KR20220149401A - Collagen compositions and methods of use thereof - Google Patents

Abstract

The present invention relates to recombinant collagen and a peptide fragment thereof. In addition, the present invention provides a novel Pichia pastoris strain for producing the recombinant collagen and the fragment thereof, and a method of using the recombinant collagen and the fragment thereof. The recombinant collagen fragment of the present invention has a molecular weight of about 50 kDa.

Description

Collagen composition and method of use thereof

Sequences submitted electronically reference to the list

The contents of the Sequence Listing (Name: 4431_0820002_Seqlisting_ST25.txt; Size: 441,401 bytes; and Created: November 12, 2021) submitted electronically as ASCII text files filed with this application are incorporated herein by reference in their entirety. .

Collagen is one of the most important proteins in the human body and is present in connective tissues such as cartilage, bones, tendons, ligaments and skin, and is a major protein in the extracellular matrix of human cells. “Recombinant collagen” refers to a family of at least 28 distinct naturally occurring collagen types made using recombinant technology.

There are many known uses for collagen. In the cosmetic and skin care industries, for example, skin care compositions comprising collagen can be used to counteract the effects of aging and environmental stress on the appearance, elasticity and thickness of the skin. For example, aging and environmental factors include fine lines, wrinkles, dry skin, excessive pore size, skin abnormalities, loss of elasticity, unwanted hair, thinning of the skin, purpura, actinic keratosis, pruritus, eczema, acne, rosacea, erythema, capillaries. It can lead to dermatological conditions including, but not limited to, vasodilation, actinic telangiectasia, skin cancer, and rhinitis. Although there are numerous skin care products on the market to improve the appearance of the skin, many consumers are hesitant to use chemically synthetic products that they perceive as not being environmentally friendly or otherwise unsafe.

In some embodiments, the present invention provides a recombinant collagen fragment having a molecular weight of about 50 kDa and at least about 85% sequence homology to the amino acid sequence set forth in SEQ ID NO: 1 or SEQ ID NO: 986. In some embodiments, the recombinant collagen fragment may not be hydroxylated. In some embodiments, the recombinant collagen fragment may be hydroxylated. In some embodiments, the collagen fragment may have the amino acid sequence set forth in SEQ ID NO: 1 or SEQ ID NO: 986. In some embodiments, the present invention provides a recombinant collagen fragment comprising the amino acid sequence according to any one of SEQ ID NOs: 2-972.

In some embodiments, the present invention provides a composition comprising the recombinant collagen fragments described herein. In some embodiments, the composition further comprises one or more peptides formed from hydrolysis of a collagen fragment having the amino acid sequence set forth in SEQ ID NO: 1 or from hydrolysis of a collagen fragment having the amino acid sequence set forth in SEQ ID NO: 986.

In some embodiments of the present invention, at least one of the one or more peptides formed from hydrolysis of a collagen fragment having the amino acid sequence set forth in SEQ ID NO: 1 has the amino acid sequence according to one of SEQ ID NOs: 2-972. In some embodiments of the invention, at least one of the one or more peptides formed from hydrolysis of a collagen fragment having the amino acid sequence set forth in SEQ ID NO: 986 has an amino acid sequence according to one of SEQ ID NOs: 2-972. In some embodiments, the composition further comprises a pharmaceutically acceptable or cosmetically acceptable excipient.

In some embodiments, the present invention provides a method of making a recombinant collagen fragment comprising the step of producing the recombinant collagen fragment in a strain of genetically engineered yeast. In some embodiments, the yeast may be Pichia pastoris . In some embodiments, yeast can be transformed with a plasmid comprising the nucleic acid sequence set forth in SEQ ID NO:973. In some embodiments, the yeast may be a yeast further transformed with a plasmid comprising the nucleic acid sequence set forth in SEQ ID NO:974. In some embodiments, the method comprises the steps of (i) fermenting genetically engineered yeast in a fermentation broth; (ii) recovering the recombinant collagen fragment secreted by the genetically engineered yeast from the fermentation broth; and (iii) optionally, purifying the recombinant collagen fragment. In some embodiments, the method further comprises hydroxylating the recombinant collagen fragment ex vivo .

In some embodiments, the present invention provides a strain of yeast that has been genetically engineered to produce the recombinant collagen fragments described herein, wherein the strain of yeast comprises a vector comprising a DNA sequence encoding the recombinant collagen. In some embodiments, the vector comprises a nucleic acid sequence comprising the DNA sequence set forth in SEQ ID NO:973. In some embodiments, the strain of yeast described herein further comprises a second vector comprising a nucleic acid sequence comprising the DNA sequence set forth in SEQ ID NO:974. In some embodiments, the strain of yeast may be Pichia pastoris .

)를 포함), 팔, 손, 다리, 배, 엉덩이, 사타구니, 등, 발 및 이들의 조합으로 이루어진 군으로부터 선택될 수 있다.In some embodiments, the present invention provides a method of treating a dermatological condition comprising administering to a subject in need thereof an effective amount of a recombinant collagen fragment described herein. In some embodiments, the present invention provides a method of treating a dermatological condition comprising administering to a subject in need thereof an effective amount of a composition disclosed herein. In some embodiments, the dermatological condition is fine lines, wrinkles, dry skin, excessive pore size, skin abnormalities, loss of elasticity, unwanted hair, thinning skin, purpura, actinic keratosis, pruritus, eczema, acne, rosacea, erythema, capillary vasodilation, actinic telangiectasia, skin cancer, or rhinitis. In some embodiments, the composition may be administered topically to a skin region. In some embodiments, the skin region is the facial surface, scalp, neck, ears, shoulders, chest (breast and/or decolletage (

), arms, hands, legs, stomach, buttocks, groin, back, feet, and combinations thereof.

In some embodiments, the present invention provides a method of increasing collagen production in a cell comprising administering to the cell an effective amount of a recombinant collagen fragment described herein. In some embodiments, the method can increase the production of type I collagen. In some embodiments, the method can increase the production of type III collagen. In some embodiments, the cell may be a fibroblast. In some embodiments, the cells may be cultured cells.

In some embodiments of the methods disclosed herein, the fragment may be formulated into a composition. In some embodiments, the fragment may have an amino acid sequence according to SEQ ID NO: 1 or SEQ ID NO: 986.

In some embodiments, the present invention is used for reducing the appearance of wrinkles, evening the skin tone, providing moisture, reducing the appearance of dark circles under the eyes, increasing the collagen content of the skin, For increasing skin density, improving skin firmness and elasticity, improving the appearance of lines and wrinkles, smoothing skin texture, increasing skin radiance and radiance, improving the appearance of sagging skin Provided is a skin care product comprising a composition described herein for use in lightening skin, lightening skin, or any combination thereof.

In some embodiments, the present invention provides a method of treating a wound in a human subject in need thereof comprising applying a composition comprising a recombinant collagen fragment disclosed herein to the wound of the subject, wherein the recombinant Applying the collagen fragment induces the production of human type I collagen, human type III collagen, or a combination thereof. In certain embodiments of these methods, the collagen fragments are topically applied to the wound.

1 shows a vector diagram of Vector A, a plasmid encoding a 50 kDa fragment of human collagen III with zeocin resistance.
2 shows a vector diagram of Vector B, a plasmid encoding a 50 kDa fragment of human collagen III, N-acetyl transferase, and beta-lactamase.
3A depicts a biomass density curve of a yeast culture expressing a 50 kDa fragment of human collagen, as detected by optical densitometry at 600 nm. The X axis is fermentation time (hours). Y axis is biomass density.
3B depicts a biomass density curve of a yeast culture expressing a 50 kDa fragment of human collagen, as detected by wet cell gravimetry. The X axis is fermentation time (hours). Y axis is wet cell weight.
Figure 3c shows the glycerol concentration of a yeast culture expressing a 50 kDa fragment of human collagen compared to the fermentation time of the culture. The X axis is fermentation time (hours). Y axis is glycerol concentration.
3D shows the rate of carbon dioxide evolution (CER) of yeast cultures expressing a 50 kDa fragment of human collagen, compared to fermentation time of the cultures. The X axis is fermentation time (hours). Y axis is CER.
4 shows the abundance of peptides of various sizes resulting from hydrolysis of a 50 kDa fragment of human collagen, as detected by mass spectrophotometric analysis. Analysis showed that various peptides appeared after 1 week of incubation at room temperature, and the peptides present were equivalent after 1 week and 3 weeks of incubation.
5 depicts a flow diagram of a process for purifying a 50 kDa fragment of unhydroxylated human collagen.
6 depicts a flow diagram of a process for purifying a 50 kDa fragment of hydroxylated human collagen.
Figure 7 shows the percentage recovery of 50 kDa fragments of human collagen during the individual steps of its purification process and during all steps as a whole up to these individual steps.
8 shows the percent hydroxylation of a 50 kDa fragment of human collagen achieved over time during an ex vivo hydroxylation reaction.
9A and 9B show thermograms of 50 kDa collagen before and after hydroxylation, respectively. Hydroxylated 50 kDa collagen forms rheology and has improved thermal stability after hydroxylation.
10 shows a circular dichroism spectrum of hydroxylated 50 kDa collagen showing the expected signature profile for helical collagen.
11A and 11B show the results of an MTT assay to determine the effect of different collagen preparations, at various concentrations, on the viability of fibroblasts. Collagen was not observed to affect cell viability.
12A and 12B show the results of a type I collagen assay to detect the effect of different collagen and collagen fragment preparations on type I collagen synthesis in treated primary human dermal fibroblasts.
13A and 13B show the results of a type III collagen assay to detect the effect of different collagen and collagen fragment preparations on type III collagen synthesis in treated primary human dermal fibroblasts.
14 shows the measured solubility and properties of collagen and collagen fragment solutions.
15A and 15B show the results of EpiOcular tests performed on human recombinant collagen III and a 50 kDa fragment of human collagen.
16A provides statistical results for each attribute objectively rated for Formulations 1 and 2.
16B and 16C provide self-assessment questions and results for Formulations 1 and 2.
16D shows the statistical results of the level of collagen in the skin before and 6 weeks after application of formulations 1 or 2.

Justice

The indefinite articles ("a" and "an") to describe an element or component mean that one or at least one of those element or component is present. Although these articles are commonly used to mean that the modified noun is a singular noun, as used herein, unless the specific case indicates otherwise, the articles "a" and "an" also include the plural. . Similarly, the definite article (“the”) as used herein also means that the modified noun may be singular or plural, unless otherwise stated in a specific case.

As used herein, the term “about” used in conjunction with a numerical value means “within 10% of the stated value” unless explicitly stated otherwise. For example, “about 5% by weight” means 4.5% to 5.5% by weight.

The term "modified" as applied to a collagen fragment disclosed herein refers to a collagen fragment comprising an amino acid sequence that is at least 70%, 80%, 90%, 95% or 99% identical or similar to the amino acid sequence of a biologically active molecule. . In some embodiments, the modified collagen fragment has an amino acid sequence of at least 75%, 80%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92 of a native or previously engineered sequence. %, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical amino acid sequences. Modified sequences may include additions, deletions, substitutions or combinations thereof to the amino acid sequence of a native or previously engineered molecule. For example, the modified collagen fragment may incorporate or delete 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 or more amino acid residues compared to the native collagen sequence. Such selection can be made to alter the looseness or compactness of the recombinant collagen. The degree of hydroxylation of collagen is related to the looseness or tightness of the collagen triple helix. Modified collagen fragments may also contain chemical modifications to the polypeptide, such as crosslinking between cysteine residues, or hydroxylated or glycosylated residues.

The terms “pharmaceutically acceptable” and “cosmetically acceptable” as applied to carriers, excipients or stabilizers that may be used in the compositions described herein refer to carriers, excipients that are not toxic to recipients at the dosages and concentrations employed. or a stabilizer.

A. Collagen

The term “collagen” refers to any one of the known collagen types, including collagen types I to XX described below, as well as any other collagen, whether natural, synthetic, semi-synthetic or recombinant. The term collagen includes collagen, collagen fragments, collagen-like proteins, triple helical collagen, alpha chains, monomers, gelatin, trimers and combinations thereof. This includes all of the collagens, modified collagens and collagen-like proteins described herein. The term also includes collagen-like proteins or collagenous proteins comprising procollagen and the motif (Gly-X-Y)n, where n is an integer. It includes molecules of collagen and collagen-like proteins, trimers of collagen molecules, fibrils of collagen and fibers of collagen fibrils. It also refers to chemically, enzymatically or recombinantly-modified collagen or collagen-like molecules that can be fibrillated, as well as of collagen, collagen-like molecules and collagenous molecules that can assemble into nanofibers. refers to fragments. Recombinant collagen molecules, whether natural or engineered, will generally contain a repeated -(Gly-X-Y)n- sequence.

As used herein, collagen is a generic term for a family of at least 28 distinct collagen types. A variety of distinct collagen types have been identified in various species including bovine, sheep, porcine, chicken, marine, plant and human collagens. Animal skin is typically type I collagen, but other types of collagen can be used to form hides, including type III collagen. The term “collagen” includes post-translationally modified and proteolyzed collagen having a triple helical structure as well as untreated (eg, procollagen). Type I collagen is the major fibrillar collagen of bone and skin comprising approximately 80-90% of the total collagen of an organism. Type I collagen is the major structural macromolecule present in the extracellular matrix of multicellular organisms and comprises approximately 20% of the total protein mass. Type I collagen is a heterotrimeric molecule comprising two α1(I) chains and one α2(I) chain encoded by the COL1A1 and COL1A2 genes, respectively. In vivo assembly of type I collagen fibrils, fibers, and fiber bundles occurs during development and provides mechanical support to tissues while allowing cell motility and nutrient transport. Other collagen types are less abundant than type I collagen and exhibit different distribution patterns. Type III collagen is the major fibrillar collagen found in skin and vascular tissues. Type III collagen is a homotrimeric collagen comprising three identical α1(III) chains encoded by the COL3A1 gene.

B. Recombinant Collagen and Recombinant Collagen Fragments

As used herein, the term “recombinant collagen” refers to a family of at least 28 distinct naturally occurring collagen types, including but not limited to collagen types I-XX, made using recombinant techniques.

In some embodiments, the recombinant collagen described herein is a recombinant collagen fragment. The recombinant collagen fragment may be a fragment of the full-length amino acid sequence of a native collagen molecule capable of forming tropocollagen (trimeric collagen), or the fragment may be a native collagen amino acid sequence (or fibrillar forming region thereof or [Gly-X-Y]n a fragment of a modified collagen molecule or a truncated collagen molecule having an amino acid sequence that is at least 70, 80, 90, 95, 96, 97, 98 or 99% identical or similar to a segment substantially comprising

Exemplary collagen sequences from which fragments can be derived include the amino acid sequences of Col1A1, col1A2, and Col3A1, such as accession number P02461.4 (SEQ ID NO: 982; human Col3A1) (www.ncbi.nlm.nih.gov/protein/124056490) ), NP_001029211.1 (SEQ ID NO: 978; bovine Col1A1) (www.ncbi.nlm.nih.gov/protein/77404252), NP_776945.1 (SEQ ID NO: 979; bovine Col1A2) (www.ncbi.nlm.nih.gov) /protein/27806257) and NP_001070299.1 (SEQ ID NO: 980; bovine Col3A1) (www.ncbi.nlm.nih.gov/protein/116003881), which are incorporated herein by reference.

Genes encoding collagen may be truncated or otherwise modified to add or remove sequences, for example, to encode collagen fragments disclosed herein. In addition, genetic modifications can be made to customize the size of the polynucleotide or vector, to target the expressed protein to the endoplasmic reticulum or other cellular or extracellular compartment, or to control the length of the encoded protein. Modifications can be made to the polynucleotide encoding the collagen fragment. For example, a polynucleotide coding sequence for a collagen or collagen fragment can be modified to encode a protein that is at least 70, 80, 90, 95, 96, 97, 98 or 100% identical or similar to a known amino acid sequence. Such modifications may include codon-modifying or codon-optimizing the polynucleotide encoding the collagen fragment.

In some embodiments, the collagen fragments disclosed herein may have a molecular weight between about 40 kDa and about 60 kDa. In some embodiments, the collagen fragment is about 40 kDa, about 41 kDa, about 42 kDa, about 43 kDa, about 44 kDa, about 45 kDa, about 46 kDa, about 47 kDa, about 48 kDa, about 49 kDa, about 50 kDa, about 51 kDa, about 52 kDa, about 53 kDa, about 54 kDa, about 55 kDa, about 56 kDa, about 57 kDa, about 58 kDa, about 59 kDa, or about 60 kDa. In certain embodiments, the collagen fragment may have a molecular weight of about 50 kDa.

In some embodiments, the collagen fragments described herein may have an amino acid chain length of from about 350 amino acids to about 600 amino acids and may overlap the amino acid sequence of SEQ ID NO: 1 or SEQ ID NO: 986. In some embodiments, the overlapping collagen fragments described herein are about 350 amino acids, about 370 amino acids, about 390 amino acids, about 400 amino acids, about 420 amino acids, about 440 amino acids, about 460 amino acids, about 480 dog amino acids, about 500 amino acids, about 510 amino acids, about 520 amino acids, about 530 amino acids, about 540 amino acids, about 550 amino acids, about 560 amino acids, about 570 amino acids, about 580 amino acids, about 590 It can be canine amino acids or about 600 amino acids in length.

In some embodiments, the collagen fragments described herein may have an amino acid sequence according to SEQ ID NO: 1 or SEQ ID NO: 986. In some embodiments, the collagen fragment is at least about 70%, at least about 75%, at least about 80%, about 85%, at least about 87.5%, at least about 90%, at least about 92.5%, at least about 95% relative to SEQ ID NO: 1 %, at least about 97.5%, at least about 98%, at least about 99% or 100% sequence homology or similarity. In some embodiments, the collagen fragment is at least about 70%, at least about 75%, at least about 80%, at least about 85%, at least about 87.5%, at least about 90%, at least about 92.5%, at least about 95%, at least about 97.5%, at least about 98%, at least about 99% or 100% sequence homology or similarity.

The amino acid sequence of SEQ ID NO: 1 is as follows:

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

서열 번호 986의 아미노산 서열은 다음과 같다: DVKSGVAVGGLAGYPGPAGPPGPPGPPGTSGHPGSPGSPGYQGPPGEPGQAGPSGPPGPPGAIGPSGPAGKDGESGRPGRPGERGLPGPPGIKGPAGIPGFPGMKGHRGFDGRNGEKGETGAPGLKGENGLPGENGAPGPMGPRGAPGERGRPGLPGAAGARGNDGARGSDGQPGPPGPPGTAGFPGSPGAKGEVGPAGSPGSNGAPGQRGEPGPQGHAGAQGPPGPPGINGSPGGKGEMGPAGIPGAPGLMGARGPPGPAGANGAPGLRGGAGEPGKNGAKGEPGPRGERGEAGIPGVPGAKGEDGKDGSPGEPGANGLPGAAGERGAPGFRGPAGPNGIPGEKGPAGERGAPGPAGPRGAAGEPGRDGVPGGPGMRGMPGSPGGPGSDGKPGPPGSQGESGRPGPPGPSGPRGQPGVMGFPGPKGNDGAPGKNGERGGPGGPGPQGPPGKNGETGPQGPPGPTGPGGDKGDTGPPGPQGLQGLPGTGGPPGENGKPGEPGPKGDAGAPGAPGGKGDAGAPGERGPPAIAGIGGEKAGGFAPYYG.

In some embodiments, the collagen fragment described herein may have an amino acid chain of about 350 amino acids to about 600 amino acids and is at least about 70%, at least about 75%, at least about SEQ ID NO: 1 or SEQ ID NO: 986. 80%, at least about 85%, at least about 87.5%, at least about 90%, at least about 92.5%, at least about 95%, at least about 97.5%, at least about 98%, at least about 99% or 100% sequence homology or similarity can have In some embodiments, such collagen fragments described herein contain about 350 amino acids, about 370 amino acids, about 390 amino acids, about 400 amino acids, about 420 amino acids, about 440 amino acids, about 460 amino acids, about 480 dog amino acids, about 500 amino acids, about 510 amino acids, about 520 amino acids, about 530 amino acids, about 540 amino acids, about 550 amino acids, about 560 amino acids, about 570 amino acids, about 580 amino acids, about 590 It can be canine amino acids or about 600 amino acids in length.

In some embodiments, the recombinant collagen may comprise a hydrolysis product of a collagen fragment, wherein the hydrolysis product may have a sequence that is part of SEQ ID NO: 1 or SEQ ID NO: 986. In some embodiments, the hydrolysis product may have a sequence according to one of SEQ ID NOs: 2-972.

In some embodiments, lysine, proline, or lysine and proline residues present in the collagen fragment are not hydroxylated. In other embodiments, the collagen fragments described herein may be hydroxylated. In some embodiments, at least 1%, 2%, 3%, 4%, 5%, 10%, 15%, 20%, 30%, 40%, 50 of lysine, proline, or lysine and proline residues in the recombinant collagen fragment %, 60%, 70%, 80%, 90%, 95% or 100% (or any intermediate value or subrange) may be hydroxylated. Hydroxylated collagen can build rheology and improve the thermal stability of collagen molecules or fragments. Hydroxylated collagen and hydroxylated collagen fragments are also resistant to high concentrations of pepsin degradation, for example, with a pepsin:total protein ratio of 1:25 to 1:1.

The degree of hydroxylation of proline, lysine or proline and lysine residues in a collagen fragment determines the melting temperature of hydrated collagen, such as a hydrogel, and sets the melting point of the hydrogel as a "control" with a known content of hydroxylated amino acid residues. It can be estimated by comparing with collagen fragments. Collagen melting temperatures can range from 25 to 40° C., with more highly hydroxylated collagens generally having higher melting temperatures.

In some embodiments, the collagen fragments described herein may have an amino acid sequence as set forth in Table 1 or Table 2 below.

[Table 1]

[Table 2]

C. Compositions Comprising Collagen Fragments

In some embodiments, the present invention provides a composition comprising one or more recombinant collagen fragments disclosed herein, and at least one pharmaceutically acceptable or cosmetically acceptable excipient. In certain embodiments, the composition may comprise a recombinant collagen fragment according to SEQ ID NO: 1 or SEQ ID NO: 986, and at least one pharmaceutically acceptable or cosmetically acceptable excipient. In further embodiments, the composition comprises at least about 70%, at least about 75%, at least about 80%, at least about 85%, at least about 87.5%, at least about 90%, at least about 92.5% for SEQ ID NO: 1 or SEQ ID NO: 986. %, at least about 95%, at least about 97.5%, at least about 98%, at least about 99% or 100% sequence homology or similarity to a recombinant collagen fragment, and at least one pharmaceutically acceptable or cosmetically acceptable excipients may be included. In yet a further embodiment, the composition comprises about 85%, about 86%, about 87%, about 88%, about 89%, about 90%, about 91%, about 92%, a recombinant collagen fragment having about 93%, about 94%, about 95%, about 96%, about 97%, about 98%, about 99%, or 100% homology or similarity, and at least one pharmaceutically acceptable or a cosmetically acceptable excipient. In yet a further embodiment, the composition comprises about 85%, about 86%, about 87%, about 88%, about 89%, about 90%, about 91%, about 92%, Recombinant collagen fragments having about 93%, about 94%, about 95%, about 96%, about 97%, about 98%, about 99%, or 100% sequence homology or similarity, and dietary supplements such as nutritional at least one excipient suitable for use in a supplement.

In some embodiments, the composition may comprise a hydrolysis product of a collagen fragment, and at least one pharmaceutically acceptable or cosmetically acceptable excipient, wherein the hydrolysis product is part of SEQ ID NO: 1 or SEQ ID NO: 986 may have a sequence. In some embodiments, the composition comprises a hydrolysis product having a sequence according to one or more of SEQ ID NOs: 2-972, and at least one pharmaceutically acceptable or cosmetically acceptable excipient. In some embodiments, the composition may comprise any of the hydrolysis products set forth in SEQ ID NOs: 2-972, and at least one pharmaceutically acceptable or cosmetically acceptable excipient. In some embodiments, the composition comprises at least about 70%, at least about 75%, at least about 80%, at least about 85%, at least about 87.5%, at least about 90%, at least about 92.5% to one of SEQ ID NOs: 2-972. , a recombinant collagen fragment having at least about 95%, at least about 97.5%, at least about 98%, at least about 99% or 100% sequence homology or similarity, and at least one pharmaceutically acceptable or cosmetically acceptable excipient. may include

In another embodiment, the composition comprises a recombinant collagen fragment according to SEQ ID NO: 1 or SEQ ID NO: 986, a hydrolysis product having a sequence according to one of SEQ ID NOs: 2 to 972, and at least one pharmaceutically acceptable or cosmetically acceptable excipients. In yet a further embodiment, the composition comprises a recombinant collagen fragment according to SEQ ID NO: 1 or SEQ ID NO: 986, a plurality of hydrolysis products having sequences according to any of SEQ ID NOs: 2 to 972, which may be identical or different, and at least one pharmaceutically acceptable or cosmetically acceptable excipient. In certain embodiments, the number of hydrolysis products present in the plurality of hydrolysis products in the composition depends on time, temperature, pH or typically according to a recombinant collagen fragment, e.g., according to SEQ ID NO: 1 or SEQ ID NO: 986. may increase as a result of other conditions that cause the recombinant collagen fragment to hydrolyze or otherwise degrade. In another embodiment, the composition is formulated such that the concentration of the recombinant collagen fragment according to SEQ ID NO: 1 or SEQ ID NO: 986 and the concentration of each fragment in the plurality of fragments remain substantially constant (i.e., ± by HPLC over a given period of time). vary by no more than 5%) or stabilized with one or more stabilizers to remain constant. In certain embodiments, the recombinant collagen fragment, such as a recombinant collagen fragment according to SEQ ID NO: 1 or SEQ ID NO: 986, comprises less than about 10%, about 10% to about 20%, about 20% to about 20% of the composition as determined by HPLC. about 30%, about 30% to about 40%, about 40% to about 50%, about 50% to about 60%, about 60% to about 70%, about 70% to about 80%, about 80% to about 90 %, or from about 90% to about 100% of non-hydrolyzed recombinant fragments may be retained. In another embodiment, the composition comprises a recombinant collagen fragment (eg, a recombinant collagen fragment according to SEQ ID NO: 1 or SEQ ID NO: 986) and a plurality of hydrolysis products of the recombinant collagen fragment (eg, one of SEQ ID NOs: 2-972). a mixture of a plurality of collagen fragments according to any one of the preceding, wherein the weight of hydrolysis products in the composition is less than about 10%, from about 10% to about 20%, from about 20% to about 30% of the weight of the collagen-related protein in the composition. , about 30% to about 40%, about 40% to about 50%, about 50% to about 60%, about 60% to about 70%, about 70% to about 80%, about 80% to about 90%, or It may include from about 90% to about 100%.

In some embodiments, the composition may comprise a recombinant collagen fragment having an amino acid chain length of about 350 amino acids to about 600 amino acids overlapping the amino acid sequence of SEQ ID NO: 1 or SEQ ID NO: 986. In some embodiments, the composition comprises about 350 amino acids, about 370 amino acids, about 390 amino acids, about 400 amino acids, about 420 amino acids, about 440 amino acids, about 460 amino acids, about 480 amino acids, about 500 amino acids amino acids, about 510 amino acids, about 520 amino acids, about 530 amino acids, about 540 amino acids, about 550 amino acids, about 560 amino acids, about 570 amino acids, about 580 amino acids, about 590 amino acids, or about 600 amino acids and recombinant collagen fragments having a length of amino acids. In certain embodiments, the composition comprises a recombinant collagen fragment having an amino acid chain length of 528 amino acids.

In some embodiments, the composition may comprise a recombinant collagen fragment having an amino acid chain length of from about 350 amino acids to about 600 amino acids, comprising at least about 70%, at least about 75% for SEQ ID NO: 1 or SEQ ID NO: 986; At least about 80%, at least about 85%, at least about 87.5%, at least about 90%, at least about 92.5%, at least about 95%, at least about 97.5%, at least about 98%, at least about 99% or 100% sequence homology or have similarities. In some embodiments, such collagen fragments described herein contain about 350 amino acids, about 370 amino acids, about 390 amino acids, about 400 amino acids, about 420 amino acids, about 440 amino acids, about 460 amino acids, about 480 dog amino acids, about 500 amino acids, about 510 amino acids, about 520 amino acids, about 530 amino acids, about 540 amino acids, about 550 amino acids, about 560 amino acids, about 570 amino acids, about 580 amino acids, about 590 It can have a length of canine amino acids or about 600 amino acids.

In some embodiments, the composition may comprise a hydrolysis product of a collagen fragment, wherein the hydrolysis product may have an amino acid chain length of from about 10 amino acids to about 75 amino acids. In some embodiments, the composition may comprise hydrolysis products of collagen fragments having an amino acid chain length of from about 20 amino acids to about 50 amino acids. In some embodiments, the hydrolysis products described herein are about 10 amino acids, about 15 amino acids, about 20 amino acids, about 25 amino acids, about 30 amino acids, about 35 amino acids, about 40 amino acids, about 45 amino acids can have a length of 5 amino acids, about 50 amino acids, about 55 amino acids, about 60 amino acids, about 65 amino acids, about 70 amino acids, or about 75 amino acids.

In some embodiments, the composition may comprise from about 5 ppm to about 500 ppm of recombinant collagen fragments. In some embodiments, the composition is about 5 ppm, about 10 ppm, about 25 ppm, about 50 ppm, about 100 ppm, about 150 ppm, about 200 ppm, about 250 ppm, about 300 ppm, about 350 ppm, about 350 ppm , about 400 ppm, about 450 ppm, or about 500 ppm of the recombinant collagen fragment. In some embodiments, the composition is about 5 ppm, about 10 ppm, about 25 ppm, about 50 ppm, about 100 ppm, about 150 ppm, about 200 ppm, about 250 ppm, about 300 ppm, about 350 ppm, about 350 ppm , about 400 ppm, about 450 ppm, or about 500 ppm of a recombinant collagen fragment having the sequence according to SEQ ID NO: 1 or SEQ ID NO: 986. In some embodiments, the composition is about 5 ppm, about 10 ppm, about 25 ppm, about 50 ppm, about 100 ppm, about 150 ppm, about 200 ppm, about 250 ppm, about 300 ppm, about 350 ppm, about 350 ppm , about 400 ppm, about 450 ppm, or about 500 ppm of one or more hydrolysis products of the recombinant collagen fragment. In some embodiments, the composition is about 5 ppm, about 10 ppm, about 25 ppm, about 50 ppm, about 100 ppm, about 150 ppm, about 200 ppm, about 250 ppm, about 300 ppm, about 350 ppm, about 350 ppm , about 400 ppm, about 450 ppm, or about 500 ppm of one or more hydrolysis products of the recombinant collagen fragment having the sequence according to SEQ ID NO: 1 or SEQ ID NO: 986. In some embodiments, the composition may comprise a mixture of a recombinant collagen fragment at a concentration of about 5 ppm to about 500 ppm and one or more hydrolysis products of the recombinant collagen fragment at a concentration of about 5 ppm to about 500 ppm. In some embodiments, the composition comprises a recombinant collagen fragment having a sequence according to SEQ ID NO: 1 or SEQ ID NO: 986 at a concentration of about 5 ppm to about 500 ppm and one or more of the recombinant collagen fragments at a concentration of about 5 ppm to about 500 ppm. mixtures of hydrolysis products.

In some embodiments, the composition can be prepared from about 0.1% to about 20% by weight of a solution of about 0.5% to about 25% by weight recombinant collagen fragments. In some of these embodiments, the composition comprises about 0.1%, about 0.2%, about 0.3%, about 0.4%, about 0.5%, about 0.6%, about 0.7%, about 0.8%, about 0.9% by volume, about 1% by volume, about 2% by volume, about 3% by volume, about 4% by volume, about 5% by volume, about 6% by volume, about 7% by volume, about 8% by volume, about 9% by volume, about 10% by volume, about 11% by volume, about 12% by volume, about 13% by volume, about 14% by volume, about 15% by volume, about 16% by volume, about 17% by volume, about 18% by volume, about 19% by volume, or about 20% by volume of the recombinant collagen fragment solution. In some of these embodiments, the recombinant collagen fragment solution comprises about 0.5%, about 0.6%, about 0.7%, about 0.8%, about 0.9%, about 1%, about 2%, about 3% by weight. %, about 4 wt%, about 5 wt%, about 6 wt%, about 7 wt%, about 8 wt%, about 9 wt%, about 10 wt%, about 11 wt%, about 12 wt%, about 13 wt% %, about 14 wt%, about 15 wt%, about 16 wt%, about 17 wt%, about 18 wt%, about 19 wt%, about 20 wt%, about 21 wt%, about 22 wt%, about 23 wt% %, about 24% or about 25% by weight recombinant collagen fragments. In some of these embodiments, the recombinant collagen fragment solution is about 0.1 wt%, about 0.2 wt%, about 0.3 wt%, about 0.4 wt%, about 0.5 wt%, about 0.6 wt%, about 0.7 wt%, about 0.8 wt% %, about 0.9 wt%, about 1 wt%, about 2 wt%, about 3 wt%, about 4 wt%, about 5 wt%, about 6 wt%, about 7 wt%, about 8 wt%, about 9 wt% %, about 10 wt%, about 11 wt%, about 12 wt%, about 13 wt%, about 14 wt%, about 15 wt%, about 16 wt%, about 17 wt%, about 18 wt%, about 19 wt% %, about 20%, about 21%, about 22%, about 23%, about 24% or about 25% by weight of a collagen fragment having the sequence according to SEQ ID NO: 1 or SEQ ID NO: 986. In some of these embodiments, the recombinant collagen fragment solution is about 0.1 wt%, about 0.2 wt%, about 0.3 wt%, about 0.4 wt%, about 0.5 wt%, about 0.6 wt%, about 0.7 wt%, about 0.8 wt% %, about 0.9 wt%, about 1 wt%, about 2 wt%, about 3 wt%, about 4 wt%, about 5 wt%, about 6 wt%, about 7 wt%, about 8 wt%, about 9 wt% %, about 10 wt%, about 11 wt%, about 12 wt%, about 13 wt%, about 14 wt%, about 15 wt%, about 16 wt%, about 17 wt%, about 18 wt%, about 19 wt% %, about 20%, about 21%, about 22%, about 23%, about 24%, or about 25% by weight of one or more hydrolysis products of recombinant collagen fragments. In some of these embodiments, the recombinant collagen fragment solution is about 0.1 wt%, about 0.2 wt%, about 0.3 wt%, about 0.4 wt%, about 0.5 wt%, about 0.6 wt%, about 0.7 wt%, about 0.8 wt% %, about 0.9 wt%, about 1 wt%, about 2 wt%, about 3 wt%, about 4 wt%, about 5 wt%, about 6 wt%, about 7 wt%, about 8 wt%, about 9 wt% %, about 10 wt%, about 11 wt%, about 12 wt%, about 13 wt%, about 14 wt%, about 15 wt%, about 16 wt%, about 17 wt%, about 18 wt%, about 19 wt% %, about 20%, about 21%, about 22%, about 23%, about 24% or about 25% by weight of one of the recombinant collagen fragments having a sequence according to one or more of SEQ ID NOs: 2-972 The above hydrolysis products are included. In some of these embodiments, the composition may be prepared using from about 0.1% to about 20% by weight of a mixture of about 0.5% to about 25% by weight of a recombinant collagen fragment and one or more hydrolysis products of the recombinant collagen fragment. have. In some of these embodiments, the composition comprises about 0.1 volume of a mixture of about 0.5% to about 25% by weight of a recombinant collagen fragment having a sequence according to SEQ ID NO: 1 or SEQ ID NO: 986 and one or more hydrolysis products of the recombinant collagen fragment. % to about 20% by volume.

