly Asn Asn Arg Leu Ala Phe

1 5 10

<210> 3554

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 3554

Cys Ala Ser Ser Leu Asp Phe Val Leu Ala Gly Ser Tyr Ser Tyr Asn

1 5 10 15

Glu Gln Phe Phe

20

<210> 3555

<211> 20

<212> PROTEIN

<213> Homo sapiens

<400> 3555

Cys Ala Ser Ser Leu Asp Phe Val Leu Ala Gly Ser Tyr Ser Tyr Asn

1 5 10 15

Glu Gln Phe Phe

20

<210> 3556

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 3556

Cys Ala Leu Asp Ile Tyr Gly Asn Asn Arg Leu Ala Phe

1 5 10

<210> 3557

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 3557

Cys Ala Glu Lys Val Pro Asn Thr Gly Asn Gln Phe Tyr Phe

1 5 10

<210> 3558

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 3558

Cys Ala Ser Ser Ser Leu Gly Thr Val Arg Thr Glu Ala Phe Phe

1 5 10 15

<210> 3559

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 3559

Cys Ala Val Glu Ala Tyr Asn Phe Asn Lys Phe Tyr Phe

1 5 10

<210> 3560

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 3560

Cys Ala Ser Arg Ser Glu Asn Thr Ile Tyr Phe

1 5 10

<210> 3561

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 3561

Cys Ile Leu Ser Asp Ser Gly Asn Thr Pro Leu Val Phe

1 5 10

<210> 3562

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 3562

Cys Ala Ser Ser Asp Trp Ala Val Ser Gly Asn Thr Ile Tyr Phe

1 5 10 15

<210> 3563

<211> 17

<212> PROTEIN

<213> Homo sapiens

<400> 3563

Cys Ala Gly Ala Ala Asn Ala Gly Gly Thr Ser Tyr Gly Lys Leu Thr

1 5 10 15

Phe

<210> 3564

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 3564

Cys Ala Ser Ser Gln Ala Gln Gly Ala Asn Tyr Gly Tyr Thr Phe

1 5 10 15

<210> 3565

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 3565

Cys Ala Glu Ile Pro Thr Phe Ser Gly Gly Tyr Asn Lys Leu Ile Phe

1 5 10 15

<210> 3566

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 3566

Cys Ala Ser Ser Leu Ala Gly Gln Glu Thr Gln Tyr Phe

1 5 10

<210> 3567

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 3567

Cys Leu Arg Gly Gly Ser Thr Leu Gly Arg Leu Tyr Phe

1 5 10

<210> 3568

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 3568

Cys Ala Ser Ser Leu Tyr Pro Thr Gly Gly Ser Gly Met Asp Glu Gln

1 5 10 15

Tyr Phe

<210> 3569

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 3569

Cys Ala Val Arg Asp Gly Asn Thr Gly Gly Phe Lys Thr Ile Phe

1 5 10 15

<210> 3570

<211> 13

<212> PROTEIN

<213> Homo sapiens

<400> 3570

Cys Ala Ser Ser Glu Leu Lys Thr Gly Gly Ala Phe Phe

1 5 10

<210> 3571

<211> 453

<212> DNA

<213> Homo sapiens

<400> 3571

atggcttttt ggctgagaag gctgggtcta catttcaggc cacatttggg gagacgaatg

60

gagtcattcc tgggaggtgt tttgctgatt ttgtggcttc aagtggactg ggtgaagagc

120

caaaagatag aacagaattc cgaggccctg aacattcagg agggtaaaac ggccaccctg

180

acctgcaact atacaaacta ttctccagca tacttacagt ggtaccgaca agatccagga

240

agaggccctg ttttcttgct actcatacgt gaaaatgaga aagaaaaaag gaaagaaaga

300

ctgaaggtca cctttgatac cacccttaaa cagagtttgt ttcatatcac agcctcccag

360

cctgcagact cagctaccta cctctgtgct ctagacattt atgggaacaa cagactcgct

420

tttgggaagg ggaaccaagt ggtggtcata cca

453

<210> 3572

<211> 415

<212> DNA

<213> Homo sapiens

<400> 3572

atgggaatca ggctcctctg tcgtgtggcc ttttgtttcc tggctgtagg cctcgtagat

60

gtgaaagtaa cccagagctc gagatatcta gtcaaaagga cgggagagaa agtttttctg

120

gaatgtgtcc aggatatgga ccatgaaaat atgttctggt atcgacaaga cccaggtctg

180

gggctacggc tgatctattt ctcatatgat gttaaaatga aagaaaaagg agatattcct

240

gaggggtaca gtgtctctag agagaagaag gagcgcttct ccctgattct ggagtccgcc

300

agcaccaacc agacatctat gtacctctgt gccagcagtt tagattttgt gctagcgggg

360

tcctactcct acaatgagca gttcttcggg ccagggacac ggctcaccgt gctag

415

<210> 3573

<211> 453

<212> DNA

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polynucleotide

<400> 3573

atggccttct ggctgaggag actgggttta cacttcagac cccatttagg cagaagaatg

60

gagagctttt taggcggcgt gctgctgatt ttatggctgc aagttgactg ggtgaagagc

120

cagaagatcg agcagaacag cgaggcttta aacattcaag aaggcaagac agccacttta

180

acttgtaact ataccaacta ctcccccgct tatttacagt ggtacagaca agatcccggc

240

agaggccccg tgtttttact gctgattcgt gagaacgaga aggagaagag gaaggagaga

300

ctgaaggtga ccttcgacac cactttaaag cagtctttat tccacatcac cgccagccag

360

cccgctgata gcgccaccta tttatgcgct ttagacatct acggcaacaa tcgtctggcc

420

ttcggcaagg gcaaccaagt tgtggtgatc ccc

453

<210> 3574

<211> 414

<212> DNA

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polynucleotide

<400> 3574

atgggcattc gtctgctgtg tcgtgtggcc ttctgctttt tagccgtggg tttagtggac

60

gtgaaggtga cccagtcctc tcgttattta gtgaagagga ccggcgagaa ggtgttttta

120

gaatgcgtgc aagatatgga ccacgagaac atgttctggt acagacaaga tcccggactg

180

ggtttaaggc tgatctactt cagctacgac gtgaagatga aggagaaggg cgacatcccc

240

gagggctact ccgtgtctcg tgagaagaag gagaggttct ctttaatttt agagtccgcc

300

agcaccaacc agaccagcat gtatttatgc gccagctctt tagactttgt gctggccggc

360

agctacagct acaacgagca gttcttcggc cccggcacca gactgaccgt gctg

414

<210> 3575

<211> 23

<212> PROTEIN

<213> Homo sapiens

<400> 3575

Ile Phe Ile Ile Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10 15

Leu Arg Glu Met Arg His Arg

20

<210> 3576

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3576

Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 3577

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3577

Ala Asn Gly Ser Leu Leu Asn Tyr Leu

15

<210> 3578

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3578

Ala Asn Gly Ser Leu Leu Asn Tyr Leu

15

<210> 3579

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3579

Ala Asn Gly Ser Leu Leu Asn Tyr Leu

15

<210> 3580

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3580

Ala Asn Gly Ser Leu Leu Asn Tyr Leu

15

<210> 3581

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3581

Ala Asn Gly Ser Leu Leu Asn Tyr Leu

15

<210> 3582

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3582

Ala Asn Gly Ser Leu Leu Asn Tyr Leu

15

<210> 3583

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3583

Ala Asn Gly Ser Leu Leu Asn Tyr Leu

15

<210> 3584

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3584

Ala Asn Gly Ser Leu Leu Asn Tyr Leu

15

<210> 3585

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3585

Ala Asn Gly Ser Leu Leu Asn Tyr Leu Arg

1 5 10

<210> 3586

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3586

Ala Asn Gly Ser Leu Leu Asn Tyr Leu Arg

1 5 10

<210> 3587

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3587

Glu Tyr Met Ala Asn Gly Ser Leu

15

<210> 3588

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3588

Glu Tyr Met Ala Asn Gly Ser Leu

15

<210> 3589

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3589

Glu Tyr Met Ala Asn Gly Ser Leu

15

<210> 3590

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3590

Glu Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 3591

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3591

Glu Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 3592

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3592

Glu Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 3593

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3593

Glu Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 3594

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3594

Glu Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 3595

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3595

Glu Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 3596

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3596

Glu Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 3597

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3597

Glu Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 3598

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3598

Glu Tyr Met Ala Asn Gly Ser Leu Leu Asn

1 5 10

<210> 3599

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3599

Glu Tyr Met Ala Asn Gly Ser Leu Leu Asn

1 5 10

<210> 3600

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 3600

Glu Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 3601

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3601

Gly Ser Leu Leu Asn Tyr Leu Arg

15

<210> 3602

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3602

Gly Ser Leu Leu Asn Tyr Leu Arg

15

<210> 3603

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3603

Gly Ser Leu Leu Asn Tyr Leu Arg Glu Met

1 5 10

<210> 3604

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3604

Gly Ser Leu Leu Asn Tyr Leu Arg Glu Met

1 5 10

<210> 3605

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3605

Ile Thr Glu Tyr Met Ala Asn Gly Ser

15

<210> 3606

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3606

Ile Thr Glu Tyr Met Ala Asn Gly Ser Leu

1 5 10

<210> 3607

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 3607

Ile Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu

1 5 10

<210> 3608

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3608

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 3609