In some embodiments, the composition comprises from about 0.0005 wt% to about 25 wt% recombinant collagen fragments, from about 0.001 wt% to about 25 wt% recombinant collagen fragments, from about 0.01 wt% to about 25 wt% recombinant collagen fragments, about 0.1 wt% to about 25 wt% recombinant collagen fragment, about 0.5 wt% to about 20 wt% recombinant collagen fragment, about 0.7 wt% to about 17 wt% recombinant collagen fragment, about 1 wt% to about 15 wt% of recombinant collagen fragment, about 2% to about 12% by weight recombinant collagen fragment, about 2% to about 10% by weight recombinant collagen fragment, about 3% to about 9% by weight recombinant collagen fragment, about 4% by weight % to about 8% by weight recombinant collagen fragment, or from about 5% to about 7% by weight recombinant collagen fragment. In some embodiments, the composition comprises about 0.0005 wt%, about 0.001 wt%, about 0.01 wt%, about 0.1 wt%, about 0.2 wt%, about 0.3 wt%, about 0.4 wt%, about 0.5 wt%, about 0.6 wt% %, about 0.7 wt%, about 0.8 wt%, about 0.9 wt%, about 1 wt%, about 2 wt%, about 3 wt%, about 4 wt%, about 5 wt%, about 6 wt%, about 7 wt% %, about 8 wt%, about 9 wt%, about 10 wt%, about 11 wt%, about 12 wt%, about 13 wt%, about 14 wt%, about 15 wt%, about 16 wt%, about 17 wt% %, about 18 wt%, about 19 wt%, about 20 wt%, about 21 wt%, about 22 wt%, about 23 wt%, about 24 wt%, or about 25 wt% recombinant collagen fragment . In some embodiments, the composition comprises about 0.0005 wt%, about 0.001 wt%, about 0.01 wt%, about 0.1 wt%, about 0.2 wt%, about 0.3 wt%, about 0.4 wt%, about 0.5 wt%, about 0.6 wt% %, about 0.7 wt%, about 0.8 wt%, about 0.9 wt%, about 1 wt%, about 2 wt%, about 3 wt%, about 4 wt%, about 5 wt%, about 6 wt%, about 7 wt% %, about 8 wt%, about 9 wt%, about 10 wt%, about 11 wt%, about 12 wt%, about 13 wt%, about 14 wt%, about 15 wt%, about 16 wt%, about 17 wt% %, about 18%, about 19%, about 20%, about 21%, about 22%, about 23%, about 24% or about 25% by weight of SEQ ID NO: 1 or SEQ ID NO: 986 It may include a collagen fragment having a sequence according to the In some embodiments, the composition comprises about 0.0005 wt%, about 0.001 wt%, about 0.01 wt%, about 0.1 wt%, about 0.2 wt%, about 0.3 wt%, about 0.4 wt%, about 0.5 wt%, about 0.6 wt% %, about 0.7 wt%, about 0.8 wt%, about 0.9 wt%, about 1 wt%, about 2 wt%, about 3 wt%, about 4 wt%, about 5 wt%, about 6 wt%, about 7 wt% %, about 8 wt%, about 9 wt%, about 10 wt%, about 11 wt%, about 12 wt%, about 13 wt%, about 14 wt%, about 15 wt%, about 16 wt%, about 17 wt% %, about 18 wt%, about 19 wt%, about 20 wt%, about 21 wt%, about 22 wt%, about 23 wt%, about 24 wt%, or about 25 wt% of one or more hydrolysis of recombinant collagen fragments product may be included. In some embodiments, the composition comprises about 0.0005 wt%, about 0.001 wt%, about 0.01 wt%, about 0.1 wt%, about 0.2 wt%, about 0.3 wt%, about 0.4 wt%, about 0.5 wt%, about 0.6 wt% %, about 0.7 wt%, about 0.8 wt%, about 0.9 wt%, about 1 wt%, about 2 wt%, about 3 wt%, about 4 wt%, about 5 wt%, about 6 wt%, about 7 wt% %, about 8 wt%, about 9 wt%, about 10 wt%, about 11 wt%, about 12 wt%, about 13 wt%, about 14 wt%, about 15 wt%, about 16 wt%, about 17 wt% %, about 18%, about 19%, about 20%, about 21%, about 22%, about 23%, about 24%, or about 25% by weight of one or more of SEQ ID NOs: 2-972 one or more hydrolysis products of a recombinant collagen fragment having a sequence according to In some embodiments, the composition comprises about 0.0005 wt%, about 0.001 wt%, about 0.01 wt%, about 0.1 wt%, about 0.2 wt%, about 0.3 wt%, about 0.4 wt%, about 0.5 wt%, about 0.6 wt% %, about 0.7 wt%, about 0.8 wt%, about 0.9 wt%, about 1 wt%, about 2 wt%, about 3 wt%, about 4 wt%, about 5 wt%, about 6 wt%, about 7 wt% %, about 8 wt%, about 9 wt%, about 10 wt%, about 11 wt%, about 12 wt%, about 13 wt%, about 14 wt%, about 15 wt%, about 16 wt%, about 17 wt% %, about 18 wt%, about 19 wt%, about 20 wt%, about 21 wt%, about 22 wt%, about 23 wt%, about 24 wt%, or about 25 wt% recombinant collagen fragments and recombinant collagen fragments thereof may contain a mixture of one or more hydrolysis products of In some embodiments, the cosmetic composition comprises about 0.0005 wt%, about 0.001 wt%, about 0.01 wt%, about 0.1 wt%, about 0.2 wt%, about 0.3 wt%, about 0.4 wt%, about 0.5 wt%, about 0.6 wt% wt%, about 0.7 wt%, about 0.8 wt%, about 0.9 wt%, about 1 wt%, about 2 wt%, about 3 wt%, about 4 wt%, about 5 wt%, about 6 wt%, about 7 wt% wt%, about 8 wt%, about 9 wt%, about 10 wt%, about 11 wt%, about 12 wt%, about 13 wt%, about 14 wt%, about 15 wt%, about 16 wt%, about 17 wt% %, about 18%, about 19%, about 20%, about 21%, about 22%, about 23%, about 24%, or about 25% by weight of SEQ ID NO: 1 or SEQ ID NO: 986 and a mixture of a recombinant collagen fragment having a sequence according to

skin care

In some embodiments, the compositions described herein can be used to improve the aesthetic appearance of the skin and/or its appendages, eg, the surface appearance and/or texture of the skin. In some embodiments, the compositions described herein can be formulated for use on the body and face, hands and feet, including treatment for the ocular region, nails, and hair. The term "surface appearance" refers to wrinkles and fine lines, facial lines in the space between the forehead and eyebrows, wrinkles and/or fine lines around the mouth, and/or in the area around the lips and the upper lip area (the area located between the upper lip and the nose). slackening of skin tone, skin tone heterogeneity (melasma, light age spots), appearance and/or visibility of pores, paper-like appearance of the skin, defects in skin microtopography such as chickenpox or acne scars, imperfections of oily skin ( visual and/or tactile irregularities in the skin and/or scalp, including a shiny appearance, etc.). The term “skin texture” may refer to skin that is slack, flabby, less firm, less elastic, and/or sagging skin.

In some embodiments, the compositions described herein can be used to improve the aesthetic appearance of skin, including improving the appearance of facial lines. Expression lines are created by the effect of stress on the skin by the muscles below. Age and environmental factors, such as exposure to sunlight, can deepen facial lines and make them permanent. The facial expression line is in the area around the hole formed by the nose (nasolabial groove), mouth (periorbital folds and so-called bitterness lines) and eyes (crow's feet), around which the skin muscles are located, and also between the eyebrows ( Glabellar or lion folds) and on the forehead are characterized by the presence of grooves.

In some embodiments, the compositions described herein can be used to improve the aesthetic appearance of skin and/or visibility of pores. Visibility of pores may be due to excess sebum, aging, loss of firmness, looseness, stress, fatigue, inadequate hygiene, climatic factors, or any combination thereof. The compositions described herein can tighten pores, making them less visible.

In some embodiments, the compositions described herein can be used to improve the paper-like appearance of skin and skin behavior to touch. Specifically, aged skin can visually take on the appearance of tobacco paper, providing an appearance similar to a sheet of papyrus. The paper-like appearance of the skin can be seen on the face and back of the hands of the elderly.

In some embodiments, a composition described herein is a composition for protecting, treating or caring for the face, hands, feet, or body, such as a day cream, night cream, makeup remover cream, sunscreen composition, skin care or It may be body milk for care, aftersun milk, skin care lotion, gel, foam, artificial tanning composition and aftershave composition. In some embodiments, a composition described herein is, for example, a solution, suspension, lotion, cream, serum, gel, balm, gel, oil, oil in cream, micellar water, face mist, face Essences, blemish balms, or complexion correcting formulations, toners (water and/or alcohol based), paints, polishes, sticks, pencils, sprays, aerosols, ointments, cleansing liquid washes, solid bars, shampoos, Hair conditioners, hair styling products, pastes, foams, powders, mousses, balms, shaving creams, wipes, strips, patches, wound dressings, adhesive bandages, hydrogels, film forming products, face and skin masks, cosmetics (e.g. foundations) , eyeliner, eye shadow), exfoliant, deodorant and antiperspirant, and the like. Exemplary formulations are provided herein.

In some embodiments, the compositions described herein can be cosmetic compositions and the at least one excipient can be a cosmetically acceptable excipient. Cosmetically acceptable excipients are excipients suitable for use in cosmetics. Exemplary cosmetically acceptable excipients are described below.

In some embodiments, the cosmetic compositions described herein may include hydrolysis products of recombinant collagen fragments and at least one excipient, eg, a cosmetically acceptable excipient. In some embodiments, a cosmetic composition described herein may comprise a recombinant collagen fragment, one or more hydrolysis products of the recombinant collagen fragment, and at least one excipient, eg, a cosmetically acceptable excipient.

In some embodiments, cosmetic compositions may include ingredients commonly used in cosmetics, eg, skin care, eye care, nail care, and hair care products. These ingredients include soaps, antibacterial agents, anti-inflammatory agents, humectants, waxy alcohols, hydrating agents, humectants, penetration enhancers, emulsifiers, natural or synthetic oils, solvents, fats, surfactants, detergents, gelling agents, emollients, antioxidants, fragrances, paints, Brighteners, fillers, thickeners, waxes, odor absorbers, dyes, colorants, powders, viscosity modifiers, anesthetics, antipruritic agents, plant extracts, conditioning agents, darkening or whitening agents, humectants, mica, minerals, polyphenols, silicone or silicone derivatives Examples include dimethicone, sunblock, vitamins, botanical medicines, alcohols such as denatured alcohol and ethanol, polyols, polyolethers, and other ingredients listed in the International Cosmetic Ingredient Dictionary and Handbook, 13th Ed. (2009), although Without limitation, this document is incorporated herein by reference in its entirety. In certain embodiments, a given component may perform more than one function and may belong to one or more classes.

In some embodiments, a composition described herein can be a dietary composition or a dietary supplement, and the at least one excipient can be, for example, a food or beverage additive. A “dietary supplement” is a formulation intended to supplement the diet and may be useful in providing nutrients or additives that may be missing from or not consumed in sufficient amounts in a person's diet. In some embodiments, the dietary supplement is any commonly used solid or for oral administration including, without limitation, capsules, tablets, pills, powders, granules or powders, soft and hard gelatin capsules and/or gummy. It may be provided in the form of a liquid formulation. Suitable excipients include, but are not limited to, lactose or milk sugar, as well as high molecular weight polyethylene glycols and the like. Exemplary dietary compositions are described below.

The compositions described herein may also include one or more of the following additional ingredients. Exemplary contemplated additional ingredients are set forth below; However, the present invention is not limited to these exemplary additional components.

In some embodiments, the compositions described herein may further comprise one or more anti-wrinkle agents. An anti-wrinkle agent is a compound that produces an increase in the synthesis and/or activity of certain enzymes in the skin when the composition is contacted with an area of wrinkled skin of the body or face, including, for example, the ocular area, which causes wrinkles and/or or reduce the outward appearance of fine lines. Exemplary anti-wrinkle agents include, but are not limited to, desquamating agents, anti-glycation agents, nitric oxide synthase inhibitors, muscle relaxants and/or dermo-decontracting agents, free radical scavengers, and mixtures thereof. doesn't happen

Additional exemplary anti-wrinkle agents that may be included in the compositions described herein include adenosine and derivatives thereof, retinol and derivatives thereof (eg, retinyl palmitate), ascorbic acid and derivatives thereof (eg, magnesium ascorbyl) phosphate and ascorbyl glucoside), tocopherol and derivatives thereof (eg tocopheryl acetate), nicotinic acid and its precursors (eg nicotinamide), ubiquinone, glutathione and derivatives thereof (eg L-2 -oxothiazolidine-4-carboxylic acid), C-glycoside compounds (also known as C-glycosyl compounds), and derivatives thereof (e.g., β-C-xylosyl derivatives, trade name PRO -XYLANE), plant extracts (e.g. loxampire extract and olive leaf extract), plant proteins and hydrolysates thereof (e.g. rice or soy protein hydrolysates), algae extracts (e.g. laminaris) eye extract), bacterial extract, sapogenin (eg diosgenin), Dioscorea extract (eg wild yam extract), α-hydroxy acids, β-hydroxy acids (eg, salicylic acid and 5-(n-octanoyl)salicylic acid), oligopeptides and pseudodipeptides and their acylated derivatives (eg, {2-[acetyl(3-(trifluoromethyl)phenyl)amino]- 3-methylbutyrylamino}acetic acid), lipopeptides such as MATRIXYL 3000 available from Croda), lycopene, manganese, magnesium salts (eg, gluconate), and combinations of any of these , but not limited thereto.

Exemplary adenosine derivatives include 2'-deoxyadenosine; 2',3'-iso-propylidene adenosine; Toyocamycin, 1-methyladenosine; N-6-methyladenosine, adenosine N-oxide, 6-methyl-mercaptopurine riboside, and 6-chloropurine riboside. Other adenosine derivatives include phenylisopropyladenosine ("PIA")/1-methylisoguanosine, Ns-cyclohexyladenosine (CHA), N6-cyclopentyladenosine (CPA), 2-chloro-Ns-cyclopentyl-adenosine, 2-Chloroadenosine, N6-phenyladenosine, 2-phenylaminoadenosine, MECA, Ne-phenethyladenosine, 2-p-(2-carboxyethyl)phenethylamino-5'-N-ethylcarboxamido-adenosine (CGS-21680), (N-ethylcarboxamido)adenosine-S-(NECA), 5'-(N-cyclopropylcarboxamido)adenosine, DPMA (PD 129,944), and metripudyl adenosine receptor agonists.

In some embodiments, the compositions described herein comprise one or more adenosine derivatives that increase intracellular concentrations of adenosine, e.g., erythro-9-(2-hydroxy-3-nonyl) adenine (“EHNA”), iodo tubersidine or a combination thereof. Additional adenosine derivatives contemplated herein include adenosine salts and alkyl esters of adenosine.

In some embodiments, the composition may further comprise one or more pearlescent agents. Pearlescent agents are pearlescent particles of any shape, especially produced by certain crustaceans within their shells. Alternatively, the pearlescent agent can be synthesized, ie made. Pearlescent agents include, but are not limited to, white pearlescent agents such as, but not limited to, mica coated with titanium oxide or bismuth oxychloride, pearlescent agents based on bismuth oxychloride, titanium oxide-coated mica coated with iron oxide, in particular coated with ferric blue or chromium oxide. colored pearlescent agents such as, but not limited to, titanium oxide-coated mica, or titanium oxide-coated mica coated with an organic pigment.

In some embodiments, the composition may further comprise one or more hydroxy acids. Examples of hydroxy acids include beta hydroxy acids such as salicylic acid, acetylsalicylic acid, and the like. Additional exemplary hydroxy acids suitable for use in the composition include polyhydroxy acids including citric acid, glycolic acid, hydroxycaproic acid, hydroxycaprylic acid, lactic acid, malic acid, tartaric acid, gluconolactone, and any thereof includes a combination of

In some embodiments, the composition may further comprise one or more emulsifiers. Emulsifiers prevent the different components (eg oil and water) from separating in the emulsion. Suitable emulsifiers include, but are not limited to, polysorbate, laureth-4, potassium cetyl sulfate, glyceryl caprylate, and any combination thereof.

In some embodiments, the composition may further comprise one or more chelating agents. Chelating agents bind metal ions and prevent them from reacting chemically with other substances in the formulation. Suitable chelating agents include, but are not limited to, sodium phytate, disodium EDTA, tetrasodium EDTA, tetrasodium glutamate diacetate, and trisodium ethylenediamine disuccinate.

In addition to the chelating agent, tetrasodium glutamate diacetate may also act as a stabilizer in any of the compositions described herein.

In some embodiments, the composition may further comprise one or more antimicrobial agents. Suitable antimicrobial agents include caprylyl glyceryl ether, benzalkonium chloride, benzethonium chloride, and chloroxylenol (PCMX), tea tree oil, witch hazel, rosemary oil, lemon oil, and any combinations thereof. including but not limited to.

In some embodiments, the composition may further comprise one or more humectants (moisture-retaining agents) to improve the moisture level of the skin. Non-limiting examples of wetting agents suitable for use in the compositions described herein are described in WO 98/22085, WO 98/18444, and WO 97/01326, including: Amino acids and derivatives thereof, such as proline and arginine aspartate, 1,3-butylene glycol, propylene glycol, pentylene glycol, water, codium tomentosum extract, creatinine, diglycerol, biosaccharide gum-1, glucamine salt, glucuronic acid salts, glutamic acid salts, polyethylene glycol ethers of glycerin (eg, glycereth 20), glycerin, glycerol monopropoxylate, glycogen, hexylene glycol, honey, hydrogenated starch hydrolysates, hydrolyzed mucopolysaccharides (eg, xanthan gum and Biosaccharide gum-1), inositol, keratin amino acids, glycosaminoglycans, methoxy PEG 10, methyl glucose-10 and -20, methyl glucose, 3-methyl-1,3-butanediol, N-acetyl glucosamine salts, polyethylene glycol and derivatives thereof (eg, PEG 15 butanediol, PEG 4, PEG 5 pentaerythitol, PEG 6, PEG 8, PEG 9), propanediol, pentaerythitol, 1,2 pentanediol, PPG- 1 Glyceryl ether, 2-pyrrolidone-5-carboxylic acid (including salts and esters thereof), saccharide isomers, sericin, silk amino acids, sodium acetyl hyaluronate, sodium hyaluronate, sodium poly-aspartate, polyglutamic acid Sodium, caprylyl glycol, sorbet 20, sorbet 6, sugars and sugar alcohols and their derivatives such as glucose, mannose and polyglycerol sorbitol, trehalose, triglycerol, trimethylolpropane, tris(hydroxymethyl)amino methane salts, and yeast extracts, and mixtures thereof.

Additional humectants suitable for use herein are glycerin, diglycerin, glycerol, erythritol, arabitol, xylitol, ribitol, mannitol, sorbitol, galactitol, fusitol, maltitol, mannose, inositol, triethyleneglycol, sodium p. polyhydric alcohols selected from the group consisting of rolidone carboxylic acid (PCA), zinc PCA and derivatives and mixtures thereof.

In some embodiments, the composition may further comprise a gelling agent comprising a polyacrylamide-based polymer. In addition to being polyacrylamide itself, the polyacrylamide-based polymer may be a derivative thereof, may be a mixture of a plurality of types of polymers, and may also be a copolymer having acrylamide and its derivatives as monomers. The gelling agent can be used to give the skin a good appearance, provide a cooling sensation to the skin, and give the skin a refreshing feeling without stickiness. In some embodiments, the gelling agent may include one or more pigments, or one or more fillers, which include inorganic pigments such as extender pigments, color pigments, and whitening pigments, organic pigments, pearlescent pigments, macromolecular powders, functional pigments. , talc, mica, kaolin, calcium carbonate, magnesium carbonate, silicic anhydride, aluminum silicate, magnesium silicate, calcium silicate, aluminum oxide, barium sulfate, red iron oxide, yellow iron oxide, black iron oxide, chromium oxide, ultramarine blue, Prussian blue , carbon black, zinc oxide, mica titanium, fishscale flakes, bismuth oxychloride, boron nitride, nylon powder, silk powder, carbomer, tar pigment, natural pigment and titanium oxide, for example amorphous or rutile and/or anatase including decision making.

In some embodiments, the composition may include pigments and/or fillers that are resistant to water and oil, and any commonly used water and/or oil repellent agents to impart water and oil repellency to pigments, for example, It may further include a fluorine compound. Representative fluorine compounds commonly used and capable of acting as water and oil repellent agents include compounds having perfluoroalkyl groups, such as perfluoroalkyl phosphates, perfluoroalkyl silanes, perfluoroalkyl silazanes, polyhexafluoro propylene oxide, perfluoroalkyl-group-containing organosiloxanes, perfluoropolyethers, perfluoro alcohols, perfluoroalkylacrylate polymers and derivatives thereof. The perfluoroalkyl phosphate can provide a uniform and stable dispersion of the pigment within the formulation of the gel composition, and the perfluoroalkyl silane can have excellent compatibility with other cosmetic ingredients. In addition, perfluoroalkyl phosphate-diethanol amine salts sold as AsahiGuard Ag530 by Asahi Glass, and perfluoroalkyl silane coupling agents such as LP-IT and LP-4T from Shin-Etsu Silicone can be used.

Representative gelling agents include, but are not limited to, those sold by Seppic under the trade names Sepigel 305, Sepigel 501, and Sepigel 600. Sepigel 305 is approximately 40% polyacrylamide, approximately 24% -C ₁₃ -C ₁₄ isoparaffin and approximately 6% laureth-7, wherein laureth-7 is of the formula C ₁₂ H ₂₅ --(OCH ₂ CH ₂ ) mixtures containing _n —OH, where n is a nonionic surfactant with an average value of 7. Sepigel 600 is a mixture of acrylamide/acrylamide-2-propane sulfonate copolymer, isohexadecane and polysorbate 80 (polyoxyethylene sorbitan mono-oleate (20 EO)). Suitable gelling agents comprising polyacrylamide-based polymers are disclosed in EP 0 503 853 (Scott Bader Company Ltd.), the disclosure of which is incorporated herein by reference.

In some embodiments, the composition may further comprise hyaluronic acid (HA). In some embodiments, the HA may be in an uncrosslinked state. In some embodiments, the HA may be in a cross-linked state. Like collagen, HA is an important structural component of human tissue. Hyaluronan, also known as hyaluronic acid (HA), is an unsulfated glycosaminoglycan widely distributed throughout the human body in connective tissue, epithelial tissue and nervous tissue. Hyaluronan is abundant in different layers of the skin, where it has multiple functions, for example, to help organize the extracellular matrix, to ensure good hydration, to act as a filler, and to participate in tissue repair mechanisms, etc. . However, with age, the amount of hyaluronan present in the skin decreases.

In some embodiments, the compositions described herein may be used with microneedle arrays, such as arrays contained in sheets or patches. The microneedle array may include a plurality of microneedles having a length sufficient to penetrate across the stratum corneum of the skin and into the viable epidermis. In some embodiments, it may be desirable to deliver the polypeptide to the epidermal/dermal junction region for cosmetic purposes.

In some embodiments, the compositions described herein can be used with microneedle sheets or patches. Microneedles and microneedle patches are suitable for delivering collagen into the epidermis and dermis of human skin of the face and body, including, for example, the eyes, cheeks, lips, decolletage and hands. In some embodiments, the microneedles for delivering the composition into the epidermis and dermis in a targeted manner are injectable microneedles, drug coated metal microneedles, or microneedles with a dissolving tip. Exemplary methods and disclosures relating to microneedles are described, for example, in Aditya et al., Kinetics of collagen microneedle drug delivery system, Journal of Drug Delivery Science and Technology , vol. 52, pp. 618-623 (August 2019) and Sun et al. Transdermal Delivery of Functional Collagen Via Polyvinylpyrrolidone Microneedles, Ann. Biomed. Eng ., 43(12):2978-2990 (2015)], each of which is incorporated by reference in its entirety.

In some embodiments, the composition may further comprise a waxy lipid, such as a ceramide. Ceramides help create a barrier to prevent permeability, which can help prevent dryness and irritation and also protect the epidermis from environmental damage.

In some embodiments, the composition may further comprise vitamin A or a vitamin A derivative. Examples of vitamin derivatives include, but are not limited to, retinoids such as retinal, retinoic acid, retinoate, retinyl esters, retinol, tretinoin, isotretinoin, adapalene, tazarotene, and the like. The term “retinoid” includes cis and trans derivatives of retinoids (eg, all-trans-retinoic acid, 13-cis-retinoic acid, 13-trans retinoic acid, and 9-cis-retinoic acid).

In some embodiments, the composition may further comprise vitamin C or a derivative thereof, such as ascorbic acid, ascorbate (eg, tetrahexyldecyl ascorbate), and the like.

In some embodiments, the composition may further comprise a B vitamin, eg, biotin, (ie, vitamin B7), niacinamide, and the like.

In some embodiments, the composition may further comprise vitamin E, such as α-, β-, γ-, and σ-tocopherols and their related corresponding tocotrienols), and the like.

In some embodiments, the composition may further comprise vitamin K and derivatives thereof.

Any vitamin, vitamin analog or derivative thereof that can be suitably formulated as a topical composition is contemplated for the present invention.

In some embodiments, the compositions disclosed herein may further comprise one or more thickening agents. A thickener, ie, a structure builder, may suspend the pigment in the composition and/or may build up viscosity. Suitable thickeners and/or structural builders for the compositions of the present invention are organically modified clays, fumed silica, trihydroxystearin, silicone gels or silicone elastomers, ammonium acryloyldimethyltaurate/VP copolymers, acrylates /C10-30 alkyl acrylate crosspolymers, and mixtures thereof.

Suitable organically modified clays include organically modified forms of hectorite, bentonite, smectite and montmorillonite clays (such as BENTONE® from Elementis Specialties, TIXO-GEL® from Sud-Chemie, and CLAYTONE® from Southern Clay Products). those sold as ), but are not limited thereto. Hydrophilically modified fumed silicas include, but are not limited to, WACKER HDK® N20 and T30 grades (Wacker-Chemie AG), and hydrophilic grades under the trade designation AEROSIL® (Evonik). Silicone gel or silicone elastomer is a "KSG" thickening series from Shin-Etsu Silicones (KSG-15, KSG-16, KSG-18, KSG-41, KSG-42, KSG-43, KSG-44), Dow Corning DOW CORNING® 9040, 9041, 9045, and 9546 silicone elastomer blends from Momentive Performance Materials, SFE839™ from Momentive Performance Materials, and Velvesil™ silicone gel, and WACKER-BELSIL® RG-100 from Wacker-Chemie Ag. not limited

In some embodiments, the compositions disclosed herein may further comprise one or more lipid-soluble/lipid-dispersible film formers. Lipid-soluble/lipid-dispersible film formers suitable for use herein include copolymers of organic silicone resins (eg, trimethylsiloxysilicates such as SRI 000 from GE Silicones) and organic silicone resins (eg, diisostearyl trimethylolpropane siloxy silicates such as SF1318 from GE Silicones); fluorinated silicone resins; acrylic and/or vinyl-based polymers including silicone and/or fluorinated forms (eg, the “KP” series of silicone acrylates from Shin-Etsu Silicones, and 3M™ Silicones “Plus” Polymers VS70 and SA70); or copolymer; polyurethanes (eg Poly derm® series derived from hydroxyester triglycerides from Alzo International); polyesters (eg, the Lexorez® series of polymeric polyesters from Inolex Chemical Company); and mixtures thereof.

In some embodiments, the compositions disclosed herein may further comprise one or more colorants. Colorants suitable for use herein include all inorganic and organic color/pigments including mineral or pearl pigments suitable for use in cosmetic compositions. Such colorants include those with or without a surface coating or treatment. Colorants may enhance the coloring of the composition, and/or light scattering, and/or light reflection effects.

In some embodiments, the compositions disclosed herein may further comprise one or more sunscreen agents, eg, mineral and/or physical sunscreen agents. Sunscreens can block UVA and/or UVB radiation. Exemplary UVA sunscreens include avobenzone, terephthalylidene dicamphor sulfonic acid, bis-disulizole disodium, disodium phenyl dibenzimidazole tetrasulfonate, diethylamino hydroxybenzoyl hexylbenzoate, bis-di ethylamino hydroxybenzoyl benzoate, bis-benzoxazolylphenyl ethylhexylamino triazine, and combinations thereof.

Exemplary UVB sunscreens include octocrylene, octinoxate, octisalate, homosalate, ensullizole, ethylhexyl triazone, enzacamene, amyloxate, diethylhexyl butamido triazine, benzylidene malonate polysiloxane , Padimate-O, trolamine salicylate, cinoxate, p-aminobenzoic acid and derivatives thereof, and combinations thereof.

Exemplary sunscreens that absorb both UVA and UVB radiation include, for example, oxybenzone, meradimate, titanium dioxide, zinc oxide, bis-octrizole, bemotrizinol, dromethrizole trisiloxane, sulisobenzone, di oxybenzone, or a combination thereof.

Specific suitable sunscreens include p-aminobenzoic acid, salts and derivatives thereof (ethyl, isobutyl, glyceryl esters, p-dimethylaminobenzoic acid), anthranilates (i.e. o-aminobenzoate, methyl, menthyl, phenyl). , benzyl, phenylethyl, linalyl, terpinyl, and cyclohexenyl esters), salicylates (amyl, phenyl, benzyl, menthyl, glyceryl, and dipropylene glycol esters), cinnamic acid derivatives (methyl and benzyl esters, Alpha-phenyl cinnamonitrile, butyl cinnamoyl pyruvate), dihydroxycinnamic acid derivatives (umbelliferone, methylumbelliferone, methylaceto umbelliferone), trihydroxycinnamic acid derivatives (esculetin, methyl S culetin, daphnetin, and glucoside, esculin and daphnin), hydrocarbons (diphenylbutadiene, stilbene), dibenzalacetone and benzalacetophenone, naphtholsulfonate (2-naphthol-3,3-disulfonic acid) and sodium salt of 2-naphthol-6,8-disulfonic acid), dihydroxynaphthoic acid and its salts, o- and p-hydroxybiphenyldisulfonate, coumarin derivatives (7 hydroxy, 7-methyl, 3-phenyl), diazoles (2-acetyl-3-bromoindazole, phenyl benzoxazole, methylnaphthoxalol, various arylbenzothiazoles), quinine salts (bisulfate, sulfate, chloride, oleate and tannate) , quinoline derivatives (8-hydroxyquinoline salt, 2-phenylquinoline), hydroxy- or methoxy substituted benzophenones, uric and viloric acids, tannic acids and their derivatives (e.g. hexaethyl ether ), (butyl carbityl) (6-propyl piperonyl) ether, hydroquinone, benzophenone (oxybenzene, sulisobenzone, dioxybenzone, benzoresorcinol, 2,2',4,4'-tetra Hydroxybenzophenone, 2,2'-dihydroxy-4,4'-dimethoxybenzophenone, octabenzone, 4-isopropyldibenzoylmethane, butylmethoxydibenzoylmethane, etocrylene, and 4- isopropyl-di-benzoylmethane, titanium dioxide, iron oxide, zinc oxide, and mixtures thereof Other cosmetically acceptable sunscreen agents and concentrations (% by weight of the total cosmetic sunscreen composition) is diethanolamine methoxycinnamate (10% or less), ethyl-bis(hydroxypropyl)aminobenzoate (5% or less), glyceryl aminobenzoate (3% or less) ), 4-isopropyl dibenzoylmethane (5% or less), 4-methylbenzylidene camphor (6% or less), terephthalidene dicamphor sulfonic acid (10% or less), and sulfisobenzone (also known as benzophenone-4) , 10% or less). In some embodiments, the compositions disclosed herein may further comprise D-aspartic acid and/or D-alanine and any salts thereof. As used herein, the term "derivatives" of D-aspartic acid and D-alanine refers to amino, carboxyl or side chains of D-aspartic acid and D-alanine, provided that the collagen-promoting effect of D-aspartic acid and D-alanine is not impaired. D-aspartic acid and D-alanine molecules covalently bound to any organic group through Exemplary organic groups include protecting groups such as an N-phenylacetyl group and a 4,4′-dimethoxytrityl (DMT) group; biopolymers such as proteins, peptides, sugars, lipids and nucleic acids; synthetic polymers such as polystyrene, polyethylene, polyvinyl, polypropylene and polyester; and functional groups such as ester groups. Ester groups include, for example, aliphatic esters such as methyl esters, and ethyl esters; and aromatic esters.

In some embodiments, the composition may further comprise one or more common skin care additives, such as, for example, conditioning agents such as silicones. In some embodiments, the composition may further comprise one or more shark liver oils, such as squalane and/or squalene. In some embodiments, the composition may further comprise one or more polysaccharides produced by microalgae, such as alguronic acid.

In some embodiments, the composition may further comprise at least one preservative. In some embodiments, the at least one preservative is a quaternary ammonium compound, a halogenated phenol, sorbic acid, potassium sorbate, benzoic acid, sodium benzoate, sodium citrate, sodium anisate, caprylhydroxamic acid, sodium levulinate, It may be phenoxyethanol or a combination thereof.

The compositions described herein can have a pH in the range of about 4 to about 8, about 4.7 to about 5.5, about 5 to about 7, about 6 to about 7, about 6.1 to about 6.8, or about 6.4 to 6.6.

soap

In some embodiments, the cosmetic compositions described herein include traditional soaps in the form of solid bars, and cleaners, makeup removers, body washes, milks, creams, which may be packaged in tubes, bottles, pump bottles, aerosol shower foam, or foam pump bottles. , a foam cream gel, or a cleansing composition or soap comprising a liquid soap in the form of a gel. The soap is collected to form a foam and can be used in a cosmetic process to clean dust residues of human keratin material in the presence of water, the formed foam and dirty residues being removed by rinsing with water, for example, on the body, face, hands, It can be used on any part of the body and face disclosed herein, including the skin of the lips, eyelids, nails, hair, eyelashes and/or eyebrows.

Traditionally, solid soaps include alkali metal fatty acid salts and potassium fatty acid soaps, and liquid soaps include four major classes of detergent formulations: (1) those based on lauryl sulfate; those based on alpha-olefin sulfonates, (3) those based on mixtures of synthetic anionic, amphoteric and/or nonionic surfactants; (4) Mixed formulations based on soap and synthetic surfactants. Liquid soaps generally include a thickening system selected from electrolytes such as, for example, sodium chloride, potassium chloride or potassium sulfate; alkanolamides such as cocamide DEA or cocamide MEA; polyethylene glycol and esters of monoacids or stearic acids, such as polyethylene glycol distearate 6000 or mixtures thereof, which are contained in a cosmetically acceptable aqueous medium. However, both solid and liquid soaps may include any suitable additional ingredients, such as those listed herein below, in any combination.

In some embodiments, the cleansing compositions or soaps described herein are linear or branched having 6 to 30 carbon atoms or 12 to 22 carbon atoms within the structural chain of glucose moieties linked by β-1,4 bonds. one or more fatty acids including saturated or unsaturated alkyl chains of, lauric acid, myristic acid, palmitic acid and stearic acid, linolenic acid, and mixtures thereof, and alkali metal hydroxides (sodium and potassium hydroxide) ), one or more inorganic bases including metal hydroxides or ammonia, or one or more cellulosic or polysaccharide compounds having one or more organic bases such as triethanolamine, monoethanolamine, monoisopropanolamine, N-methylglucamine, lysine and arginine may further include.

In some embodiments, the compositions described herein comprise one or more anionic salts of the following types, including alkali metal salts, such as sodium salts, ammonium salts, amine salts, aminoalcohol salts, or salts of alkaline earth metals, such as magnesium. It may further include surfactants or salts: alkyl sulfates, alkyl ether sulfates, alkyl amido ether sulfates, alkyl aryl polyether sulfates; monoglyceride sulfate; alkylsulfonates, alkylamidesulfonates, alkylarylsulfonates, α-olefin-sulfonates, paraffin-sulfonates; alkylsulfosuccinates, alkylethersulfosuccinates, alkylamide-sulfosuccinates; alkyl sulfoacetate; acyl sarcosinate; and acylglutamate, alkyl and acyl groups of all such compounds having 6 to 24 carbon atoms and aryl groups representing phenyl or benzyl groups, C ₆ -C ₂₄ alkyl esters of polyglycoside carboxylic acids, such as alkyl glucoside citrates, alkyl polyglycoside tartrates and alkyl polyglycoside sulfosuccinates, alkylsulfosuccinnamates, acylsethionates and N-acyltaurates, alkyl or acyl groups of all such compounds having 12 to 20 carbon atoms and/or acylactylates and mixtures thereof, wherein the acyl group contains from 8 to 20 carbon atoms. In some embodiments, alkyl-D-galactoside uronic acid, polyoxyalkylenated (C ₆ -C ₂₄ ) ether carboxylic acid, polyoxyalkylenated (C ₆ -C ₂₄ ) aryl (C ₆ -C ₂₄ ) polyoxyalkylenated ether carboxylic acids, polyoxyalkylenated (C ₆ -C ₂₄ ) alkyl amidoether carboxylic acids, especially those containing from 2 to 50 ethylene oxide groups; and alkali metal, ammonium, amine, aminoalcohol or alkaline earth metal salts thereof may also be suitable.

Suitable C ₆ -C ₂₄ alkyl ether sulfate salts containing 1 to 30 ethylene oxide groups include alkali metal or alkaline earth metal, ammonium, amine or amino alcohol salts, sodium salts and oxy having an average number of ethylene oxide groups from 1 to 4 Ethylenated (C ₁₂ -C ₁₄ ) alkyl ethersulfates, such as sodium laureth sulfate (CTFA name), such as TEXAPON AOS 225 UP TEXAPON N702 TEXAPON NSW by COGNIS or EMPICOL ESB3 / FL2 by the company Huntsman, EMPICOL Includes commercially available products sold as ESB3 / FL3, EMPICOL ESB70 / FL2.

Suitable amphoteric surfactants include, but are not limited to, derivatives of secondary or tertiary aliphatic amines, wherein the aliphatic group is a linear or branched chain containing from 8 to 22 carbon atoms. Amphoteric surfactants contain at least one water-soluble anionic group, such as a carboxylate, sulfonate, sulfate, phosphate or phosphonate group, (C ₈ -C ₂₀ ) alkylbetaine, sulfobetaine, (C ₈ -C ₂₀ ) alkylamido (C ₆ -C ₈ ) alkylbetaine or (C ₈ -C ₂₀ ) alkylamidoalkyl (C ₆ -C ₈ ) sulfobetaine, and mixtures thereof.

Suitable amine derivatives include those sold under the name MIRANOL®, which are described in US Pat. No. 2,528,378 and US Pat. No. 2,781,354, and in the CTFA Dictionary (3rd edition, 1982). Further suitable amine derivatives include those classified in the CTFA Dictionary (5th edition, 1993) under the names: cocoamphodiacetate disodium, lauroamphodiacetate disodium, caprylamhodiacetate disodium, caprylo Amphodiacetate disodium, cocoamphodipropionate disodium, lauroamphodipropionate disodium, capryloamphodipropionate disodium, capryloamphodipropionate disodium, lauroamphodipropionic acid , cocoamphodipropionic acid, and cocoamphodiacetate sold under the trade name MIRANOL® C2M concentrated by Rhodia. Suitable alkyl (C ₈ -C ₂₀ ) betaines include cocamidopropyl betaine and cocobetaine such as MIRATAINE BB/FLA from RHODIA or EMPIGEN BB/FL from Huntsman.

In some embodiments, the cleansing compositions or soaps described herein may be sulfate-free and may include a sulfate-free surfactant system.

In some embodiments, the cleansing compositions or soaps described herein may further comprise one or more thickening agents of the nonionic cellulosic compound type. Suitable cellulosic compounds include methylcellulose and ethylcellulose; hydroxyalkylcelluloses such as hydroxymethylcellulose, hydroxyethylcellulose and hydroxypropylcellulose; mixed hydroxyalkyl-alkylcellulose celluloses such as hydroxypropyl-methylcellulose, hydroxyethyl-methylcellulose, hydroxyethylethylcellulose and hydroxybutyl-methylcellulose, and hydroxyalkylcelluloses modified with alkyl chains. non-ionic cellulose ethers, but are not limited thereto. Suitable hydroxypropyl methylcelluloses include the commercially available products of METHOCEL E, F, J and K sold by Dow Coming, and even more particularly METHOCEL E 4MQG or METHOCEL F 4M. Suitable cellulosic components may be in crystalline form, microcrystalline form, or mixtures thereof.

In some embodiments, the cleansing composition or soap described herein comprises an electrolyte such as sodium chloride, potassium chloride or potassium sulfate; alkanolamides such as cocamide DEA or cocamide MEA; Polyethylene glycol and esters of monoacid or stearic acid such as polyethylene glycol distearate 6000 or mixtures thereof, polysaccharide biopolymers such as xanthan gum, guar gum, alginates, synthetic polymers such as CARBOPOL 980 sold by NOVEON , polyacrylic such as CARBOPOL 1382, acrylate/acrylonitrile copolymer such as HYPAN SS201 sold by KINGSTON, clay such as smectite, modified or unmodified hectorite such as BENTONE product sold by Rheox, Southern Clay one or more additional thickening agents, including the LAPONITE product marketed by Products, the VEEGUM HS product marketed by RT Vanderbilt, and mixtures thereof.

In some embodiments, the cleansing compositions or soaps described herein may further comprise one or more nonionic surfactants. These are well known compounds (see "Handbook of Surfactants" by MR PORTER, Blackie & Son editions (Glasgow and London), 1991, pp 116-178), alcohols, alpha-diols, (C ₁ -C ₂₀ ) alkyl phenols or polyethoxylated, polypropoxylated or polyglycerolated fatty acids (eg, having a fatty chain comprising 8 to 18 atoms, and the number of ethylene oxide groups or propylene oxide in the range from 2 to 50) and the number of glycerol groups may range from 2 to 30), copolymers of ethylene oxide and propylene, condensates of ethylene oxide and propylene oxide on fatty alcohols; polyethoxylated fatty amides having 2 to 30 moles of ethylene oxide, polyglycerolated fatty amides comprising an average of 1 to 5 glycerol groups; polyethoxylated fatty amines having 2 to 30 moles of ethylene oxide, ethoxylated sorbitan fatty acid esters having 2 to 30 moles of ethylene oxide; Sucrose fatty acid esters, polyethylene glycol fatty acid esters, (C ₆ -C ₂₄ ) alkyl polyglycosides, N-alkyl (C ₆ -C ₂₄ ) glucamine derivatives, amine oxides such as alkyl (C ₁₀ -C ₁₄ ) amines. oxides or oxides of N-acyl (C ₁₀ -C ₁₄ )-aminopropylmorpholine, and mixtures thereof.