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3609

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 3610

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3610

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 3611

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3611

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 3612

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3612

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 3613

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3613

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 3614

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3614

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 3615

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3615

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 3616

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3616

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 3617

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3617

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 3618

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3618

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 3619

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3619

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 3620

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3620

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 3621

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3621

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 3622

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3622

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 3623

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3623

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 3624

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3624

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 3625

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3625

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 3626

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3626

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 3627

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3627

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 3628

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3628

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 3629

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3629

Met Ala Asn Gly Ser Leu Leu Asn Tyr Leu

1 5 10

<210> 3630

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3630

Met Ala Asn Gly Ser Leu Leu Asn Tyr Leu

1 5 10

<210> 3631

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3631

Met Ala Asn Gly Ser Leu Leu Asn Tyr Leu

1 5 10

<210> 3632

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3632

Met Ala Asn Gly Ser Leu Leu Asn Tyr Leu

1 5 10

<210> 3633

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3633

Met Ala Asn Gly Ser Leu Leu Asn Tyr Leu

1 5 10

<210> 3634

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3634

Met Ala Asn Gly Ser Leu Leu Asn Tyr Leu

1 5 10

<210> 3635

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3635

Met Ala Asn Gly Ser Leu Leu Asn Tyr Leu

1 5 10

<210> 3636

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3636

Met Ala Asn Gly Ser Leu Leu Asn Tyr Leu

1 5 10

<210> 3637

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3637

Met Ala Asn Gly Ser Leu Leu Asn Tyr Leu

1 5 10

<210> 3638

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3638

Met Ala Asn Gly Ser Leu Leu Asn Tyr Leu

1 5 10

<210> 3639

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 3639

Met Ala Asn Gly Ser Leu Leu Asn Tyr Leu Arg

1 5 10

<210> 3640

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 3640

Met Ala Asn Gly Ser Leu Leu Asn Tyr Leu Arg

1 5 10

<210> 3641

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3641

Asn Gly Ser Leu Leu Asn Tyr Leu

15

<210> 3642

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3642

Asn Gly Ser Leu Leu Asn Tyr Leu Arg

15

<210> 3643

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3643

Asn Gly Ser Leu Leu Asn Tyr Leu Arg

15

<210> 3644

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3644

Asn Gly Ser Leu Leu Asn Tyr Leu Arg

15

<210> 3645

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3645

Asn Gly Ser Leu Leu Asn Tyr Leu Arg

15

<210> 3646

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3646

Ser Leu Leu Asn Tyr Leu Arg Glu Met

15

<210> 3647

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3647

Ser Leu Leu Asn Tyr Leu Arg Glu Met

15

<210> 3648

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3648

Ser Leu Leu Asn Tyr Leu Arg Glu Met

15

<210> 3649

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3649

Ser Leu Leu Asn Tyr Leu Arg Glu Met

15

<210> 3650

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3650

Ser Leu Leu Asn Tyr Leu Arg Glu Met

15

<210> 3651

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3651

Ser Leu Leu Asn Tyr Leu Arg Glu Met

15

<210> 3652

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3652

Ser Leu Leu Asn Tyr Leu Arg Glu Met

15

<210> 3653

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3653

Ser Leu Leu Asn Tyr Leu Arg Glu Met

15

<210> 3654

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3654

Ser Leu Leu Asn Tyr Leu Arg Glu Met

15

<210> 3655

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3655

Ser Leu Leu Asn Tyr Leu Arg Glu Met

15

<210> 3656

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3656

Ser Leu Leu Asn Tyr Leu Arg Glu Met

15

<210> 3657

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3657

Ser Leu Leu Asn Tyr Leu Arg Glu Met

15

<210> 3658

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3658

Ser Leu Leu Asn Tyr Leu Arg Glu Met

15

<210> 3659

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3659

Ser Leu Leu Asn Tyr Leu Arg Glu Met

15

<210> 3660

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3660

Ser Leu Leu Asn Tyr Leu Arg Glu Met

15

<210> 3661

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3661

Ser Leu Leu Asn Tyr Leu Arg Glu Met

15

<210> 3662

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3662

Ser Leu Leu Asn Tyr Leu Arg Glu Met

15

<210> 3663

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3663

Ser Leu Leu Asn Tyr Leu Arg Glu Met

15

<210> 3664

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3664

Ser Leu Leu Asn Tyr Leu Arg Glu Met

15

<210> 3665

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3665

Ser Leu Leu Asn Tyr Leu Arg Glu Met Arg

1 5 10

<210> 3666

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3666

Ser Leu Leu Asn Tyr Leu Arg Glu Met Arg

1 5 10

<210> 3667

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3667

Thr Glu Tyr Met Ala Asn Gly Ser Leu

15

<210> 3668

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3668

Thr Glu Tyr Met Ala Asn Gly Ser Leu

15

<210> 3669

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3669

Thr Glu Tyr Met Ala Asn Gly Ser Leu

15

<210> 3670

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3670

Thr Glu Tyr Met Ala Asn Gly Ser Leu

15

<210> 3671

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3671

Thr Glu Tyr Met Ala Asn Gly Ser Leu

15

<210> 3672

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3672

Thr Glu Tyr Met Ala Asn Gly Ser Leu

15

<210> 3673

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3673

Thr Glu Tyr Met Ala Asn Gly Ser Leu

15

<210> 3674

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3674

Thr Glu Tyr Met Ala Asn Gly Ser Leu

15

<210> 3675

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3675

Thr Glu Tyr Met Ala Asn Gly Ser Leu

15

<210> 3676

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3676

Thr Glu Tyr Met Ala Asn Gly Ser Leu

15

<210> 3677

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3677

Thr Glu Tyr Met Ala Asn Gly Ser Leu

15

<210> 3678

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3678

Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu

1 5 10

<210> 3679

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3679

Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu

1 5 10

<210> 3680

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3680

Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu

1 5 10

<210> 3681

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3681

Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu

1 5 10

<210> 3682

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3682

Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu

1 5 10

<210> 3683

<211> 12

<212> PROTEIN

<213> Homo sapiens

<400> 3683

Thr Glu Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 3684

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3684

Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 3685

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3685

Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 3686

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3686

Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 3687

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3687

Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 3688

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3688

Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 3689

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3689

Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 3690

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3690

Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 3691

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3691

Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 3692

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3692

Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 3693

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3693

Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 3694

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3694

Tyr Met Ala Asn Gly Ser Leu Leu Asn

15

<210> 3695

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3695

Tyr Met Ala Asn Gly Ser Leu Leu Asn

15

<210> 3696

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3696

Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 3697

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3697

Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 3698

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3698

Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 3699

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3699

Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 3700

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3700

Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 3701

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3701

Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 3702

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3702

Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 3703

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3703

Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 3704

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3704

Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 3705

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3705

Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 3706

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3706

Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 3707

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3707

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 3708

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3708

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 3709

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3709

Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 3710

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3710

Met Ala Asn Gly Ser Leu Leu Asn Tyr

15

<210> 3711

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3711

Tyr Met Ala Asn Gly Ser Leu Leu Asn Tyr

1 5 10

<210> 3712

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3712

Glu Tyr Met Ala Asn Gly Ser Leu Leu

15

<210> 3713

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3713

Ser Leu Leu Asn Tyr Leu Arg Glu Met

15

<210> 3714

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3714

Met Ala Asn Gly Ser Leu Leu Asn Tyr Leu

1 5 10

<210> 3715

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3715

Tyr Met Ala Asn Gly Ser Leu Leu Asn

15

<210> 3716

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3716

Ser Leu Leu Asn Tyr Leu Arg Glu Met

15

<210> 3717

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3717

Met Ala Asn Gly Ser Leu Leu Asn Tyr Leu

1 5 10

<210> 3718

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3718

Ser Leu Leu Asn Tyr Leu Arg Glu Met

15

<210> 3719

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3719

Met Ala Asn Gly Ser Leu Leu Asn Tyr Leu

1 5 10

<210> 3720

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3720

Leu Ile Met Gln Leu Met Pro Phe

15

<210> 3721

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3721

Leu Thr Ser Thr Val Gln Leu Ile Met

15

<210> 3722

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3722

Gln Leu Ile Met Gln Leu Met Pro Phe

15

<210> 3723

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3723

Ser Thr Val Gln Leu Ile Met Gln Leu

15

<210> 3724

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3724

Ser Thr Val Gln Leu Ile Met Gln Leu Met

1 5 10

<210> 3725

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3725

Thr Ser Thr Val Gln Leu Ile Met Gln Leu

1 5 10

<210> 3726

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3726

Thr Val Gln Leu Ile Met Gln Leu

15

<210> 3727

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3727

Thr Val Gln Leu Ile Met Gln Leu Met

15

<210> 3728

<211> 8

<212> PROTEIN

<213> Homo sapiens

<400> 3728

Val Gln Leu Ile Met Gln Leu Met

15

<210> 3729

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3729

Leu Thr Ser Thr Val Gln Leu Ile Met

15

<210> 3730

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3730

Cys Leu Thr Ser Thr Val Gln Leu Ile Met

1 5 10

<210> 3731

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3731

Met Gln Leu Met Pro Phe Gly Cys Leu Leu

1 5 10

<210> 3732

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3732

Met Gln Leu Met Pro Phe Gly Cys Leu

15

<210> 3733

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3733

Leu Ile Met Gln Leu Met Pro Phe Gly Cys

1 5 10

<210> 3734

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3734

Gln Leu Ile Met Gln Leu Met Pro Phe

15

<210> 3735

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3735

Cys Leu Thr Ser Thr Val Gln Leu Ile Met

1 5 10

<210> 3736

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3736

Ile Met Gln Leu Met Pro Phe Gly Cys Leu

1 5 10

<210> 3737

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3737

Ile Met Gln Leu Met Pro Phe Gly Cys

15

<210> 3738

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3738

Leu Ile Met Gln Leu Met Pro Phe Gly

15

<210> 3739

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3739

Val Gln Leu Ile Met Gln Leu Met Pro Phe

1 5 10

<210> 3740

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3740

Gln Leu Ile Met Gln Leu Met Pro Phe Gly

1 5 10

<210> 3741

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3741

Ser Thr Val Gln Leu Ile Met Gln Leu

15

<210> 3742

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3742

Gln Leu Ile Met Gln Leu Met Pro Phe

15

<210> 3743

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3743

Val Gln Leu Ile Met Gln Leu Met Pro Phe

1 5 10

<210> 3744

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3744

Ile Met Gln Leu Met Pro Phe Gly Cys Leu

1 5 10

<210> 3745

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3745

Met Gln Leu Met Pro Phe Gly Cys Leu Leu

1 5 10

<210> 3746

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3746

Met Gln Leu Met Pro Phe Gly Cys Leu

15

<210> 3747

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3747

Gln Leu Ile Met Gln Leu Met Pro Phe

15

<210> 3748

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3748

Ile Met Gln Leu Met Pro Phe Gly Cys Leu

1 5 10

<210> 3749

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3749

Met Gln Leu Met Pro Phe Gly Cys Leu

15

<210> 3750

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3750

Met Gln Leu Met Pro Phe Gly Cys Leu Leu

1 5 10

<210> 3751

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3751

Val Gln Leu Ile Met Gln Leu Met Pro Phe

1 5 10

<210> 3752

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3752

Gln Leu Ile Met Gln Leu Met Pro Phe

15

<210> 3753

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3753

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

1 5 10

<210> 3754

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3754

Val Leu Pro Glu Pro His Leu Ala Leu

15

<210> 3755

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3755

His Val Leu Pro Glu Pro His Leu Ala Leu

1 5 10

<210> 3756

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3756

Ala Leu Gln Pro Leu Gln Pro His Ala

15

<210> 3757

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3757

Ala Ile Gln Pro Val Leu Trp Thr Thr

15

<210> 3758

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 3758

Ala Pro Ala Ile Gln Pro Val Leu Trp Thr Thr

1 5 10

<210> 3759

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3759

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 3760

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3760

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3761

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3761

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 3762