Further suitable nonionic surfactants are alkyl polyglucosides (APG), maltose esters, polyglycerolated fatty alcohols, glucamine derivatives such as 2-ethylhexyloxycarbonyl-N-methylglucamine, and their mixtures, but are not limited thereto. Suitable alkylpolyglucosides include those containing alkyl groups containing 6 to 30 carbon atoms and hydrophilic groups (glucosides). Exemplary alkylpolyglucosides are the product sold under the name Mydol 10® by the company Kao Chemicals, the product sold under the name Plantaren 2000 UP® by the company Cognis, and the product sold under the name Oramix NS 10® by the company SEPPIC. decylglucoside (alkyl-C9/C11-polyglucoside (1.4)), including products that are laurylglucoside sold by the company Cognis as Plantaren 1200 N® and Plantacare 1200®, and cocoglucosides, for example the products sold under the name Plantacare 818/UP® by the company Cognis.

Suitable maltose derivatives are those described in document EP-A-566 438 such as O-octanoyl-6′-D-maltose or O-dodecanoyl-6′-D-maltose described in document FR-2 739 556 Includes toss.

In some embodiments, the cleansing composition or soap may be formulated in a cosmetically acceptable aqueous medium. Suitable cosmetically acceptable aqueous media include, in addition to water, one or more solvents, for example lower alcohols containing 1 to 6 carbon atoms, such as ethanol; polyols such as glycerin; glycols such as butylene glycol, isoprene glycol, propylene glycol, polyethylene glycols such as PEG-8, sorbitol, sugars such as glucose, fructose, maltose, lactose, sucrose, and mixtures thereof. The amount of solvent(s) in the compositions disclosed herein can range from 0.1 to 95% by weight.

In some embodiments, the cleansing compositions or soaps described herein may further comprise one or more cationic polymers of the polyquaternium type, which may provide softness and lubricity to the foaming composition. Suitable cationic polymers include polyquaternium 5, such as the product MERQUAT 5 sold by the company CALGON, polyquaternium 6, such as the product SALCARE SC 30 sold by the company CIBA, and the product MERQUAT 100 sold by the company CALGON, poly Quaternium 7, such as the products MERQUAT S, MERQUAT 2200 and MERQUAT 550 sold by the company CALGON, and the SALCARE SC 10 product sold by the company CIBA, Polyquaternium 10, such as the product sold by the company Amerchol Polymer JR400, Poly Quaternium 11, such as products sold by ISPs GAFQUAT 755, GAFQUAT 755N and GAFQUAT 734, Polyquaternium 15, such as products sold by the company ROHM ROHAGIT KF 720 F, Polyquaternium 16, such as products sold by BASF LUVIQUAT FC905, LUVIQUAT FC370, LUVIQUAT HM552 and LUVIQUAT FC550, Polyquaternium 22, such as the product Merquat 280 sold by the company Calgon, Polyquaternium 28, such as the product STYLEZE CC10 sold by the ISP, Polyquaternium 39, such as The product MERQUAT PLUS 3330 sold by Calgon, Polyquaternium 44, such as the product LUVIQUAT CARE sold by the company BASF, Polyquaternary 46, such as the product LUVIQUAT HOLD sold by the company BASF, Polyquaternium 47, such as in Calgon Cationic guar, including the product MERQUAT 2001 sold by the company Rhodia, such as the product Jaguar sold by the company Rhodia, may also be used as the cationic polymer.

In some embodiments, the cleansing compositions or soaps described herein may further comprise one or more adjuvants or additives used in cosmetic compositions. Suitable adjuvants or additives are oils, actives, fragrances, preservatives, sequestering agents, pearlizing or opacifying agents, pigments, pearlizing agents, inorganic or organic fillers such as talc, kaolin, silica powder or polyethylene, soluble dyes, or any of these Combinations include, but are not limited to.

Examples of oils include vegetable oils (jojoba, avocado, sesame, sunflower, corn, soybean, safflower, grape seed), mineral oils (petroleum, optionally hydrogenated isoparaffin), synthetic oils (isopropyl myristate, cetearyl octanoate) , polyisobutylene, ethyl hexyl palmitate, alkyl benzoate), volatile or non-volatile silicone oils such as polydimethylsiloxane (PDMS) and cyclodimethylsiloxane or cyclomethicone, and fluorinated or fluorosilicone oils and mixtures thereof.

Exemplary active agents include sunscreens, exfoliants, moisturizers, bleaches, pro-pigments, alpha-hydroxy acids, antibacterial agents, anti-radical agents, anti-fouling agents, anti-inflammatory agents, retinoids, extracts of algae, mushrooms, vegetables, yeast, bacteria, hydrolyzed, partially hydrolyzed, or unhydrolyzed proteins, enzymes, hormones, vitamins and derivatives thereof, flavonoids and isoflavones, and mixtures thereof.

The cleansing compositions or soaps described herein may have a pH in the range of 6 to 10 depending on the application selected. Adjusting the pH to the desired value is usually a base (organic or inorganic) in the composition, for example ammonia or a primary, secondary or tertiary (poly)amine such as monoethanolamine, diethanolamine, triethanolamine, by adding isopropanolamine or 1,3-propanediamine, or by adding an inorganic or organic acid, for example a carboxylic acid, such as citric acid. In the context of a shower gel, the pH can vary from 8 to 10.

In some embodiments, the cleansing compositions described herein contain optional additives such as colorants, fragrances, antibacterial agents, preservatives, antioxidants, beads (aromatic, exfoliating or moisturizing), mica, glitter, shea butter, shea butter beads, opacity It may further include firearms, pearlizing agents, and other such ingredients. In some embodiments, the composition has a high clarity (about 2 to about 25 NTU), a targeted viscosity (about 4,000 to about 10,000 centipoise) to facilitate dispensing from an orifice ranging from about 1/4 to about 1/8. ), and a yield value (3 to about 15 Pascals) that allows the composition to suspend various additives with uniformity of distribution and improved stability (eg, about 8 months at 120°F (49°C)). , and any combination thereof.

In some embodiments, the cleansing composition or soap may further comprise one or more humectants/emollients. Moisturizers can be included in bars or liquid soap compositions to provide conditioning benefits to the skin. The term “moisturizer” describes a substance that imparts a smooth and soft feel to the skin surface.

There are two ways to reduce water loss from the stratum corneum. One is to deposit an occlusive layer on the surface of the skin that reduces the rate of evaporation. A second method is to add a non-occlusive hygroscopic material to the stratum corneum that will retain water, and make this water available to the stratum corneum, thereby altering its physical properties and producing a cosmetically desirable effect. Non-occlusive moisturizers also function by improving the lubricity of the skin.

Both occlusive and non-occlusive humectants are contemplated for use in the compositions described herein. Exemplary humectants include long chain fatty acids, liquid water soluble polyols, glycerin, propylene glycol, sorbitol, polyethylene glycol, ethoxylated/propoxylated ethers of methyl glucose (eg methyl glucose-20), ethoxylated/propoxylated lanolin alcohols Sylated ethers (e.g., Solulan-75® available from Amerchol Co.), coconut and tallow fatty acids, liquid water-soluble polyols (e.g., glycerin, propylene glycol, butylene glycol, hexylene glycol, polypropylene glycol and polyethylene glycol).

Nonocclusive moisturizers can occur naturally in the stratum corneum of the skin, such as sodium pyrrolidone carboxylic acid, lactic acid, urea, L-proline, guanidine and pyrrolidone. Examples of other non-occlusive humectants are the hexadecyl, myristyl, isodecyl or isopropyl esters of adipic acid, lactic acid, oleic acid, stearic acid, isostearic acid, myristic acid or linoleic acid, as well as a number of their corresponding alcohol esters ( sodium isostearoyl-2-lactylate, sodium caprylic lactylate), hydrolyzed proteins and other collagen-derived proteins, aloe vera gel and acetamide MEA (N-acetyl ethanolamine). Other examples of occlusive and non-occlusive types of moisturizers are disclosed in "Emollients--A Critical Evaluation," by J. Mausner, Cosmetics & Toiletries, May 1981, which is incorporated herein by reference.

Exemplary occlusive humectants include petrolatum, mineral oil, beeswax, silicone, lanolin and oil-soluble lanolin derivatives, saturated and unsaturated fatty alcohols such as behenyl alcohol, squalene, squalane, and various animal and plant oils such as almond oil, peanut oil, wheat Germ oil, linseed oil, jojoba oil, apricot seed oil, walnut, palm, pistachio, sesame seed, rapeseed oil, cade oil, corn oil, peach seed oil, poppy seed oil, pine oil, castor oil, soybean oil, avocado oil, safflower oil, coconut oil, hazelnut oil, olive oil, grapeseed oil and sunflower seed oil.

hair care

In some embodiments, the composition is a hair care composition comprising ingredients commonly used in hair care products. These ingredients include cleansing agents, foaming agents, hydrating agents, surfactants, detergents, gelling agents, fragrances, botanical extracts, conditioning agents, humectants, silicones or silicone derivatives, thickeners, sun blocks, vitamins, alcohols, polyols, polyol ethers, and may include, but are not limited to, other commonly used ingredients in shampoos, conditioners, and styling agents. Hair care products generally include one or more surfactants, one or more viscosity modifiers, one or more preservatives, and one or more fragrances, and any or a combination of the ingredients listed below.

In general, hair can be susceptible to damage and brittleness under the action of external atmospheric factors such as light or bad weather and also by mechanical or chemical treatments such as brushing, combing, dyeing, bleaching, perm waving and/or relaxing, Over time, hair may become dry, rough, dull and/or brittle. To overcome these drawbacks, it is common to use care compositions that properly condition the hair to provide satisfactory cosmetic properties, especially in terms of smoothness, shine, softness, flexibility, lightness, natural feel and good loosening properties. it is customary Such hair care compositions can be, for example, shampoos, conditioning shampoos, hair conditioners, masks, serums, gels, hair lotions and creams, which can be rinsed off or leave-in compositions. In various embodiments, such compositions are formulated with cationic surfactants, cationic polymers, silicones and/or fatty substances, such as fatty alcohols, to provide satisfactory cosmetic properties in general in terms of softness, smoothness and flexibility to the hair. a combination of sexual conditioning agents. An exemplary composition may include a silicone, which is known to improve the cosmetic properties of the hair in terms of smoothness and flexibility (shown in US Pat. No. 5,374,421, each incorporated herein by reference).

In some embodiments, the hair care composition comprises at least one non-amino polyalkylsiloxane, at least one oxyethylenated polymer in the presence of a fatty alcohol, at least one non-amino amino comprising at least one alkyl chain having at least 12 carbon atoms. polyalkylsiloxanes, one or more oxyethylenated polymers and/or one or more fatty alcohols. Exemplary oxyethylenated polymers can have a weight average molecular weight of 10 ⁶ or greater. In some embodiments, the oxyethylenated polymer can be selected from compounds having the formula H(OCH ₂ CH ₂ ) _z OH, wherein z is an integer of 30,000 or greater. In certain embodiments, z may range from 30,000 to 120,000, or from 40,000 to 95,000. In some embodiments, the oxyethylenated polymer is PEG-45M (z = 45,000), such as the product sold under the name Polyox WSR N 60 K by the company Amerchol, and PEG-90M (z = 90 000), and these may be a mixture of

In some embodiments, the hair care composition may further comprise one or more fatty alcohols. The term “fatty alcohol” means any saturated or unsaturated, linear or branched alcohol containing at least 8 carbon atoms and not oxyalkylated. Exemplary fatty alcohols are solids at room temperature (25° C.) and atmospheric pressure (1.013*10 ⁵ Pa). Exemplary fatty alcohols include cetyl alcohol, stearyl alcohol, oleyl alcohol, behenyl alcohol, linoleyl alcohol, palmitoleyl alcohol, arachidonyl alcohol, erucyl alcohol, cetylstearyl (or cetearyl) alcohol, and mixtures thereof.

In some embodiments, the hair care composition may further comprise one or more conditioning agents including cationic surfactants, cationic polymers, and mixtures thereof. The term “cationic surfactant” means a surfactant that is positively charged when contained in the compositions described herein. Suitable cationic surfactants may be selected from primary, secondary or tertiary fatty amines (optionally polyoxyalkylated), or salts thereof, and quaternary ammonium salts, and mixtures thereof. An exemplary fatty amine is stearamidopropyl dimethylamine. Exemplary quaternary ammonium salts are dialkyldimethylammonium or alkyltrimethylammonium salts in which the alkyl group contains approximately 16 to 22 carbon atoms, in particular behenyltrimethylammonium, distearyldimethylammonium, cetyltrimethylammonium or benzyldimethylammonium. tetraalkylammonium salts, including stearylammonium salts, or on the other hand, palmitylamidopropyltrimethylammonium salt, stearamidopropyltrimethylammonium salt, stearamidopropyldimethylcetearylammonium salt, or Van Dyk stearamidopropyldimethyl(myristyl acetate)ammonium salt sold under the name CERAPHYL 70 by the company

The term “cationic polymer” means any polymer containing a cationic group, which may be non-silicic, and/or a group capable of being ionized into a cationic group. Exemplary cationic polymers are any known for hair styling, for example, patent application EP-A-0 337 354 and French patent application FR-A-2 270 846, 2 383 660, 2 598 611, 2 470 596 and 2 519 863, each of which is incorporated by reference in its entirety. Additional exemplary cationic polymers contain units comprising primary, secondary, tertiary and/or quaternary amine groups that may form part of the main polymer chain or may be supported by side substituents directly linked thereto. includes doing Suitable cationic polymers may have a weight average molecular weight greater than 10 ⁵ , including polymers of the polyamine, polyaminoamide and polyquaternary ammonium types, including those described in FR 2 505 348 and 2 542 997 and , each of which is incorporated by reference in its entirety.

In some embodiments, the hair care composition may further comprise a “non-sulfate” cleansing agent, foaming agent, or surfactant. Suitable "non-sulfate" agents include, but are not limited to, sodium lauroyl methyl isethionate propanediol, sodium methyl oleoyl taurate, and sodium cocoyl isethionate.

In some embodiments, the hair care composition may further comprise any of the following ingredients or mixtures thereof: quaternary ammonium compounds synthetically derived from rapeseed, vinylpyrrolidone and/or vinylimidazole quaternary polymers of, for example LUVIQUAT FC 905, FC 550 and FC 370 by the company BASF and the products sold under the name LUVIQUAT Excellence, cellulose ether derivatives comprising quaternary ammonium groups, cations grafted with water-soluble quaternary ammonium monomers A cationic polysaccharide comprising a cationic cellulose copolymer or cellulose derivative, and a cationic cellulose comprising cationic galactomannan gum. Exemplary cellulose ether derivatives comprising quaternary ammonium groups are described in French Patent 1 492 597. These polymers are also defined in the CTFA dictionary as quaternary ammonium of hydroxyethylcellulose reacted with an epoxide substituted with a trimethylammonium group. Cationic cellulose copolymers or cellulose derivatives grafted with water-soluble quaternary ammonium monomers are described in US Pat. No. 4,131,576, such as methacryloylethyltrimethylammonium, methacrylamidopropyltrimethylammonium or dimethyldiallylammonium, among others. hydroxyalkyl celluloses grafted with salts, for example hydroxymethyl, hydroxyethyl or hydroxypropyl cellulose.

Suitable related celluloses, such as alkylhydroxyethylcelluloses quaternized with C ₈ -C ₃₀ fatty chains, include, for example, the product QUATRISOFT LM 200 (INCI name Polyquaternium-24) sold by the company Amerchol/Dow Chemical and Croda CRODACEL QM (INCI name PG-hydroxyethylcellulose cocodimonium chloride), CRODACEL QL (C ₁₂ alkyl) (INCI name PG-hydroxyethylcellulose lauryldimonium chloride) and CRODACEL QS (C ₁₈ alkyl) (INCI name PG-hydroxyethylcellulose stearyldimonium chloride). Other suitable fatty-chain hydroxyethylcellulose derivatives include the commercially available product SOFTCAT Polymer SL from Amerchol/Dow chemical under the INCI name Polyquaternium-67, such as SL-100, SL-60, SL-30 and SL-5. do. Suitable cationic galactomannan gums are described in US Pat. Nos. 3,589,578 and 4 031 307. Suitable cellulosic components may be in crystalline form, microcrystalline form, or mixtures thereof.

In some embodiments, the hair care composition comprises one or more cationic proteins or cationic protein hydrolysates, polyalkyleneimines including polyethyleneimine, polymers containing vinylpyridine or vinylpyridinium units, polyamines and epichlorohydrin. Condensates, quaternary polyureylenes and chitin derivatives, animal protein hydrolysates bearing trimethylbenzylammonium groups, such as products sold under the name Crotein BTA by the company Croda and referred to in the CTFA dictionary as benzyltrimonium hydrolyzed animal protein , protein hydrolysates bearing a quaternary ammonium group on the polypeptide chain, wherein the ammonium group comprises at least one alkyl radical having 1 to 18 carbon atoms.

In some embodiments, the hair care composition further comprises one or more quaternized plant proteins, such as those derived from wheat, corn or soy protein, eg, quaternized wheat proteins, comprising cocodimonium hydrolysates in the CTFA dictionary. Sold under the name Hydrotriticum WQ or QM by the company Croda, referred to as digested wheat protein, Hydrotriticum QL, referred to in the CTFA dictionary as laurdimonium hydrolyzed wheat protein, or else steardimonium in the CTFA dictionary Hydrotriticum QS, referred to as hydrolyzed wheat protein.

In some embodiments, the hair care composition may further comprise one or more polyamines, for example POLYQUART R H sold by Cognis, referred to in the CTFA dictionary by the name polyethylene glycol tallow polyamine. Further suitable polymers include, inter alia, those sold under the name Lupamin by the company BASF, and the products sold under the names Lupamin 9095, Lupamin 5095, Lupamin 1095, Lupamin 9030 and Lupamin 9010.

In some embodiments, the hair care composition may further comprise one or more fatty substances that are liquid at room temperature (25° C.) and atmospheric pressure (1.013*10 ⁵ Pa). The term "fatty substance" means an organic compound that is insoluble in water (solubility of less than 5%, less than 1%, or less than 0.1%) at room temperature (25° C.) and atmospheric pressure (1.013*10 ⁵ Pa). Fatty substances are generally soluble in organic solvents such as chloroform, dichloromethane, carbon tetrachloride, ethanol, benzene, toluene, tetrahydrofuran (THF), liquid petroleum jelly or decamethylcyclopentasiloxane under the same temperature and pressure conditions. . The liquid fatty material of the present invention may be non-polyoxyethylenated and non-polyglycerolated. The term “oil” means a “fatty substance” that is liquid at room temperature (25° C.) and atmospheric pressure (1.013*10 ⁵ Pa). The term "non-silicone oil" means an oil which does not contain any silicon atoms (Si), and the term "silicone oil" means an oil which contains at least one silicon atom. Liquid fatty substances are non-silicone oils, such as in particular C ₆ -C ₁₆ liquid hydrocarbons, liquid hydrocarbons containing more than 16 carbon atoms, non-silicone oils of animal origin, triglycerides of vegetable or synthetic origin, fluoro oils , liquid fatty acids and/or fatty alcohol esters other than triglycerides, and mixtures thereof. Liquid hydrocarbons may be linear, branched or optionally cyclic, including hexane, cyclohexane, undecane, dodecane, tridecane or isoparaffins such as isohexadecane, isodecane or isododecane, and mixtures thereof. . Suitable linear or branched liquid hydrocarbons of mineral or synthetic origin containing more than 16 carbon atoms are from liquid paraffin, petroleum jelly, liquid petroleum jelly, mineral oil, polydecene and hydrogenated polyisobutene, such as PARLEAM and mixtures thereof. can be selected. It is possible to use hydrocarbon-based oils of animal origin, such as perhydrosqualene.

Exemplary triglycerides of plant or synthetic origin are liquid fatty acid triglycerides comprising 6 to 30 carbon atoms, such as heptanoic or octanoic acid triglycerides, or alternatively more specifically plant oils, such as coconut. oil, sunflower oil, corn oil, soybean oil, marrow oil, grapeseed oil, sesame oil, hazelnut oil, apricot oil, macadamia oil, arara oil, castor oil, avocado oil, jojoba oil, shea butter oil, or synthetic caprylic/capric triglycerides, such as those sold by the company Stearineries Dubois, or those sold under the names MIGLYOL 810, 812 and 818 by the company Dynamit Nobel, and mixtures thereof. . Suitable fluoro oils include perfluoromethylcyclopentane and perfluoro-1,3-dimethylcyclohexane, such as FLUTEC PC1 and FLUTEC PC3 from BNFL Fluorochemicals; perfluoro-1,2-dimethylcyclobutane; Perfluoroalkanes such as dodecafluoropentane and tetradecafluorohexane, sold under the names PF 5050 and PF 5060 by the company 3M, or bromoperfluorooctyl sold under the name FORALKYL by the company Atochem ; nonafluoromethoxybutane and nonafluoroethoxyisobutane; perfluoromorpholine derivatives such as 4-trifluoromethyl perfluoromorpholine sold under the name PF 5052 by the company 3M.

Suitable monoesters include dihydroabiethyl behenate; octyldodecyl behenate; isocetyl behenate; cetyl lactate; C ₁₂ -C ₁₅ alkyl lactate; isostearyl lactate; lauryl lactate; linoleyl lactate; oleyl lactate; (iso)stearyl octanoate; isocetyl octanoate; octyl octanoate; cetyl octanoate; decyl oleate; isocetyl isostearate; isocetyl laurate; isocetyl stearate; isodecyl octanoate; isodecyl oleate; isononyl isononanoate; isostearyl palmitate; methyl acetyl ricinoleate; myristyl stearate; octyl isononanoate; 2-ethylhexyl isononate; octyl palmitate; octyl pelargonate; octyl stearate; octyldodecyl erucate; oleyl erucate; ethyl and isopropyl palmitate; 2-ethylhexyl palmitate, 2-octyldecyl palmitate, alkyl myristates such as isopropyl, butyl, cetyl, 2-octyldodecyl, myristyl or stearyl myristate, hexyl stearate, butyl stearate, isobutyl stearate; dioctyl maleate, hexyl laurate, 2-hexyldecyl laurate, and mixtures thereof.

In some embodiments, the hair care composition comprises diethyl sebacate, diisopropyl sebacate, diisopropyl adipate, di(n-propyl) adipate, dioctyl adipate, diisostearyl adipate, dioctyl maleate. Eate, glyceryl undecylenate, octyldodecyl stearoyl stearate, pentaerythrityl monoricinoleate, pentaerythrityl tetraisononanoate, pentaerythrityl tetrapelagonate, pentaerythrityl tetra isostearate, pentaerythrityl tetraoctanoate, propylene glycol dicaprylate, propylene glycol dicaprate, tridecyl erucate, triisopropyl citrate, triisostearyl citrate, glyceryl trilactate, glyceryl trioctanoate, trioctyldodecyl citrate, trioleyl citrate, propylene glycol dioctanoate, neopentyl glycol diheptanoate, diethylene glycol diisononanoate, and polyethylene glycol distearate, and mixtures thereof.

In some embodiments, the hair care composition may further comprise one or more fatty esters, one or more sugar esters, and/or one or more diesters of C ₆ -C ₃₀ , such as C ₁₂ -C ₂₂ fatty acids. The term "sugar" means an oxygen-bearing hydrocarbon-based compound with or without aldehyde or ketone functionality and containing some alcohol functionality comprising at least 4 carbon atoms. Suitable sugars include monosaccharides, oligosaccharides or polysaccharides such as sucrose (or saccharose), glucose, galactose, ribose, fucose, maltose, fructose, mannose, arabinose, xylose and lactose, and their derivatives such as alkyl derivatives such as methyl derivatives such as methylglucose. Suitable esters are oleate, laurate, palmitate, myristate, behenate, cocoate, stearate, linoleate, linolenate, caprate, arachidonate or mixtures thereof, such as oleate/palmitate. , oleate/stearate or palmitate/stearate mixed esters. Suitable monoesters and diesters also include mono- or di-oleates of sucrose, of glucose or of methylglucose, including the products sold under the name GLUCATE DO by the company Amerchol, which is methylglucose dioleate; -stearate, -behenate, -oleopalmitate, -linoleate, -linolenate or -oleostearate. Further exemplary esters or mixtures of esters of fatty acids with sugars that may also be mentioned include: the products sold under the names F160, F140, F110, F90, F70 and SL40 by the company Crodesta (each

73% monoesters and 27% diesters and triesters, 61% monoesters and 39% diesters, triesters and tetraesters, 52% monoesters and 48% diesters, triesters and tetraesters, 45% monoesters and sucrose palmitate/stearate, and sucrose mono laurate formed from 55% diesters, triesters and tetraesters, 39% monoesters and 61% diesters, triesters and tetraesters); the product under the name Ryoto Sugar Esters, for example sucrose behenate sold under the reference B370 and formed from 20% monoester and 80% diester-triester-polyester; Sucrose mono-dipalmitate/stearate sold by the company Goldschmidt under the name TEGOSOFT PSE.

In some embodiments, the hair care composition may further comprise a pH modifier such as citric acid and/or sodium hydroxide. Any commonly used pH-modifier for hair care compositions is contemplated for use herein.

In various embodiments, the hair care composition may further comprise any of the following ingredients and/or mixtures thereof: Sodium Lauroyl Methyl Isethionate (Cleansing and Foaming Agent), as discussed hereinabove A liquid fatty material comprising a silicone oil different from a non-amino polyalkylsiloxane that has been prepared, and an organomodified polysiloxane comprising at least one functional group selected from an amino group, an aryl group and an alkoxy group. Organopolysiloxanes are more fully defined in Walter Noll's Chemistry and Technology of Silicones (1968), Academic Press, which is incorporated herein by reference in its entirety. They may be volatile or non-volatile. Suitable cyclic polydialkylsiloxanes are octamethylcyclotetrasiloxane sold under the name VOLATILE SILICONE 7207 by Union Carbide or SILBIONE 70045 V2 by Rhodia, sold under the name VOLATILE SILICONE 7158 by Union Carbide or SILBIONE 70045 V5 by Rhodia decamethylcyclopentasiloxane, and mixtures thereof. Also suitable are cyclocopolymers of the dimethylsiloxane/methylalkylsiloxane type, such as VOLATILE SILICONE FZ 3109 sold by the company Union Carbide. Exemplary cyclic polydialkylsiloxanes having organosilicon compounds are octamethylcyclotetrasiloxane and tetra(trimethylsilyl)pentaerythritol (50/50), and octamethylcyclotetrasiloxane and oxy-1,1′-bis(2). ,2,2′,2′,3,3′-hexatrimethylsilyloxy)neopentane, linear volatile polydialkylsiloxanes such as those sold under the name SH 200 by the company Toray Silicone. Silicones falling within this category are also described in Cosmetics and Toiletries, Vol. 91, January 76, pp. 27-32, Todd & Byers, "Volatile Silicone Fluids for Cosmetics"].

Exemplary suitable non-volatile polydialkylsiloxanes are polydimethylsiloxanes having trimethylsilyl end groups, such as SILBIONE oils of the 47 and 70 047 series sold by Rhodia or MIRASIL oils, such as oil 70 047 V 500 000 ; oils of the MIRASIL series sold by Rhodia; 200 series oils from Dow Corning, such as DC200 having a viscosity of 60 000 mm 2 /s; Poly with dimethylsilanol end groups known under the designation dimethiconol (CTFA), such as VISCASIL oils from General Electric and certain oils of the SF series from General Electric (SF 96, SF 18), and oils from series 48 from Rhodia. dimethylsiloxane.

Exemplary organomodified silicones include polyalkylarylsiloxanes, and products sold under the following names: Rhodia's 70 641 series of SILBIONE oils; Oils of the RHODORSIL 70 633 and 763 series from Rhodia; Oil from Dow Corning Dow Corning 556 Cosmetic Grade Fluid; Bayer's PK series of silicones, such as the product PK20; Silicones of the PN and PH series from Bayer, such as the products PN1000 and PH1000, certain oils from the SF series of General Electric such as SF 1023, SF 1154, SF 1250 and SF 1265, under the name GP 4 Silicone Fluid and GP 7100 by Genesee Products sold or sold under the designations Q2 8220 and Dow Corning 929 or 939 by the company Dow Corning.

In various embodiments, the hair care composition comprises one or more additional surfactants different from the cationic surfactants described above, including anionic surfactants, amphoteric or zwitterionic surfactants, nonionic surfactants, and mixtures thereof. may additionally include. Exemplary anionic surfactants include alkyl sulfates, alkyl ether sulfates, alkylamido ether sulfates, alkylarylpolyether sulfates, monoglyceride sulfates, alkylsulfonates, alkylamidesulfonates, alkylarylsulfonates, α-olefin sulfonates. , paraffin sulfonates, alkylsulfosuccinates, alkylether sulfosuccinates, alkylamide sulfosuccinates, alkylsulfoacetates, acylsarcosinates, acylglutamates, alkylsulfosuccinamates, acylsethionates and N- (C ₁ -C ₄ )alkyl N-acyltaurate, alkyl monoester and salt of polyglycoside-polycarboxylic acid, acylactylate, D-calactoside uronic acid salt, alkyl ether carboxylic acid salt, alkyl aryl ether carboxylic acid salts, alkylamido ether carboxylic acid salts; and the corresponding unsalted forms of all these compounds; (unless otherwise stated) includes the alkyl and acyl groups of all these compounds, which generally contain from 6 to 24 carbon atoms and the aryl group generally represents a phenyl group. Anionic surfactants in salt form may include alkali metal salts such as sodium or potassium salts, sodium salts, ammonium salts, amine salts and amino alcohol salts or alkaline earth metal salts such as magnesium salts. Exemplary amino alcohol salts are monoethanolamine, diethanolamine and triethanolamine salts, monoisopropanolamine, diisopropanolamine or triisopropanolamine salts, 2-amino-2-methyl-1-propanol salts, 2-amino-2 -methyl-1,3-propanediol salt and tris(hydroxymethyl)aminomethane salt.

Suitable anionic surfactants also include mild anionic surfactants, ie, anionic surfactants without sulfate functionality, including polyoxyalkylenated alkyl ether carboxylic acids; polyoxyalkylated alkylaryl ether carboxylic acids; polyoxyalkylenated alkylamido ether carboxylic acids, especially those containing from 2 to 50 ethylene oxide groups; alkyl-D-galactoside uronic acid; acyl sarcosinate, acyl glutamate; and alkylpolyglycoside carboxylic acid esters, such as those sold under the name AKYPO RLM 45 CA from Kao.

Exemplary suitable amphoteric or zwitterionic surfactant(s) are secondary or tertiary aliphatic amine derivatives that are optionally quaternized, wherein the aliphatic group is a linear or branched chain containing 8 to 22 carbon atoms, and the amine Derivatives are those containing at least one anionic group, for example a carboxylate, sulfonate, sulfate, phosphate or phosphonate group, such as (C ₈ -C ₂₀ )alkylbetaines, sulfobetaines, (C ₈ ) -C ₂₀ )alkylamido(C ₃ -C ₈ )alkylbetaine or (C ₈ -C ₂₀ )alkylamido(C ₆ -C ₈ )alkylsulfobetaine. Any suitable secondary or tertiary aliphatic amine derivative may be present in coconut oil or as hydrolyzed linseed oil and the like. Representative compounds are disodium cocoamphodiacetate, disodium lauroamphodiacetate, disodium caprylamphodiacetate, disodium capryloamphodiacetate, disodium cocoamphodipropionate, disodium lauroamphodipro Classified in the CTFA Dictionary (5th edition, 1993) under the names of cionate, disodium capryloamphodipropionate, disodium capryloamphodipropionate, lauroamphodipropionic acid, and cocoamphodipropionic acid.

By way of example, cocoamphodiacetate sold by the company Rhodia under the trade name MIRANOL C2M concentrate, and sodium diethylaminopropyl cocoaspartamide sold by the company Chimex under the name Chimexane HB are suitable for use in the disclosed compositions.

Suitable nonionic surfactants are described in Handbook of Surfactants by MR Porter, published by Blackie & Son (Glasgow and London), 1991, pp. 116-178, including fatty alcohols, fatty α-diols, fatty (C ₁ -C ₂₀ )alkylphenols and fatty acids, which may be ethoxylated, propoxylated or glycerolated and may be 8 to 18 may contain at least one fatty chain comprising carbon atoms, and the number of ethylene oxide or propylene oxide groups may range from 1 to 200, and the number of glycerol groups may range from 1 to 30. Condensates of fatty alcohols with ethylene oxide and propylene oxide, ethoxylated fatty amides with 1 to 30 ethylene oxide units, polyglycerolated fatty amides comprising on average 1 to 5, in particular 1.5 to 4 glycerol groups, 1 to 30 Ethoxylated fatty acid esters of sorbitan containing ethylene oxide units, fatty acid esters of sucrose, fatty acid esters of polyethylene glycol, (C ₆ -C ₂₄ )alkylpolyglycosides, oxyethylenated vegetable oils, N-(C ₆ ) -C ₂₄ )alkylglucamine derivatives, amine oxides such as (C ₁₀ -C ₁₄ )alkylamine oxide or N-(C ₁₀ -C ₁₄ )acylaminopropylmorpholine oxide are also for use in the compositions disclosed herein. Suitable.

Further suitable nonionic surfactants are alkyl polyglucosides (APG), maltose esters, polyglycerolated fatty alcohols, glucamine derivatives such as 2-ethylhexyloxycarbonyl-N-methylglucamine, and their mixtures. Alkylpolyglucosides are those containing an alkyl group containing 6 to 30 carbon atoms and containing a hydrophilic group (glucoside). Exemplary alkylpolyglucosides are the product sold under the name Mydol 10® by the company Kao Chemicals, the product sold under the name Plantaren 2000 UP® by the company Cognis, and the product sold under the name Oramix NS 10® by the company SEPPIC. decylglucoside (alkyl-C9/C11-polyglucoside (1.4)), including products that are laurylglucoside sold by the company Cognis as Plantaren 1200 N® and Plantacare 1200®, and cocoglucosides, for example the products sold under the name Plantacare 818/UP® by the company Cognis.

Suitable maltose derivatives are those described in document EP-A-566 438, such as O-octanoyl-6′-D-maltose or O-dodecanoyl-6′-D-maltose described in document FR-2 739 556 Includes toss. Each of these documents is incorporated by reference in its entirety.

In some embodiments, the hair care composition may be formulated in a cosmetically acceptable medium. The term “cosmetically acceptable medium” means a medium compatible with human keratin fibers, such as hair. The cosmetically acceptable medium can be from water or from lower alcohols such as ethanol and isopropanol; water and at least one cosmetically acceptable solvent selected from polyols and polyol ethers, including 2-butoxyethanol, propylene glycol, propylene glycol monomethyl ether, diethylene glycol monoethyl ether and monomethyl ether, and mixtures thereof It can be formed from a mixture with

In some embodiments, the hair care composition may further comprise any of the following additives, or mixtures thereof: solids different from fatty alcohols, such as waxes, anionic, nonionic or amphoteric polymers or mixtures thereof. Fatty substances, anti-dandruff agents, anti-seborrhoea agents, agents for preventing hair loss and/or promoting hair regrowth, and vitamins and provitamins, including panthenol, sunscreens, inorganic or organic pigments, sequestering agents, plasticizers, Solubilizers, acidifying agents, inorganic or organic thickeners, in particular polymeric thickeners different from oxyethylenated polymers, opacifying agents or pearlescent agents, antioxidants, hydroxy acids, fragrances and/or preservatives.

nail care

In some embodiments, the cosmetic composition may include ingredients commonly used in nail care products. Nail care products include, but are not limited to, nail strengtheners, nail treatments including top coats, and base coats, nail polishes, nail polish removers, hand skincare, foot skincare, desiccants, and correction pens including nail polish removers not limited

In some embodiments, the nail care composition may be a nail treatment composition. The nail treatment composition may include a composition for the treatment of an infested nail or nail deformity, a composition for the topical treatment of a nail infection, including a fungal infection, a nail enhancer, a top coat, a base coat, a polish remover, or any combination thereof. . In some embodiments, the nail treatment composition is a topical nail lacquer or polish, cream, solution, suspension, lotion, serum, gel, balm, gel, oil, oil in cream, and/or scrub for treating the hands and/or feet. It can be formulated as

In some embodiments, the nail treatment composition may be a nail strengthening agent. The nail hardener may treat the nails and toenails to harden, strengthen and promote growth of the nail and to prevent or minimize breakage, cracking, splitting and peeling;

Any used to prevent and heal quarter cracks while increasing horseshoe growth, having a protein consistency similar to human fingernails and toenails, including lanolin, butter, beeswax, rosin, copper acetate and turpentine Known compositions may be included. In some embodiments, the nail treatment composition may further comprise titanium dioxide, such as TI-PURE R900 from E.I.DuPont.

In some embodiments, the nail treatment composition may be a base coat. In some embodiments, the base coat is methyl methacrylate (MMA) to form a polymer composed of at least one polymer that provides adhesion, for example, polymethyl methacrylate (PMMA) and polymethacrylic acid (PMAA). ) and a polymer copolymerized from methacrylic acid (MAA), wherein the MAA monomer fraction can vary from 0 to 100%. In some embodiments, polymers suitable for use as a base coat are hydroxyethyl methacrylate (HEMA), hydroxypropyl methacrylate (HPMA), ethyl methacrylate (EMA), tetrahydrofurfuryl methacrylate ( THFMA), pyromellitic dianhydride di(meth)acrylate, pyromellitic dianhydride glyceryl dimethacrylate, pyromellitic acid dimethacrylate, methacroyloxyethyl maleate, 2-hydroxyethyl methacrylic rate/succinate, 1,3-glycerol dimethacrylate/succinate adduct, monoethyl methacrylate phthalate, and mixtures thereof. In some embodiments, the base coat may further comprise a non-reactive, solvent-soluble, film-forming polymer such as a cellulose ester such as cellulose acetate alkylate, cellulose acetate butyrate, or cellulose acetate propionate. The above exemplary components are not limiting.