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3762

Met Phe Leu Lys Ala Glu Ser Lys Ile

15

<210> 3763

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3763

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 3764

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3764

Val Leu Trp Thr Thr Pro Pro Leu Gln His

1 5 10

<210> 3765

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3765

Tyr Met Phe Leu Lys Ala Glu Ser Lys

15

<210> 3766

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3766

Lys Ile Met Phe Ala Thr Leu Gln Arg

15

<210> 3767

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3767

Phe Ala Thr Leu Gln Arg Ser Ser Leu

15

<210> 3768

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3768

Glu Pro His Leu Ala Leu Gln Pro Leu

15

<210> 3769

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3769

Gln Pro Val Leu Trp Thr Thr Pro Pro Leu

1 5 10

<210> 3770

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3770

Gly Pro Pro Ala Arg Val Pro Ala Val

15

<210> 3771

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3771

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 3772

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3772

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 3773

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3773

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 3774

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3774

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10

<210> 3775

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3775

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 3776

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3776

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10

<210> 3777

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3777

Leu His Phe Cys Arg Ser Ser Ile Met

15

<210> 3778

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3778

Glu Pro His Leu Ala Leu Gln Pro Leu

15

<210> 3779

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3779

Phe Ala Thr Leu Gln Arg Ser Ser Leu

15

<210> 3780

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3780

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 3781

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3781

Phe Leu Lys Ala Glu Ser Lys Ile Met

15

<210> 3782

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3782

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 3783

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3783

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu

1 5 10

<210> 3784

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3784

Val Leu Pro Glu Pro His Leu Ala Leu

15

<210> 3785

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3785

His Val Leu Pro Glu Pro His Leu Ala Leu

1 5 10

<210> 3786

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3786

Ala Leu Gln Pro Leu Gln Pro His Ala

15

<210> 3787

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3787

Ala Ile Gln Pro Val Leu Trp Thr Thr

15

<210> 3788

<211> 11

<212> PROTEIN

<213> Homo sapiens

<400> 3788

Ala Pro Ala Ile Gln Pro Val Leu Trp Thr Thr

1 5 10

<210> 3789

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3789

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 3790

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3790

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3791

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3791

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 3792

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3792

Met Phe Leu Lys Ala Glu Ser Lys Ile

15

<210> 3793

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3793

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 3794

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3794

Val Leu Trp Thr Thr Pro Pro Leu Gln His

1 5 10

<210> 3795

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3795

Tyr Met Phe Leu Lys Ala Glu Ser Lys

15

<210> 3796

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3796

Lys Ile Met Phe Ala Thr Leu Gln Arg

15

<210> 3797

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3797

Phe Ala Thr Leu Gln Arg Ser Ser Leu

15

<210> 3798

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3798

Glu Pro His Leu Ala Leu Gln Pro Leu

15

<210> 3799

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3799

Gln Pro Val Leu Trp Thr Thr Pro Pro Leu

1 5 10

<210> 3800

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3800

Gly Pro Pro Ala Arg Val Pro Ala Val

15

<210> 3801

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3801

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 3802

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3802

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 3803

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3803

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 3804

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3804

Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

1 5 10

<210> 3805

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3805

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 3806

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3806

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe

1 5 10

<210> 3807

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3807

Leu His Phe Cys Arg Ser Ser Ile Met

15

<210> 3808

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3808

Glu Pro His Leu Ala Leu Gln Pro Leu

15

<210> 3809

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3809

Phe Ala Thr Leu Gln Arg Ser Ser Leu

15

<210> 3810

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3810

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 3811

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3811

Phe Leu Lys Ala Glu Ser Lys Ile Met

15

<210> 3812

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3812

Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10

<210> 3813

<211> 14

<212> PROTEIN

<213> Homo sapiens

<400> 3813

Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser Leu

1 5 10

<210> 3814

<211> 16

<212> PROTEIN

<213> Homo sapiens

<400> 3814

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

<210> 3815

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 3815

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His

<210> 3816

<211> 21

<212> PROTEIN

<213> Homo sapiens

<400> 3816

Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val

1 5 10 15

Pro Phe Asp Leu His

20

<210> 3817

<211> 25

<212> PROTEIN

<213> Homo sapiens

<400> 3817

Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr

1 5 10 15

Met Phe Leu Lys Ala Glu Ser Lys Ile

20 25

<210> 3818

<211> 26

<212> PROTEIN

<213> Homo sapiens

<400> 3818

Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His Phe Cys

1 5 10 15

Arg Ser Ser Ile Met Lys Pro Lys Arg Asp

20 25

<210> 3819

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 3819

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

20 25 30

His

<210> 3820

<211> 15

<212> PROTEIN

<213> Homo sapiens

<400> 3820

Gly Gly Ala Ala Thr Thr Ala Ala Gly Ala Gly Ala Ala Gly Cys

1 5 10 15

<210> 3821

<211> 5

<212> PROTEIN

<213> Homo sapiens

<400> 3821

Glu Leu Arg Glu Ala

15

<210> 3822

<211> 5

<212> PROTEIN

<213> Homo sapiens

<400> 3822

Glu Leu Arg Glu Ala

15

<210> 3823

<211> 4

<212> PROTEIN

<213> Homo sapiens

<400> 3823

Tyr Val Met Ala

1

<210> 3824

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3824

Val Leu Pro Glu Pro His Leu Ala Leu

15

<210> 3825

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3825

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 3826

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3826

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3827

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3827

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 3828

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3828

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 3829

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3829

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 3830

<211> 201

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<400> 3830

Met Arg Arg Leu Ser Ala Ala Arg Arg Ala Gly Thr Ser Cys Ala Asn

1 5 10 15

Cys Gln Thr Thr Thr Thr Thr Leu Trp Arg Arg Asn Ala Asn Gly Asp

20 25 30

Pro Val Cys Asn Ala Cys Gly Leu Tyr Tyr Lys Leu His Asn Ile Asn

35 40 45

Arg Pro Leu Thr Met Lys Lys Glu Gly Ile Gln Thr Arg Asn Arg Lys

50 55 60

Met Ser Ser Lys Ser Lys Lys Cys Lys Lys Val His Asp Ser Leu Glu

65 70 75 80

Asp Phe Pro Lys Asn Ser Ser Phe Pro Gly Arg Pro Leu Gln Thr His

85 90 95

Val Leu Pro Glu Pro His Leu Ala Leu Gln Pro Leu Gln Pro His Ala

100 105 110

Asp His Ala His Ala Asp Ala Pro Ala Ile Gln Pro Val Leu Trp Thr

115 120 125

Thr Pro Pro Leu Gln His Gly His Arg His Gly Leu Glu Pro Cys Ser

130 135 140

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

145 150 155 160

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

165 170 175

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

180 185 190

Ser Leu Trp Cys Leu Cys Ser Asn His

195 200

<210> 3831

<211> 201

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<400> 3831

Met Arg Arg Leu Ser Ala Ala Arg Arg Ala Gly Thr Ser Cys Ala Asn

1 5 10 15

Cys Gln Thr Thr Thr Thr Thr Leu Trp Arg Arg Asn Ala Asn Gly Asp

20 25 30

Pro Val Cys Asn Ala Cys Gly Leu Tyr Tyr Lys Leu His Asn Ile Asn

35 40 45

Arg Pro Leu Thr Met Lys Lys Glu Gly Ile Gln Thr Arg Asn Arg Lys

50 55 60

Met Ser Ser Lys Ser Lys Lys Cys Lys Lys Val His Asp Ser Leu Glu

65 70 75 80

Asp Phe Pro Lys Asn Ser Ser Phe Pro Gly Arg Pro Leu Gln Thr His

85 90 95

Val Leu Pro Glu Pro His Leu Ala Leu Gln Pro Leu Gln Pro His Ala

100 105 110

Asp His Ala His Ala Asp Ala Pro Ala Ile Gln Pro Val Leu Trp Thr

115 120 125

Thr Pro Pro Leu Gln His Gly His Arg His Gly Leu Glu Pro Cys Ser

130 135 140

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

145 150 155 160

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

165 170 175

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

180 185 190

Ser Leu Trp Cys Leu Cys Ser Asn His

195 200

<210> 3832

<211> 201

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<400> 3832

Met Arg Arg Leu Ser Ala Ala Arg Arg Ala Gly Thr Ser Cys Ala Asn

1 5 10 15

Cys Gln Thr Thr Thr Thr Thr Leu Trp Arg Arg Asn Ala Asn Gly Asp

20 25 30

Pro Val Cys Asn Ala Cys Gly Leu Tyr Tyr Lys Leu His Asn Ile Asn

35 40 45

Arg Pro Leu Thr Met Lys Lys Glu Gly Ile Gln Thr Arg Asn Arg Lys

50 55 60

Met Ser Ser Lys Ser Lys Lys Cys Lys Lys Val His Asp Ser Leu Glu

65 70 75 80

Asp Phe Pro Lys Asn Ser Ser Phe Pro Gly Arg Pro Leu Gln Thr His

85 90 95

Val Leu Pro Glu Pro His Leu Ala Leu Gln Pro Leu Gln Pro His Ala

100 105 110

Asp His Ala His Ala Asp Ala Pro Ala Ile Gln Pro Val Leu Trp Thr

115 120 125

Thr Pro Pro Leu Gln His Gly His Arg His Gly Leu Glu Pro Cys Ser

130 135 140

Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu

145 150 155 160

His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met

165 170 175

Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser

180 185 190

Ser Leu Trp Cys Leu Cys Ser Asn His

195 200

<210> 3833

<211> 110

<212> PROTEIN

<213> Homo sapiens

<400> 3833

Pro Gly Arg Pro Leu Gln Thr His Val Leu Pro Glu Pro His Leu Ala

1 5 10 15

Leu Gln Pro Leu Gln Pro His Ala Asp His Ala Asp Ala Pro Ala Ile

20 25 30

Gln Pro Val Leu Trp Thr Thr Pro Pro Leu Gln His His Arg His Gly

35 40 45

Leu Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala

50 55 60

Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met Lys Pro Lys

65 70 75 80

Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile Met Phe Ala

85 90 95

Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn His

100 105 110

<210> 3834

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3834

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3835

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3835

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 3836

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3836

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 3837

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3837

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3838

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3838

Lys Ile Met Phe Ala Thr Leu Gln Arg

15

<210> 3839

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3839

Lys Ile Met Phe Ala Thr Leu Gln Arg

15

<210> 3840

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3840

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 3841

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3841

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 3842

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3842

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 3843

<211> 33

<212> PROTEIN

<213> Homo sapiens

<400> 3843

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

1 5 10 15

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

20 25 30

His

<210> 3844

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3844

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 3845

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3845

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 3846

<211> 18

<212> PROTEIN

<213> Homo sapiens

<400> 3846

Ser Met Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp

1 5 10 15

Leu His

<210> 3847

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3847

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 3848

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3848

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3849

<211> 600

<212> DNA

<213> Homo sapiens

<400> 3849

cgaaggctgt ctgcagccag gagagcaggg acgtcctgtg cgaactgtca gaccaccaca

60

accacactct ggagggaggaa tgccaatggg gaccctgtct gcaatgcctg tgggctctac

120

tacaagcttc acaatattaa cagacccctg actatgaaga aggaaggcat ccagaccaga

180

aaccgaaaaa tgtctagcaa atccaaaaag tgcaaaaaag tgcatgactc actggaggac

240

ttccccaaga acagctcgtt tcccggccgc cctctccaga cacatgtcct ccctgagcca

300

catctcgccc ttcagccact ccagccacat gctgaccacg cccacgccga tgcacccgcc

360

atccagcctg tcctttggac cacaccaccc ctccagcatg gtcaccgcca tgggttagag

420

ccctgctcga tgctcacagg gcccccagcg agagtccctg cagtcccttt cgacttgcat

480

ttttgcagga gcagtatcat gaagcctaaa cgcgatggat atatgttttt gaaggcagaa

540

agcaaaatta tgtttgccac tttgcaaagg agctcactgt ggtgtctgtg ttccaaccac

600

<210> 3850

<211> 602

<212> DNA

<213> Homo sapiens

<400> 3850

cgaaggctgt ctgcagccag gagagcaggg acgtcctgtg cgaactgtca gaccaccaca

60

accacactct ggagggaggaa tgccaatggg gaccctgtct gcaatgcctg tgggctctac

120

tacaagcttc acaatattaa cagacccctg actatgaaga aggaaggcat ccagaccaga

180

aaccgaaaaa tgtctagcaa atccaaaaag tgcaaaaaag tgcatgactc actggaggac

240

ttccccaaga acagctcgtt taacccggcc gccctctcca gacacatgtc ctccctgagc

300

cacatctcgc ccttcagcca ctccagccac atgctgacca cgcccacgcc gatgcacccg

360

ccatccagcc tgtcctttgg accacaccac ccctccagca tggtcaccgc catgggttag

420

agccctgctc gatgctcaca gggcccccag cgagagtccc tgcagtccct ttcgacttgc

480

atttttgcag gagcagtatc atgaagccta aacgcgatgg atatatgttt ttgaaggcag

540

aaagcaaaat tatgtttgcc actttgcaaa ggagctcact gtggtgtctg tgttccaacc

600

ac

602

<210> 3851

<211> 197

<212> PROTEIN

<213> Homo sapiens

<400> 3851

Arg Arg Leu Ser Ala Ala Arg Arg Ala Gly Thr Ser Cys Ala Asn Cys

1 5 10 15

Gln Thr Thr Thr Thr Thr Leu Trp Arg Arg Asn Ala Asn Gly Asp Pro

20 25 30

Val Cys Asn Ala Cys Gly Leu Tyr Tyr Lys Leu His Asn Ile Asn Arg

35 40 45

Pro Leu Thr Met Lys Lys Glu Gly Ile Gln Thr Arg Asn Arg Lys Met

50 55 60

Ser Ser Lys Ser Lys Lys Cys Lys Lys Val His Asp Ser Leu Glu Asp

65 70 75 80

Phe Pro Lys Asn Ser Ser Phe Asn Pro Ala Ala Leu Ser Arg His Met

85 90 95

Ser Ser Leu Ser His Ile Ser Pro Phe Ser His Ser Ser His Met Leu

100 105 110

Thr Thr Pro Thr Pro Met His Pro Pro Ser Ser Leu Ser Phe Gly Pro

115 120 125

His His Pro Ser Ser Met Val Thr Ala Met Gly Ser Pro Ala Arg Cys

130 135 140

Ser Gln Gly Pro Gln Arg Glu Ser Leu Gln Ser Leu Ser Thr Cys Ile

145 150 155 160

Phe Ala Gly Ala Val Ser Ser Leu Asn Ala Met Asp Ile Cys Phe Arg

165 170 175

Gln Lys Ala Lys Leu Cys Leu Pro Leu Cys Lys Gly Ala His Cys Gly

180 185 190

Val Cys Val Pro Thr

195

<210> 3852

<211> 200

<212> PROTEIN

<213> Homo sapiens

<400> 3852

Arg Arg Leu Ser Ala Ala Arg Arg Ala Gly Thr Ser Cys Ala Asn Cys

1 5 10 15

Gln Thr Thr Thr Thr Thr Leu Trp Arg Arg Asn Ala Asn Gly Asp Pro

20 25 30

Val Cys Asn Ala Cys Gly Leu Tyr Tyr Lys Leu His Asn Ile Asn Arg

35 40 45

Pro Leu Thr Met Lys Lys Glu Gly Ile Gln Thr Arg Asn Arg Lys Met

50 55 60

Ser Ser Lys Ser Lys Lys Cys Lys Lys Val His Asp Ser Leu Glu Asp

65 70 75 80

Phe Pro Lys Asn Ser Ser Phe Pro Gly Arg Pro Leu Gln Thr His Val

85 90 95

Leu Pro Glu Pro His Leu Ala Leu Gln Pro Leu Gln Pro His Ala Asp

100 105 110

His Ala His Ala Asp Ala Pro Ala Ile Gln Pro Val Leu Trp Thr Thr

115 120 125

Pro Pro Leu Gln His Gly His Arg His Gly Leu Glu Pro Cys Ser Met

130 135 140

Leu Thr Gly Pro Pro Ala Arg Val Pro Ala Val Pro Phe Asp Leu His

145 150 155 160

Phe Cys Arg Ser Ser Ile Met Lys Pro Lys Arg Asp Gly Tyr Met Phe

165 170 175

Leu Lys Ala Glu Ser Lys Ile Met Phe Ala Thr Leu Gln Arg Ser Ser

180 185 190

Leu Trp Cys Leu Cys Ser Asn His

195 200

<210> 3853

<211> 201

<212> PROTEIN

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polypeptide

<220>

<221> OTHER_CHARACTERISTIC

<222> (104)..(105)

<223> May or may not be present

<220>

<221> OTHER_CHARACTERISTIC

<222> (137)..(137)

<223> May or may not be present

<220>

<221> MOD_RES

<222> (140)..(140)

<223> Met or Leu

<220>

<221> MOD_RES

<222> (167)..(167)

<223> Val or Ile

<220>

<221> MOD_RES

<222> (185)..(185)

<223>Leu or Met

<220>

<221> OTHER_CHARACTERISTIC

<222> (200)..(201)