In some embodiments, the nail treatment composition may be a top coat, such as a quick drying top coat. The top coat is a base resin that is cellulose acetate butyrate, a film former that is a methacrylate polymer, a monofunctional methacrylate and a crosslinker (i.e., bifunctional and trifunctional methacrylates).

a thermal or photoinitiator(s) included together in a solution of a thermosetting or photocurable monomer, a fatty ester and an alcohol, and a photoreactive coating. Suitable solvents include acetates and alcohols, particularly ethyl acetate, butyl acetate, and isopropyl alcohol. The photoreactive coating may comprise photoreactive monomers including the following methacrylate monomers: cyclohexyl methacrylate, n-decyl methacrylate, 2-ethyl hexyl methacrylate, ethyl methacrylate, hydride hydroxy propyl methacrylate, isobornyl methacrylate, 2-methoxy ethyl methacrylate; difunctional and trifunctional methacrylate monomers, crosslinking agents such as diurethane dimethacrylate, ethylene glycol dimethacrylate, 1,10-decanediol dimethacrylate, 1,6-hexanediol dimethacrylate, and Trimethylolpropane trimethacrylate. Commercially available photoinitiators suitable for use include benzoin methyl ether, 2-hydroxy-2-methyl-1-phenyl-1-propanone (“Darocur 1173”), diethoxyacetophenone, and benzyl dike including but not limited to masks. Photoinitiators are oligomeric mixtures of phenyl propanone, such as mixtures of 2,4,6-trimethylbenzophenone and 4-methylbenzophenone, and oligomers sold under the names "Esacure KIP 100F" and "Esacure TZT Photoinitiator" by Sartomer. is a mixture of -[2-hydroxy-2-methyl-1[4-(1-methylvinyl)phenyl]propanone] and 2-hydroxy-2-methyl-phenyl propanone

In some embodiments, the nail care composition may be a nail polish or a nail enamel composition. In some embodiments, the nail polish or nail enamel composition comprises a nitrocellulose film former, a latex film former, a polycarbodiimide film former, a low volatility organic compound (VOC), and a polycarbodiimide film former can be included as The polycarbodiimide may comprise a polymer having a plurality of carbodiimide groups added to the polymer backbone. For example, US Pat. No. 5,352,400, the disclosure of which is incorporated herein by reference, discloses polymers and copolymers derived from alpha-methylstyryl-isocyanate. Suitable polycarbodiimide compounds include those known under the name of the supplier Nisshinbo (CARBODILITE series, V-02, V02-L2, SV-02, E-02, V-10, SW-12G, E-03A); Picassian, and those sold commercially by 3M.

In some embodiments, the nail polish or nail enamel composition comprises a carboxyl functional acrylate latex polymer, a carboxyl functional polyurethane latex polymer, a carboxyl functional silicone latex polymer, a carboxyl functional non-acrylate latex polymer and these It may further comprise one or more latex polymers comprising a mixture of In various embodiments, suitable latex polymers can be film-forming latex polymers or non-film-forming latex polymers. In some embodiments, the latex polymer is prepared from vinyl monomers, (meth)acrylic monomers, (meth)acrylamide monomers, mono- and dicarboxylic unsaturated acids, esters of (meth)acrylic monomers, and amides of (meth)acrylic monomers. carboxyl functional acrylate latex polymers such as those resulting from homopolymerization or copolymerization of selected ethylenically unsaturated monomers. The term “(meth)acryl” and variations thereof, as used herein, means acrylic or methacryl. The (meth)acrylic monomer may be selected, for example, from acrylic acid, methacrylic acid, citraconic acid, itaconic acid, maleic acid, fumaric acid, crotonic acid, and maleic anhydride. Esters of (meth)acrylic monomers include, but are not limited to, C1-C8 alkyl (meth)acrylates such as methyl (meth)acrylate, ethyl (meth)acrylate, propyl (meth)acrylate, isopropyl (meth)acrylate ) acrylate, butyl (meth) acrylate, tert-butyl (meth) acrylate, pentyl (meth) acrylate, isopentyl (meth) acrylate, neopentyl (meth) acrylate, hexyl (meth) acrylate, Isohexyl (meth) acrylate, 2-ethylhexyl (meth) acrylate, cyclohexyl (meth) acrylate, isohexyl (meth) acrylate, heptyl (meth) acrylate, isoheptyl (meth) acrylate, octyl (meth)acrylate, isooctyl (meth)acrylate, allyl (meth)acrylate, and combinations thereof. Amides of (meth)acrylic monomers are for example

(meth)acrylamide, in particular N-alkyl (meth)acrylamide, in particular N-ethyl (meth)acrylamide, N-t-butyl (meth)acrylamide, N-t-octyl (meth)acrylamide, N-methylol (meth) ) such as acrylamide and N-diacetone (meth)acrylamide

N--(C1-C12)alkyl (meth)acrylates, and any combination thereof.

Vinyl monomers include vinyl cyanide compounds such as acrylonitrile and methacrylonitrile; vinyl esters such as vinyl formate, vinyl acetate, vinyl propionate, vinyl neodecanoate, vinyl pivalate, vinyl benzoate and vinyl t-butyl benzoate, triallyl cyanurate; vinyl halides such as vinyl chloride and vinylidene chloride; Aromatic mono- or divinyl compounds such as styrene, .alpha.-methylstyrene, chlorostyrene, alkylstyrene, divinylbenzene and diallyl phthalate, as well as para-styrenesulfonic acid, vinylsulfonic acid, 2-(meth)acrylic acid royloxyethylsulfonic acid, 2-(meth)acrylamido-2-methylpropylsulfonic acid, and mixtures thereof.

It should be understood that the list of monomers herein is not limiting and that any monomer known to those skilled in the art can be used, including acrylic and/or vinyl monomers (including monomers modified with silicone chains).

In some non-limiting exemplary embodiments, the carboxyl functional acrylate latex polymer is an aqueous dispersion of methacrylic acid/ethyl acrylate copolymer (INCI: acrylate copolymer such as LUVIFLEX SOFT from BASF), PEG/PPG- 23/6 dimethicone citraconate/C10-30 alkyl PEG-25 methacrylate/acrylic acid/methacrylic acid/ethyl acrylate/trimethylolpropane PEG-15 triacrylate copolymer (INCI: polyacrylate-2 crosslinked) Polymers such as Fixate Superhold.TM. from Lubrizol, styrene/acrylic copolymers such as Acudyne Shine from Dow Chemical, ethylhexyl acrylate/methyl methacrylate/butyl acrylate/acrylic acid/methacrylic acid copolymer (INCI: Acrylate/ethylhexyl acrylate copolymer such as Daitosol 5000SJ, Daito Kasei Kogyo), acrylic/acrylate copolymer (INCI name: acrylate copolymer such as Daitosol 5000AD, Daito Kasei Kogyo), acrylate copolymer such as trade name Acrylate/hydroxyester acrylate copolymer, Dow, known under the trade name Dermacryl AQF (Akzo Nobel), under the trade name LUVIMER MAE (BASF), or under the trade name BALANCE CR (AKZO NOBEL), under the trade name ACUDYNE 180 POLYMER (Dow Chemical) a styrene/acrylate copolymer known under the trade name Acudyne Bold by Chemical, a styrene/acrylate/ammonium methacrylate copolymer known under the trade name SYNTRAN PC5620 CG by Interpolymer, and mixtures thereof.

In some embodiments, the nail care composition may include a nail polish remover. The nail polish remover may include polyhydric alcohol compounds including glycerin, glycols, polyglycerin, esters of polyhydric alcohols, and mixtures thereof. Glycols may contain from 2 to 12 carbon atoms, such as, for example, glycerin, propylene glycol, butylene glycol, propane diol, hexylene glycol, polyglycerin, dipropylene glycol and diethylene glycol. Suitable esters of polyhydric alcohols include liquid esters of saturated or unsaturated, linear or branched C1-C26 polyhydric alcohols. Examples of suitable esters of polyhydric alcohols include, but are not limited to, esters of dihydroxy, trihydroxy, tetrahydroxy or pentahydroxy alcohols. Esters of polyhydric alcohols include glyceryl esters such as glyceryl triglycolate, glyceryl tricitrate, glyceryl trilactate, glyceryl trilactate, glyceryl tributanoate, glyceryl triheptanoate, glyceryl trioctanoate and the like.

The nail polish remover may further comprise a low carbon alcohol containing 1 to 8 carbon atoms. Low carbon alcohols may contain 2 to 6 carbon atoms, such as 2 to 5 carbon atoms. Examples of low carbon alcohols include, but are not limited to, ethanol, propanol, butanol, pentanol, isopropanol, isobutanol, and isopentanol. The nail polish remover may further include a high boiling ester compound including, but not limited to, carbonate esters, adipates, sebacates, and succinates. Exemplary high-boiling ester compounds include alkylene carbonates such as propylene carbonate, dimethyl succinate, diethyl succinate, dimethyl glutarate, diethyl glutarate, dimethyl sebacate, diethyl sebacate, diisopropyl Sebacate, bis(2-ethylhexyl)sebacate, dimethyl adipate, diisopropyl adipate, di-n-propyl adipate, dioctyl adipate, bis(2-ethylhexyl) adipate, diisoste Aryl adipate, ethyl maleate, bis(2-ethylhexyl) maleate, triisopropyl citrate, triisocetyl citrate, triisostearyl citrate, trioctyldodecyl citrate and trioleyl citrate including but not limited to.

Nail polish removers include nonionic, anionic, cationic, amphiphilic and amphoteric polymers, and other known rheology modifiers such as cellulosic thickeners such as hydroxyethylcellulose, hydroxypropylcellulose, methylcellulose, and ethylhydride. It may further include a thickener including, but not limited to, oxyethylcellulose. Certain notable cellulose derivatives include hydroxyl-modified cellulosic polymers such as hydroxyethylcellulose, for example those having a molecular weight of at least 500,000 Daltons, such as NATROSOL 250 HHR and hydroxypropyl cellulose, such as KLUCEL MF (two all available from Ashland, Covington, ky). The thickening agent may be a polysaccharide such as fructan, glucan, galactan and mannan or heteropolysaccharide such as hemicellulose, pullulan or branched polysaccharide such as gum arabic and amylopectin, or mixed polysaccharide such as starch. The thickener may be an acrylic thickener (acrylic thickener) or an acrylamide thickener (acrylamide thickener). The thickener may comprise at least one monomer that performs a weak acid function, such as acrylic acid, methacrylic acid, itaconic acid, crotonic acid, maleic acid and/or fumaric acid. The thickener may comprise a monomer having a function of a sulfonic acid type or a phosphonic acid type, for example a monomer performing a strong acid function such as 2-acrylamido-2-methylpropane sulfonic acid (AMPS). Thickeners include crosslinking agents such as methylene bisacrylamide (MBA), ethylene glycol diacrylate, polyethylene glycol dimethacrylate, diacrylamide, cyanomethacrylate, vinyloxyethacrylate or methacrylate, formaldehyde, glyoxal, and compositions of the glycidyl ether type such as ethylene glycol diglycidyl ether or epoxide. Suitable acrylic thickeners are disclosed in US Patent Application Publication Nos. 2004/0028637 and 2008/0196174, both of which are incorporated herein by reference. In some embodiments, the thickening agent may include organoclay (hydrophobically treated clay) or hydrophilic clay.

In some embodiments, the thickener may include an abrasive compound (polishing system). An “abrasive compound” is a compound capable of providing abrasion or mechanical exfoliation. The abrasive particles may include perlite, pumice stone, zeolite, hydrated silica, calcium carbonate, dicalcium phosphate dihydrate, calcium pyrophosphate, alumina, sodium bicarbonate, polylactic acid as well as synthetic polymeric materials such as polyethylene, polypropylene, polyethylene terephthalate, poly methylyl methacrylate or nylon. In certain embodiments, suitable hard abrasives include perlite, such as cosmetic grade perlite available from Imerys under the designation IMERCARE 270P-Scrub. In certain embodiments, the soft abrasive includes sugar, ground fruit kernels or shell powder, such as apricot kernels, coconut husk, or spherical wax (eg, carnauba jojoba); Arginine Shell Powder and the like.

In some embodiments, the nail care composition may further comprise additives commonly used in cosmetic compositions and known to those skilled in the art, including solvents, preservatives, fragrances, oils, waxes, surfactants, antioxidants, free radical scavengers, humectants, dispersants, defoamers, neutralizers, stabilizers, active ingredients selected from essential oils, UV screening agents, sunscreens, humectants, vitamins, proteins, ceramides, plant extracts, fibers, and the like, and mixtures thereof.

dietary composition

In some embodiments, the compositions described herein may be dietary compositions useful for providing collagen to a subject in need thereof. For example, and in some embodiments, consumption of a dietary composition described herein may provide health and/or skin benefits such as increasing collagen intake, alleviating joint pain, and improving skin health. . In certain embodiments, the composition may be in the form of a powder, capsule, liquid, or any other suitable form.

In some embodiments, the dietary composition may include one or more nutritional ingredients such as: ascorbic acid, biotin, chromium nicotinate, copper citrate, calcium D-pantothenate, cyanocobalamin, flaxseed, linum usitatissimum , folic acid, fructooligosaccharide (fiber), magnesium oxide, manganese citrate, maltodextrin, medium chain triglycerite, flavor, niacinnamide, potassium citrate, potassium iodide, riboflavin, sugarcane (saccharum officinarum), sodium molybdate dihydrate , Sodium Selenite (Selenium), Soy Protein Isolate, Stevia Leaf Extract/Stevia Rebaudiana, Thiamine HCl, Tricalcium Phosphate, Vitamin A Palmitate, Vitamin D3, Xanthan Gum, Zinc Citrate, Cellulose Gum, Guar Gum, Pyridoxine hydrochloride, salt, tocopherol, antioxidants such as resveratrol, CoQ10, acai berry, lycopene and pomegranate, natural or artificial sweeteners such as glucose, sucrose, fructose, saccharides, cyclamate, aspartamine, sucralose, aspartame, acetonitrile sulfam K, or sorbitol, flavorings such as flavored extracts, volatile oils, chocolate flavoring (eg, decaffeinated cocoa or chocolate substitutes such as chocolate, carob), peanut butter flavoring, cookie crumbs, vanilla, or any commercial fragrances available as , and any combination thereof.

In some embodiments, as mentioned above, the composition described herein may be in the form of an alcohol-based or water-based toner. Exemplary toner formulations are provided below.

alcohol toner

water-based toner

In some of the above-mentioned embodiments, the compositions described herein may be in the form of a cream, gel or serum. Exemplary cream, gel and serum formulations are provided below.

cream

gel

serum

In some embodiments described above, the composition described herein may be a shampoo or conditioner. Exemplary shampoo or conditioner formulations are provided below.

shampoo

conditioner for hair

D. Yeast strains

The present invention may use yeast to produce the collagen fragments described herein. In some embodiments, modified yeast can be used to produce collagen fragments. Suitable yeasts include the genera Pichia, Candida, Komatagaella, Hansenula, Cryptococcus, Saccharomyces, and combinations thereof. In some embodiments, the yeast may be from the genus Pichia . Yeast can be modified or hybridized. Hybridized yeast can be produced by breeding different strains of the same species, different species of the same genus, or strains of different genera. Examples of yeast strains suitable for producing the collagen fragments disclosed herein include Pichia pastoris, Pichia membranifaciens, Pichia deserticola, Pichia cephalocerea. cephalocereana), Pichia eremophila, Pichia myanmarensis, Pichia anomala, Pichia nakasei, Pichia siamensis , Pichia heedii, Pichia barkeri, Pichia norvegensis, Pichia thermomethanolica, Pichia stipites, P. Pichia subpelliculosa, Pichia exigua, Pichia occidentalis, Pichia cactophila, and the like.

In one embodiment, a Pichia pastoris strain can be engineered to express a codon-optimized polynucleotide encoding a collagen fragment.

In some embodiments, the collagen fragment encoded by the yeast host cell is fused to a polypeptide sequence that promotes its secretion from yeast. For example, the vector may encode a chimeric gene comprising a coding sequence for a collagen fragment fused to a sequence encoding a secreted peptide. Secretory sequences that can be used for this purpose include Saccharomyces alpha matching factor prepro sequence, Saccharomyces alpha matching factor pre sequence, PHO1 secretion signal, α-amylase from Aspergillus niger . signal sequence, protein with internal repeat 1 signal sequence, glucoamylase signal sequence from Aspergillus awamori, serum albumin signal sequence from Homo sapiens , Kluyveromyces maxianus ( Kluyveromcyes maxianus) derived inulinase signal sequence, Saccharomyces cerevisiae derived invertase signal sequence, Saccharomyces cerevisiae derived a killer protein signal sequence and a lysozyme signal sequence from Gallus gallus . Other secretory sequences known in the art may also be used.

In some embodiments, one or more of the following yeast promoters may be incorporated into a vector to promote transcription of mRNA encoding a protein of interest (eg, a collagen fragment). Promoters are known in the art, pAOX1, pDas1, pDas2, pPMP20, pCAT, pDF, pGAP, pFDH1, pFLD1, pTAL1, pFBA2, pAOX2, pRKI1, pRPE2, pPEX5, pTALDAK1, pFGH1, pADH2, pTPI , pPFK1, pGPM1, and pGCW14.

In some embodiments, a yeast terminator sequence is incorporated into a vector to terminate transcription of an mRNA encoding a protein of interest (eg, a collagen fragment). Terminators include AOX1 TT, Das1 TT, Das2 TT, AOD TT, PMP TT, Cat1 TT, TPI TT, FDH1 TT, TEF1 TT, FLD1 TT, GCW14 TT, FBA2 TT, ADH2 TT, FBP1 TT, and GAP TT. It is not limited thereto.

In some embodiments, the recombinant collagen fragments described herein are produced in a strain of genetically engineered yeast. In some embodiments, the yeast is Pichia pastoris .

In some embodiments, the yeast has been transformed with a plasmid (vector) comprising the nucleic acid sequence set forth in SEQ ID NO:973. In some embodiments, to improve recombinant protein expression, the yeast has been transformed again (ie, double transformed) with a second plasmid. In some embodiments, the yeast has been double transformed with a plasmid comprising the nucleic acid sequence set forth in SEQ ID NO:974.

In some embodiments, the recombinant collagen fragments described herein are prepared by a method comprising:

(i) fermenting the yeast strain in the fermentation broth;

(ii) recovering the recombinant collagen fragment secreted by the yeast strain from the fermentation broth; and

(iii) optionally purifying the recombinant collagen fragment.

In some embodiments, the recombinant collagen fragment may then be subjected to ex vivo hydroxylation.

In some embodiments, recombinant collagen fragments can be produced in strains of genetically engineered yeast. In some embodiments, the yeast may be Pichia pastoris . In some embodiments, yeast can be transformed with a plasmid comprising the nucleic acid sequence set forth in SEQ ID NO:973. In some embodiments, yeast can be double transformed with a plasmid comprising the nucleic acid sequence set forth in SEQ ID NO:974.

DNA can be introduced into yeast strains by electroporation. Transformants can be selected, for example, using host yeast cells that are auxotrophic for leucine, tryptophan, uracil or histidine along with selectable marker genes such as LEU2, TRP1, URA3, HIS3, or LEU2-D. The DNA sequence for the collagen fragment can be introduced into yeast via a vector, for example by electroporation. DNA can be inserted into the vector. Suitable vectors are pHTX1-BiDi-P4HA-Pre-P4HB hygro, pHTX1-BiDi-P4HA-PHO1-P4HB hygro, pGCW14-pGAP1-BiDi-P4HA-Prepro-P4HB G418, pGCW14-pGAP1-BiDi-P4HA-PHO1-P4HB Hygro , pDF-Col3A1 modified zeocin, pCAT-Col3A1 modified zeocin, pDF-Col3A1 modified zeocin with AOX1 landing pad, pHTX1-BiDi-P4HA-Pre-Pro-P4HB hygro. Vectors typically included at least one restriction site for linearization of DNA. Once within the yeast strain, DNA is inserted into the yeast genome and can be used to generate collagen fragments.

In some embodiments, the present invention provides a strain of yeast, eg, Pichia pastoris , that has been genetically engineered to produce a recombinant collagen fragment described herein, wherein the strain of yeast comprises a DNA sequence encoding the recombinant collagen fragment. It contains a vector containing. In some embodiments, the vector may comprise a nucleic acid sequence comprising the DNA sequence set forth in SEQ ID NO:973. In some embodiments, the vector may comprise a nucleic acid sequence comprising the DNA sequence set forth in SEQ ID NO:974. In some embodiments, the vector is inserted into the yeast via electroporation.

In some embodiments, the present invention provides a vector comprising a DNA sequence for producing a collagen fragment, wherein the vector comprises the nucleic acid sequence set forth in SEQ ID NO:973.

In some embodiments, the present invention provides a vector comprising a DNA sequence for producing a collagen fragment, wherein the vector comprises the nucleic acid sequence set forth in SEQ ID NO:974.

In some embodiments, the present invention provides a strain of collagen fragment-producing yeast comprising a vector comprising a DNA sequence for producing a recombinant collagen fragment described herein.

Promoters can improve production of the recombinant protein and can be included in a vector comprising a sequence encoding a protein of interest (eg, a collagen fragment described herein). Promoters suitable for use in preparing the collagen fragments disclosed herein include AOX1 methanol-inducible promoter, pDF de-repression promoter, pCAT de-repression promoter, Das1-Das2 methanol-induced bidirectional promoter, pHTX1 constitutive bidirectional promoter, pGCW14-pGAP1 constitutive bidirectional promoter. promoters and combinations thereof. Suitable methanol inducible promoters include, but are not limited to, AOX2, Das 1, Das 2, pDF, pCAT, pPMP20, pFDH1, pFLD1, pTAL2, pFBA2, pPEX5, pDAK1, pFGH1, pRKI1, pREP2, and combinations thereof.

A terminator may be placed at the end of each open reading frame used for vectors incorporated in yeast. A DNA sequence for the terminator may be inserted into the vector. In the case of replication vectors, an origin of replication is required to initiate replication. The DNA sequence for the origin of replication is inserted into the vector. One or more DNA sequences containing homology to the yeast genome may be incorporated into the vector to facilitate recombination and incorporation into the yeast genome or to stabilize the vector once transformed into yeast cells.

The vector may also include at least one selection marker that is generally used to select for successfully transformed yeast cells. Markers are sometimes associated with antibiotic resistance, and markers may also be associated with the ability to grow with or without specific amino acids (nutritional markers). Suitable auxotrophic markers include, but are not limited to, ADE, HIS, URA, LEU, LYS, TRP, and combinations thereof. To provide for selection of yeast cells containing the recombinant vector, at least one DNA sequence for a selection marker may be incorporated into the vector.

The engineered yeast cells described above can be used as hosts to produce the collagen fragments described herein. To do so, cells may be placed in a medium in a fermentation chamber supplied with dissolved oxygen and a carbon source (eg, glycerol) under controlled pH conditions for a period ranging from 12 hours to 1 week. Suitable media include, but are not limited to, buffered glycerol complex medium (BMGY), buffered methanol complex medium (BMMY), and yeast extract peptone dextrose (YPD).

E. How to use

Increased intracellular collagen production

The present inventors have surprisingly found that the collagen fragments described in the present invention can induce the production of type I and type III collagen in cells such as fibroblasts. Thus, when applied to cells such as fibroblasts or other suitable cells, the collagen fragments described herein (i.e., the collagen fragment having the amino acid sequence of SEQ ID NO: 1 or SEQ ID NO: 986 or compositions comprising such fragments) advantageously It can induce collagen formation in the cells to which it is applied.

Accordingly, in some embodiments, the present invention provides a method of increasing collagen production in a cell comprising administering to the cell a collagen fragment described herein. Such administration may consist of directly exposing the cells to the collagen fragments in an amount sufficient to induce the cells to produce higher amounts of collagen. In some embodiments, the method comprises administering the collagen fragment as part of a composition comprising the collagen fragment and at least one pharmaceutically acceptable excipient. In some embodiments, the collagen fragment may be administered to a cell in its native context, such as in an organism or tissue. In some embodiments, the collagen fragments may be topically applied to the skin. In some embodiments, the collagen fragments may be topically applied to human skin. In some embodiments, the collagen fragment may be administered to the cultured cells as part of the culture medium.

In some embodiments, the cell may be a fibroblast. In some embodiments, the cell may be a fibroblast in its native context (eg, in human skin). In some embodiments, the cell may be a primary human fibroblast. In some embodiments, the cell may be a muscle cell, a transformed human cell, a cardiomyocyte, an endothelial cell, a stem cell, or an induced pluripotent stem cell.

In some embodiments, a recombinant collagen fragment disclosed herein, or a composition comprising one or more fragments, is administered to a cut, laceration, cut, tear, abrasion, abrasion or It can be applied to wounds such as scratches. As part of the wound healing process, fibroblasts migrate to the wound site and produce the necessary collagen for wound repair. The cells eventually fill the wound cavity with a network of interlaced strands of collagen, which sooner or later arrange themselves into rigid bands and form permanent new tissue. Thus, in some embodiments, the recombinant collagen fragment according to SEQ ID NO: 1 or SEQ ID NO: 986 or a composition comprising said fragment is cut, lacerated, cut, torn to increase collagen production at the site of a wound and/or tissue surrounding it. , can be applied to wounds such as abrasions, abrasions or scratches. In some embodiments, one or more hydrolysis products of a recombinant collagen fragment according to SEQ ID NO: 1 or SEQ ID NO: 986 or a composition comprising such hydrolysis products are cleaved to increase collagen production at the wound site and/or surrounding tissues thereof , can be applied to wounds such as lacerations, cuts, tears, abrasions, abrasions or scratches. In some embodiments, a composition comprising a mixture of a recombinant collagen fragment according to SEQ ID NO: 1 or SEQ ID NO: 986 and one or more hydrolysates thereof is used to increase collagen production at the wound site and/or surrounding tissues thereof by cutting, laceration, and/or tearing. , can be applied to wounds such as cuts, tears, abrasions, abrasions or scratches.

Accordingly, in certain embodiments, the present invention provides a composition comprising recombinant collagen fragments, hydrolysis products of recombinant collagen fragments, or a combination thereof to a wound, such as a cut, laceration, cut, tear, abrasion, abrasion, or scratch. provide a way In certain embodiments, the wound may be that of a human subject. In some embodiments, the method comprises providing a composition for promoting collagen production and wound healing in the skin of a subject in need thereof, wherein the composition comprises a recombinant collagen fragment described herein (e.g., fragment comprising SEQ ID NO: 1 or SEQ ID NO: 986). In some embodiments, the method comprises providing a composition for promoting collagen production and wound healing in the skin of a subject in need thereof, wherein the composition comprises hydrolysis of one or more recombinant collagen fragments described herein. products (eg, hydrolysis products comprising one or more of SEQ ID NOs: 2-972). In some embodiments, the method comprises providing a composition for promoting collagen production and wound healing in the skin of a subject in need thereof, wherein the composition comprises a recombinant collagen fragment and its composition, as described herein. mixtures of one or more hydrolysis products of recombinant collagen fragments (eg, a mixture of fragments comprising SEQ ID NO: 1 or SEQ ID NO: 986 and hydrolysis products comprising SEQ ID NOs: 2-972).

In some embodiments, the method may comprise administering to the cell a collagen fragment having the amino acid sequence of SEQ ID NO: 1 or SEQ ID NO: 986. In some embodiments, the method comprises administering to a cell a hydrolysis product resulting from hydrolysis of a collagen fragment having the amino acid sequence of SEQ ID NO: 1 or SEQ ID NO: 986 (e.g., having the sequence according to SEQ ID NO: 2-972) administering one or more hydrolysis products). In some embodiments, the method comprises administering to the cell a recombinant collagen fragment described herein and one or more hydrolysis products of the recombinant collagen fragment. In some embodiments, the method comprises administering to the cell a collagen fragment having the amino acid sequence of SEQ ID NO: 1 or SEQ ID NO: 986, and one or more hydrolysis products of the fragment having the sequence according to SEQ ID NO: 2-972 can do.

In some embodiments, the method can increase the production of type I collagen. In some embodiments, the method can increase the production of type III collagen. In some embodiments, the method can increase the production of both type I and type III collagen.

skin care

In some embodiments, a composition described herein can be a skin care composition that can be used to treat an area of skin by topically applying the skin care composition to the skin area.

In some embodiments, the compositions described herein can be skin care compositions that can be used to treat skin, hair and nails by consuming the composition as a dietary supplement.

In some embodiments, administration to the skin of a composition described herein can improve or maintain the quality of the skin and reduce or eliminate signs of aging. Signs of aging include, but are not limited to, all externally visible and tactile signs as well as any other macroscopic or microscopic effects due to skin aging. These signs may be induced or caused by intrinsic or extrinsic factors (eg, age-related aging and/or environmental damage). These signs include the occurrence of structural breaks, such as wrinkles and thick and deep wrinkles, fine lines, skin folds, crevices, bumps, large pores (eg, associated with adnexal structures such as sweat ducts, sebaceous glands or hair follicles), or unevenness or roughness, loss of skin elasticity (loss and/or inactivation of functional skin elastin), sagging (including swelling around the eyes and chin), loss of skin firmness, loss of skin tightness, loss of skin recoil from deformation, discoloration (under the eyes) including circles), spots, paleness, hyperpigmented skin areas such as age spots and freckles, keratosis, abnormal differentiation, hyperkeratosis, elastofibrosis, collagen degradation, and stratum corneum, dermis, epidermis, skin vasculature (e.g., telangiectasia or spider blood vessels) and other histological changes in underlying tissues (fat and/or muscle), particularly those closest to the skin.

In some embodiments, the present invention provides a method of treating a dermatological condition comprising administering to a subject in need thereof an effective amount of a composition comprising recombinant collagen fragments. In some embodiments, the dermatological condition is fine lines, wrinkles, dry skin, excessive pore size, skin abnormalities, loss of elasticity, unwanted hair, thinning skin, purpura, actinic keratosis, pruritus, eczema, acne, rosacea, erythema, capillary vasodilation, actinic telangiectasia, skin cancer, or rhinitis.

In some embodiments, the composition may be administered topically to a skin region. In some embodiments, the skin region is the facial surface, scalp, neck, ears, shoulders, chest (including breast and/or décolletage), arms, hands, legs, stomach, buttocks, groin, back, feet, and combinations thereof It can be selected from the group consisting of.

In some embodiments, the composition may be administered topically to the facial surface. In some embodiments, the facial surface may be selected from the group consisting of forehead, eyes, periorbital surface, chin surface, per orbital surface, nasal surface, buccal skin surface, and combinations thereof.

In some embodiments, the present invention provides a method of improving collagen production in the skin comprising administering an effective amount of a composition comprising recombinant collagen fragments.

In some embodiments, the present invention is used for reducing the appearance of wrinkles, evening the skin tone, providing moisture, reducing the appearance of dark circles under the eyes, increasing the collagen content of the skin, For increasing skin density, improving skin firmness and elasticity, improving the appearance of lines and wrinkles, smoothing skin texture, increasing skin radiance and radiance, improving the appearance of sagging skin Provided is a skin care product comprising a composition described herein for use in lightening skin, lightening skin, or any combination thereof.

embodiment

E1. A recombinant collagen fragment having a molecular weight of about 40 kDa to about 60 kDa.

E2. The recombinant collagen fragment of embodiment 1 having a molecular weight of about 50 kDa.

E3. The recombinant collagen fragment of embodiment 1 or 2, wherein the collagen fragment has a length of about 350 amino acids to about 530 amino acids.

E4. The recombinant collagen fragment according to any one of embodiments 1-3, wherein the recombinant collagen fragment has a length of 528 amino acids.

E5. The recombinant collagen fragment according to any one of embodiments 1-4, wherein the recombinant collagen fragment is not hydroxylated.

E6. The recombinant collagen fragment according to any one of embodiments 1-4, wherein the recombinant collagen fragment is hydroxylated.

E7. The recombinant collagen fragment according to any one of embodiments 1 to 6, wherein the collagen fragment has an amino acid sequence according to one of SEQ ID NOs: 1 to 972.

E8. The recombinant collagen fragment of embodiment 7, wherein the collagen fragment has the amino acid sequence set forth in SEQ ID NO: 1.

E9. A composition comprising the recombinant collagen fragment of any one of embodiments 1-8.

E10. The composition according to embodiment 9, wherein the collagen fragment has an amino acid sequence according to one of SEQ ID NOs: 2 to 972.

E11. The composition of embodiment 9, wherein the one or more peptides are formed from hydrolysis of a recombinant collagen fragment having the amino acid sequence according to SEQ ID NO: 1.

E12. The composition of embodiment 11, wherein the composition further comprises one or more peptides formed from hydrolysis of the recombinant collagen fragment.

E13. The composition according to embodiment 12, wherein the one or more peptides have an amino acid sequence according to one of SEQ ID NOs: 2-972.

E14. The composition of any one of embodiments 9-13, wherein the one or more peptides have a length of between 10 amino acids and 50 amino acids.

E15. The composition of any one of embodiments 9-14, further comprising a pharmaceutically acceptable or cosmetically acceptable excipient.

E16. A cosmetic composition comprising the recombinant collagen fragment of any one of embodiments 1 to 8 and a cosmetically acceptable carrier.

E17. The recombinant collagen of any one of embodiments 1-8, wherein the recombinant collagen fragment is produced in a strain of genetically engineered yeast.

E18. The recombinant collagen fragment of embodiment 17, wherein the yeast is Pichia pastoris .

E19. The recombinant collagen fragment of embodiment 17 or 18, wherein the yeast is transformed with a plasmid comprising the nucleic acid sequence set forth in SEQ ID NO:973.

E20. The recombinant collagen fragment according to any one of embodiments 17 to 19, wherein the yeast is double transformed with a plasmid comprising the nucleic acid sequence set forth in SEQ ID NO: 974.

E21. The recombinant collagen fragment of any one of embodiments 1-7, wherein the recombinant collagen is prepared using a method comprising:

(i) fermenting the genetically engineered yeast in a fermentation broth;

(ii) recovering the recombinant collagen fragment secreted by the genetically engineered yeast from the fermentation broth; and

(iii) optionally purifying the recombinant collagen fragment.

E22. The recombinant collagen fragment of embodiment 21, wherein the method further comprises in vitro hydroxylation of the recombinant collagen fragment.

E23. A method for producing the recombinant collagen fragment of any one of embodiments 1 to 8, comprising producing the recombinant collagen fragment in a strain of genetically engineered yeast.

E24. The method of embodiment 23, wherein the yeast is Pichia pastoris .

E25. The method of embodiment 23 or 24, wherein the yeast is transformed with a plasmid comprising the nucleic acid sequence set forth in SEQ ID NO:973.

E26. The method according to any one of embodiments 23 to 26, wherein the yeast is a yeast doubly transformed with a plasmid comprising the nucleic acid sequence set forth in SEQ ID NO: 974.

E27. The method according to any one of embodiments 23 to 26, comprising the steps of:

(i) fermenting the genetically engineered yeast in a fermentation broth;

(ii) recovering the recombinant collagen fragment secreted by the genetically engineered yeast from the fermentation broth; and

(iii) optionally purifying the recombinant collagen fragment.

E28. The method of embodiment 27, further comprising hydroxylating the recombinant collagen fragment ex vivo.

E29. A strain of yeast genetically engineered to produce the recombinant collagen fragment of any one of embodiments 1-8, wherein the strain of yeast comprises a vector comprising a DNA sequence encoding the recombinant collagen.

E30. The strain of yeast according to embodiment 29, wherein the vector comprises a nucleic acid sequence comprising the DNA sequence set forth in SEQ ID NO:973.

E31. The strain of yeast according to embodiment 30, further comprising a second vector comprising a nucleic acid sequence comprising the DNA sequence set forth in SEQ ID NO:974.

E32. The strain of yeast according to any one of embodiments 29 to 31, wherein the vector is inserted into the yeast via electroporation.

E33. The strain of yeast according to any one of embodiments 29 to 32, wherein the strain of yeast is Pichia pastoris .

E34. A vector comprising a DNA sequence for producing a collagen fragment, wherein the vector comprises the nucleic acid sequence set forth in SEQ ID NO:973.

E35. A vector comprising a DNA sequence for producing a collagen fragment, wherein the vector comprises the nucleic acid sequence set forth in SEQ ID NO:974.

E36. A strain of collagen-producing yeast comprising a vector comprising a DNA sequence for producing the recombinant collagen fragment of any one of embodiments 1-8.

E37. A method of treating a dermatological condition comprising administering to a subject in need thereof an effective amount of the composition of any one of embodiments 9-16.

E38. The dermatological condition of embodiment 37, wherein the dermatological condition is fine lines, wrinkles, dry skin, excessive pore size, skin discoloration, loss of elasticity, unwanted hair, thinning skin, purpura, actinic keratosis, pruritus, eczema, acne, rosacea, erythema, telangiectasia, actinic telangiectasia, skin cancer, or rhinitis.

E39. The method of embodiment 37 or 38, wherein the composition is administered topically to a skin region.

E40. The skin region of embodiment 39, wherein the skin region is the facial surface, scalp, neck, ears, shoulders, chest (including breast and/or décolletage), arms, hands, legs, belly, buttocks, groin, back, feet and their selected from the group consisting of combinations.

E41. The method of embodiment 40, wherein the composition is administered topically to a facial surface.

E42. The method of embodiment 41, wherein the facial surface is selected from the group consisting of forehead, eye, periorbital surface, chin surface, periorbital surface, nasal surface, buccal skin surface, and combinations thereof.

E43. A method of improving skin comprising administering to a subject in need thereof an effective amount of the composition of any one of embodiments 9-16.

E44. The skin of embodiment 43, wherein the skin is characterized by fine lines, wrinkles, dryness, excessive pore size, skin discoloration, reduced elasticity, unwanted hair, thinning skin, purpura, actinic keratosis, pruritus, eczema, acne, rosacea, erythema, capillaries ectasia, actinic telangiectasia, skin cancer, or rhinitis.

E45. The method of embodiment 43 or 44, wherein the administering is topical.

E46. A method of increasing collagen production in a cell comprising administering to the cell an effective amount of the fragment of any one of embodiments 1-8.

E47. The method of embodiment 46, wherein the method increases production of type I collagen.

E48. The method of embodiment 46 or 47, wherein the method increases the production of type III collagen.

E49. The method of any one of embodiments 46-48, wherein the cell is a fibroblast.

E50. The method of any one of embodiments 46-49, wherein the cells are cultured cells.

E51. The method of any one of embodiments 46-50, wherein the administering is to a human.

E52. The method of embodiment 51, wherein the administering is topical administration to the skin.

E53. The skin region of embodiment 52, wherein the skin region is the facial surface, scalp, neck, ears, shoulders, chest (including breast and/or décolletage), arms, hands, legs, belly, buttocks, groin, back, feet and their selected from the group consisting of combinations.

E54. The method of any one of embodiments 46-48, wherein the fragment is formulated into a composition.

E55. The method of embodiment 54, wherein the composition is administered topically to a facial surface.

E56. The method of embodiment 55, wherein the facial surface is selected from the group consisting of forehead, eye, periorbital surface, chin surface, periorbital surface, nasal surface, buccal skin surface, and combinations thereof.

E57. For reducing the appearance of wrinkles, evening the skin tone, providing moisture, reducing the appearance of dark circles under the eyes, increasing the collagen content of the skin, increasing skin density, skin For improving firmness and elasticity, for improving the appearance of lines and wrinkles, for smoothing skin texture, for increasing skin radiance and radiance, for improving the appearance of sagging skin, for whitening skin, or A skin care product comprising the composition of any one of embodiments 9 to 16 for use in any combination thereof.

E58. A method of treating a wound in a human subject in need thereof, comprising applying the composition of any one of embodiments 9 to 16 to the wound of the subject, wherein applying the recombinant collagen fragment comprises human type I collagen. , inducing the production of human type III collagen or a combination thereof.

E59. The method of embodiment 58, wherein the collagen fragment is topically applied to the wound.

E60. The recombinant collagen fragment according to any one of embodiments 1 to 6, wherein the collagen fragment has an amino acid sequence according to one of SEQ ID NO: 986.

E61. A composition comprising the recombinant collagen fragment of any one of embodiment 60.

E62. The composition of embodiment 61, wherein the one or more peptides are formed from hydrolysis of a recombinant collagen fragment having the amino acid sequence according to SEQ ID NO: 986.

E63. The composition of embodiment 62, wherein the composition further comprises one or more peptides formed from hydrolysis of the recombinant collagen fragment.

E64. The composition according to embodiment 63, wherein the one or more peptides have an amino acid sequence according to one of SEQ ID NO: 2 to SEQ ID NO: 972.

E65. The composition of any one of embodiments 62-64, wherein the one or more peptides have a length of between 10 amino acids and 50 amino acids.

E66. The composition of any one of embodiments 61-65, further comprising a pharmaceutically acceptable or cosmetically acceptable excipient.

E67. A cosmetic composition comprising the recombinant collagen fragment of any one of embodiment 60 and a cosmetically acceptable carrier.

E68. The recombinant collagen of any one of embodiment 60, wherein the recombinant collagen fragment is produced in a strain of genetically engineered yeast.

E69. The recombinant collagen fragment of embodiment 68, wherein the yeast is Pichia pastoris .

E70. The recombinant collagen fragment of embodiment 68 or 69, wherein the yeast is transformed with a plasmid comprising the nucleic acid sequence set forth in SEQ ID NO:973.

E71. The recombinant collagen fragment according to any one of embodiments 68 to 70, wherein the yeast is double transformed with a plasmid comprising the nucleic acid sequence set forth in SEQ ID NO:974.

E72. The recombinant collagen fragment of embodiment 60, wherein the recombinant collagen is prepared using a method comprising:

(i) fermenting the genetically engineered yeast in a fermentation broth;

(ii) recovering the recombinant collagen fragment secreted by the genetically engineered yeast from the fermentation broth; and

(iii) optionally purifying the recombinant collagen fragment.

E73. The recombinant collagen fragment of embodiment 72, wherein the method further comprises in vitro hydroxylation of the recombinant collagen fragment.

E74. A method for producing the recombinant collagen fragment of embodiment 60, comprising the step of producing the recombinant collagen fragment in a strain of genetically engineered yeast.

E75. The method of embodiment 74, wherein the yeast is Pichia pastoris .

E76. The method of embodiment 74 or embodiment 75, wherein the yeast is transformed with a plasmid comprising the nucleic acid sequence set forth in SEQ ID NO:973.

E77. The method according to any one of embodiments 72 to 75, wherein the yeast is a yeast doubly transformed with a plasmid comprising the nucleic acid sequence set forth in SEQ ID NO: 974.

E78. The method according to any one of embodiments 72 to 77, comprising the steps of:

(i) fermenting the genetically engineered yeast in a fermentation broth;

(ii) recovering the recombinant collagen fragment secreted by the genetically engineered yeast from the fermentation broth; and

(iii) optionally purifying the recombinant collagen fragment.

E79. The method of embodiment 78, further comprising hydroxylating the recombinant collagen fragment ex vivo.

E80. A strain of yeast genetically engineered to produce the recombinant collagen fragment of embodiment 60, wherein the strain of yeast comprises a vector comprising a DNA sequence encoding the recombinant collagen.

E81. The strain of yeast according to embodiment 80, wherein the vector comprises a nucleic acid sequence comprising the DNA sequence set forth in SEQ ID NO:973.

E82. The strain of yeast of embodiment 81, further comprising a second vector comprising a nucleic acid sequence comprising the DNA sequence set forth in SEQ ID NO:974.

E83. The strain of yeast according to any one of embodiments 80 to 82, wherein the vector is inserted into the yeast via electroporation.

E84. The strain of yeast according to any one of embodiments 80 to 83, wherein the strain of yeast is Pichia pastoris .

E85. A strain of collagen-producing yeast comprising a vector comprising a DNA sequence for producing the recombinant collagen fragment of embodiment 60.

E86. A method of treating a dermatological condition comprising administering to a subject in need thereof an effective amount of the composition of any one of embodiments 61-67.

E87. The dermatological condition of embodiment 86, wherein the dermatological condition is fine lines, wrinkles, dry skin, excessive pore size, skin discoloration, loss of elasticity, unwanted hair, thinning skin, purpura, actinic keratosis, pruritus, eczema, acne, rosacea, erythema, telangiectasia, actinic telangiectasia, skin cancer, or rhinitis.

E88. The method of embodiment 86 or 87, wherein the composition is administered topically to a skin region.

E89. The skin region of embodiment 88, wherein the skin region is the facial surface, scalp, neck, ears, shoulders, chest (including breast and/or décolletage), arms, hands, legs, belly, buttocks, groin, back, feet and their selected from the group consisting of combinations.

E90. The method of embodiment 89, wherein the composition is administered topically to a facial surface.

E90. The method of embodiment 90, wherein the facial surface is selected from the group consisting of forehead, eye, periorbital surface, chin surface, periorbital surface, nasal surface, buccal skin surface, and combinations thereof.

E92. A method of improving skin comprising administering to a subject in need thereof an effective amount of the composition of any one of embodiments 61-67.

E93. The skin of embodiment 92, wherein the skin is characterized by fine lines, wrinkles, dryness, excessive pore size, skin abnormalities, reduced elasticity, unwanted hair, thinning skin, purpura, actinic keratosis, pruritus, eczema, acne, rosacea, erythema, capillaries ectasia, actinic telangiectasia, skin cancer, or rhinitis.

E94. The method of embodiment 92 or 93, wherein the administering is topical.

E95. A method of increasing collagen production in a cell comprising administering to the cell an effective amount of the fragment of embodiment 60.

E96. The method of embodiment 95, wherein the method increases production of type I collagen.

E97. The method of embodiment 95 or 96, wherein the method increases the production of type III collagen.

E98. The method of any one of embodiments 95-97, wherein the cell is a fibroblast.

E99. The method of any one of embodiments 95-98, wherein the cells are cultured cells.

E100. The method of any one of embodiments 95-99, wherein the administering is to a human.

E101. The method of embodiment 100, wherein the administering is topical administration to the skin.

E102. The skin region of embodiment 101, wherein the skin region is the facial surface, scalp, neck, ears, shoulders, chest (including breast and/or décolletage), arms, hands, legs, belly, buttocks, groin, back, feet and their selected from the group consisting of combinations.

E103. The method of any one of embodiments 95-97, wherein the fragment is formulated into a composition.

E104. The method of embodiment 103, wherein the composition is administered topically to a facial surface.

E105. The method of embodiment 104, wherein the facial surface is selected from the group consisting of forehead, eye, periorbital surface, chin surface, periorbital surface, nasal surface, buccal skin surface, and combinations thereof.

E106. For reducing the appearance of wrinkles, evening the skin tone, providing moisture, reducing the appearance of dark circles under the eyes, increasing the collagen content of the skin, increasing skin density, skin For improving firmness and elasticity, for improving the appearance of lines and wrinkles, for smoothing skin texture, for increasing skin radiance and radiance, for improving the appearance of sagging skin, for whitening skin, or A skin care product comprising the composition of embodiment 60 for use in any combination thereof.

E107. A method of treating a wound in a human subject in need thereof, comprising the step of applying the composition of embodiment 60 to the wound of the subject, wherein applying the recombinant collagen fragment comprises human type I collagen, human type III collagen or these A method of inducing the generation of a combination of

E108. The method of embodiment 107, wherein the collagen fragment is topically applied to the wound.

Example

Example 1: Producing Cleaved Human Collagen III Fragments pichia generation of strains

A plasmid encoding a secretory signal-secreted 50 kDa human collagen (“50 kDa human collagen fragment”) having an amino acid sequence according to SEQ ID NO: 986, designated as vector A and shown in FIG. 1 , is zeocin resistant as follows: composed. To generate the secretion signal fragment, the vector of SEQ ID NO: 984 was amplified through polymerase chain reaction (PCR) with primer 1 (SEQ ID NO: 975) and primer 2 (SEQ ID NO: 976). PCR was performed using PHUSION, using 25 cycles of 95°C for 30 seconds, 60°C for 30 seconds, and 72°C for 15 seconds, followed by an initial denaturation of 2 minutes at 95°C, and a final extension at 72°C for 5 minutes. PLUS DNA POLYMERASE. To generate a 50 kDa collagen fragment comprising amino acids according to SEQ ID NO: 986, the vector of SEQ ID NO: 985 was amplified via PCR with primers 3 and 4 (SEQ ID NO: 981 and SEQ ID NO: 977), respectively. PCR was performed using 25 cycles of 95°C for 30 seconds, 60°C for 30 seconds, and 72°C for 1 minute after an initial denaturation of 2 minutes at 95°C, and a final extension at 72°C for 5 minutes. . The backbone of the MMV132 vector (see U.S. 2019/0040400, incorporated herein by reference in its entirety) was digested with Mly I restriction endonuclease. All DNA fragments were purified by agarose gel electrophoresis. Fragments were assembled using Gibson Assembly® Master Mix (New England BioLabs).

The resulting circular plasmid DNA was transformed into DH5α E. coli. Zeocin-resistant transformants were obtained after overnight growth at 37°C. The 50 kDa collagen fragment construct was confirmed by Sanger sequencing. Plasmid DNA from positive clones was purified by PureLink™ HiPure Plasmid Midiprep Kit (Invitrogen). DNA was linearized by Swa I digestion.

For the expression of the 50 kDa collagen fragment, the linearized plasmid was transformed into the PP97 Komagataella phaffii strain by electroporation with the BIO-RAD GENE PULSER XCELL Total System. Transformants were grown at 30° C. on YPD agar containing 1M sorbitol and 500 μg/mL zeocin. The resulting strain containing a 50 kDa human collagen fragment under zeocin resistance was designated as Pichia strain 1.

To further improve recombinant protein expression, a second transformation of the 50 kDa human collagen fragment construct was performed with a norseothricin N-acetyl transferase (NAT) marker. First, molecular cloning was performed to generate the necessary plasmid DNA. A new vector encoding the signal sequence, 50 kDa human collagen fragment, NAT and beta-lactamase, designated vector B, was generated as follows (see FIG. 2 ). Vector A (FIG. 1) was digested with Xba I and Eco RV restriction enzymes. The vector of SEQ ID NO: 983 containing NAT resistance was digested with Nde I and Bsa I restriction enzymes. A 50 kDa human collagen fragment and a vector fragment containing NAT resistance were each purified from an agarose gel. The fragments were ligated via Gibson assembly to transform into DH5α competent E. coli. For carbenicillin-resistant transformants, a 50 kDa human collagen fragment construct was confirmed by Sanger sequencing. Plasmid DNA was purified via midiprep, linearized with Swa I restriction enzyme, and transformed into Pichia strain 1. The resulting double transformed strain was designated as Pichia strain 2.

To identify Pichia clones with high expression levels, small-scale cultures were grown for 40 hours in 96 deep well blocks. Cells were pelleted by centrifugation and the supernatant was harvested. Recombinant protein expression was assessed via sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Western blotting was performed using customized primary antibodies against C-telopeptide of collagen (Abmart) and IRDye® 800CW goat anti-mouse IgG secondary antibody (LI-COR).

Screening for collagen production was performed by a sandwich enzyme-linked immunosorbent assay (ELISA). This assay uses the aforementioned custom C-tello antibody as capture antibody (Abmart) and a commercially available detection antibody, anti-COL3A horseradish peroxidase-conjugate (sc-271249, Santa Cruz). A signal was generated by 3,3',5,5'-tetramethylbenzidine (TMB) and the reaction was stopped with 2M sulfuric acid. Signals were detected by measuring absorbance at 450 nm with a spectrophotometer. Using this method, Pichia strain 3 was selected as the best clone.

Example 2: Fermentation of selected clones

The three-step fermentation process was started by propagating Pichia strain 3 clones in shake flasks, followed by seed fermentation lasting approximately 23-27 hours, which was then used for seeding into production fermentors. The production fermentor ran for about 72 hours with a 24 hour batch step followed by a 48 hour feed-batch step. Glycerol was used as the carbon source and a glycerol feed was started at the end of the batch phase to maintain a constant maximum OTR value of 150 mmol/L per hour. An OTR of 150 mmol per L per hour was maintained by a constant glycerol feed and by adjusting the initial pressure to 800 mbar overpressure and 1 vvm aeration. The pH was controlled to 6±0.05 by automated addition of 25% ammonium hydroxide, and the temperature and DO were controlled at 32° C. and 25% (saturated at 800 mbar overpressure), respectively. Samples were taken throughout the fermentation and the OD ₆₀₀ , wet cell weight, dry weight, residual nitrogen, and residual glycerol were measured. (FIGS. 3A-3D).

Example 3: Purification of cleaved human collagen III fragments

Fermentation supernatant recovery

The fermentation broth contained a supernatant containing secreted 50 kDa human collagen (“50 kDa human collagen fragment”) having the amino acid sequence according to SEQ ID NO: 986, first recovered via centrifugation. Depending on the scale of the process, the supernatant was recovered by batch centrifugation using a Sorvall centrifuge (10 min, 10° C., 17568 x g) or using a disk stack centrifuge. For recovery of the supernatant via disk stack centrifugation, the fermentation broth was diluted with deionized water to a wet cell weight (WCW) of 200 g/kg. A disk stack centrifuge (GEA HFC-15) was operated at maximum bowl speed and a feed rate of 350 L/h. After passing the feed through the centrifuge once, the discharged solids were again diluted with 200 g/kg of WCW before the second pass. The supernatant from both passes was pooled and the second clarification continued. A flow chart showing the process of purifying the resulting 50 kDa human collagen fragment is shown in FIGS. 5 and 6 . Fig. 5 shows the purification process for preparing non-hydroxylated 50 kDa human collagen, and Fig. 6 shows the purification process for preparing hydroxylated 50 kDa human collagen.

cake filtration

Cake filtration was performed as a secondary clarification step using a Metchem 470 mm filter press. Per plate used, 0.379 kg of Celite 512 diatomaceous earth was mixed with 20 kg water and applied as a precoat on a filter press. 0.5 wt % Celite 512 Diatomaceous Earth and 0.5 wt % Celite SuperCel Fine DE were added to the supernatant and material and passed through a filter press to remove residual particulate matter.

UF enrichment

Before concentration of the collagen solution, the pH was adjusted to 4 by addition of 50% sulfuric acid. The volume of the resulting solution was reduced by at least 10-fold via cross flow filtration using a spiral wound PES membrane with a molecular weight cutoff of 10 kDa.

Diafiltration

Diafiltration was performed to remove small impurities such as salts from the product. Prior to diafiltration, the pH was adjusted to 8 by addition of acid (50% sulfuric acid) or base (10 N sodium hydroxide) if necessary. Diafiltration was performed on either a KrosFlo® KR2i filtration skid equipped with a 10 kDa mPES hollow fiber module or an Alfa Laval M20 filtration skid equipped with a 10 kDa PES spiral wound module. Deionized water was used as the diafiltration medium, and diafiltration was continued until the conductivity of the solution remained stable.

preservation

The product of diafiltration is diluted by addition of deionized water (DI) to reach a concentration of 2% dissolved solids, during which dilution, 1,2-hexanediol and butylene glycol are added to 3% and 5% respectively. % effective concentration was reached.

A chart showing the percentage recovery of 50 kDa human collagen fragments during individual steps of the purification process and during all steps up to these individual steps as a whole is shown in FIG. 7 .

Example 4: Characterization of cleaved human collagen III fragments

Mass spectrometry (MS) and sequencing

After the Strap protocol as previously described with slight modifications, digestion was performed in solution using an S-trap micro spin column (ProtiFi, Huntington, NY, USA). A sample of protein (30 μg) in 25 μL of 50 mM TEAB pH 8.5, 6 M urea, 2 M thiourea, 1% SDS, 10 mM DTT was reduced at 34° C. for 1 hour, then in the dark for 45 minutes at room temperature. Alkylation with 50 mM iodoacetamide followed by quenching with a final concentration of 40 mM dithiothreitol (DTT). After quenching, 12% phosphoric acid was added to a final concentration of 1.2%. Then, it was diluted 1:7 (v/v) with 90% methanol, 0.1 M Ambic pH 7.9. The samples were then placed on an S-trap spin column and centrifuged at 4000 x g for 30 seconds. Then washed 3 times with 150 μL 90% methanol, 0.1 M Ambic 7.9. Digestion was performed by adding 125 μL LysC at 120 ng/μL (1:10 w/w) in 0.1 M Ambic on top of the spin column. The LysC solution was absorbed on a spin column, a highly hydrophilic matrix, and incubated overnight (16 hours) at 37°C. After incubation, the digested peptides were eluted from the S-trap column sequentially using 40 μL each of 50 mM TEAB pH 8.5 followed by 0.2% formic acid and finally 50% acetonitrile-0.2% formic acid. The three eluted peptide washes were pooled together and evaporated to dryness by a Speedvac SC110 (Thermo Savant, Milford, Mass.). Half (15 μg) of Lys-digested peptide was reconstituted and digested with 33 μL chymotrypsin at 60 ng/μL in 50 mM Ambic (1:7.5 w/w) at 37° C. for 16 h. The digestion was stopped by adding 10 μL 5% FA and evaporated to dryness.

The doubly digested peptide was reconstituted in 150 μL of 0.5% formic acid (“FA”), and 2.5 μL was injected into the nanoLC-MS/MS system. LysC-chymotryptic peptide was eluted with a 60 min gradient from 5% to 33% ACN-0.1% FA at 300 nL/min. The operation of Orbitrap Fusion is basically the same as described above, with an additional EThcD MS2 scan of the ion trap for 3-7 charged ions and a CID MS2 scan of 2-3 charged ions in a 3-second “Top Speed” workflow. was converted to The corrected ETD parameters (reaction time and maximum reagent injection time) were applied to the ETD supplemented with an additional 20% HCD activation energy to generate EThcD MS2 spectra.

By combining the results for both LysC and chymotrypsin sequential digestion and trypsin single digestion, 97.1% sequence coverage of the target sequence was obtained. The nucleotides of the reconstructed sequence were found to be 100% identical to the relevant part of the human collagen III protein.

Example 5: ex vivo Hydroxylation Reaction and Analysis

reaction

Fermentation supernatant containing non-hydroxylated 50 kDa human collagen (unhydroxylated "50 kDa human collagen fragment") having the amino acid sequence according to SEQ ID NO: 986 was partially purified using salt precipitation. Ammonium sulfate was added to the precipitate as a salt to a final concentration of 800 mM, the pH was adjusted to 4±0.05 with 50% sulfuric acid, and the supernatant was incubated at room temperature for 30 minutes with mixing. 50 kDa human collagen fragments were recovered from the supernatant by centrifugation at 17000 x g and the resulting pellet resuspended in half volume deionized water.

The PP547 cell mass was separately resuspended in lysis buffer (50 mM sodium phosphate) to a concentration of 30-45% w/w. The pH of the lysis feed was adjusted to 9±0.05 with 2M citric acid and/or 2M sodium hydroxide. This feed was then dissolved in a bead mill according to standard dissolution times, volumes and cleaning methods.

The lysis product was mixed with purified supernatant containing 50 kDa human collagen fragment with gentle stirring on a magnetic stirrer, then 25-65 mM AKG, 25-65 mM DTT and 2-5 mM ascorbic acid were added as dry powder. . During the addition of AKG, DTT and ascortate, the pH was continuously measured and adjusted to avoid going below pH 6.5 ± 0.05 (pH < 6.5 inactivates the P4H enzyme). Then 0.1 to 0.25 mM ferrous sulfate was added from 0.5M freshly prepared stock solution. This reaction feed was then transferred to a reaction vessel equipped with pH control, temperature control, mixing control and aeration control. Once the reaction feed is added to the vessel, aeration is set to 1-2 vvm, mixed at 150-500 rpm depending on tank OTR configuration, temperature control is set at 26-32° C., and pH control is set at 7.5±0.05. was set. After 5 hours of reaction, the vessel pH is adjusted to 4±0.05 via automated addition of 2M citric acid, the temperature of the reaction vessel is adjusted to 20-26° C., and nitrogen is sparged through the system to achieve zero dissolved oxygen (DO). was maintained. After 16 hours of incubation under the conditions described above, the first purification was performed by centrifuging the reaction product at 17000 x g. After the primary clarification, a secondary clarification was performed using diatomaceous earth in the cake filtration system. The clarified reaction product was cooled to 12° C. and concentrated in an ultrafiltration system with a 10 kDa cutoff to reduce the volume by a factor of 10 to 15. The hydroxylated 50 kDa collagen fragment is then precipitated from solution using 800 mM sodium sulfate. In some cases, further precipitation may be performed using 1M sodium chloride. The precipitated protein is then resuspended in deionized water and retained by diafiltration using either 0.01 N HCl, 0.001 N HCl or deionized water, depending on the final application of 50 kDa human collagen fragments, using a 10 kDa cutoff. The salt was removed. As a final step, the diafiltration product was clarified by further centrifugation at 17,000×g for 10 minutes to remove all particulate matter. Figure 8 shows the percent hydroxylation of 50 kDa human collagen fragments achieved over time during this ex vivo hydroxylation reaction. 9A and 9B show thermograms of 50 kDa human collagen fragments before and after hydroxylation, respectively.

Hydrolyzed Peptide Analysis

The final purified product contains a 50 kDa human collagen fragment and co-purified natural protease. Incubation at room temperature (T = 25° C.) allows the protease to further hydrolyze the 50 kDa human collagen fragment to produce short collagen peptides. The final product was incubated at room temperature for 3 weeks to study the rate and extent of hydrolysis. Samples were analyzed by mass spectrometry after 1 and 3 weeks of incubation at room temperature (T = 25° C.). (Fig. 4). No enzymatic digestion was performed to confirm the relative abundance and sequence of the short collagen peptides. MS spectra showed that the peptide distribution did not change after the first week, with almost 70% of the short peptides (1-6 kDa) being 1-1.5 kDa in length. No peptides greater than 6 kDa were measured in this assay. Mapping of the peptides showed that the detected peptides covered 97% of the initial recombinant collagen amino acid sequence (SEQ ID NO: 986). Peptides identified by mass spectrometry after 1 week incubation are provided in Table 1 above. Peptides identified by mass spectrometry after 3 weeks of incubation are provided in Table 2 above.

Example 6: Stimulation of Collagen I and Collagen III Synthesis by Cleaved Human Collagen III in Fibroblast Cells

A fibroblast cell culture model was used to evaluate the ability of the test substance to exert an effect on collagen synthesis. This study also evaluated the viability of cells after exposure to test substances.

MTT test

Changes in cell number can be assessed via the MTT assay. The MTT assay is a colorimetric analysis of the metabolic activity of cells, reflecting the number of viable cells. Reduction of MTT by mitochondria forms insoluble purple formazine crystals, which are extracted from cells with isopropanol and quantified spectrophotometrically. The intensity of the purple color is directly proportional to the metabolic activity of the cells and inversely proportional to the toxicity of the test substance.

Fibroblasts were seeded into individual wells of 24-well plates in 0.5 ml of fibroblast growth medium (FGM) and incubated overnight at 37±2° C. and 5±1% CO ₂ . The next day, the medium was removed via aspiration to remove any non-adherent cells and replaced with 0.5 ml of fresh FGM. Cells were grown until confluent, changing the medium every 48 to 72 hours. Upon reaching confluency, cells were treated with DMEM supplemented with 1.5% FBS for 24 h to wash away any effects from growth factors contained in normal culture medium. After this 24 hour washout period, cells were treated with the indicated concentrations of test substances (see FIGS. 11A and 11B ) and lysed in FGM with 1.5% FBS. TGF-B (50 ng/ml) was used as a positive control to induce collagen expression. Untreated cells (negative control) were obtained in DMEM with only 1.5% FBS. As a negative control, cells were treated with 100 μM bDcAMP in FGM with 1.5% FBS. Cells were incubated for 48 hours and cell culture medium was collected at the end of the incubation period and stored frozen (-75° C.) or assayed immediately. The material was tested three times.

Samples tested included a 50 kDa fragment of unhydroxylated type III human collagen (SEQ ID NO: 986) (“hcol III 50 kDa non-hydroxylated”), hydroxylated (28%) type III human collagen (also SEQ ID NO: 986). No. 986), 50 kDa fragment ("hcol III 50 kDa; 28% hydroxylated"), full length bovine collagen 3 with hydroxylation (7%) ("full length bcol 3"), marine collagen (Ashland) ), Acacia Collagen (Lipoid Kosmetik AG), Recombinant Human Collagen 21 (Geltor) (“HumColl21”), BIOLLAGEN (Jland Biotech), and Full Length Type III Bovine Collagen with Hydroxylation (45%) (“Full Length bcol3”) It was. Each collagen sample was diluted to various percentage concentrations in FGM, tissue culture medium with 1.5% FBS (see FIGS. 11A and 11B ). A 50 kDa fragment of unhydroxylated type III human collagen (SEQ ID NO: 986) was tested at 0.1 wt%, 0.05 wt%, 0.01 wt%, 0.005 wt%, and 0.001 wt% in culture medium. A 50 kDa fragment of hydroxylated type III human collagen (SEQ ID NO: 986) was tested at 0.01 wt%, 0.005 wt%, 0.001 wt%, 0.0005 wt%, and 0.0001 wt% in culture medium. Full-length type III bovine collagen with 7% hydroxylation was tested at 0.05 wt %, 0.01 wt %, 0.005 wt %, 0.001 wt %, and 0.0005 wt % in culture medium. Marine collagen was tested at 1 wt %, 0.5 wt %, 0.01 wt %, 0.05 wt % and 0.01 wt % in the culture medium. Acacia collagen was tested at 1 wt%, 0.5 wt%, 0.01 wt%, 0.05 wt% and 0.01 wt% in the culture medium. Human collagen 21 was tested at 0.1 wt%, 0.05 wt%, 0.01 wt%, 0.005 wt%, and 0.001 wt% in culture medium. Human collagen 21 was tested at 0.1 wt%, 0.05 wt%, 0.01 wt%, 0.005 wt%, and 0.001 wt% in culture medium. Human collagen 21 was tested at 0.1 wt%, 0.05 wt%, 0.01 wt%, 0.005 wt%, and 0.001 wt% in culture medium. Full length bovine type III collagen with 45% hydroxylation was tested at 0.015 wt%, 0.003 wt%, 0.0015 wt%, 0.0003 wt%, and 0.00015 wt% in culture medium.

After 2 days of incubation, the cell culture medium was removed (see above) and the fibroblasts were washed twice with PBS to remove any residual test material. After the final wash, 500 μl of DMEM supplemented with 0.5 mg/ml MTT was added to each well and the cells were incubated at 37±2° C. and 5±1% CO ₂ for 1 hour. After incubation, the DMEM/MTT solution was removed, the cells were washed once again with PBS, and then 0.5 ml of isopropyl alcohol was added to the wells to extract purple formazine crystals. 200 microliters of isopropyl extract was transferred to a 96-well plate and the plate was read at 540 nm using isopropyl alcohol as a blank. Mean MTT absorbance values for negative control cells were calculated and used to represent 100% cell viability. The individual MTT values from cells subjected to various treatments were then divided by the mean value of negative control cells and expressed as a percentage to determine the change in cell viability induced by each treatment.

The results of the MTT assay are shown in FIGS. 11A and 11B . As shown, the tested collagen was not observed to affect cell viability. A sample of each treated cell was at least as viable as untreated control cells.

Type I Collagen Assay

Fibroblasts are a major source of extracellular matrix peptides, including collagen. Procollagen is a large peptide synthesized by fibroblasts in the dermal layer of the skin and is a precursor of collagen. As the procollagen is processed to form a mature collagen protein, the propeptide portion is cleaved into the form of a type I C-peptide. Both the mature collagen protein and the type I C-peptide fragment are then released into the extracellular environment. As collagen is synthesized, type I C-peptide fragments accumulate in the tissue culture medium. Since there is a 1:1 stoichiometric ratio between the two portions of the procollagen peptide, the assay for type I C-peptide reflects the amount of collagen synthesized. To determine the effect of different forms of collagen on collagen synthesis and secretion, type I C-peptides were assayed via an ELISA-based method.

Fibroblasts were seeded into individual wells of 24-well plates in 0.5 ml of fibroblast growth medium (FGM) and incubated overnight at 37±2° C. and 5±1% CO ₂ . The next day, the medium was removed via aspiration to remove any non-adherent cells and replaced with 0.5 ml of fresh FGM. Cells were grown until confluent, changing the medium every 48-72 hours. Upon reaching confluency, cells were treated with DMEM supplemented with 1.5% FBS for 24 h to wash away any effects from growth factors contained in normal culture medium. After this 24 hour washout period, cells were treated with the test substances described below (see FIGS. 12A and 12B ) at the indicated concentrations dissolved in FGM with 1.5% FBS. TGF-B (50 ng/ml) was used as a positive control to induce collagen expression. Untreated cells (negative control) were obtained in DMEM with only 1.5% FBS. Cells were incubated for 48 hours and cell culture medium was collected at the end of the incubation period and stored frozen (-75° C.) or assayed immediately. The material was tested three times.

Samples tested included a 50 kDa fragment of unhydroxylated type III human collagen (SEQ ID NO: 986), a 50 kDa fragment of hydroxylated (28%) type III human collagen (also SEQ ID NO: 986), hydroxylated ( 7%) full length bovine collagen 3, marine collagen (Ashland), acacia collagen (Lipoid Kosmetik AG), recombinant human collagen 21 (Geltor), BIOLLAGEN (Jland Biotech), and full length III with hydroxylation (45%) It was a type of bovine collagen. Each collagen sample was diluted to various percentage concentrations in FGM, tissue culture medium with 1.5% FBS (see FIGS. 11A and 11B ). A 50 kDa fragment of unhydroxylated type III human collagen (SEQ ID NO: 986) was tested at 0.1 wt%, 0.05 wt%, 0.01 wt%, 0.005 wt%, and 0.001 wt% in culture medium. A 50 kDa fragment of hydroxylated type III human collagen (SEQ ID NO: 986) was tested at 0.01 wt%, 0.005 wt%, 0.001 wt%, 0.0005 wt%, and 0.0001 wt% in culture medium. Full-length type III bovine collagen with 7% hydroxylation was tested at 0.05 wt %, 0.01 wt %, 0.005 wt %, 0.001 wt %, and 0.0005 wt % in culture medium. Marine collagen was tested at 1 wt %, 0.5 wt %, 0.01 wt %, 0.05 wt % and 0.01 wt % in the culture medium. Acacia collagen was tested at 1 wt%, 0.5 wt%, 0.01 wt%, 0.05 wt% and 0.01 wt% in the culture medium. Human collagen 21 was tested at 0.1 wt%, 0.05 wt%, 0.01 wt%, 0.005 wt%, and 0.001 wt% in culture medium. Human collagen 21 was tested at 0.1 wt%, 0.05 wt%, 0.01 wt%, 0.005 wt%, and 0.001 wt% in culture medium. Human collagen 21 was tested at 0.1 wt%, 0.05 wt%, 0.01 wt%, 0.005 wt%, and 0.001 wt% in culture medium. Full length bovine type III collagen with 45% hydroxylation was tested at 0.015 wt%, 0.003 wt%, 0.0015 wt%, 0.0003 wt%, and 0.00015 wt% in culture medium.

For the ELISA assay, a series of Type I C-peptide standards ranging from 0 ng/ml to 640 ng/ml were prepared. Next, remove any unnecessary strips from the plate frame and then add 100 μl of peroxidase-labeled anti-procollagen type I-C peptide antibody to each well used in the assay to generate ELISA microplates. prepared. Then, 20 μl of either sample (collected tissue culture medium) or standards were added to the appropriate wells, covered with microplates and incubated at 37° C. for 3±0.25 hours.

After incubation, wells were aspirated and washed three times with 400 μl of wash buffer. After the last wash was removed, 100 μl of peroxidase substrate solution (hydrogen peroxide + tetramethylbenzidine as chromagen) was added to each well and the plate was incubated at room temperature for 15±5 minutes. After incubation, 100 μl of stop solution (1 N sulfuric acid) was added to each well and the plate was read using a microplate reader at 450 nm. To quantify the amount of each substance present, a standard curve was generated using known concentrations of each substance. A regression analysis was performed to establish the best fit line for these data points. The absorbance values for the test and untreated samples were used to estimate the amount of each substance present in each sample. Treatment means were compared using ANOVA, n=3 for each treatment. Statistical significance was set at p < 0.05.

The results of the type I collagen assay are shown in FIGS. 12A and 12B . These results were obtained after treating the cells with various weight percentage concentrations of each collagen solution. These data indicate that 0.1% of a 50 kDa fragment of human collagen (SEQ ID NO: 986) unexpectedly increased the amount of type I collagen secreted by the treated fibroblasts. Treatment with a 50 kDa fragment of human collagen at 0.1 wt % (final concentration) increased collagen I expression by more than 200% compared to untreated cells. This effect was observed in the 50 kDa fragment of unhydroxylated human collagen (SEQ ID NO: 986) but not in the hydroxylated one, and this difference was the highest concentration (0.1%) of the untested hydroxylated fragment. due to collagen. Cells were treated separately with a variety of different collagens at equal or even higher concentrations. Cells were treated with human collagen, particularly hydrolyzed marine collagen, acacia collagen, human collagen 21, and collagen in a range of sizes similar to or smaller than the 50 kDa fragment of BIOLLAGEN. These collagens of similar size did not affect collagen I production, even when these collagens were tested at percentage concentrations up to 10-fold higher than the 50 kDa fragment. Cells were treated with full-length bovine collagen III, both approximately 7% hydroxylated and approximately 45% hydroxylated. Full-length bovine collagen III was able to induce collagen I expression, but only if it was highly hydroxylated (~45%). Accordingly, these data indicate that compositions comprising a 50 kDa fragment of human collagen are useful when increased production of type I collagen is desired.

Type III Collagen Assay

Type III collagen is a large pro-peptide synthesized by dermal fibroblasts. As the peptide is processed to form a mature type III collagen protein, the pro-peptide portion is cleaved (type III N-peptide). Both the mature collagen protein and the type III N-peptide fragment are then released into the extracellular environment. As collagen is synthesized, type III N-peptide fragments accumulate in the tissue culture medium. Since there is a 1:1 stoichiometric ratio between the two portions of the procollagen peptide, the assay for type III N-peptide reflects the amount of collagen synthesized. To determine the effect of different forms of collagen on collagen synthesis and secretion, type III N-peptides were assayed via an ELISA-based method.

Fibroblasts were seeded into individual wells of 24-well plates in 0.5 ml of fibroblast growth medium (FGM) and incubated overnight at 37±2° C. and 5±1% CO ₂ . The next day, the medium was removed via aspiration to remove any non-adherent cells and replaced with 0.5 ml of fresh FGM. Cells were grown until confluent, changing the medium every 48-72 hours. Upon reaching confluency, cells were treated with DMEM supplemented with 1.5% FBS for 24 h to wash away any effects from growth factors contained in normal culture medium. After this 24 hour washout period, cells were treated with the test substances described below (see FIGS. 13A and 13B ) at the indicated concentrations dissolved in FGM with 1.5% FBS. TGF-B (50 ng/ml) was used as a positive control to induce collagen expression. Untreated cells (negative control) were obtained in DMEM with only 1.5% FBS. Cells were incubated for 48 hours and cell culture medium was collected at the end of the incubation period and stored frozen (-75° C.) or assayed immediately. The material was tested three times.

Samples tested were a 50 kDa fragment of unhydroxylated type III human collagen (SEQ ID NO: 986), a 50 kDa fragment of hydroxylated (28%) type III human collagen (SEQ ID NO: 986), hydroxylated (7 %) full-length bovine collagen 3, marine collagen (Ashland), acacia collagen (Lipoid Kosmetik AG), recombinant human collagen 21 (Geltor), BIOLLAGEN (Jland Biotech), and full-length type III with hydroxylation (45%) It was bovine collagen. Each collagen sample was diluted to various percentage concentrations in FGM, tissue culture medium with 1.5% FBS (see FIGS. 11A and 11B ). A 50 kDa fragment of unhydroxylated type III human collagen (SEQ ID NO: 986) was tested at 0.1 wt%, 0.05 wt%, 0.01 wt%, 0.005 wt%, and 0.001 wt% in culture medium. A 50 kDa fragment of hydroxylated type III human collagen (SEQ ID NO: 986) was tested at 0.01 wt%, 0.005 wt%, 0.001 wt%, 0.0005 wt%, and 0.0001 wt% in culture medium. Full-length type III bovine collagen with 7% hydroxylation was tested at 0.05% by volume, 0.01% by volume, 0.005% by volume, 0.001% by volume, and 0.0005% by volume in culture medium. Marine collagen was tested at 1% by volume, 0.5% by volume, 0.01% by volume, 0.05% by volume and 0.01% by volume in culture medium. Acacia collagen was tested at 1% by volume, 0.5% by volume, 0.01% by volume, 0.05% by volume and 0.01% by volume in the culture medium. Human collagen 21 was tested at 0.1% by volume, 0.05% by volume, 0.01% by volume, 0.005% by volume and 0.001% by volume in culture medium. Human collagen 21 was tested at 0.1% by volume, 0.05% by volume, 0.01% by volume, 0.005% by volume and 0.001% by volume in culture medium. Human collagen 21 was tested at 0.1% by volume, 0.05% by volume, 0.01% by volume, 0.005% by volume and 0.001% by volume in culture medium. Full length bovine type III collagen with 45% hydroxylation was tested at 0.015% by volume, 0.003% by volume, 0.0015% by volume, 0.0003% by volume, and 0.00015% by volume in culture medium.

For the ELISA assay, a series of standards was prepared and 100 μl of these standards or samples were added to the wells of a type III collagen ELISA plate. The plates were then incubated at 37° C. for 1.5 hours. Then, after this incubation, the ELISA plate was washed twice with wash buffer, and then 100 μl of the detection antibody solution was applied. The ELISA plates were then incubated at 37° C. for 1 hour. After incubation, all ELISA plates were washed with washing solution, then 100 μl of HRP conjugate solution was added and incubated at 37° C. for 30 minutes. After this incubation, the ELISA plates were washed again, 100 μl of the substrate solution was added to each well, and the well-plates were incubated at room temperature for 10-30 minutes to allow the color reaction to occur. At the end of the chromogenic reaction, 100 μl of stop solution was added to each well and the plate was read at 460 nm using a plate reader. To quantify the amount of each substance present, a standard curve was generated using known concentrations of each substance. A regression analysis was performed to establish a line that best fit these data points. The absorbance values for the test and untreated samples were used to estimate the amount of each substance present in each sample. Treatment means were compared using ANOVA, n=3 for each treatment. Statistical significance was set at p < 0.05.

The results of the type III collagen assay are shown in FIGS. 13A and 13B . These results were obtained after treating the cells with various weight percentage concentrations of each collagen solution. These results indicate that treatment with 0.1% of a 50 kDa fragment of human collagen (SEQ ID NO: 986) unexpectedly increased the amount of type III collagen secreted by treated fibroblasts by more than 200% compared to untreated cells. . A small but still significant effect was also observed after treatment with 0.01% of a 50 kDa fragment of human collagen (SEQ ID NO: 986; both hydroxylated and non-hydroxylated). After treatment with bovine collagen III (7% hydroxylated), acacia collagen, human collagen 21 or BIOLLAGEN, no effect on collagen III production was observed, even when these collagens were tested at percentage concentrations up to 10-fold higher than the 50 kDa fragment. was not observed. Full-length bovine collagen III was able to induce collagen I expression, but only if it was highly hydroxylated (~45%). Marine collagen induced an effect on collagen III expression only when tested at a 10-fold higher percentage concentration than the 50 kDa fragment of human collagen. Thus, these data indicate that compositions comprising a 50 kDa fragment of human collagen are useful when increased production of type III collagen is desired.