<223> May or may not be present

<400> 3853

Arg Arg Leu Ser Ala Ala Arg Arg Ala Gly Thr Ser Cys Ala Asn Cys

1 5 10 15

Gln Thr Thr Thr Thr Thr Leu Trp Arg Arg Asn Ala Asn Gly Asp Pro

20 25 30

Val Cys Asn Ala Cys Gly Leu Tyr Tyr Lys Leu His Asn Ile Asn Arg

35 40 45

Pro Leu Thr Met Lys Lys Glu Gly Ile Gln Thr Arg Asn Arg Lys Met

50 55 60

Ser Ser Lys Ser Lys Lys Cys Lys Lys Val His Asp Ser Leu Glu Asp

65 70 75 80

Phe Pro Lys Asn Ser Ser Phe Asn Gly Ala Ala Leu Gln Arg His Met

85 90 95

Leu Pro Glu Pro His Ile Ala Leu Gln Pro Leu Gln His His Ala Asp

100 105 110

His Ala His Ala Asp Ala Pro Ala His Gln Pro Ser Leu Leu Ser Phe

115 120 125

Gly Pro His Gln His Gly His Arg Val His Ala Xaa Glu Pro Cys Ala

130 135 140

Arg Cys Ser Gln Gly Pro Ala Arg Glu Pro Ala Gln Pro Leu Asp Leu

145 150 155 160

Cys Ile Cys Ala Gly Ala Xaa Met Lys Leu Asn Ala Asp Asp Ile Cys

165 170 175

Phe Arg Gln Ala Ala Lys Leu Cys Xaa Phe Ala Cys Leu Gln Ala His

180 185 190

Cys Gly Trp Cys Leu Cys Ser Asn His

195 200

<210> 3854

<211> 624

<212> DNA

<213> Homo sapiens

<400> 3854

gaattcgacg cccatgag aaggctgagc gccgctagaa gagccggcac cagctgcgcc

60

aactgccaga ccaccaccac caccctgtgg agaaggaacg ccaacggcga tcccgtgtgt

120

aacgcctgcg gcctgtacta caagctgcac aacatcaaca ggcccctgac catgaagaag

180

gagggcatcc agaccaggaa caggaagatg tccagcaaga gcaagaagtg caagaaggtg

240

cacgacagcc tggaggactt ccccaagaac agcagcttcc ccggaagacc cctgcagaca

300

cacgtgctgc ccgagcctca tctggccctg cagcctctcc agccccatgc cgatcatgcc

360

cacgccgatg cccctgccat ccaacccgtg ctgtggacca cccctcctct gcagcacgga

420

cacagacacg gcctggagcc ctgtagcatg ctgacaggac ctcccgccag agtgcctgcc

480

gtgcctttcg acctgcactt ctgcagaagc agcatcatga agcccaagag ggacggctat

540

atgttcctga aggccgagtc caagatcatg ttcgccaccc tgcagagaag ctccctgtgg

600

tgcctgtgca gcaaccacgg atcc

624

<210> 3855

<211> 759

<212> DNA

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polynucleotide

<400> 3855

tgacgcaaat gggcggtagg cgtgtacggt gggaggtcta tataagcaga gcttctagag

60

ctagcgaatt cgacgccacc atgagaaggc tgagcgccgc tagaagagcc ggcaccagct

120

gcgccaactg ccagaccacc accaccaccc tgtggagaag gaacgccaac ggcgatcccg

180

tgtgtaacgc ctgcggcctg tactacaagc tgcacaacat caacaggccc ctgaccatga

240

agaagggagg catccagacc aggaacagga agatgtccag caagagcaag aagtgcaaga

300

aggtgcacga cagcctggag gacttcccca agaacagcag cttccccgga agacccctgc

360

agacacacgt gctgcccgag cctcatctgg ccctgcagcc tctccagccc catgccgatc

420

atgcccacgc cgatgcccct gccatccaac ccgtgctgtg gaccacccct cctctgcagc

480

acggacacag acacggcctg gagccctgta gcatgctgac aggacctccc gccagagtgc

540

ctgccgtgcc tttcgacctg cacttctgca gaagcagcat catgaagccc aagagggacg

600

gctatatgtt cctgaaggcc gagtccaaga tcatgttcgc caccctgcag agaagctccc

660

tgtggtgcct gtgcagcaac cacggatccg cggccgctga gggcagagga agtcttctaa

720

catgcggtga cgtggaggag aatcccggcc cttccggga

759

<210> 3856

<211> 624

<212> DNA

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polynucleotide

<400> 3856

gaattcgacg cccatgag aaggctgagc gccgctagaa gagccggcac cagctgcgcc

60

aactgccaga ccaccaccac caccctgtgg agaaggaacg ccaacggcga tcccgtgtgt

120

aacgcctgcg gcctgtacta caagctgcac aacatcaaca ggcccctgac catgaagaag

180

gagggcatcc agaccaggaa caggaagatg tccagcaaga gcaagaagtg caagaaggtg

240

cacgacagcc tggaggactt ccccaagaac agcagcttcc ccggaagacc cctgcagaca

300

cacgtgctgc ccgagcctca tctggccctg cagcctctcc agccccatgc cgatcatgcc

360

cacgccgatg cccctgccat ccaacccgtg ctgtggacca cccctcctct gcagcacgga

420

cacagacacg gcctggagcc ctgtagcatg ctgacaggac ctcccgccag agtgcctgcc

480

gtgcctttcg acctgcactt ctgcagaagc agcatcatga agcccaagag ggacggctat

540

atgttcctga aggccgagtc caagatcatg ttcgccaccc tgcagagaag ctccctgtgg

600

tgcctgtgca gcaaccacgg atcc

624

<210> 3857

<211> 113

<212> PROTEIN

<213> Homo sapiens

<400> 3857

Pro Gly Arg Pro Leu Gln Thr His Val Leu Pro Glu Pro His Leu Ala

1 5 10 15

Leu Gln Pro Leu Gln Pro His Ala Asp His Ala His Ala Asp Ala Pro

20 25 30

Ala Ile Gln Pro Val Leu Trp Thr Thr Pro Pro Leu Gln His Gly His

35 40 45

Arg His Gly Leu Glu Pro Cys Ser Met Leu Thr Gly Pro Pro Ala Arg

50 55 60

Val Pro Ala Val Pro Phe Asp Leu His Phe Cys Arg Ser Ser Ile Met

65 70 75 80

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu Lys Ala Glu Ser Lys Ile

85 90 95

Met Phe Ala Thr Leu Gln Arg Ser Ser Leu Trp Cys Leu Cys Ser Asn

100 105 110

His

<210> 3858

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3858

Ser Met Leu Thr Gly Pro Pro Ala Arg Val

1 5 10

<210> 3859

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3859

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3860

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3860

Lys Pro Lys Arg Asp Gly Tyr Met Phe

15

<210> 3861

<211> 10

<212> PROTEIN

<213> Homo sapiens

<400> 3861

Lys Pro Lys Arg Asp Gly Tyr Met Phe Leu

1 5 10

<210> 3862

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3862

Glu Ser Lys Ile Met Phe Ala Thr Leu

15

<210> 3863

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3863

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3864

<211> 9

<212> PROTEIN

<213> Homo sapiens

<400> 3864

Met Leu Thr Gly Pro Pro Ala Arg Val

15

<210> 3865

<211> 840

<212> DNA

<213> Homo sapiens

<400> 3865

acagatccaa gctgtgaccg gcgcctactc tagagctagc gaattcgacg ccaccatggg

60

cattcgtctg ctgtgtcgtg tggccttctg ctttttagcc gtgggtttag tggacgtgaa

120

ggtgacccag tcctctcgtt atttagtgaa gaggaccggc gagaaggtgt ttttagaatg

180

cgtgcaagat atggaccacg agaacatgtt ctggtacaga caagatcccg gactgggttt

240

aaggctgatc tacttcagct acgacgtgaa gatgaaggag aagggcgaca tccccgaggg

300

ctactccgtg tctcgtgaga agaaggagag gttctcttta attttagagt ccgccagcac

360

caaccagacc agcatgtatt tatgcgccag ctctttagac tttgtgctgg ccggcagcta

420

cagctacaac gagcagttct tcggccccgg caccagactg accgtgctgg aggacctgaa

480

caaggtcttt cctcccgaag tggccgtgtt tgagcccagc gaggccgaga tcagccatac

540

ccagaaggcc acactcgtgt gcctggccac cggcttcttt cccgaccatg tggagctgag

600

ctggtgggtg aacggcaagg aggtccactc cggagtcagc accgatcccc agcctctcaa

660

agagcagccc gctctcaacg actccaggta ttgcctgtcc agcaggctga gagtcagcgc

720