Example 7: Further characterization of cleaved human collagen III fragments

An additional assay was performed on a 50 kDa fragment of human collagen (SEQ ID NO: 986) to further characterize the fragment.

physical properties

Purified non-hydroxylated and purified hydroxylated formulations of a 50 kDa fragment of human collagen (SEQ ID NO: 986) were evaluated for solubility and properties in various solutions. These properties were compared with that of full-length bovine collagen 3. The following samples were each dissolved at a concentration of 1% by weight in deionized water containing 1% phenoxyethanol for preservation:

One. Unhydroxylated Human Collagen 3 50 kDa Fragment

2. Hydroxylated (28%) Human Collagen 3 50 kDa Fragment

3. Full Length Bovine Collagen 3 with 7% Hydroxylation

4. Full Length Bovine Collagen 3 with 45% Hydroxylation

The dissolved collagen solutions were compared against COLLUME (2%; Geltor), human collagen 21 (2%; Geltor), and marine collagen NPNF (Tri-K), each treated in the same manner. The analysis results are shown in FIG. 14 . The 50 kDa collagen fragments tested were soluble and non-viscous, with little or no color or odor.

Four collagen samples were also added at 3 wt % in the seven base formulations to test compatibility and performance. Such base solutions include gel (carbomer system), serum (ammonium acryloyldimethyltaurate/VP copolymer and acrylate/C10-30 alkyl acrylate crosspolymer system), cream emulsion (oil/water), hair conditioner (containing cetrimonium chloride and behentrimonium methosulfate), shampoo/cleanser (sulfate-free), water-based toner, and alcohol-based toner. Non-hydroxylated collagen was compatible with all base formulations tested, whereas hydroxylated collagen was compatible with all base formulations except alcoholic toners. Moreover, the 50 kDa human collagen fragment showed more compatibility than full-length bovine collagen across the range of tested base formulations.

These results demonstrate that a 50 kDa fragment of human collagen is a viable material with potential applications in personal care formulations, if properly incorporated into appropriate formulations. In general, it exhibited good color and odor and could be easily incorporated into the formulations tested. The properties of collagen fragments provide possible advantages in skin care formulations in terms of enhancing elasticity, reducing wrinkles, smoothing, preventing moisture-loss, firming, and film formation. No upper limits were observed for the levels of use of these substances in particular formulation types with regard to aesthetics or compatibility. No negative skin feel was observed for any included levels of any 1% solution.

HRIPT test for skin irritation

To determine the irritation and hypersensitivity (contact allergy) potential of a 50 kDa human collagen fragment (SEQ ID NO: 986), a volunteer study was conducted in which a collagen solution was repeatedly applied to human skin. The study included testing of both hydroxylated and non-hydroxylated collagen fragment solutions.

Patches containing 7.5 mm paper discs were immersed in a solution containing 2% by weight of a 50 kDa human collagen fragment (SEQ ID NO: 986). The patch was then applied directly to the skin in the intrascapular region of the dorsal to the left and right of the midline and the subject was released with instructions not to wet the test area or expose it to direct sunlight. Each patient was administered one patch for each collagen solution to be tested. The patch remained in place for 48 hours after the first application. Subjects were instructed not to remove the patch 48 hours prior to the scheduled visit. Subjects were then instructed to remove the patch 24 hours post application for the remainder of the study. The procedure was repeated until a series of 9 consecutive 24-hour exposures were made 3 times a week for 3 consecutive weeks. Prior to each reapplication, the test site was assessed by trained laboratory personnel. After a rest period of 10-14 days, a retest/test dose was applied once to previously unexposed test sites. Retest sites were evaluated by trained laboratory personnel 48 and 96 hours after application.

No adverse events of any kind were reported during the course of the study in any of 55 test subjects for the collagen solution. In comparison, administration of a positive control (2% sodium lauryl sulfate solution) resulted in a grade 4 reaction (erythema, induration and blisters) in 1 subject and a grade 1 reaction (over at least 3/4 of the patch area) in 3 subjects. erythema). Thus, the 50 kDa human collagen fragment showed no indication of the potential to elicit the mentioned dermal irritation or hypersensitivity (contact allergy).

Example 8: Application of cosmetic composition

To characterize the effect of applying a 50 kDa human collagen fragment (SEQ ID NO: 986) to human skin, a volunteer study was conducted in which a collagen solution was repeatedly applied to human skin. Two different formulations were applied, each containing a 50 kDa human collagen fragment in a composition comprising 1.5% xantham gum (Kelltrol® CG-BT), 0.2% potassium sorbate, 0.3% sodium benzoate, and 0.05% citric acid. was included, and the pH was 5.2. Formulation 1 contained a 50 kDa human collagen fragment at a final concentration of 0.05%, and Formulation 2 contained a solution of a 50 kDa human collagen fragment at a final concentration of 0.002%. Twenty-five subjects applied Formulation 1 on a daily basis for 12 weeks, while 24 subjects applied Formulation 2 on a daily basis for 12 weeks.

Objective clinical efficacy assessments were performed by expert clinical raters before application initiation, 6 weeks after application, and 12 weeks after application. The raters examined the skin for texture and smoothness (visual), skin tone uniformity, firmness (visual), radiance, sagging, and lines/wrinkles, using a 10-point ordinal scale of the face. The results of these evaluations are shown in FIG. 16A in relation to the degree of improvement. In the case of texture/smoothness (visual), skin tone uniformity, firmness (visual), sagging and lines/wrinkles, statistically significant improvements were observed after 6 and 12 weeks of use of the products of dose 1 and dose 2. In the case of luster, a statistically significant improvement was observed after 6 and 12 weeks of using the product at dose 1, but only after 12 weeks of using the product at dose 2.

Subjects also underwent a subjective self-assessment at 6 and 12 weeks after application. These assessments took the form of a series of questions presented to the subjects listed in FIGS. 16B and 16C . In general, both Formulation 1 and Formulation 2 were consistently characterized as leading to improvement in skin condition, with >50% of patients stating improvement (ie, agreeing or strongly agreeing) for almost all questions.

Spectrophotometric intradermal analysis (SIA) was performed using a SIAscope® (Astron Clinica Ltd.) to determine the level of collagen in the skin before application of either Formulation 1 or Formulation 2 and 6 weeks and 12 weeks after application. 16D , application of both Formulation 1 and Formulation 2 resulted in an 18% increase in collagen levels after 6 weeks of application and a 25% increase in collagen after 12 weeks of application, with a slight improvement in collagen in almost all patients. became

The viscoelasticity (tightness and elasticity) of the skin was measured by applying suction to the skin surface using a cutometer MPA 580 (Courage+Khazaka, Germany). For dose 1, a statistically significant decrease in RO was observed after 12 weeks of product use compared to T0, indicating an improvement in skin firmness. For doses 1 and 2, a statistically significant increase in elasticity was observed after 6 and 12 weeks of product use compared to T0.

The scope and scope of the present invention should not be limited by any of the foregoing exemplary embodiments, but only in accordance with the following claims and their equivalents.

SEQUENCE LISTING <110> MODERN MEADOW, INC. DAI, LIXIN <120> COLLAGEN COMPOSITIONS AND METHODS OF USE THEREOF <130> 4431.0820002 <160> 986 <170> PatentIn version 3.5 <210> 1 <211> 528 <212> PRT <213> Artificial Sequence <220> <223> 50 kDa human collagen fragment <400> 1 Asp Val Lys Ser Gly Val Ala Val Gly Gly Leu Ala Gly Tyr Pro Gly 1 5 10 15 Pro Ala Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Thr Ser Gly His 20 25 30 Pro Gly Ser Pro Gly Ser Pro Gly Tyr Gln Gly Pro Pro Gly Glu Pro 35 40 45 Gly Gln Ala Gly Pro Ser Gly Pro Pro Gly Pro Pro Gly Ala Ile Gly 50 55 60 Pro Ser Gly Pro Ala Gly Lys Asp Gly Glu Ser Gly Arg Pro Gly Arg 65 70 75 80 Pro Gly Glu Arg Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala 85 90 95 Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe Asp Gly 100 105 110 Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys Gly Glu 115 120 125 Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly Pro Arg 130 135 140 Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly 145 150 155 160 Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro 165 170 175 Pro Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys 180 185 190 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 195 200 205 Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro 210 215 220 Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly Lys Gly Glu Met 225 230 235 240 Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met Gly Ala Arg Gly 245 250 255 Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly Gly 260 265 270 Ala Gly Glu Pro Gly Lys Asn Gly Ala Lys Gly Glu Pro Gly Pro Arg 275 280 285 Gly Glu Arg Gly Glu Ala Gly Ile Pro Gly Val Pro Gly Ala Lys Gly 290 295 300 Glu Asp Gly Lys Asp Gly Ser Pro Gly Glu Pro Gly Ala Asn Gly Leu 305 310 315 320 Pro Gly Ala Ala Gly Glu Arg Gly Ala Pro Gly Phe Arg Gly Pro Ala 325 330 335 Gly Pro Asn Gly Ile Pro Gly Glu Lys Gly Pro Ala Gly Glu Arg Gly 340 345 350 Ala Pro Gly Pro Ala Gly Pro Arg Gly Ala Ala Gly Glu Pro Gly Arg 355 360 365 Asp Gly Val Pro Gly Gly Pro Gly Met Arg Gly Met Pro Gly Ser Pro 370 375 380 Gly Gly Pro Gly Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly 385 390 395 400 Glu Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln 405 410 415 Pro Gly Val Met Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro 420 425 430 Gly Lys Asn Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly 435 440 445 Pro Pro Gly Lys Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro 450 455 460 Thr Gly Pro Gly Gly Asp Lys Gly Asp Thr Gly Pro Pro Gly Pro Gln 465 470 475 480 Gly Leu Gln Gly Leu Pro Gly Thr Gly Gly Pro Pro Gly Glu Asn Gly 485 490 495 Lys Pro Gly Glu Pro Gly Pro Lys Gly Asp Ala Gly Ala Pro Gly Ala 500 505 510 Pro Gly Gly Lys Gly Asp Ala Gly Ala Pro Gly Glu Arg Gly Pro Pro 515 520 525 <210> 2 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 2 Ala Ala Gly Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln 1 5 10 15 Pro Gly Pro Pro Gly Pro Pro Gly Thr Ala 20 25 <210> 3 <211> 35 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 3 Ala Ala Gly Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln 1 5 10 15 Pro Gly Pro Pro Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro 20 25 30 Gly Ala Lys 35 <210> 4 <211> 41 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 4 Ala Ala Gly Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln 1 5 10 15 Pro Gly Pro Pro Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro 20 25 30 Gly Ala Lys Gly Glu Val Gly Pro Ala 35 40 <210> 5 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 5 Ala Ala Gly Glu Pro Gly Arg Asp Gly Val Pro Gly Gly Pro Gly Met 1 5 10 15 Arg Gly Met Pro Gly 20 <210> 6 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 6 Ala Ala Gly Glu Pro Gly Arg Asp Gly Val Pro Gly Gly Pro Gly Met 1 5 10 15 Arg Gly Met Pro Gly Ser Pro Gly Gly Pro Gly 20 25 <210> 7 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 7 Ala Ala Gly Glu Arg Gly Ala Pro Gly Phe Arg Gly Pro Ala Gly Pro 1 5 10 15 Asn <210> 8 <211> 13 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 8 Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn 1 5 10 <210> 9 <211> 34 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 9 Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro 1 5 10 15 Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly 20 25 30 Leu Met <210> 10 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 10 Ala Gly Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro 1 5 10 15 Gly Pro Pro Gly Pro Pro Gly Thr Ala 20 25 <210> 11 <211> 40 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 11 Ala Gly Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro 1 5 10 15 Gly Pro Pro Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly 20 25 30 Ala Lys Gly Glu Val Gly Pro Ala 35 40 <210> 12 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 12 Ala Gly Glu Pro Gly Arg Asp Gly Val Pro Gly Gly Pro Gly Met Arg 1 5 10 15 Gly Met Pro Gly Ser Pro Gly Gly Pro Gly 20 25 <210> 13 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 13 Ala Gly Glu Arg Gly Ala Pro Gly Phe Arg Gly Pro Ala Gly Pro Asn 1 5 10 15 <210> 14 <211> 10 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 14 Ala Gly Ile Pro Gly Ala Pro Gly Leu Met 1 5 10 <210> 15 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 15 Ala Gly Ile Pro Gly Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Pro 1 5 10 15 Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg 20 25 <210> 16 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 16 Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His 1 5 10 <210> 17 <211> 14 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 17 Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly 1 5 10 <210> 18 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 18 Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe 1 5 10 15 <210> 19 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 19 Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe Asp 1 5 10 15 Gly Arg Asn <210> 20 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 20 Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe Asp 1 5 10 15 Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys 20 25 30 <210> 21 <211> 34 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 21 Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe Asp 1 5 10 15 Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys Gly 20 25 30 Glu Asn <210> 22 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 22 Ala Gly Lys Asp Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg 1 5 10 15 Gly Leu Pro Gly Pro Pro Gly Ile Lys 20 25 <210> 23 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 23 Ala Gly Lys Asp Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg 1 5 10 15 Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala 20 25 <210> 24 <211> 13 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 24 Ala Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Thr Ser 1 5 10 <210> 25 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 25 Ala Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Thr Ser Gly His 1 5 10 15 <210> 26 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 26 Ala Gly Pro Ser Gly Pro Pro Gly Pro Pro Gly Ala Ile Gly Pro Ser 1 5 10 15 <210> 27 <211> 43 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 27 Ala Gly Pro Ser Gly Pro Pro Gly Pro Pro Gly Ala Ile Gly Pro Ser 1 5 10 15 Gly Pro Ala Gly Lys Asp Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly 20 25 30 Glu Arg Gly Leu Pro Gly Pro Pro Gly Ile Lys 35 40 <210> 28 <211> 55 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 28 Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro 1 5 10 15 Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly 20 25 30 Ile Asn Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile 35 40 45 Pro Gly Ala Pro Gly Leu Met 50 55 <210> 29 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 29 Ala Gly Tyr Pro Gly Pro Ala Gly Pro Pro Gly Pro Pro Gly Pro Pro 1 5 10 15 Gly Thr Ser <210> 30 <211> 55 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 30 Ala Gly Tyr Pro Gly Pro Ala Gly Pro Pro Gly Pro Pro Gly Pro Pro 1 5 10 15 Gly Thr Ser Gly His Pro Gly Ser Pro Gly Ser Pro Gly Tyr Gln Gly 20 25 30 Pro Pro Gly Glu Pro Gly Gln Ala Gly Pro Ser Gly Pro Pro Gly Pro 35 40 45 Pro Gly Ala Ile Gly Pro Ser 50 55 <210> 31 <211> 32 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 31 Ala Ile Gly Pro Ser Gly Pro Ala Gly Lys Asp Gly Glu Ser Gly Arg 1 5 10 15 Pro Gly Arg Pro Gly Glu Arg Gly Leu Pro Gly Pro Pro Gly Ile Lys 20 25 30 <210> 32 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 32 Ala Lys Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala 1 5 10 15 Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly 20 25 <210> 33 <211> 41 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 33 Ala Lys Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala 1 5 10 15 Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln 20 25 30 Gly Pro Pro Gly Pro Pro Gly Ile Asn 35 40 <210> 34 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 34 Ala Asn Gly Ala Pro Gly Leu Arg Gly Gly Ala Gly Glu Pro Gly Lys 1 5 10 15 Asn Gly Ala Lys Gly Glu Pro Gly Pro Arg 20 25 <210> 35 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 35 Ala Asn Gly Leu Pro Gly Ala Ala Gly Glu Arg Gly Ala Pro Gly Phe 1 5 10 15 Arg Gly Pro Ala Gly Pro Asn 20 <210> 36 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 36 Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala 1 5 10 15 Arg <210> 37 <211> 38 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 37 Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala 1 5 10 15 Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro 20 25 30 Gly Pro Pro Gly Thr Ala 35 <210> 38 <211> 14 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 38 Ala Pro Gly Leu Lys Gly Glu Asn Gly Leu Pro Gly Glu Asn 1 5 10 <210> 39 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 39 Ala Pro Gly Leu Lys Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala 1 5 10 15 Pro Gly Pro Met Gly Pro Arg 20 <210> 40 <211> 14 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 40 Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Pro Gly Pro Ala 1 5 10 <210> 41 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 41 Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala 1 5 10 15 Asn <210> 42 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 42 Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala 1 5 10 15 Asn Gly Ala Pro Gly Leu Arg 20 <210> 43 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 43 Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala 1 5 10 15 Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn 20 25 <210> 44 <211> 11 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 44 Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn 1 5 10 <210> 45 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 45 Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly 1 5 10 15 <210> 46 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 46 Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly 1 5 10 15 Lys <210> 47 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 47 Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly 1 5 10 15 Lys Gly Glu Met Gly Pro Ala 20 <210> 48 <211> 35 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 48 Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly 1 5 10 15 Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met 20 25 30 Gly Ala Arg 35 <210> 49 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 49 Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro 1 5 10 15 Pro Gly Pro Pro Gly Thr Ala 20 <210> 50 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 50 Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro 1 5 10 15 Pro Gly Pro Pro Gly Thr Ala Gly Phe 20 25 <210> 51 <211> 38 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 51 Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro 1 5 10 15 Pro Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys 20 25 30 Gly Glu Val Gly Pro Ala 35 <210> 52 <211> 44 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 52 Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro 1 5 10 15 Pro Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys 20 25 30 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn 35 40 <210> 53 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 53 Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu 1 5 10 15 Arg <210> 54 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 54 Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu 1 5 10 15 Arg Gly Gly Ala Gly Glu Pro Gly Lys Asn 20 25 <210> 55 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 55 Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr 1 5 10 15 Ala <210> 56 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 56 Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr 1 5 10 15 Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys 20 25 <210> 57 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 57 Asp Ala Gly Ala Pro Gly Ala Pro Gly Gly Lys Gly Asp Ala Gly Ala 1 5 10 15 Pro Gly Glu Arg Gly Pro Pro 20 <210> 58 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 58 Asp Gly Ala Pro Gly Lys Asn Gly Glu Arg Gly Gly Pro Gly Gly Pro 1 5 10 15 Gly Pro Gln Gly Pro Pro Gly 20 <210> 59 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 59 Asp Gly Ala Pro Gly Lys Asn Gly Glu Arg Gly Gly Pro Gly Gly Pro 1 5 10 15 Gly Pro Gln Gly Pro Pro Gly Lys Asn 20 25 <210> 60 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 60 Asp Gly Ala Pro Gly Lys Asn Gly Glu Arg Gly Gly Pro Gly Gly Pro 1 5 10 15 Gly Pro Gln Gly Pro Pro Gly Lys Asn Gly Glu 20 25 <210> 61 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 61 Asp Gly Ala Pro Gly Lys Asn Gly Glu Arg Gly Gly Pro Gly Gly Pro 1 5 10 15 Gly Pro Gln Gly Pro Pro Gly Lys Asn Gly Glu Thr Gly 20 25 <210> 62 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 62 Asp Gly Ala Pro Gly Lys Asn Gly Glu Arg Gly Gly Pro Gly Gly Pro 1 5 10 15 Gly Pro Gln Gly Pro Pro Gly Lys Asn Gly Glu Thr Gly Pro 20 25 30 <210> 63 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 63 Asp Gly Ala Pro Gly Lys Asn Gly Glu Arg Gly Gly Pro Gly Gly Pro 1 5 10 15 Gly Pro Gln Gly Pro Pro Gly Lys Asn Gly Glu Thr Gly Pro Gln 20 25 30 <210> 64 <211> 32 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 64 Asp Gly Ala Pro Gly Lys Asn Gly Glu Arg Gly Gly Pro Gly Gly Pro 1 5 10 15 Gly Pro Gln Gly Pro Pro Gly Lys Asn Gly Glu Thr Gly Pro Gln Gly 20 25 30 <210> 65 <211> 35 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 65 Asp Gly Ala Pro Gly Lys Asn Gly Glu Arg Gly Gly Pro Gly Gly Pro 1 5 10 15 Gly Pro Gln Gly Pro Pro Gly Lys Asn Gly Glu Thr Gly Pro Gln Gly 20 25 30 Pro Pro Gly 35 <210> 66 <211> 36 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 66 Asp Gly Ala Pro Gly Lys Asn Gly Glu Arg Gly Gly Pro Gly Gly Pro 1 5 10 15 Gly Pro Gln Gly Pro Pro Gly Lys Asn Gly Glu Thr Gly Pro Gln Gly 20 25 30 Pro Pro Gly Pro 35 <210> 67 <211> 38 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 67 Asp Gly Ala Pro Gly Lys Asn Gly Glu Arg Gly Gly Pro Gly Gly Pro 1 5 10 15 Gly Pro Gln Gly Pro Pro Gly Lys Asn Gly Glu Thr Gly Pro Gln Gly 20 25 30 Pro Pro Gly Pro Thr Gly 35 <210> 68 <211> 40 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 68 Asp Gly Ala Pro Gly Lys Asn Gly Glu Arg Gly Gly Pro Gly Gly Pro 1 5 10 15 Gly Pro Gln Gly Pro Pro Gly Lys Asn Gly Glu Thr Gly Pro Gln Gly 20 25 30 Pro Pro Gly Pro Thr Gly Pro Gly 35 40 <210> 69 <211> 41 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 69 Asp Gly Ala Pro Gly Lys Asn Gly Glu Arg Gly Gly Pro Gly Gly Pro 1 5 10 15 Gly Pro Gln Gly Pro Pro Gly Lys Asn Gly Glu Thr Gly Pro Gln Gly 20 25 30 Pro Pro Gly Pro Thr Gly Pro Gly Gly 35 40 <210> 70 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 70 Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro 1 5 10 15 Gly <210> 71 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 71 Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro 1 5 10 15 Gly Thr Ala <210> 72 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 72 Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro 1 5 10 15 Gly Thr Ala Gly 20 <210> 73 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 73 Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro 1 5 10 15 Gly Thr Ala Gly Phe 20 <210> 74 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 74 Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro 1 5 10 15 Gly Thr Ala Gly Phe Pro Gly 20 <210> 75 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 75 Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro 1 5 10 15 Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys 20 25 <210> 76 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 76 Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro 1 5 10 15 Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly 20 25 <210> 77 <211> 34 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 77 Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro 1 5 10 15 Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly 20 25 30 Pro Ala <210> 78 <211> 35 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 78 Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro 1 5 10 15 Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly 20 25 30 Pro Ala Gly 35 <210> 79 <211> 38 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 79 Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro 1 5 10 15 Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly 20 25 30 Pro Ala Gly Ser Pro Gly 35 <210> 80 <211> 40 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 80 Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro 1 5 10 15 Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly 20 25 30 Pro Ala Gly Ser Pro Gly Ser Asn 35 40 <210> 81 <211> 52 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 81 Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro 1 5 10 15 Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly 20 25 30 Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu 35 40 45 Pro Gly Pro Gln 50 <210> 82 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 82 Asp Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg Gly Leu Pro 1 5 10 15 Gly Pro Pro Gly Ile Lys 20 <210> 83 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 83 Asp Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg Gly Leu Pro 1 5 10 15 Gly Pro Pro Gly Ile Lys Gly Pro Ala 20 25 <210> 84 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 84 Asp Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly Glu Ser Gly Arg Pro 1 5 10 15 Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln Pro Gly Val Met 20 25 30 <210> 85 <211> 13 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 85 Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr Ala 1 5 10 <210> 86 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 86 Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys 1 5 10 15 <210> 87 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 87 Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys 1 5 10 15 Gly Glu Asn Gly Leu Pro Gly Glu Asn 20 25 <210> 88 <211> 34 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 88 Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys 1 5 10 15 Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly 20 25 30 Pro Arg <210> 89 <211> 49 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 89 Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys 1 5 10 15 Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly 20 25 30 Pro Arg Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala 35 40 45 Ala <210> 90 <211> 52 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 90 Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys 1 5 10 15 Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly 20 25 30 Pro Arg Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala 35 40 45 Ala Gly Ala Arg 50 <210> 91 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 91 Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys Gly Glu Asn Gly Leu 1 5 10 15 Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly Pro Arg 20 25 <210> 92 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 92 Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met Gly Ala 1 5 10 15 Arg <210> 93 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 93 Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly Pro 1 5 10 15 Arg <210> 94 <211> 35 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 94 Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly Pro 1 5 10 15 Arg Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala 20 25 30 Gly Ala Arg 35 <210> 95 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 95 Glu Pro Gly Gln Ala Gly Pro Ser Gly Pro Pro Gly Pro Pro Gly Ala 1 5 10 15 Ile Gly Pro Ser 20 <210> 96 <211> 14 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 96 Glu Arg Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala 1 5 10 <210> 97 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 97 Glu Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln 1 5 10 15 Pro Gly Val Met 20 <210> 98 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 98 Glu Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln 1 5 10 15 Pro Gly Val Met Gly Phe Pro Gly Pro Lys Gly Asn 20 25 <210> 99 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 99 Glu Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg Gly Leu Pro Gly Pro 1 5 10 15 Pro Gly Ile Lys 20 <210> 100 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 100 Glu Thr Gly Ala Pro Gly Leu Lys Gly Glu Asn Gly Leu Pro Gly Glu 1 5 10 15 Asn <210> 101 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 101 Glu Thr Gly Ala Pro Gly Leu Lys Gly Glu Asn Gly Leu Pro Gly Glu 1 5 10 15 Asn Gly Ala Pro Gly Pro Met Gly Pro Arg 20 25 <210> 102 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 102 Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly Pro Gly Gly Asp 1 5 10 15 <210> 103 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 103 Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln 1 5 10 15 Arg Gly Glu Pro Gly Pro Gln 20 <210> 104 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 104 Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln 1 5 10 15 Arg Gly Glu Pro Gly Pro Gln Gly His 20 25 <210> 105 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 105 Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln 1 5 10 15 Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly 20 25 <210> 106 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 106 Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln 1 5 10 15 Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln 20 25 <210> 107 <211> 38 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 107 Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln 1 5 10 15 Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro Pro 20 25 30 Gly Pro Pro Gly Ile Asn 35 <210> 108 <211> 44 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 108 Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln 1 5 10 15 Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro Pro 20 25 30 Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly Lys 35 40 <210> 109 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 109 Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu 1 5 10 15 Lys Gly Glu Asn 20 <210> 110 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 110 Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu 1 5 10 15 Lys Gly Glu Asn Gly Leu Pro Gly Glu Asn 20 25 <210> 111 <211> 35 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 111 Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu 1 5 10 15 Lys Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met 20 25 30 Gly Pro Arg 35 <210> 112 <211> 14 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 112 Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala 1 5 10 <210> 113 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 113 Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly Ser 1 5 10 15 Pro Gly Ser Asn 20 <210> 114 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 114 Gly Ala Ala Gly Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly 1 5 10 15 Gln Pro Gly Pro Pro Gly Pro Pro 20 <210> 115 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 115 Gly Ala Ala Gly Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly 1 5 10 15 Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr Ala 20 25 <210> 116 <211> 36 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 116 Gly Ala Ala Gly Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly 1 5 10 15 Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser 20 25 30 Pro Gly Ala Lys 35 <210> 117 <211> 42 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 117 Gly Ala Ala Gly Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly 1 5 10 15 Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser 20 25 30 Pro Gly Ala Lys Gly Glu Val Gly Pro Ala 35 40 <210> 118 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 118 Gly Ala Ala Gly Glu Pro Gly Arg Asp Gly Val Pro Gly Gly Pro Gly 1 5 10 15 Met Arg Gly Met Pro Gly 20 <210> 119 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 119 Gly Ala Ala Gly Glu Pro Gly Arg Asp Gly Val Pro Gly Gly Pro Gly 1 5 10 15 Met Arg Gly Met Pro Gly Ser Pro Gly Gly Pro Gly 20 25 <210> 120 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 120 Gly Ala Ala Gly Glu Arg Gly Ala Pro Gly Phe Arg Gly Pro Ala Gly 1 5 10 15 Pro Asn <210> 121 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 121 Gly Ala Ile Gly Pro Ser Gly Pro Ala Gly Lys Asp Gly Glu Ser Gly 1 5 10 15 Arg Pro Gly Arg Pro Gly Glu Arg 20 <210> 122 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 122 Gly Ala Ile Gly Pro Ser Gly Pro Ala Gly Lys Asp Gly Glu Ser Gly 1 5 10 15 Arg Pro Gly Arg Pro Gly Glu Arg Gly Leu Pro Gly Pro Pro 20 25 30 <210> 123 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 123 Gly Ala Ile Gly Pro Ser Gly Pro Ala Gly Lys Asp Gly Glu Ser Gly 1 5 10 15 Arg Pro Gly Arg Pro Gly Glu Arg Gly Leu Pro Gly Pro Pro Gly Ile 20 25 30 Lys <210> 124 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 124 Gly Ala Lys Gly Glu Pro Gly Pro Arg Gly Glu Arg Gly Glu Ala Gly 1 5 10 15 Ile Pro Gly Val Pro Gly 20 <210> 125 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 125 Gly Ala Lys Gly Glu Pro Gly Pro Arg Gly Glu Arg Gly Glu Ala Gly 1 5 10 15 Ile Pro Gly Val Pro Gly Ala Lys 20 <210> 126 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 126 Gly Ala Lys Gly Glu Pro Gly Pro Arg Gly Glu Arg Gly Glu Ala Gly 1 5 10 15 Ile Pro Gly Val Pro Gly Ala Lys Gly 20 25 <210> 127 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 127 Gly Ala Lys Gly Glu Pro Gly Pro Arg Gly Glu Arg Gly Glu Ala Gly 1 5 10 15 Ile Pro Gly Val Pro Gly Ala Lys Gly Glu Asp Gly Lys 20 25 <210> 128 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 128 Gly Ala Lys Gly Glu Pro Gly Pro Arg Gly Glu Arg Gly Glu Ala Gly 1 5 10 15 Ile Pro Gly Val Pro Gly Ala Lys Gly Glu Asp Gly Lys Asp Gly 20 25 30 <210> 129 <211> 32 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 129 Gly Ala Lys Gly Glu Pro Gly Pro Arg Gly Glu Arg Gly Glu Ala Gly 1 5 10 15 Ile Pro Gly Val Pro Gly Ala Lys Gly Glu Asp Gly Lys Asp Gly Ser 20 25 30 <210> 130 <211> 39 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 130 Gly Ala Lys Gly Glu Pro Gly Pro Arg Gly Glu Arg Gly Glu Ala Gly 1 5 10 15 Ile Pro Gly Val Pro Gly Ala Lys Gly Glu Asp Gly Lys Asp Gly Ser 20 25 30 Pro Gly Glu Pro Gly Ala Asn 35 <210> 131 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 131 Gly Ala Lys Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly 1 5 10 15 Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln 20 25 <210> 132 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 132 Gly Ala Lys Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly 1 5 10 15 Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly 20 25 <210> 133 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 133 Gly Ala Lys Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly 1 5 10 15 Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly His 20 25 <210> 134 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 134 Gly Ala Lys Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly 1 5 10 15 Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala 20 25 30 Gln <210> 135 <211> 42 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 135 Gly Ala Lys Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly 1 5 10 15 Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala 20 25 30 Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn 35 40 <210> 136 <211> 9 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 136 Gly Ala Asn Gly Ala Pro Gly Leu Arg 1 5 <210> 137 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 137 Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly Gly Ala Gly Glu Pro Gly 1 5 10 15 Lys Asn <210> 138 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 138 Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly Gly Ala Gly Glu Pro Gly 1 5 10 15 Lys Asn Gly Ala Lys 20 <210> 139 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 139 Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly Gly Ala Gly Glu Pro Gly 1 5 10 15 Lys Asn Gly Ala Lys Gly Glu Pro Gly Pro Arg 20 25 <210> 140 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 140 Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly Gly Ala Gly Glu Pro Gly 1 5 10 15 Lys Asn Gly Ala Lys Gly Glu Pro Gly Pro Arg Gly 20 25 <210> 141 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 141 Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly Gly Ala Gly Glu Pro Gly 1 5 10 15 Lys Asn Gly Ala Lys Gly Glu Pro Gly Pro Arg Gly Glu Arg 20 25 30 <210> 142 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 142 Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly Gly Ala Gly Glu Pro Gly 1 5 10 15 Lys Asn Gly Ala Lys Gly Glu Pro Gly Pro Arg Gly Glu Arg Gly 20 25 30 <210> 143 <211> 34 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 143 Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly Gly Ala Gly Glu Pro Gly 1 5 10 15 Lys Asn Gly Ala Lys Gly Glu Pro Gly Pro Arg Gly Glu Arg Gly Glu 20 25 30 Ala Gly <210> 144 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 144 Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala 1 5 10 15 <210> 145 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 145 Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly 1 5 10 15 <210> 146 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 146 Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly 1 5 10 15 Ala <210> 147 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 147 Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly 1 5 10 15 Ala Arg <210> 148 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 148 Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly 1 5 10 15 Ala Arg Gly Asn 20 <210> 149 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 149 Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly 1 5 10 15 Ala Arg Gly Asn Asp 20 <210> 150 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 150 Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly 1 5 10 15 Ala Arg Gly Asn Asp Gly 20 <210> 151 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 151 Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly 1 5 10 15 Ala Arg Gly Asn Asp Gly Ala 20 <210> 152 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 152 Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly 1 5 10 15 Ala Arg Gly Asn Asp Gly Ala Arg 20 <210> 153 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 153 Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly 1 5 10 15 Ala Arg Gly Asn Asp Gly Ala Arg Gly 20 25 <210> 154 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 154 Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly 1 5 10 15 Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser 20 25 <210> 155 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 155 Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly 1 5 10 15 Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp 20 25 <210> 156 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 156 Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly 1 5 10 15 Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly 20 25 <210> 157 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 157 Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly 1 5 10 15 Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln 20 25 <210> 158 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 158 Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly 1 5 10 15 Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly 20 25 30 <210> 159 <211> 32 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 159 Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly 1 5 10 15 Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro 20 25 30 <210> 160 <211> 34 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 160 Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly 1 5 10 15 Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro 20 25 30 Pro Gly <210> 161 <211> 35 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 161 Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly 1 5 10 15 Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro 20 25 30 Pro Gly Pro 35 <210> 162 <211> 37 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 162 Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly 1 5 10 15 Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro 20 25 30 Pro Gly Pro Pro Gly 35 <210> 163 <211> 39 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 163 Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly 1 5 10 15 Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro 20 25 30 Pro Gly Pro Pro Gly Thr Ala 35 <210> 164 <211> 48 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 164 Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly 1 5 10 15 Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro 20 25 30 Pro Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys 35 40 45 <210> 165 <211> 52 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 165 Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly 1 5 10 15 Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro 20 25 30 Pro Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys 35 40 45 Gly Glu Val Gly 50 <210> 166 <211> 54 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 166 Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly 1 5 10 15 Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro 20 25 30 Pro Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys 35 40 45 Gly Glu Val Gly Pro Ala 50 <210> 167 <211> 55 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 167 Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly 1 5 10 15 Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro 20 25 30 Pro Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys 35 40 45 Gly Glu Val Gly Pro Ala Gly 50 55 <210> 168 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 168 Gly Ala Pro Gly Leu Lys Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly 1 5 10 15 Ala Pro Gly Pro Met Gly Pro Arg 20 <210> 169 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 169 Gly Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Pro Gly Pro Ala 1 5 10 15 <210> 170 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 170 Gly Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly 1 5 10 15 Ala Asn <210> 171 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 171 Gly Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly 1 5 10 15 Ala Asn Gly Ala Pro 20 <210> 172 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 172 Gly Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly 1 5 10 15 Ala Asn Gly Ala Pro Gly Leu Arg 20 <210> 173 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 173 Gly Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly 1 5 10 15 Ala Asn Gly Ala Pro Gly Leu Arg Gly Gly Ala Gly Glu Pro Gly Lys 20 25 30 Asn <210> 174 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 174 Gly Ala Pro Gly Leu Arg Gly Gly Ala Gly Glu Pro Gly Lys Asn Gly 1 5 10 15 Ala Lys Gly Glu Pro Gly Pro Arg Gly Glu Arg Gly Glu Ala 20 25 30 <210> 175 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 175 Gly Ala Pro Gly Pro Ala Gly Pro Arg Gly Ala Ala Gly Glu Pro Gly 1 5 10 15 Arg Asp Gly Val Pro Gly 20 <210> 176 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 176 Gly Ala Pro Gly Pro Ala Gly Pro Arg Gly Ala Ala Gly Glu Pro Gly 1 5 10 15 Arg Asp Gly Val Pro Gly Gly Pro Gly Met Arg Gly Met Pro Gly 20 25 30 <210> 177 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 177 Gly Ala Pro Gly Pro Met Gly Pro Arg Gly Ala Pro Gly Glu Arg Gly 1 5 10 15 Arg Pro Gly Leu Pro 20 <210> 178 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 178 Gly Ala Pro Gly Pro Met Gly Pro Arg Gly Ala Pro Gly Glu Arg Gly 1 5 10 15 Arg Pro Gly Leu Pro Gly 20 <210> 179 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 179 Gly Ala Pro Gly Pro Met Gly Pro Arg Gly Ala Pro Gly Glu Arg Gly 1 5 10 15 Arg Pro Gly Leu Pro Gly Ala Ala 20 <210> 180 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 180 Gly Ala Pro Gly Pro Met Gly Pro Arg Gly Ala Pro Gly Glu Arg Gly 1 5 10 15 Arg Pro Gly Leu Pro Gly Ala Ala Gly 20 25 <210> 181 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 181 Gly Ala Pro Gly Pro Met Gly Pro Arg Gly Ala Pro Gly Glu Arg Gly 1 5 10 15 Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala 20 25 <210> 182 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 182 Gly Ala Pro Gly Pro Met Gly Pro Arg Gly Ala Pro Gly Glu Arg Gly 1 5 10 15 Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala Arg 20 25 <210> 183 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 183 Gly Ala Pro Gly Pro Met Gly Pro Arg Gly Ala Pro Gly Glu Arg Gly 1 5 10 15 Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala Arg Gly Asn 20 25 <210> 184 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 184 Gly Ala Pro Gly Pro Met Gly Pro Arg Gly Ala Pro Gly Glu Arg Gly 1 5 10 15 Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala Arg Gly Asn Asp Gly Ala 20 25 30 Arg <210> 185 <211> 34 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 185 Gly Ala Pro Gly Pro Met Gly Pro Arg Gly Ala Pro Gly Glu Arg Gly 1 5 10 15 Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala Arg Gly Asn Asp Gly Ala 20 25 30 Arg Gly <210> 186 <211> 48 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 186 Gly Ala Pro Gly Pro Met Gly Pro Arg Gly Ala Pro Gly Glu Arg Gly 1 5 10 15 Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala Arg Gly Asn Asp Gly Ala 20 25 30 Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr Ala 35 40 45 <210> 187 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 187 Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly 1 5 10 15 Ala Gln Gly Pro Pro Gly Pro Pro 20 <210> 188 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 188 Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly 1 5 10 15 Ala Gln Gly Pro Pro Gly Pro Pro Gly 20 25 <210> 189 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 189 Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly 1 5 10 15 Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn 20 25 <210> 190 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 190 Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly 1 5 10 15 Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly 20 25 <210> 191 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 191 Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly 1 5 10 15 Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser 20 25 <210> 192 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 192 Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly 1 5 10 15 Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly 20 25 30 <210> 193 <211> 32 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 193 Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly 1 5 10 15 Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly 20 25 30 <210> 194 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 194 Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly 1 5 10 15 Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly 20 25 30 Lys <210> 195 <211> 36 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 195 Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly 1 5 10 15 Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly 20 25 30 Lys Gly Glu Met 35 <210> 196 <211> 37 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 196 Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly 1 5 10 15 Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly 20 25 30 Lys Gly Glu Met Gly 35 <210> 197 <211> 39 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 197 Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly 1 5 10 15 Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly 20 25 30 Lys Gly Glu Met Gly Pro Ala 35 <210> 198 <211> 48 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 198 Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly 1 5 10 15 Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly 20 25 30 Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met 35 40 45 <210> 199 <211> 49 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 199 Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly 1 5 10 15 Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly 20 25 30 Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met 35 40 45 Gly <210> 200 <211> 50 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 200 Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly 1 5 10 15 Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly 20 25 30 Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met 35 40 45 Gly Ala 50 <210> 201 <211> 51 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 201 Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly 1 5 10 15 Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly 20 25 30 Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met 35 40 45 Gly Ala Arg 50 <210> 202 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 202 Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn 1 5 10 <210> 203 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 203 Gly Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly 1 5 10 15 Pro Pro Gly Pro Pro 20 <210> 204 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 204 Gly Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly 1 5 10 15 Pro Pro Gly Pro Pro Gly Thr Ala 20 <210> 205 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 205 Gly Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly 1 5 10 15 Pro Pro Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly 20 25 <210> 206 <211> 32 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 206 Gly Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly 1 5 10 15 Pro Pro Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala 20 25 30 <210> 207 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 207 Gly Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly 1 5 10 15 Pro Pro Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala 20 25 30 Lys <210> 208 <211> 39 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 208 Gly Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly 1 5 10 15 Pro Pro Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala 20 25 30 Lys Gly Glu Val Gly Pro Ala 35 <210> 209 <211> 40 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 209 Gly Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly 1 5 10 15 Pro Pro Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala 20 25 30 Lys Gly Glu Val Gly Pro Ala Gly 35 40 <210> 210 <211> 43 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 210 Gly Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly 1 5 10 15 Pro Pro Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala 20 25 30 Lys Gly Glu Val Gly Pro Ala Gly Ser Pro Gly 35 40 <210> 211 <211> 45 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 211 Gly Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly 1 5 10 15 Pro Pro Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala 20 25 30 Lys Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn 35 40 45 <210> 212 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 212 Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn 1 5 10 <210> 213 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 213 Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly 1 5 10 15 Leu <210> 214 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 214 Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly 1 5 10 15 Leu Arg <210> 215 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 215 Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly 1 5 10 15 Leu Arg Gly <210> 216 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 216 Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly 1 5 10 15 Leu Arg Gly Gly 20 <210> 217 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 217 Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly 1 5 10 15 Leu Arg Gly Gly Ala 20 <210> 218 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 218 Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly 1 5 10 15 Leu Arg Gly Gly Ala Gly 20 <210> 219 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 219 Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly 1 5 10 15 Leu Arg Gly Gly Ala Gly Glu 20 <210> 220 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 220 Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly 1 5 10 15 Leu Arg Gly Gly Ala Gly Glu Pro Gly 20 25 <210> 221 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 221 Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly 1 5 10 15 Leu Arg Gly Gly Ala Gly Glu Pro Gly Lys Asn 20 25 <210> 222 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 222 Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly 1 5 10 15 Leu Arg Gly Gly Ala Gly Glu Pro Gly Lys Asn Gly 20 25 <210> 223 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 223 Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly 1 5 10 15 Leu Arg Gly Gly Ala Gly Glu Pro Gly Lys Asn Gly Ala 20 25 <210> 224 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 224 Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly 1 5 10 15 Leu Arg Gly Gly Ala Gly Glu Pro Gly Lys Asn Gly Ala Lys 20 25 30 <210> 225 <211> 32 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 225 Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly 1 5 10 15 Leu Arg Gly Gly Ala Gly Glu Pro Gly Lys Asn Gly Ala Lys Gly Glu 20 25 30 <210> 226 <211> 34 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 226 Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly 1 5 10 15 Leu Arg Gly Gly Ala Gly Glu Pro Gly Lys Asn Gly Ala Lys Gly Glu 20 25 30 Pro Gly <210> 227 <211> 36 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 227 Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly 1 5 10 15 Leu Arg Gly Gly Ala Gly Glu Pro Gly Lys Asn Gly Ala Lys Gly Glu 20 25 30 Pro Gly Pro Arg 35 <210> 228 <211> 39 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 228 Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly 1 5 10 15 Leu Arg Gly Gly Ala Gly Glu Pro Gly Lys Asn Gly Ala Lys Gly Glu 20 25 30 Pro Gly Pro Arg Gly Glu Arg 35 <210> 229 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 229 Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly 1 5 10 15 Thr Ala <210> 230 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 230 Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly 1 5 10 15 Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys 20 25 <210> 231 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 231 Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly 1 5 10 15 Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro 20 25 30 Ala <210> 232 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 232 Gly Asp Lys Gly Asp Thr Gly Pro Pro Gly Pro Gln Gly Leu Gln Gly 1 5 10 15 Leu Pro Gly Thr Gly Gly Pro Pro Gly Glu Asn 20 25 <210> 233 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 233 Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys 1 5 10 <210> 234 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 234 Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys Gly Glu Asn Gly 1 5 10 15 Leu Pro Gly Glu Asn 20 <210> 235 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 235 Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys Gly Glu Asn Gly 1 5 10 15 Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met 20 25 <210> 236 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 236 Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys Gly Glu Asn Gly 1 5 10 15 Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly Pro Arg 20 25 30 <210> 237 <211> 48 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 237 Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys Gly Glu Asn Gly 1 5 10 15 Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly Pro Arg Gly Ala 20 25 30 Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala Arg 35 40 45 <210> 238 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 238 Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met 1 5 10 15 <210> 239 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 239 Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met Gly 1 5 10 15 Ala Arg <210> 240 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 240 Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met Gly 1 5 10 15 Ala Arg Gly Pro Pro Gly Pro Ala 20 <210> 241 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 241 Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met Gly 1 5 10 15 Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn 20 25 <210> 242 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 242 Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met Gly 1 5 10 15 Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu 20 25 30 Arg <210> 243 <211> 42 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 243 Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met Gly 1 5 10 15 Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu 20 25 30 Arg Gly Gly Ala Gly Glu Pro Gly Lys Asn 35 40 <210> 244 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 244 Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met 1 5 10 15 <210> 245 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 245 Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly 1 5 10 15 Pro Arg <210> 246 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 246 Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly 1 5 10 15 Pro Arg Gly <210> 247 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 247 Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly 1 5 10 15 Pro Arg Gly Ala Pro Gly 20 <210> 248 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 248 Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly 1 5 10 15 Pro Arg Gly Ala Pro Gly Glu Arg 20 <210> 249 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 249 Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly 1 5 10 15 Pro Arg Gly Ala Pro Gly Glu Arg Gly 20 25 <210> 250 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 250 Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly 1 5 10 15 Pro Arg Gly Ala Pro Gly Glu Arg Gly Arg 20 25 <210> 251 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 251 Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly 1 5 10 15 Pro Arg Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala 20 25 30 Ala <210> 252 <211> 35 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 252 Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly 1 5 10 15 Pro Arg Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala 20 25 30 Ala Gly Ala 35 <210> 253 <211> 36 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 253 Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly 1 5 10 15 Pro Arg Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala 20 25 30 Ala Gly Ala Arg 35 <210> 254 <211> 38 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 254 Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly 1 5 10 15 Pro Arg Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala 20 25 30 Ala Gly Ala Arg Gly Asn 35 <210> 255 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 255 Gly Glu Pro Gly Ala Asn Gly Leu Pro Gly Ala Ala Gly Glu Arg Gly 1 5 10 15 Ala Pro Gly Phe Arg Gly Pro Ala Gly Pro Asn 20 25 <210> 256 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 256 Gly Glu Pro Gly Pro Lys Gly Asp Ala Gly Ala Pro Gly Ala Pro Gly 1 5 10 15 Gly Lys Gly Asp Ala Gly Ala Pro Gly 20 25 <210> 257 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 257 Gly Glu Pro Gly Pro Lys Gly Asp Ala Gly Ala Pro Gly Ala Pro Gly 1 5 10 15 Gly Lys Gly Asp Ala Gly Ala Pro Gly Glu 20 25 <210> 258 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 258 Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro Gly 1 5 10 15 Pro Pro Gly Ile Asn 20 <210> 259 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 259 Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro Gly 1 5 10 15 Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro 20 25 30 Ala <210> 260 <211> 42 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 260 Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro Gly 1 5 10 15 Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro 20 25 30 Ala Gly Ile Pro Gly Ala Pro Gly Leu Met 35 40 <210> 261 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 261 Gly Glu Pro Gly Pro Arg Gly Glu Arg Gly Glu Ala Gly Ile Pro Gly 1 5 10 15 Val Pro Gly Ala Lys Gly Glu Asp Gly Lys Asp Gly 20 25 <210> 262 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 262 Gly Glu Pro Gly Gln Ala Gly Pro Ser Gly Pro Pro Gly Pro Pro Gly 1 5 10 15 Ala Ile Gly Pro Ser 20 <210> 263 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 263 Gly Glu Pro Gly Gln Ala Gly Pro Ser Gly Pro Pro Gly Pro Pro Gly 1 5 10 15 Ala Ile Gly Pro Ser Gly Pro Ala Gly Lys Asp 20 25 <210> 264 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 264 Gly Glu Pro Gly Arg Asp Gly Val Pro Gly Gly Pro Gly Met Arg Gly 1 5 10 15 Met Pro Gly Ser Pro Gly Gly Pro Gly 20 25 <210> 265 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 265 Gly Glu Arg Gly Glu Ala Gly Ile Pro Gly Val Pro Gly Ala Lys Gly 1 5 10 15 <210> 266 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 266 Gly Glu Arg Gly Glu Ala Gly Ile Pro Gly Val Pro Gly Ala Lys Gly 1 5 10 15 Glu Asp Gly Lys Asp Gly 20 <210> 267 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 267 Gly Glu Arg Gly Glu Ala Gly Ile Pro Gly Val Pro Gly Ala Lys Gly 1 5 10 15 Glu Asp Gly Lys Asp Gly Ser Pro Gly Glu Pro Gly Ala Asn 20 25 30 <210> 268 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 268 Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly 1 5 10 15 Lys <210> 269 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 269 Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly 1 5 10 15 Lys Asn <210> 270 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 270 Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly 1 5 10 15 Lys Asn Gly <210> 271 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 271 Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly 1 5 10 15 Lys Asn Gly Glu Thr Gly Pro 20 <210> 272 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 272 Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly 1 5 10 15 Lys Asn Gly Glu Thr Gly Pro Gln 20 <210> 273 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 273 Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly 1 5 10 15 Lys Asn Gly Glu Thr Gly Pro Gln Gly 20 25 <210> 274 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 274 Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly 1 5 10 15 Lys Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro 20 25 <210> 275 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 275 Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly 1 5 10 15 Lys Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly 20 25 <210> 276 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 276 Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly 1 5 10 15 Lys Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro 20 25 <210> 277 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 277 Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly 1 5 10 15 Lys Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr 20 25 30 <210> 278 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 278 Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly 1 5 10 15 Lys Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly 20 25 30 <210> 279 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 279 Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly 1 5 10 15 Lys Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly Pro 20 25 30 Gly <210> 280 <211> 34 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 280 Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly 1 5 10 15 Lys Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly Pro 20 25 30 Gly Gly <210> 281 <211> 35 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 281 Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly 1 5 10 15 Lys Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly Pro 20 25 30 Gly Gly Asp 35 <210> 282 <211> 36 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 282 Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly 1 5 10 15 Lys Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly Pro 20 25 30 Gly Gly Asp Lys 35 <210> 283 <211> 37 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 283 Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly 1 5 10 15 Lys Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly Pro 20 25 30 Gly Gly Asp Lys Gly 35 <210> 284 <211> 38 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 284 Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly 1 5 10 15 Lys Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly Pro 20 25 30 Gly Gly Asp Lys Gly Asp 35 <210> 285 <211> 40 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 285 Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly 1 5 10 15 Lys Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly Pro 20 25 30 Gly Gly Asp Lys Gly Asp Thr Gly 35 40 <210> 286 <211> 43 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 286 Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly 1 5 10 15 Lys Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly Pro 20 25 30 Gly Gly Asp Lys Gly Asp Thr Gly Pro Pro Gly 35 40 <210> 287 <211> 45 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 287 Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly 1 5 10 15 Lys Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly Pro 20 25 30 Gly Gly Asp Lys Gly Asp Thr Gly Pro Pro Gly Pro Gln 35 40 45 <210> 288 <211> 46 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 288 Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly 1 5 10 15 Lys Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly Pro 20 25 30 Gly Gly Asp Lys Gly Asp Thr Gly Pro Pro Gly Pro Gln Gly 35 40 45 <210> 289 <211> 48 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 289 Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly 1 5 10 15 Lys Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly Pro 20 25 30 Gly Gly Asp Lys Gly Asp Thr Gly Pro Pro Gly Pro Gln Gly Leu Gln 35 40 45 <210> 290 <211> 49 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 290 Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly 1 5 10 15 Lys Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly Pro 20 25 30 Gly Gly Asp Lys Gly Asp Thr Gly Pro Pro Gly Pro Gln Gly Leu Gln 35 40 45 Gly <210> 291 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 291 Gly Glu Arg Gly Leu Pro Gly Pro Pro Gly Ile Lys 1 5 10 <210> 292 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 292 Gly Glu Arg Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala 1 5 10 15 <210> 293 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 293 Gly Glu Arg Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala Gly 1 5 10 15 Ile Pro Gly Phe Pro Gly Met Lys 20 <210> 294 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 294 Gly Glu Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly 1 5 10 15 Gln Pro Gly Val Met 20 <210> 295 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 295 Gly Glu Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly 1 5 10 15 Gln Pro Gly Val Met Gly Phe Pro Gly Pro Lys Gly Asn 20 25 <210> 296 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 296 Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg Gly Leu Pro Gly 1 5 10 15 Pro Pro Gly Ile Lys 20 <210> 297 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 297 Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg Gly Leu Pro Gly 1 5 10 15 Pro Pro Gly Ile Lys Gly 20 <210> 298 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 298 Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg Gly Leu Pro Gly 1 5 10 15 Pro Pro Gly Ile Lys Gly Pro Ala 20 <210> 299 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 299 Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg Gly Leu Pro Gly 1 5 10 15 Pro Pro Gly Ile Lys Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met 20 25 30 Lys <210> 300 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 300 Gly Glu Thr Gly Ala Pro Gly Leu Lys Gly Glu Asn Gly Leu Pro Gly 1 5 10 15 Glu Asn <210> 301 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 301 Gly Glu Thr Gly Ala Pro Gly Leu Lys Gly Glu Asn Gly Leu Pro Gly 1 5 10 15 Glu Asn Gly Ala Pro Gly Pro Met Gly Pro Arg 20 25 <210> 302 <211> 45 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 302 Gly Glu Thr Gly Ala Pro Gly Leu Lys Gly Glu Asn Gly Leu Pro Gly 1 5 10 15 Glu Asn Gly Ala Pro Gly Pro Met Gly Pro Arg Gly Ala Pro Gly Glu 20 25 30 Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala Arg 35 40 45 <210> 303 <211> 47 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 303 Gly Glu Thr Gly Ala Pro Gly Leu Lys Gly Glu Asn Gly Leu Pro Gly 1 5 10 15 Glu Asn Gly Ala Pro Gly Pro Met Gly Pro Arg Gly Ala Pro Gly Glu 20 25 30 Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala Arg Gly Asn 35 40 45 <210> 304 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 304 Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly Pro Gly 1 5 10 15 <210> 305 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 305 Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly Pro Gly Gly 1 5 10 15 Asp <210> 306 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 306 Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly Pro Gly Gly 1 5 10 15 Asp Lys Gly Asp Thr Gly 20 <210> 307 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 307 Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly Pro Gly Gly 1 5 10 15 Asp Lys Gly Asp Thr Gly Pro Pro Gly 20 25 <210> 308 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 308 Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly Pro Gly Gly 1 5 10 15 Asp Lys Gly Asp Thr Gly Pro Pro Gly Pro Gln 20 25 <210> 309 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 309 Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly Pro Gly Gly 1 5 10 15 Asp Lys Gly Asp Thr Gly Pro Pro Gly Pro Gln Gly 20 25 <210> 310 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 310 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 <210> 311 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 311 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln <210> 312 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 312 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu 20 <210> 313 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 313 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro 20 <210> 314 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 314 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro Gly 20 <210> 315 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 315 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro Gly Pro 20 <210> 316 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 316 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro Gly Pro Gln 20 <210> 317 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 317 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro Gly Pro Gln Gly 20 25 <210> 318 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 318 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro Gly Pro Gln Gly His 20 25 <210> 319 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 319 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala 20 25 <210> 320 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 320 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly 20 25 <210> 321 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 321 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala 20 25 <210> 322 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 322 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln 20 25 30 <210> 323 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 323 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly 20 25 30 <210> 324 <211> 32 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 324 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro 20 25 30 <210> 325 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 325 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro 20 25 30 Pro <210> 326 <211> 34 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 326 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro 20 25 30 Pro Gly <210> 327 <211> 35 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 327 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro 20 25 30 Pro Gly Pro 35 <210> 328 <211> 36 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 328 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro 20 25 30 Pro Gly Pro Pro 35 <210> 329 <211> 37 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 329 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro 20 25 30 Pro Gly Pro Pro Gly 35 <210> 330 <211> 39 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 330 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro 20 25 30 Pro Gly Pro Pro Gly Ile Asn 35 <210> 331 <211> 40 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 331 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro 20 25 30 Pro Gly Pro Pro Gly Ile Asn Gly 35 40 <210> 332 <211> 41 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 332 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro 20 25 30 Pro Gly Pro Pro Gly Ile Asn Gly Ser 35 40 <210> 333 <211> 43 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 333 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro 20 25 30 Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly 35 40 <210> 334 <211> 44 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 334 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro 20 25 30 Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly 35 40 <210> 335 <211> 45 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 335 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro 20 25 30 Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly Lys 35 40 45 <210> 336 <211> 46 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 336 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro 20 25 30 Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly Lys Gly 35 40 45 <210> 337 <211> 48 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 337 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro 20 25 30 Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly Lys Gly Glu Met 35 40 45 <210> 338 <211> 49 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 338 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro 20 25 30 Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly Lys Gly Glu Met 35 40 45 Gly <210> 339 <211> 51 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 339 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro 20 25 30 Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly Lys Gly Glu Met 35 40 45 Gly Pro Ala 50 <210> 340 <211> 52 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 340 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro 20 25 30 Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly Lys Gly Glu Met 35 40 45 Gly Pro Ala Gly 50 <210> 341 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 341 Gly Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly 1 5 10 15 Leu Lys <210> 342 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 342 Gly Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly 1 5 10 15 Leu Lys Gly <210> 343 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 343 Gly Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly 1 5 10 15 Leu Lys Gly Glu Asn 20 <210> 344 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 344 Gly Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly 1 5 10 15 Leu Lys Gly Glu Asn Gly 20 <210> 345 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 345 Gly Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly 1 5 10 15 Leu Lys Gly Glu Asn Gly Leu Pro Gly Glu Asn 20 25 <210> 346 <211> 36 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 346 Gly Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly 1 5 10 15 Leu Lys Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro 20 25 30 Met Gly Pro Arg 35 <210> 347 <211> 51 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 347 Gly Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly 1 5 10 15 Leu Lys Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro 20 25 30 Met Gly Pro Arg Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro 35 40 45 Gly Ala Ala 50 <210> 348 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 348 Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe Asp Gly Arg Asn Gly 1 5 10 15 Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys 20 25 <210> 349 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 349 Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe Asp Gly Arg Asn Gly 1 5 10 15 Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys Gly Glu Asn 20 25 30 <210> 350 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 350 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn 1 5 10 15 <210> 351 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 351 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly 1 5 10 15 Glu Arg <210> 352 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 352 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly 1 5 10 15 Glu Arg Gly <210> 353 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 353 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly 1 5 10 15 Glu Arg Gly Gly 20 <210> 354 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 354 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly 1 5 10 15 Glu Arg Gly Gly Pro 20 <210> 355 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 355 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly 1 5 10 15 Glu Arg Gly Gly Pro Gly 20 <210> 356 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 356 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly 1 5 10 15 Glu Arg Gly Gly Pro Gly Gly 20 <210> 357 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 357 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly 1 5 10 15 Glu Arg Gly Gly Pro Gly Gly Pro 20 <210> 358 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 358 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly 1 5 10 15 Glu Arg Gly Gly Pro Gly Gly Pro Gly 20 25 <210> 359 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 359 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly 1 5 10 15 Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro 20 25 <210> 360 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 360 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly 1 5 10 15 Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln 20 25 <210> 361 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 361 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly 1 5 10 15 Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly 20 25 <210> 362 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 362 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly 1 5 10 15 Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro 20 25 <210> 363 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 363 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly 1 5 10 15 Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro 20 25 30 <210> 364 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 364 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly 1 5 10 15 Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly 20 25 30 <210> 365 <211> 32 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 365 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly 1 5 10 15 Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly Lys 20 25 30 <210> 366 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 366 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly 1 5 10 15 Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly Lys 20 25 30 Asn <210> 367 <211> 34 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 367 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly 1 5 