caccttttgg cagaatccca ggaaccactt caggtgccag gtccagttct atggcctgag

780

cgagaacgac gagtgacaca ggatagagct aagcccgtga cccagattgt cagcgccgag

840

<210> 3866

<211> 1035

<212> DNA

<213> Homo sapiens

<400> 3866

atgggcattc gtctgctgtg tcgtgtggcc ttctgctttt tagccgtggg tttagtggac

60

gtgaaggtga cccagtcctc tcgttattta gtgaagagga ccggcgagaa ggtgttttta

120

gaatgcgtgc aagatatgga ccacgagaac atgttctggt acagacaaga tcccggactg

180

ggtttaaggc tgatctactt cagctacgac gtgaagatga aggagaaggg cgacatcccc

240

gagggctact ccgtgtctcg tgagaagaag gagaggttct ctttaatttt agagtccgcc

300

agcaccaacc agaccagcat gtatttatgc gccagctctt tagactttgt gctggccggc

360

agctacagct acaacgagca gttcttcggc cccggcacca gactgaccgt gctggaggac

420

ctgaacaagg tctttcctcc cgaagtggcc gtgtttgagc ccagcgaggc cgagatcagc

480

catacccaga aggccacact cgtgtgcctg gccaccggct tctttcccga ccatgtggag

540

ctgagctggt gggtgaacgg caaggaggtc cactccggag tcagcaccga tccccagcct

600

ctcaaagagc agcccgctct caacgactcc aggtattgcc tgtccagcag gctgagagtc

660

agcgccacct tttggcagaa tccaggaac cacttcaggt gccaggtcca gttctatggc

720

ctgagcgaga acgacgagtg gacacaggat agagctaagc ccgtgaccca gattgtcagc

780

gccgaggcct ggggcagagc cgactgtgga ttcacaagcg tgtcctatca gcaaggcgtg

840

ctcagcgcca ccattctgta cgagatcctg ctgggcaaag ccaccctgta cgctgtgctg

900

gtgtccgctc tggtgctgat ggctatggtc aagaggaagg actttcggat caggcgcagc

960

ggaagcggag tgaagcaaac cctcaacttc gacctgctca agctggccgg agatgtggaa

1020

agcaatcccg gaccc

1035

<210> 3867

<211> 267

<212> DNA

<213> Homo sapiens

<400> 3867

cagattgtca gcgccgaggc ctggggcaga gccgactgtg gattcacaag cgtgtcctat

60

cagcaaggcg tgctcagcgc caccattctg tacgagatcc tgctgggcaa agccaccctg

120

tacgctgtgc tggtgtccgc tctggtgctg atggctatgg tcaagaggaa ggactttcgg

180

atcaggcgca gcggaagcgg agtgaagcaa accctcaact tcgacctgct caagctggcc

240

ggagatgtgg aaagcaatcc cggaccc

267

<210> 3868

<211> 1034

<212> DNA

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polynucleotide

<400> 3868

atgggcattc gtctgctgtg tcgtgtggcc ttctgctttt tagccgtggg tttagtggac

60

gtgaaggtga cccagtcctc tcgttattta gtgaagagga ccggcgagaa ggtgttttta

120

gaatgcgtgc aagatatgga ccacgagaac atgttctggt acagacaaga tcccggactg

180

ggtttaaggc tgatctactt cagctacgac gtgaagatga aggagaaggg cgacatcccc

240

gagggctact ccgtgtctcg tgagaagaag gagaggttct ctttaatttt agagtccgcc

300

agcaccaacc agaccagcat gtatttatgc gccagctctt tagactttgt gctggccggc

360

agctacagct acaacgagca gttcttcggc cccggcacca gactgaccgt gctggaggac

420

ctgaacaagg tctttcctcc cgaagtggcc gtgtttgagc ccagcgaggc cgagatcagc

480

catacccaga aggccacact cgtgtgcctg gccaccggct tctttcccga ccatgtggag

540

ctgagctggt gggtgaacgg caaggaggtc cactccggag tcagcaccga tccccagcct

600

ctcaaagagc agcccgctct caacgactcc aggtattgcc tgtccagcag gctgagagtc

660

agcgccacct tttggcagaa tccaggaac cacttcaggt gccaggtcca gttctatggc

720

ctgagcgaga acgacgagtg acacaggata gagctaagcc cgtgacccag attgtcagcg

780

ccgaggcctg gggcagagcc gactgtggat tcacaagcgt gtcctatcag caaggcgtgc

840

tcagcgccac cattctgtac gagatcctgc tgggcaaagc caccctgtac gctgtgctgg

900

tgtccgctct ggtgctgatg gctatggtca agaggaagga ctttcggatc aggcgcagcg

960

gaagcggagt gaagcaaacc ctcaacttcg acctgctcaa gctggccgga gatgtggaaa

1020

gcaatcccgg accc

1034

<210> 3869

<211> 878

<212> DNA

<213> Homo sapiens

<400> 3869

tttaggcggc gtgctgctga ttttatggct gcaagttgac tgggtgaaga gccagaagat

60

cgagcagaac agcgaggctt taaacattca agaaggcaag acagccactt taacttgtaa

120

ctataccaac tactcccccg cttatttaca gtggtacaga caagatcccg gcagaggccc

180

cgtgttttta ctgctgattc gtgagaacga gaaggagaag aggaaggaga gactgaaggt

240

gaccttcgac accactttaa agcagtcttt attccacatc accgccagcc agcccgctga

300

tagcgccacc tatttatgcg ctttagacat ctacggcaac aatcgtctgg ccttcggcaa

360

gggcaaccaa gttgtggtga tccccgatat tcagaatccc gatcccgctg tgtaccagct

420

gagggattcc aagtcctccg ataagtccgt ctgtctgttc accgacttcg atagccagac

480

caacgtgagc caaagcaagg actccgacgt gtatatcaca gacaagaccg tgctggacat

540

gaggagcatg gacttcaaga gcaatagcgc cgtggcctgg tccaataaga gcgatttcgc

600

ctgcgccaac gccttcaaca atagcatcat tcccgaggac accttcttcc ccagccccga

660

aagcagctgc gatgtgaaac tggtggagaa gtcctttgag accgacacca acctcaactt

720

ccagaacctc tccgtgatcg gattcaggat tctgctgctg aaggtggctg gctttaacct

780

gctgatgacc ctcaggctgt ggtccagcta aggatccgtc gacaatcaac ctctggatta

840

caaaatttgt gaaagattga ctggtattct taactatg

878

<210> 3870

<211> 876

<212> DNA

<213> Homo sapiens

<400> 3870

atggccttct ggctgaggag actgggttta cacttcagac cccatttagg cagaagaatg

60

gagagctttt taggcggcgt gctgctgatt ttatggctgc aagttgactg ggtgaagagc

120

cagaagatcg agcagaacag cgaggcttta aacattcaag aaggcaagac agccacttta

180

acttgtaact ataccaacta ctcccccgct tatttacagt ggtacagaca agatcccggc

240

agaggccccg tgtttttact gctgattcgt gagaacgaga aggagaagag gaaggagaga

300

ctgaaggtga ccttcgacac cactttaaag cagtctttat tccacatcac cgccagccag

360

cccgctgata gcgccaccta tttatgcgct ttagacatct acggcaacaa tcgtctggcc

420

ttcggcaagg gcaaccaagt tgtggtgatc cccgatattc agaatcccga tcccgctgtg

480

taccagctga gggattccaa gtcctccgat aagtccgtct gtctgttcac cgacttcgat

540

agccagacca acgtgagcca aagcaaggac tccgacgtgt atatcacaga caagaccgtg

600

ctggacatga ggagcatgga cttcaagagc aatagcgccg tggcctggtc caataagagc

660

gatttcgcct gcgccaacgc cttcaacaat agcatcattc ccgaggacac cttcttcccc

720

agccccgaaa gcagctgcga tgtgaaactg gtggagaagt cctttgagac cgacaccaac

780

ctcaacttcc agaacctctc cgtgatcgga ttcaggattc tgctgctgaa ggtggctggc

840

tttaacctgc tgatgaccct caggctgtgg tccagc

876

<210> 3871

<211> 613

<212> DNA

<213> Homo sapiens

<400> 3871

tgtggaaagc aatcccggac ccatggcctt ctggctgagg agactgggtt tacacttcag

60

accccattta ggcagaagaa tggagagctt tttaggcggc gtgctgctga ttttatggct

120

gcaagttgac tgggtgaaga gccagaagat cgagcagaac agcgaggctt taaacattca

180

agaaggcaag acagccactt taacttgtaa ctataccaac tactcccccg cttatttaca

240

gtggtacaga caagatcccg gcagaggccc cgtgttttta ctgctgattc gtgagaacga

300

gaaggagaag aggaaggaga gactgaaggt gaccttcgac accactttaa agcagtcttt

360

attccacatc accgccagcc agcccgctga tagcgccacc tatttatgcg ctttagacat

420

ctacggcaac aatcgtctgg ccttcggcaa gggcaaccaa gttgtggtga tccccgatat

480

tcagaatccc gatcccgctg tgtaccagct gagggattcc aagtcctccg ataagtccgt

540

ctgtctgttc accgacttcg atagccagac caacgtgagc caaagcaagg actccgacgt

600

gtatatcaca gac

613

<210> 3872

<211> 876

<212> DNA

<213> Artificial sequence

<220>

<223> Description of artificial sequence: Synthetic

polynucleotide

<400> 3872

atggccttct ggctgaggag actgggttta cacttcagac cccatttagg cagaagaatg

60

gagagctttt taggcggcgt gctgctgatt ttatggctgc aagttgactg ggtgaagagc

120

cagaagatcg agcagaacag cgaggcttta aacattcaag aaggcaagac agccacttta

180

acttgtaact ataccaacta ctcccccgct tatttacagt ggtacagaca agatcccggc

240

agaggccccg tgtttttact gctgattcgt gagaacgaga aggagaagag gaaggagaga

300

ctgaaggtga ccttcgacac cactttaaag cagtctttat tccacatcac cgccagccag

360

cccgctgata gcgccaccta tttatgcgct ttagacatct acggcaacaa tcgtctggcc

420

ttcggcaagg gcaaccaagt tgtggtgatc cccgatattc agaatcccga tcccgctgtg

480

taccagctga gggattccaa gtcctccgat aagtccgtct gtctgttcac cgacttcgat

540

agccagacca acgtgagcca aagcaaggac tccgacgtgt atatcacaga caagaccgtg

600

ctggacatga ggagcatgga cttcaagagc aatagcgccg tggcctggtc caataagagc

660

gatttcgcct gcgccaacgc cttcaacaat agcatcattc ccgaggacac cttcttcccc

720

agccccgaaa gcagctgcga tgtgaaactg gtggagaagt cctttgagac cgacaccaac

780

ctcaacttcc agaacctctc cgtgatcgga ttcaggattc tgctgctgaa ggtggctggc

840

tttaacctgc tgatgaccct caggctgtgg tccagc

876

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Claims (22)

1. A method of obtaining a population of immunoreactive T cells containing a T cell receptor (TCR) specific for the peptide:MHC complex, where the peptide of the peptide:MHC complex is a mutant GATA3 peptide sequence containing at least 8 contiguous amino acids from PGRPLQTHVLPEPHLALQPLQPHADHAHADAPAIQPVLWTTPPLQHGHRHGLEPCSMLTGPPARVPAVPFDLHFCRSSIMKPKRD GYMFLKAESKIMFAT LQRSSLWCLCSNH ( SEQ ID NO: 2), comprising: contacting a population of immune cells with (i) a polynucleotide containing a sequence encoding a polypeptide containing said mutant GATA3 peptide sequence, or (ii) a polypeptide containing said mutant GATA3 peptide sequence; wherein the immune cell population is a population of immune cells lacking cells expressing CD14 and CD25, and wherein the immune cell population includes a population of FMS-like receptor tyrosine kinase ligand 3 (FLT3L) stimulated antigen presenting cells (APCs) and a population of T cells, and thereby obtaining a population of T cells containing a TCR specific for the peptide:MHC complex. 2. The method according to claim 1, where the method includes, before contacting, removing cells expressing CD14 and CD25 from the population of immune cells. 3. The method according to claim 1 or 2, including stimulating APC in a population of immune cells using FLT3L. 4. Method according to any one of paragraphs. 1-3, wherein the polynucleotide comprising a sequence encoding a polypeptide containing said GATA3 mutant peptide sequence is RNA, optionally wherein the RNA is mRNA. 5. Method according to any one of paragraphs. 1-4, wherein the polypeptide containing said GATA3 mutant peptide sequence contains at least one of the following sequences: TLQRSSLWCL (SEQ ID NO: 3753), VLPEPHLAL (SEQ ID NO: 3754), HVLPEPHLAL (SEQ ID NO: 3755), ALQPLQPHA (SEQ ID NO: 3756), AIQPVLWTT (SEQ ID NO: 3757), APAIQPVLWTT (SEQ ID NO : 3758), SMLTGPPARV (SEQ ID NO: 3759), MLTGPPARV (SEQ ID NO: 3760) and/or YMFLKAESKI (SEQ ID NO: 3761); and/or MFLKAESKI (SEQ ID NO: 3762) and/or YMFLKAESKI (SEQ ID NO: 3763) VLWTTPPLQH (SEQ ID NO: 3764), YMFLKAESK (SEQ ID NO: 3765) and/or KIMFATLQR (SEQ ID NO: 3766); and/or FATLQRSSL (SEQ ID NO: 3767), EPHLALQPL (SEQ ID NO: 3768), QPVLWTTPPL (SEQ ID NO: 3769), GPPARVPAV (SEQ ID NO: 3770), MFATLQRSSL (SEQ ID NO: 3771), KPKRDGYMF (SEQ ID NO : 3772) and/or KPKRDGYMFL (SEQ ID NO: 3773) and/or IMKPKRDGYM (SEQ ID NO: 3774), MFATLQRSSL (SEQ ID NO: 3775), FLKAESKIMF (SEQ ID NO: 3776), LHFCRSSIM (SEQ ID NO: 3777), EPHLALQPL (SEQ ID NO: 3778), FATLQRSSL (SEQ ID NO : 3779), ESKIMFATL (SEQ ID NO: 3780), FLKAESKIM (SEQ ID NO: 3781) and/or YMFLKAESKI (SEQ ID NO: 3782). 6. Method according to any one of paragraphs. 1-4, wherein the polypeptide containing said GATA3 mutant peptide sequence contains at least two of the following sequences: TLQRSSLWCL (SEQ ID NO: 3783), VLPEPHLAL (SEQ ID NO: 3784), HVLPEPHLAL (SEQ ID NO: 3785), ALQPLQPHA (SEQ ID NO: 3786), AIQPVLWTT (SEQ ID NO: 3787), APAIQPVLWTT (SEQ ID NO : 3788), SMLTGPPARV (SEQ ID NO: 3789), MLTGPPARV (SEQ ID NO: 3790) and/or YMFLKAESKI (SEQ ID NO: 3791); and/or MFLKAESKI (SEQ ID NO: 3792) and/or YMFLKAESKI (SEQ ID NO: 3793); and/or VLWTTPPLQH (SEQ ID NO: 3794), YMFLKAESK (SEQ ID NO: 3795) and/or KIMFATLQR (SEQ ID NO: 3796); and/or FATLQRSSL (SEQ ID NO: 3797), EPHLALQPL (SEQ ID NO: 3798), QPVLWTTPPL (SEQ ID NO: 3799), GPPARVPAV (SEQ ID NO: 3800), MFATLQRSSL (SEQ ID NO: 3801), KPKRDGYMF (SEQ ID NO : 3802) and/or KPKRDGYMFL (SEQ ID NO: 3803) and/or IMKPKRDGYM (SEQ ID NO: 3804), MFATLQRSSL (SEQ ID NO: 3805), FLKAESKIMF (SEQ ID NO: 3806), LHFCRSSIM (SEQ ID NO: 3807), EPHLALQPL (SEQ ID NO: 3808), FATLQRSSL (SEQ ID NO : 3809), ESKIMFATL (SEQ ID NO: 3810), FLKAESKIM (SEQ ID NO: 3811) and/or YMFLKAESKI (SEQ ID NO: 3812). 7. Method according to any one of paragraphs. 1-4, wherein the polypeptide containing said GATA3 mutant peptide sequence contains a sequence selected from the group consisting of ESKIMFATLQRSSL (SEQ ID NO: 3813), KPKRDGYMFLKAESKI (SEQ ID NO: 3814), SMLTGPPARVPAVPFDLH (SEQ ID NO: 3815) , EPCSMLTGPPARVPAVPFDLH (SEQ ID NO: 3816), LHFCRSSIMKPKRDGYMFLKAESKI (SEQ ID NO: 3817), GPPARVPAVPFDLHFCRSSIMKPKRD (SEQ ID NO: 3818) and KPKRDGYMFLKAESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 819). 8. Method according to any one of paragraphs. 1-7, wherein the polypeptide containing said GATA3 mutant peptide sequence comprises PGRPLQTHVLPEPHLALQPLQPHADHAHADAPAIQPVLWTTPPLQHGHRHGL (SEQ ID NO: 3) or EPCSMLTGPPARVPAVPFDLHFCRSSIMKPKRDGYMFLKAESKIMFATLQRSSLWCLCSNH (SEQ ID NO: 4). 9. Method according to any one of paragraphs. 1-8, wherein the polypeptide containing the specified GATA3 mutant peptide sequence contains SEQ ID NO: 2.

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