10 15 Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly Lys 20 25 30 Asn Gly <210> 368 <211> 35 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 368 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly 1 5 10 15 Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly Lys 20 25 30 Asn Gly Glu 35 <210> 369 <211> 36 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 369 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly 1 5 10 15 Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly Lys 20 25 30 Asn Gly Glu Thr 35 <210> 370 <211> 37 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 370 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly 1 5 10 15 Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly Lys 20 25 30 Asn Gly Glu Thr Gly 35 <210> 371 <211> 38 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 371 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly 1 5 10 15 Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly Lys 20 25 30 Asn Gly Glu Thr Gly Pro 35 <210> 372 <211> 39 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 372 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly 1 5 10 15 Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly Lys 20 25 30 Asn Gly Glu Thr Gly Pro Gln 35 <210> 373 <211> 40 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 373 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly 1 5 10 15 Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly Lys 20 25 30 Asn Gly Glu Thr Gly Pro Gin Gly 35 40 <210> 374 <211> 43 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 374 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly 1 5 10 15 Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly Lys 20 25 30 Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly 35 40 <210> 375 <211> 46 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 375 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly 1 5 10 15 Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly Lys 20 25 30 Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly 35 40 45 <210> 376 <211> 51 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 376 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly 1 5 10 15 Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly Lys 20 25 30 Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly Pro Gly 35 40 45 Gly Asp Lys 50 <210> 377 <211> 13 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 377 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly 1 5 10 <210> 378 <211> 14 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 378 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro 1 5 10 <210> 379 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 379 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala 1 5 10 15 <210> 380 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 380 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 <210> 381 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 381 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 Ser <210> 382 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 382 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 Ser Pro Gly <210> 383 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 383 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 Ser Pro Gly Ser Asn 20 <210> 384 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 384 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 Ser Pro Gly Ser Asn Gly 20 <210> 385 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 385 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 Ser Pro Gly Ser Asn Gly Ala 20 <210> 386 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 386 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 Ser Pro Gly Ser Asn Gly Ala Pro Gly 20 25 <210> 387 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 387 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg 20 25 <210> 388 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 388 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly 20 25 <210> 389 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 389 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu 20 25 <210> 390 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 390 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro 20 25 30 <210> 391 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 391 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly 20 25 30 <210> 392 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 392 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro 20 25 30 Gln <210> 393 <211> 34 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 393 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro 20 25 30 Gln Gly <210> 394 <211> 35 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 394 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro 20 25 30 Gln Gly His 35 <210> 395 <211> 36 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 395 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro 20 25 30 Gln Gly His Ala 35 <210> 396 <211> 37 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 396 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro 20 25 30 Gln Gly His Ala Gly 35 <210> 397 <211> 38 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 397 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro 20 25 30 Gln Gly His Ala Gly Ala 35 <210> 398 <211> 39 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 398 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro 20 25 30 Gln Gly His Ala Gly Ala Gln 35 <210> 399 <211> 40 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 399 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro 20 25 30 Gln Gly His Ala Gly Ala Gln Gly 35 40 <210> 400 <211> 42 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 400 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro 20 25 30 Gln Gly His Ala Gly Ala Gln Gly Pro Pro 35 40 <210> 401 <211> 43 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 401 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro 20 25 30 Gln Gly His Ala Gly Ala Gln Gly Pro Pro Gly 35 40 <210> 402 <211> 46 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 402 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro 20 25 30 Gln Gly His Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly 35 40 45 <210> 403 <211> 48 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 403 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro 20 25 30 Gln Gly His Ala Gly Ala Gly Pro Pro Gly Pro Pro Gly Ile Asn 35 40 45 <210> 404 <211> 49 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 404 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro 20 25 30 Gln Gly His Ala Gly Ala Gly Pro Pro Gly Pro Pro Gly Ile Asn 35 40 45 Gly <210> 405 <211> 52 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 405 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro 20 25 30 Gln Gly His Ala Gly Ala Gly Pro Pro Gly Pro Pro Gly Ile Asn 35 40 45 Gly Ser Pro Gly 50 <210> 406 <211> 54 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 406 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro 20 25 30 Gln Gly His Ala Gly Ala Gly Pro Pro Gly Pro Pro Gly Ile Asn 35 40 45 Gly Ser Pro Gly Gly Lys 50 <210> 407 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 407 Gly Phe Arg Gly Pro Ala Gly Pro Asn Gly Ile Pro Gly Glu Lys Gly 1 5 10 15 Pro Ala Gly Glu Arg Gly Ala Pro Gly Pro Ala 20 25 <210> 408 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 408 Gly Gly Ala Gly Glu Pro Gly Lys Asn Gly Ala Lys Gly Glu Pro Gly 1 5 10 15 Pro Arg <210> 409 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 409 Gly Gly Ala Gly Glu Pro Gly Lys Asn Gly Ala Lys Gly Glu Pro Gly 1 5 10 15 Pro Arg Gly Glu Arg Gly Glu Ala Gly Ile Pro 20 25 <210> 410 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 410 Gly Gly Ala Gly Glu Pro Gly Lys Asn Gly Ala Lys Gly Glu Pro Gly 1 5 10 15 Pro Arg Gly Glu Arg Gly Glu Ala Gly Ile Pro Gly 20 25 <210> 411 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 411 Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly 1 5 10 15 Leu Met <210> 412 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 412 Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly 1 5 10 15 Leu Met Gly Ala 20 <210> 413 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 413 Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly 1 5 10 15 Leu Met Gly Ala Arg 20 <210> 414 <211> 32 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 414 Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly Lys Asn Gly 1 5 10 15 Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly Pro Gly Gly Asp 20 25 30 <210> 415 <211> 48 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 415 Gly Gly Pro Gly Met Arg Gly Met Pro Gly Ser Pro Gly Gly Pro Gly 1 5 10 15 Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly Glu Ser Gly Arg 20 25 30 Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln Pro Gly Val Met 35 40 45 <210> 416 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 416 Gly Gly Pro Gly Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly 1 5 10 15 Glu Ser Gly Arg Pro Gly Pro Pro Gly 20 25 <210> 417 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 417 Gly Gly Pro Gly Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly 1 5 10 15 Glu Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser 20 25 <210> 418 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 418 Gly Gly Pro Gly Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly 1 5 10 15 Glu Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg 20 25 30 <210> 419 <211> 32 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 419 Gly Gly Pro Gly Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly 1 5 10 15 Glu Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln 20 25 30 <210> 420 <211> 36 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 420 Gly Gly Pro Gly Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly 1 5 10 15 Glu Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln 20 25 30 Pro Gly Val Met 35 <210> 421 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 421 Gly His Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn 1 5 10 15 <210> 422 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 422 Gly His Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly 1 5 10 15 <210> 423 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 423 Gly His Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly 1 5 10 15 Ser Pro Gly <210> 424 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 424 Gly His Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly 1 5 10 15 Ser Pro Gly Gly Lys 20 <210> 425 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 425 Gly His Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly 1 5 10 15 Ser Pro Gly Gly Lys Gly Glu Met Gly 20 25 <210> 426 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 426 Gly His Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly 1 5 10 15 Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala 20 25 <210> 427 <211> 36 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 427 Gly His Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly 1 5 10 15 Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala 20 25 30 Pro Gly Leu Met 35 <210> 428 <211> 37 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 428 Gly His Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly 1 5 10 15 Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala 20 25 30 Pro Gly Leu Met Gly 35 <210> 429 <211> 38 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 429 Gly His Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly 1 5 10 15 Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala 20 25 30 Pro Gly Leu Met Gly Ala 35 <210> 430 <211> 39 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 430 Gly His Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly 1 5 10 15 Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala 20 25 30 Pro Gly Leu Met Gly Ala Arg 35 <210> 431 <211> 45 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 431 Gly His Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly 1 5 10 15 Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala 20 25 30 Pro Gly Leu Met Gly Ala Arg Gly Pro Pro Gly Pro Ala 35 40 45 <210> 432 <211> 48 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 432 Gly His Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly 1 5 10 15 Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala 20 25 30 Pro Gly Leu Met Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn 35 40 45 <210> 433 <211> 54 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 433 Gly His Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly 1 5 10 15 Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala 20 25 30 Pro Gly Leu Met Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn 35 40 45 Gly Ala Pro Gly Leu Arg 50 <210> 434 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 434 Gly His Pro Gly Ser Pro Gly Ser Pro Gly Tyr Gln Gly Pro Pro Gly 1 5 10 15 Glu Pro Gly <210> 435 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 435 Gly His Pro Gly Ser Pro Gly Ser Pro Gly Tyr Gln Gly Pro Pro Gly 1 5 10 15 Glu Pro Gly Gln Ala 20 <210> 436 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 436 Gly His Pro Gly Ser Pro Gly Ser Pro Gly Tyr Gln Gly Pro Pro Gly 1 5 10 15 Glu Pro Gly Gln Ala Gly 20 <210> 437 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 437 Gly His Pro Gly Ser Pro Gly Ser Pro Gly Tyr Gln Gly Pro Pro Gly 1 5 10 15 Glu Pro Gly Gln Ala Gly Pro Ser 20 <210> 438 <211> 36 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 438 Gly His Pro Gly Ser Pro Gly Ser Pro Gly Tyr Gln Gly Pro Pro Gly 1 5 10 15 Glu Pro Gly Gln Ala Gly Pro Ser Gly Pro Pro Gly Pro Pro Gly Ala 20 25 30 Ile Gly Pro Ser 35 <210> 439 <211> 39 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 439 Gly His Pro Gly Ser Pro Gly Ser Pro Gly Tyr Gln Gly Pro Pro Gly 1 5 10 15 Glu Pro Gly Gln Ala Gly Pro Ser Gly Pro Pro Gly Pro Pro Gly Ala 20 25 30 Ile Gly Pro Ser Gly Pro Ala 35 <210> 440 <211> 54 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 440 Gly His Pro Gly Ser Pro Gly Ser Pro Gly Tyr Gln Gly Pro Pro Gly 1 5 10 15 Glu Pro Gly Gln Ala Gly Pro Ser Gly Pro Pro Gly Pro Pro Gly Ala 20 25 30 Ile Gly Pro Ser Gly Pro Ala Gly Lys Asp Gly Glu Ser Gly Arg Pro 35 40 45 Gly Arg Pro Gly Glu Arg 50 <210> 441 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 441 Gly His Arg Gly Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly 1 5 10 15 Ala Pro Gly Leu Lys 20 <210> 442 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 442 Gly His Arg Gly Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly 1 5 10 15 Ala Pro Gly Leu Lys Gly Glu Asn 20 <210> 443 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 443 Gly His Arg Gly Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly 1 5 10 15 Ala Pro Gly Leu Lys Gly Glu Asn Gly 20 25 <210> 444 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 444 Gly His Arg Gly Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly 1 5 10 15 Ala Pro Gly Leu Lys Gly Glu Asn Gly Leu Pro Gly Glu Asn 20 25 30 <210> 445 <211> 39 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 445 Gly His Arg Gly Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly 1 5 10 15 Ala Pro Gly Leu Lys Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala 20 25 30 Pro Gly Pro Met Gly Pro Arg 35 <210> 446 <211> 45 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 446 Gly His Arg Gly Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly 1 5 10 15 Ala Pro Gly Leu Lys Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala 20 25 30 Pro Gly Pro Met Gly Pro Arg Gly Ala Pro Gly Glu Arg 35 40 45 <210> 447 <211> 9 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 447 Gly Ile Lys Gly Pro Ala Gly Ile Pro 1 5 <210> 448 <211> 13 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 448 Gly Ile Lys Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly 1 5 10 <210> 449 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 449 Gly Ile Lys Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly 1 5 10 15 <210> 450 <211> 9 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 450 Gly Ile Pro Gly Ala Pro Gly Leu Met 1 5 <210> 451 <211> 10 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 451 Gly Ile Pro Gly Ala Pro Gly Leu Met Gly 1 5 10 <210> 452 <211> 11 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 452 Gly Ile Pro Gly Ala Pro Gly Leu Met Gly Ala 1 5 10 <210> 453 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 453 Gly Ile Pro Gly Ala Pro Gly Leu Met Gly Ala Arg 1 5 10 <210> 454 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 454 Gly Ile Pro Gly Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Gly 1 5 10 15 <210> 455 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 455 Gly Ile Pro Gly Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Gly 1 5 10 15 Pro Ala <210> 456 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 456 Gly Ile Pro Gly Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Gly 1 5 10 15 Pro Ala Gly <210> 457 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 457 Gly Ile Pro Gly Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Gly 1 5 10 15 Pro Ala Gly Ala Asn 20 <210> 458 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 458 Gly Ile Pro Gly Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Gly 1 5 10 15 Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg 20 25 <210> 459 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 459 Gly Ile Pro Gly Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Gly 1 5 10 15 Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly 20 25 <210> 460 <211> 36 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 460 Gly Ile Pro Gly Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Gly 1 5 10 15 Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly Gly Ala Gly Glu 20 25 30 Pro Gly Lys Asn 35 <210> 461 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 461 Gly Ile Pro Gly Glu Lys Gly Pro Ala Gly Glu Arg Gly Ala Pro Gly 1 5 10 15 Pro Ala <210> 462 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 462 Gly Ile Pro Gly Glu Lys Gly Pro Ala Gly Glu Arg Gly Ala Pro Gly 1 5 10 15 Pro Ala Gly <210> 463 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 463 Gly Ile Pro Gly Glu Lys Gly Pro Ala Gly Glu Arg Gly Ala Pro Gly 1 5 10 15 Pro Ala Gly Pro Arg 20 <210> 464 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 464 Gly Ile Pro Gly Glu Lys Gly Pro Ala Gly Glu Arg Gly Ala Pro Gly 1 5 10 15 Pro Ala Gly Pro Arg Gly 20 <210> 465 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 465 Gly Ile Pro Gly Glu Lys Gly Pro Ala Gly Glu Arg Gly Ala Pro Gly 1 5 10 15 Pro Ala Gly Pro Arg Gly Ala 20 <210> 466 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 466 Gly Ile Pro Gly Glu Lys Gly Pro Ala Gly Glu Arg Gly Ala Pro Gly 1 5 10 15 Pro Ala Gly Pro Arg Gly Ala Ala 20 <210> 467 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 467 Gly Ile Pro Gly Glu Lys Gly Pro Ala Gly Glu Arg Gly Ala Pro Gly 1 5 10 15 Pro Ala Gly Pro Arg Gly Ala Ala Gly 20 25 <210> 468 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 468 Gly Ile Pro Gly Glu Lys Gly Pro Ala Gly Glu Arg Gly Ala Pro Gly 1 5 10 15 Pro Ala Gly Pro Arg Gly Ala Ala Gly Glu Pro Gly 20 25 <210> 469 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 469 Gly Ile Pro Gly Glu Lys Gly Pro Ala Gly Glu Arg Gly Ala Pro Gly 1 5 10 15 Pro Ala Gly Pro Arg Gly Ala Ala Gly Glu Pro Gly Arg 20 25 <210> 470 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 470 Gly Ile Pro Gly Glu Lys Gly Pro Ala Gly Glu Arg Gly Ala Pro Gly 1 5 10 15 Pro Ala Gly Pro Arg Gly Ala Ala Gly Glu Pro Gly Arg Asp 20 25 30 <210> 471 <211> 34 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 471 Gly Ile Pro Gly Glu Lys Gly Pro Ala Gly Glu Arg Gly Ala Pro Gly 1 5 10 15 Pro Ala Gly Pro Arg Gly Ala Ala Gly Glu Pro Gly Arg Asp Gly Val 20 25 30 Pro Gly <210> 472 <211> 35 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 472 Gly Ile Pro Gly Glu Lys Gly Pro Ala Gly Glu Arg Gly Ala Pro Gly 1 5 10 15 Pro Ala Gly Pro Arg Gly Ala Ala Gly Glu Pro Gly Arg Asp Gly Val 20 25 30 Pro Gly Gly 35 <210> 473 <211> 37 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 473 Gly Ile Pro Gly Glu Lys Gly Pro Ala Gly Glu Arg Gly Ala Pro Gly 1 5 10 15 Pro Ala Gly Pro Arg Gly Ala Ala Gly Glu Pro Gly Arg Asp Gly Val 20 25 30 Pro Gly Gly Pro Gly 35 <210> 474 <211> 39 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 474 Gly Ile Pro Gly Glu Lys Gly Pro Ala Gly Glu Arg Gly Ala Pro Gly 1 5 10 15 Pro Ala Gly Pro Arg Gly Ala Ala Gly Glu Pro Gly Arg Asp Gly Val 20 25 30 Pro Gly Gly Pro Gly Met Arg 35 <210> 475 <211> 11 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 475 Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His 1 5 10 <210> 476 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 476 Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg 1 5 10 <210> 477 <211> 14 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 477 Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe 1 5 10 <210> 478 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 478 Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe Asp 1 5 10 15 <210> 479 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 479 Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe Asp Gly 1 5 10 15 Arg <210> 480 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 480 Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe Asp Gly 1 5 10 15 Arg Asn <210> 481 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 481 Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe Asp Gly 1 5 10 15 Arg Asn Gly Glu Lys 20 <210> 482 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 482 Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe Asp Gly 1 5 10 15 Arg Asn Gly Glu Lys Gly 20 <210> 483 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 483 Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe Asp Gly 1 5 10 15 Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys 20 25 30 <210> 484 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 484 Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe Asp Gly 1 5 10 15 Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys Gly Glu 20 25 30 Asn <210> 485 <211> 39 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 485 Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe Asp Gly 1 5 10 15 Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys Gly Glu 20 25 30 Asn Gly Leu Pro Gly Glu Asn 35 <210> 486 <211> 48 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 486 Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe Asp Gly 1 5 10 15 Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys Gly Glu 20 25 30 Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly Pro Arg 35 40 45 <210> 487 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 487 Gly Lys Asp Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg Gly 1 5 10 15 Leu Pro Gly Pro Pro Gly Ile Lys 20 <210> 488 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 488 Gly Lys Asp Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg Gly 1 5 10 15 Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala 20 25 <210> 489 <211> 36 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 489 Gly Lys Asp Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg Gly 1 5 10 15 Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala Gly Ile Pro Gly Phe 20 25 30 Pro Gly Met Lys 35 <210> 490 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 490 Gly Lys Asp Gly Ser Pro Gly Glu Pro Gly Ala Asn Gly Leu Pro Gly 1 5 10 15 Ala <210> 491 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 491 Gly Lys Asp Gly Ser Pro Gly Glu Pro Gly Ala Asn Gly Leu Pro Gly 1 5 10 15 Ala Ala Gly Glu Arg Gly Ala Pro Gly 20 25 <210> 492 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 492 Gly Lys Asp Gly Ser Pro Gly Glu Pro Gly Ala Asn Gly Leu Pro Gly 1 5 10 15 Ala Ala Gly Glu Arg Gly Ala Pro Gly Phe Arg Gly Pro Ala Gly Pro 20 25 30 Asn <210> 493 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 493 Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu 1 5 10 15 Met <210> 494 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 494 Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu 1 5 10 15 Met Gly <210> 495 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 495 Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu 1 5 10 15 Met Gly Ala <210> 496 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 496 Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu 1 5 10 15 Met Gly Ala Arg 20 <210> 497 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 497 Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu 1 5 10 15 Met Gly Ala Arg Gly Pro Pro Gly Pro Ala 20 25 <210> 498 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 498 Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu 1 5 10 15 Met Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn 20 25 <210> 499 <211> 35 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 499 Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu 1 5 10 15 Met Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro 20 25 30 Gly Leu Arg 35 <210> 500 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 500 Gly Lys Pro Gly Glu Pro Gly Pro Lys Gly Asp Ala Gly Ala Pro Gly 1 5 10 15 Ala Pro Gly Gly Lys Gly Asp Ala Gly Ala Pro Gly 20 25 <210> 501 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 501 Gly Lys Pro Gly Glu Pro Gly Pro Lys Gly Asp Ala Gly Ala Pro Gly 1 5 10 15 Ala Pro Gly Gly Lys Gly Asp Ala Gly Ala Pro Gly Glu 20 25 <210> 502 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 502 Gly Lys Pro Gly Glu Pro Gly Pro Lys Gly Asp Ala Gly Ala Pro Gly 1 5 10 15 Ala Pro Gly Gly Lys Gly Asp Ala Gly Ala Pro Gly Glu Arg 20 25 30 <210> 503 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 503 Gly Lys Pro Gly Glu Pro Gly Pro Lys Gly Asp Ala Gly Ala Pro Gly 1 5 10 15 Ala Pro Gly Gly Lys Gly Asp Ala Gly Ala Pro Gly Glu Arg Gly 20 25 30 <210> 504 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 504 Gly Lys Pro Gly Glu Pro Gly Pro Lys Gly Asp Ala Gly Ala Pro Gly 1 5 10 15 Ala Pro Gly Gly Lys Gly Asp Ala Gly Ala Pro Gly Glu Arg Gly Pro 20 25 30 Pro <210> 505 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 505 Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly Glu Ser Gly Arg Pro Gly 1 5 10 15 Pro Pro Gly Pro Ser Gly Pro Arg 20 <210> 506 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 506 Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly Glu Ser Gly Arg Pro Gly 1 5 10 15 Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln 20 25 <210> 507 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 507 Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly Glu Ser Gly Arg Pro Gly 1 5 10 15 Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln Pro Gly Val Met 20 25 30 <210> 508 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 508 Gly Leu Ala Gly Tyr Pro Gly Pro Ala Gly Pro Pro Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly Thr Ser 20 <210> 509 <211> 57 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 509 Gly Leu Ala Gly Tyr Pro Gly Pro Ala Gly Pro Pro Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly Thr Ser Gly His Pro Gly Ser Pro Gly Ser Pro Gly Tyr 20 25 30 Gln Gly Pro Pro Gly Glu Pro Gly Gln Ala Gly Pro Ser Gly Pro Pro 35 40 45 Gly Pro Pro Gly Ala Ile Gly Pro Ser 50 55 <210> 510 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 510 Gly Leu Lys Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly 1 5 10 15 Pro Met Gly Pro Arg 20 <210> 511 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 511 Gly Leu Met Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly 1 5 10 15 Ala Pro Gly Leu Arg 20 <210> 512 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 512 Gly Leu Pro Gly Ala Ala Gly Ala Arg Gly Asn Asp Gly Ala Arg Gly 1 5 10 15 Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr Ala 20 25 30 <210> 513 <211> 45 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 513 Gly Leu Pro Gly Ala Ala Gly Ala Arg Gly Asn Asp Gly Ala Arg Gly 1 5 10 15 Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr Ala Gly Phe 20 25 30 Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala 35 40 45 <210> 514 <211> 14 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 514 Gly Leu Pro Gly Ala Ala Gly Glu Arg Gly Ala Pro Gly Phe 1 5 10 <210> 515 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 515 Gly Leu Pro Gly Ala Ala Gly Glu Arg Gly Ala Pro Gly Phe Arg 1 5 10 15 <210> 516 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 516 Gly Leu Pro Gly Ala Ala Gly Glu Arg Gly Ala Pro Gly Phe Arg Gly 1 5 10 15 <210> 517 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 517 Gly Leu Pro Gly Ala Ala Gly Glu Arg Gly Ala Pro Gly Phe Arg Gly 1 5 10 15 Pro Ala Gly <210> 518 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 518 Gly Leu Pro Gly Ala Ala Gly Glu Arg Gly Ala Pro Gly Phe Arg Gly 1 5 10 15 Pro Ala Gly Pro Asn 20 <210> 519 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 519 Gly Leu Pro Gly Ala Ala Gly Glu Arg Gly Ala Pro Gly Phe Arg Gly 1 5 10 15 Pro Ala Gly Pro Asn Gly Ile Pro Gly Glu Lys Gly 20 25 <210> 520 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 520 Gly Leu Pro Gly Ala Ala Gly Glu Arg Gly Ala Pro Gly Phe Arg Gly 1 5 10 15 Pro Ala Gly Pro Asn Gly Ile Pro Gly Glu Lys Gly Pro Ala Gly Glu 20 25 30 Arg <210> 521 <211> 37 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 521 Gly Leu Pro Gly Ala Ala Gly Glu Arg Gly Ala Pro Gly Phe Arg Gly 1 5 10 15 Pro Ala Gly Pro Asn Gly Ile Pro Gly Glu Lys Gly Pro Ala Gly Glu 20 25 30 Arg Gly Ala Pro Gly 35 <210> 522 <211> 42 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 522 Gly Leu Pro Gly Ala Ala Gly Glu Arg Gly Ala Pro Gly Phe Arg Gly 1 5 10 15 Pro Ala Gly Pro Asn Gly Ile Pro Gly Glu Lys Gly Pro Ala Gly Glu 20 25 30 Arg Gly Ala Pro Gly Pro Ala Gly Pro Arg 35 40 <210> 523 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 523 Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met 1 5 10 <210> 524 <211> 13 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 524 Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly 1 5 10 <210> 525 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 525 Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly Pro Arg 1 5 10 15 <210> 526 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 526 Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly Pro Arg Gly 1 5 10 15 <210> 527 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 527 Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly Pro Arg Gly 1 5 10 15 Ala Pro Gly <210> 528 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 528 Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly Pro Arg Gly 1 5 10 15 Ala Pro Gly Glu Arg Gly Arg 20 <210> 529 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 529 Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly Pro Arg Gly 1 5 10 15 Ala Pro Gly Glu Arg Gly Arg Pro Gly 20 25 <210> 530 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 530 Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly Pro Arg Gly 1 5 10 15 Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala 20 25 30 Arg <210> 531 <211> 35 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 531 Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly Pro Arg Gly 1 5 10 15 Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala 20 25 30 Arg Gly Asn 35 <210> 532 <211> 40 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 532 Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly Pro Arg Gly 1 5 10 15 Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala 20 25 30 Arg Gly Asn Asp Gly Ala Arg Gly 35 40 <210> 533 <211> 44 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 533 Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly Pro Arg Gly 1 5 10 15 Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala 20 25 30 Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln 35 40 <210> 534 <211> 54 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 534 Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly Pro Arg Gly 1 5 10 15 Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala 20 25 30 Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro 35 40 45 Gly Pro Pro Gly Thr Ala 50 <210> 535 <211> 9 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 535 Gly Leu Pro Gly Pro Pro Gly Ile Lys 1 5 <210> 536 <211> 10 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 536 Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly 1 5 10 <210> 537 <211> 11 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 537 Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro 1 5 10 <210> 538 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 538 Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala 1 5 10 <210> 539 <211> 13 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 539 Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala Gly 1 5 10 <210> 540 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 540 Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala Gly Ile Pro 1 5 10 15 <210> 541 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 541 Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala Gly Ile Pro Gly 1 5 10 15 <210> 542 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 542 Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala Gly Ile Pro Gly 1 5 10 15 Phe <210> 543 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 543 Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala Gly Ile Pro Gly 1 5 10 15 Phe Pro Gly Met 20 <210> 544 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 544 Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala Gly Ile Pro Gly 1 5 10 15 Phe Pro Gly Met Lys 20 <210> 545 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 545 Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala Gly Ile Pro Gly 1 5 10 15 Phe Pro Gly Met Lys Gly 20 <210> 546 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 546 Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala Gly Ile Pro Gly 1 5 10 15 Phe Pro Gly Met Lys Gly His 20 <210> 547 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 547 Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala Gly Ile Pro Gly 1 5 10 15 Phe Pro Gly Met Lys Gly His Arg 20 <210> 548 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 548 Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala Gly Ile Pro Gly 1 5 10 15 Phe Pro Gly Met Lys Gly His Arg Gly Phe 20 25 <210> 549 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 549 Gly Leu Pro Gly Thr Gly Gly Pro Pro Gly Glu Asn 1 5 10 <210> 550 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 550 Gly Leu Arg Gly Gly Ala Gly Glu Pro Gly Lys Asn Gly Ala Lys Gly 1 5 10 15 Glu Pro Gly Pro Arg Gly Glu Arg Gly Glu Ala Gly Ile Pro 20 25 30 <210> 551 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 551 Gly Met Pro Gly Ser Pro Gly Gly Pro Gly Ser Asp Gly Lys Pro Gly 1 5 10 15 Pro Pro Gly <210> 552 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 552 Gly Met Pro Gly Ser Pro Gly Gly Pro Gly Ser Asp Gly Lys Pro Gly 1 5 10 15 Pro Pro Gly Ser Gln 20 <210> 553 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 553 Gly Met Pro Gly Ser Pro Gly Gly Pro Gly Ser Asp Gly Lys Pro Gly 1 5 10 15 Pro Pro Gly Ser Gln Gly 20 <210> 554 <211> 36 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 554 Gly Met Pro Gly Ser Pro Gly Gly Pro Gly Ser Asp Gly Lys Pro Gly 1 5 10 15 Pro Pro Gly Ser Gln Gly Glu Ser Gly Arg Pro Gly Pro Pro Gly Pro 20 25 30 Ser Gly Pro Arg 35 <210> 555 <211> 42 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 555 Gly Met Pro Gly Ser Pro Gly Gly Pro Gly Ser Asp Gly Lys Pro Gly 1 5 10 15 Pro Pro Gly Ser Gln Gly Glu Ser Gly Arg Pro Gly Pro Pro Gly Pro 20 25 30 Ser Gly Pro Arg Gly Gln Pro Gly Val Met 35 40 <210> 556 <211> 45 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 556 Gly Met Arg Gly Met Pro Gly Ser Pro Gly Gly Pro Gly Ser Asp Gly 1 5 10 15 Lys Pro Gly Pro Pro Gly Ser Gln Gly Glu Ser Gly Arg Pro Gly Pro 20 25 30 Pro Gly Pro Ser Gly Pro Arg Gly Gln Pro Gly Val Met 35 40 45 <210> 557 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 557 Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly Glu Arg Gly Gly Pro Gly 1 5 10 15 Gly Pro Gly Pro Gln Gly Pro Pro Gly Lys Asn 20 25 <210> 558 <211> 34 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 558 Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly Glu Arg Gly Gly Pro Gly 1 5 10 15 Gly Pro Gly Pro Gln Gly Pro Pro Gly Lys Asn Gly Glu Thr Gly Pro 20 25 30 Gln Gly <210> 559 <211> 38 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 559 Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly Glu Arg Gly Gly Pro Gly 1 5 10 15 Gly Pro Gly Pro Gln Gly Pro Pro Gly Lys Asn Gly Glu Thr Gly Pro 20 25 30 Gln Gly Pro Pro Gly Pro 35 <210> 560 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 560 Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly Thr Ala 20 <210> 561 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 561 Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly Thr Ala Gly 20 <210> 562 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 562 Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly Thr Ala Gly Phe 20 <210> 563 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 563 Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly Thr Ala Gly Phe Pro Gly 20 25 <210> 564 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 564 Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser 20 25 <210> 565 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 565 Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys 20 25 30 <210> 566 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 566 Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly 20 25 30 <210> 567 <211> 34 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 567 Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu 20 25 30 Val Gly <210> 568 <211> 36 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 568 Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu 20 25 30 Val Gly Pro Ala 35 <210> 569 <211> 37 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 569 Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu 20 25 30 Val Gly Pro Ala Gly 35 <210> 570 <211> 38 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 570 Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu 20 25 30 Val Gly Pro Ala Gly Ser 35 <210> 571 <211> 40 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 571 Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu 20 25 30 Val Gly Pro Ala Gly Ser Pro Gly 35 40 <210> 572 <211> 42 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 572 Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu 20 25 30 Val Gly Pro Ala Gly Ser Pro Gly Ser Asn 35 40 <210> 573 <211> 48 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 573 Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu 20 25 30 Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg 35 40 45 <210> 574 <211> 50 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 574 Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu 20 25 30 Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg 35 40 45 Gly Glu 50 <210> 575 <211> 54 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 575 Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu 20 25 30 Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg 35 40 45 Gly Glu Pro Gly Pro Gln 50 <210> 576 <211> 55 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 576 Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu 20 25 30 Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg 35 40 45 Gly Glu Pro Gly Pro Gln Gly 50 55 <210> 577 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 577 Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly Gly Ala Gly 1 5 10 15 Glu Pro Gly <210> 578 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 578 Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met 1 5 10 <210> 579 <211> 13 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 579 Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met Gly 1 5 10 <210> 580 <211> 14 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 580 Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met Gly Ala 1 5 10 <210> 581 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 581 Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met Gly Ala Arg 1 5 10 15 <210> 582 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 582 Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met Gly Ala Arg Gly 1 5 10 15 Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg 20 25 30 <210> 583 <211> 9 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 583 Gly Pro Ala Gly Ile Pro Gly Phe Pro 1 5 <210> 584 <211> 10 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 584 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly 1 5 10 <210> 585 <211> 11 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 585 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met 1 5 10 <210> 586 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 586 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys 1 5 10 <210> 587 <211> 13 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 587 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly 1 5 10 <210> 588 <211> 14 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 588 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His 1 5 10 <210> 589 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 589 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg 1 5 10 15 <210> 590 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 590 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly 1 5 10 15 <210> 591 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 591 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly 1 5 10 15 Phe <210> 592 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 592 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly 1 5 10 15 Phe Asp <210> 593 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 593 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly 1 5 10 15 Phe Asp Gly <210> 594 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 594 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly 1 5 10 15 Phe Asp Gly Arg 20 <210> 595 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 595 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly 1 5 10 15 Phe Asp Gly Arg Asn 20 <210> 596 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 596 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly 1 5 10 15 Phe Asp Gly Arg Asn Gly 20 <210> 597 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 597 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly 1 5 10 15 Phe Asp Gly Arg Asn Gly Glu 20 <210> 598 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 598 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly 1 5 10 15 Phe Asp Gly Arg Asn Gly Glu Lys 20 <210> 599 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 599 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly 1 5 10 15 Phe Asp Gly Arg Asn Gly Glu Lys Gly 20 25 <210> 600 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 600 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly 1 5 10 15 Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu 20 25 <210> 601 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 601 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly 1 5 10 15 Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr 20 25 <210> 602 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 602 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly 1 5 10 15 Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly 20 25 <210> 603 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 603 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly 1 5 10 15 Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala 20 25 <210> 604 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 604 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly 1 5 10 15 Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro 20 25 30 <210> 605 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 605 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly 1 5 10 15 Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly 20 25 30 <210> 606 <211> 32 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 606 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly 1 5 10 15 Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu 20 25 30 <210> 607 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 607 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly 1 5 10 15 Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu 20 25 30 Lys <210> 608 <211> 34 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 608 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly 1 5 10 15 Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu 20 25 30 Lys Gly <210> 609 <211> 36 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 609 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly 1 5 10 15 Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu 20 25 30 Lys Gly Glu Asn 35 <210> 610 <211> 40 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 610 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly 1 5 10 15 Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu 20 25 30 Lys Gly Glu Asn Gly Leu Pro Gly 35 40 <210> 611 <211> 42 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 611 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly 1 5 10 15 Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu 20 25 30 Lys Gly Glu Asn Gly Leu Pro Gly Glu Asn 35 40 <210> 612 <211> 48 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 612 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly 1 5 10 15 Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu 20 25 30 Lys Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met 35 40 45 <210> 613 <211> 51 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 613 Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly 1 5 10 15 Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu 20 25 30 Lys Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met 35 40 45 Gly Pro Arg 50 <210> 614 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 614 Gly Pro Ala Gly Lys Asp Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly 1 5 10 15 Glu Arg Gly Leu Pro Gly Pro Pro 20 <210> 615 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 615 Gly Pro Ala Gly Lys Asp Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly 1 5 10 15 Glu Arg Gly Leu Pro Gly Pro Gly 20 25 <210> 616 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 616 Gly Pro Ala Gly Lys Asp Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly 1 5 10 15 Glu Arg Gly Leu Pro Gly Pro Pro Gly Ile Lys 20 25 <210> 617 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 617 Gly Pro Ala Gly Lys Asp Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly 1 5 10 15 Glu Arg Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala 20 25 30 <210> 618 <211> 39 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 618 Gly Pro Ala Gly Lys Asp Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly 1 5 10 15 Glu Arg Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala Gly Ile 20 25 30 Pro Gly Phe Pro Gly Met Lys 35 <210> 619 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 619 Gly Pro Ala Gly Pro Asn Gly Ile Pro Gly Glu Lys Gly Pro Ala Gly 1 5 10 15 Glu Arg Gly Ala Pro Gly Pro Ala Gly Pro Arg 20 25 <210> 620 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 620 Gly Pro Ala Gly Pro Pro Gly Pro Pro Gly Pro Pro 1 5 10 <210> 621 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 621 Gly Pro Gly Met Arg Gly Met Pro Gly Ser Pro Gly Gly Pro Gly Ser 1 5 10 15 Asp Gly Lys Pro Gly Pro Pro Gly 20 <210> 622 <211> 47 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 622 Gly Pro Gly Met Arg Gly Met Pro Gly Ser Pro Gly Gly Pro Gly Ser 1 5 10 15 Asp Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly Glu Ser Gly Arg Pro 20 25 30 Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln Pro Gly Val Met 35 40 45 <210> 623 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 623 Gly Pro Gly Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly Glu 1 5 10 15 Ser Gly Arg Pro Gly Pro Pro Gly 20 <210> 624 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 624 Gly Pro Gly Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly Glu 1 5 10 15 Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly 20 25 <210> 625 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 625 Gly Pro Gly Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly Glu 1 5 10 15 Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg 20 25 <210> 626 <211> 35 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 626 Gly Pro Gly Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly Glu 1 5 10 15 Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln Pro 20 25 30 Gly Val Met 35 <210> 627 <211> 43 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 627 Gly Pro Gly Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly Glu 1 5 10 15 Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln Pro 20 25 30 Gly Val Met Gly Phe Pro Gly Pro Lys Gly Asn 35 40 <210> 628 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 628 Gly Pro Met Gly Pro Arg Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly 1 5 10 15 Leu Pro Gly Ala Ala 20 <210> 629 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 629 Gly Pro Met Gly Pro Arg Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly 1 5 10 15 Leu Pro Gly Ala Ala Gly Ala Arg 20 <210> 630 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 630 Gly Pro Asn Gly Ile Pro Gly Glu Lys Gly Pro Ala Gly Glu Arg Gly 1 5 10 15 Ala Pro Gly Pro Ala 20 <210> 631 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 631 Gly Pro Pro Gly Ala Ile Gly Pro Ser Gly Pro Ala Gly Lys Asp Gly 1 5 10 15 Glu Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg 20 25 <210> 632 <211> 36 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 632 Gly Pro Pro Gly Ala Ile Gly Pro Ser Gly Pro Ala Gly Lys Asp Gly 1 5 10 15 Glu Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg Gly Leu Pro Gly Pro 20 25 30 Pro Gly Ile Lys 35 <210> 633 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 633 Gly Pro Pro Gly Glu Pro Gly Gln Ala Gly Pro Ser Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly <210> 634 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 634 Gly Pro Pro Gly Glu Pro Gly Gln Ala Gly Pro Ser Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly Ala Ile Gly Pro Ser 20 <210> 635 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 635 Gly Pro Pro Gly Glu Pro Gly Gln Ala Gly Pro Ser Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly Ala Ile Gly Pro Ser Gly Pro Ala Gly Lys Asp 20 25 30 <210> 636 <211> 51 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 636 Gly Pro Pro Gly Glu Pro Gly Gln Ala Gly Pro Ser Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly Ala Ile Gly Pro Ser Gly Pro Ala Gly Lys Asp Gly Glu 20 25 30 Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg Gly Leu Pro Gly Pro Pro 35 40 45 Gly Ile Lys 50 <210> 637 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 637 Gly Pro Pro Gly Ile Lys Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly 1 5 10 15 Met Lys <210> 638 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 638 Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly Lys Gly Glu Met Gly 1 5 10 15 Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met 20 25 <210> 639 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 639 Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg 1 5 10 15 <210> 640 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 640 Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly 1 5 10 15 <210> 641 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 641 Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly 1 5 10 15 Gly <210> 642 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 642 Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly 1 5 10 15 Gly Ala <210> 643 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 643 Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly 1 5 10 15 Gly Ala Gly <210> 644 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 644 Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly 1 5 10 15 Gly Ala Gly Glu 20 <210> 645 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 645 Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly 1 5 10 15 Gly Ala Gly Glu Pro 20 <210> 646 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 646 Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly 1 5 10 15 Gly Ala Gly Glu Pro Gly 20 <210> 647 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 647 Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly 1 5 10 15 Gly Ala Gly Glu Pro Gly Lys 20 <210> 648 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 648 Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly 1 5 10 15 Gly Ala Gly Glu Pro Gly Lys Asn 20 <210> 649 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 649 Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly 1 5 10 15 Gly Ala Gly Glu Pro Gly Lys Asn Gly 20 25 <210> 650 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 650 Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly 1 5 10 15 Gly Ala Gly Glu Pro Gly Lys Asn Gly Ala 20 25 <210> 651 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 651 Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly 1 5 10 15 Gly Ala Gly Glu Pro Gly Lys Asn Gly Ala Lys 20 25 <210> 652 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 652 Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly 1 5 10 15 Gly Ala Gly Glu Pro Gly Lys Asn Gly Ala Lys Gly 20 25 <210> 653 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 653 Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly 1 5 10 15 Gly Ala Gly Glu Pro Gly Lys Asn Gly Ala Lys Gly Glu 20 25 <210> 654 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 654 Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly 1 5 10 15 Gly Ala Gly Glu Pro Gly Lys Asn Gly Ala Lys Gly Glu Pro Gly 20 25 30 <210> 655 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 655 Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly 1 5 10 15 Gly Ala Gly Glu Pro Gly Lys Asn Gly Ala Lys Gly Glu Pro Gly Pro 20 25 30 Arg <210> 656 <211> 34 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 656 Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly 1 5 10 15 Gly Ala Gly Glu Pro Gly Lys Asn Gly Ala Lys Gly Glu Pro Gly Pro 20 25 30 Arg Gly <210> 657 <211> 35 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 657 Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly 1 5 10 15 Gly Ala Gly Glu Pro Gly Lys Asn Gly Ala Lys Gly Glu Pro Gly Pro 20 25 30 Arg Gly Glu 35 <210> 658 <211> 36 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 658 Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly 1 5 10 15 Gly Ala Gly Glu Pro Gly Lys Asn Gly Ala Lys Gly Glu Pro Gly Pro 20 25 30 Arg Gly Glu Arg 35 <210> 659 <211> 37 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 659 Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly 1 5 10 15 Gly Ala Gly Glu Pro Gly Lys Asn Gly Ala Lys Gly Glu Pro Gly Pro 20 25 30 Arg Gly Glu Arg Gly 35 <210> 660 <211> 38 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 660 Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly 1 5 10 15 Gly Ala Gly Glu Pro Gly Lys Asn Gly Ala Lys Gly Glu Pro Gly Pro 20 25 30 Arg Gly Glu Arg Gly Glu 35 <210> 661 <211> 39 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 661 Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly 1 5 10 15 Gly Ala Gly Glu Pro Gly Lys Asn Gly Ala Lys Gly Glu Pro Gly Pro 20 25 30 Arg Gly Glu Arg Gly Glu Ala 35 <210> 662 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 662 Gly Pro Pro Gly Pro Pro Gly Ala Ile Gly Pro Ser 1 5 10 <210> 663 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 663 Gly Pro Pro Gly Pro Pro Gly Ala Ile Gly Pro Ser Gly Pro Ala 1 5 10 15 <210> 664 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 664 Gly Pro Pro Gly Pro Pro Gly Ala Ile Gly Pro Ser Gly Pro Ala Gly 1 5 10 15 Lys Asp Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg 20 25 30 <210> 665 <211> 39 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 665 Gly Pro Pro Gly Pro Pro Gly Ala Ile Gly Pro Ser Gly Pro Ala Gly 1 5 10 15 Lys Asp Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg Gly Leu 20 25 30 Pro Gly Pro Pro Gly Ile Lys 35 <210> 666 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 666 Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly Lys Gly 1 5 10 15 Glu Met Gly Pro Ala 20 <210> 667 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 667 Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly Lys Gly 1 5 10 15 Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met 20 25 30 <210> 668 <211> 32 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 668 Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly Lys Gly 1 5 10 15 Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met Gly Ala 20 25 30 <210> 669 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 669 Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly Lys Gly 1 5 10 15 Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met Gly Ala 20 25 30 Arg <210> 670 <211> 48 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 670 Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly Lys Gly 1 5 10 15 Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met Gly Ala 20 25 30 Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg 35 40 45 <210> 671 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 671 Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Thr Ser 1 5 10 <210> 672 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 672 Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Thr Ser Gly His Pro Gly 1 5 10 15 <210> 673 <211> 48 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 673 Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Thr Ser Gly His Pro Gly 1 5 10 15 Ser Pro Gly Ser Pro Gly Tyr Gln Gly Pro Pro Gly Glu Pro Gly Gln 20 25 30 Ala Gly Pro Ser Gly Pro Pro Gly Pro Pro Gly Ala Ile Gly Pro Ser 35 40 45 <210> 674 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 674 Gly Pro Pro Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly 1 5 10 15 Ala Lys <210> 675 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 675 Gly Pro Pro Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly 1 5 10 15 Ala Lys Gly Glu Val Gly Pro Ala 20 <210> 676 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 676 Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln Pro Gly Val Met 1 5 10 15 <210> 677 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 677 Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln Pro Gly Val Met Gly 1 5 10 15 Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn 20 25 30 <210> 678 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 678 Gly Pro Pro Gly Ser Gln Gly Glu Ser Gly Arg Pro Gly Pro Pro Gly 1 5 10 15 Pro Ser Gly Pro Arg Gly Gln Pro Gly Val Met 20 25 <210> 679 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 679 Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly 1 5 10 15 Glu Val Gly Pro Ala 20 <210> 680 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 680 Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly 1 5 10 15 Ile Asn <210> 681 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 681 Gly Pro Arg Gly Ala Ala Gly Glu Pro Gly Arg Asp Gly Val Pro Gly 1 5 10 15 Gly Pro Gly Met Arg Gly Met Pro Gly 20 25 <210> 682 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 682 Gly Pro Arg Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly 1 5 10 15 Ala Ala <210> 683 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 683 Gly Pro Arg Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly 1 5 10 15 Ala Ala Gly Ala 20 <210> 684 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 684 Gly Pro Arg Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly 1 5 10 15 Ala Ala Gly Ala Arg 20 <210> 685 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 685 Gly Pro Arg Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly 1 5 10 15 Ala Ala Gly Ala Arg Gly Asn 20 <210> 686 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 686 Gly Pro Arg Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly 1 5 10 15 Ala Ala Gly Ala Arg Gly Asn Asp Gly Ala Arg Gly 20 25 <210> 687 <211> 42 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 687 Gly Pro Arg Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly 1 5 10 15 Ala Ala Gly Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln 20 25 30 Pro Gly Pro Pro Gly Pro Pro Gly Thr Ala 35 40 <210> 688 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 688 Gly Pro Arg Gly Gln Pro Gly Val Met Gly Phe Pro Gly Pro Lys Gly 1 5 10 15 Asn <210> 689 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 689 Gly Pro Arg Gly Gln Pro Gly Val Met Gly Phe Pro Gly Pro Lys Gly 1 5 10 15 Asn Asp Gly Ala Pro Gly Lys Asn 20 <210> 690 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 690 Gly Pro Ser Gly Pro Ala Gly Lys Asp Gly Glu Ser Gly Arg Pro Gly 1 5 10 15 Arg Pro Gly Glu Arg Gly Leu Pro Gly Pro Gly Ile Lys 20 25 30 <210> 691 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 691 Gly Pro Ser Gly Pro Ala Gly Lys Asp Gly Glu Ser Gly Arg Pro Gly 1 5 10 15 Arg Pro Gly Glu Arg Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro 20 25 30 Ala <210> 692 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 692 Gly Pro Ser Gly Pro Pro Gly Pro Pro Gly Ala Ile Gly Pro Ser 1 5 10 15 <210> 693 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 693 Gly Pro Ser Gly Pro Arg Gly Gln Pro Gly Val Met Gly Phe Pro Gly 1 5 10 15 Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn 20 25 <210> 694 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 694 Gly Gln Ala Gly Pro Ser Gly Pro Pro Gly Pro Pro Gly Ala Ile Gly 1 5 10 15 Pro Ser <210> 695 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 695 Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr Ala 1 5 10 <210> 696 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 696 Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly 1 5 10 15 Ser Pro Gly Ala Lys 20 <210> 697 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 697 Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly 1 5 10 15 Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala 20 25 <210> 698 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 698 Gly Gln Pro Gly Val Met Gly Phe Pro Gly Pro Lys 1 5 10 <210> 699 <211> 14 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 699 Gly Gln Pro Gly Val Met Gly Phe Pro Gly Pro Lys Gly Asn 1 5 10 <210> 700 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 700 Gly Gln Pro Gly Val Met Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly 1 5 10 15 Ala Pro Gly Lys Asn 20 <210> 701 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 701 Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly 1 5 10 15 Pro Pro Gly Pro Pro Gly Ile Asn 20 <210> 702 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 702 Gly Arg Asp Gly Val Pro Gly Gly Pro Gly Met Arg Gly Met Pro Gly 1 5 10 15 Ser Pro Gly Gly Pro Gly 20 <210> 703 <211> 54 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 703 Gly Arg Asp Gly Val Pro Gly Gly Pro Gly Met Arg Gly Met Pro Gly 1 5 10 15 Ser Pro Gly Gly Pro Gly Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser 20 25 30 Gln Gly Glu Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg 35 40 45 Gly Gln Pro Gly Val Met 50 <210> 704 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 704 Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys Gly 1 5 10 15 Glu Asn Gly Leu Pro Gly Glu Asn 20 <210> 705 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 705 Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys Gly 1 5 10 15 Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly Pro 20 25 30 Arg <210> 706 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 706 Gly Arg Pro Gly Glu Arg Gly Leu Pro Gly Pro Pro Gly Ile Lys 1 5 10 15 <210> 707 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 707 Gly Arg Pro Gly Glu Arg Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly 1 5 10 15 Pro Ala <210> 708 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 708 Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala Arg 1 5 10 <210> 709 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 709 Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala Arg Gly Asn Asp Gly 1 5 10 15 Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr 20 25 30 Ala <210> 710 <211> 42 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 710 Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala Arg Gly Asn Asp Gly 1 5 10 15 Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr 20 25 30 Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys 35 40 <210> 711 <211> 48 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 711 Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala Arg Gly Asn Asp Gly 1 5 10 15 Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr 20 25 30 Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala 35 40 45 <210> 712 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 712 Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln Pro Gly 1 5 10 15 Val Met <210> 713 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 713 Gly Arg Pro Gly Arg Pro Gly Glu Arg Gly Leu Pro Gly Pro Pro Gly 1 5 10 15 Ile Lys <210> 714 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 714 Gly Arg Pro Gly Arg Pro Gly Glu Arg Gly Leu Pro Gly Pro Pro Gly 1 5 10 15 Ile Lys Gly Pro Ala 20 <210> 715 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 715 Gly Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly Glu Ser Gly 1 5 10 15 Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln Pro Gly Val 20 25 30 Met <210> 716 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 716 Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr Ala 1 5 10 15 <210> 717 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 717 Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr Ala Gly 1 5 10 15 Phe Pro Gly Ser Pro Gly Ala Lys 20 <210> 718 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 718 Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr Ala Gly 1 5 10 15 Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala 20 25 30 <210> 719 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 719 Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly 1 5 10 15 His Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn 20 25 30 <210> 720 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 720 Gly Ser Pro Gly Glu Pro Gly Ala Asn Gly Leu Pro Gly Ala Ala Gly 1 5 10 15 Glu Arg Gly Ala Pro Gly Phe Arg Gly Pro Ala Gly Pro Asn 20 25 30 <210> 721 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 721 Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly 1 5 10 15 Ala Pro Gly <210> 722 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 722 Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly 1 5 10 15 Ala Pro Gly Leu Met 20 <210> 723 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 723 Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly 1 5 10 15 Ala Pro Gly Leu Met Gly 20 <210> 724 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 724 Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly 1 5 10 15 Ala Pro Gly Leu Met Gly Ala 20 <210> 725 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 725 Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly 1 5 10 15 Ala Pro Gly Leu Met Gly Ala Arg 20 <210> 726 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 726 Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly 1 5 10 15 Ala Pro Gly Leu Met Gly Ala Arg Gly 20 25 <210> 727 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 727 Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly 1 5 10 15 Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Pro Gly 20 25 <210> 728 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 728 Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly 1 5 10 15 Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Pro Gly Pro Ala 20 25 30 <210> 729 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 729 Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly 1 5 10 15 Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly 20 25 30 <210> 730 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 730 Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly 1 5 10 15 Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala 20 25 30 Asn <210> 731 <211> 39 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 731 Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly 1 5 10 15 Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala 20 25 30 Asn Gly Ala Pro Gly Leu Arg 35 <210> 732 <211> 48 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 732 Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly 1 5 10 15 Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala 20 25 30 Asn Gly Ala Pro Gly Leu Arg Gly Gly Ala Gly Glu Pro Gly Lys Asn 35 40 45 <210> 733 <211> 39 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 733 Gly Ser Pro Gly Gly Pro Gly Ser Asp Gly Lys Pro Gly Pro Pro Gly 1 5 10 15 Ser Gln Gly Glu Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro 20 25 30 Arg Gly Gln Pro Gly Val Met 35 <210> 734 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 734 Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly 1 5 10 15 Pro Gln <210> 735 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 735 Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly 1 5 10 15 Pro Gln Gly His Ala Gly Ala Gln 20 <210> 736 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 736 Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly 1 5 10 15 Pro Gln Gly His Ala Gly Ala Gln Gly Pro 20 25 <210> 737 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 737 Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly 1 5 10 15 Pro Gln Gly His Ala Gly Ala Gln Gly Pro Pro 20 25 <210> 738 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 738 Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly 1 5 10 15 Pro Gln Gly His Ala Gly Ala Gln Gly Pro Pro Gly 20 25 <210> 739 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 739 Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly 1 5 10 15 Pro Gln Gly His Ala Gly Ala Gln Gly Pro Pro Gly Pro 20 25 <210> 740 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 740 Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly 1 5 10 15 Pro Gln Gly His Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro 20 25 30 <210> 741 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 741 Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly 1 5 10 15 Pro Gln Gly His Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly 20 25 30 <210> 742 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 742 Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly 1 5 10 15 Pro Gln Gly His Ala Gly Ala Gly Gly Pro Pro Gly Pro Pro Gly Ile 20 25 30 Asn <210> 743 <211> 34 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 743 Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly 1 5 10 15 Pro Gln Gly His Ala Gly Ala Gly Gly Pro Pro Gly Pro Pro Gly Ile 20 25 30 Asn Gly <210> 744 <211> 35 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 744 Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly 1 5 10 15 Pro Gln Gly His Ala Gly Ala Gly Gly Pro Pro Gly Pro Pro Gly Ile 20 25 30 Asn Gly Ser 35 <210> 745 <211> 37 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 745 Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly 1 5 10 15 Pro Gln Gly His Ala Gly Ala Gly Gly Pro Pro Gly Pro Pro Gly Ile 20 25 30 Asn Gly Ser Pro Gly 35 <210> 746 <211> 38 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 746 Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly 1 5 10 15 Pro Gln Gly His Ala Gly Ala Gly Gly Pro Pro Gly Pro Pro Gly Ile 20 25 30 Asn Gly Ser Pro Gly Gly 35 <210> 747 <211> 39 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 747 Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly 1 5 10 15 Pro Gln Gly His Ala Gly Ala Gly Gly Pro Pro Gly Pro Pro Gly Ile 20 25 30 Asn Gly Ser Pro Gly Gly Lys 35 <210> 748 <211> 40 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 748 Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly 1 5 10 15 Pro Gln Gly His Ala Gly Ala Gly Gly Pro Pro Gly Pro Pro Gly Ile 20 25 30 Asn Gly Ser Pro Gly Gly Lys Gly 35 40 <210> 749 <211> 42 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 749 Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly 1 5 10 15 Pro Gln Gly His Ala Gly Ala Gly Gly Pro Pro Gly Pro Pro Gly Ile 20 25 30 Asn Gly Ser Pro Gly Gly Lys Gly Glu Met 35 40 <210> 750 <211> 43 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 750 Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly 1 5 10 15 Pro Gln Gly His Ala Gly Ala Gly Gly Pro Pro Gly Pro Pro Gly Ile 20 25 30 Asn Gly Ser Pro Gly Gly Lys Gly Glu Met Gly 35 40 <210> 751 <211> 45 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 751 Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly 1 5 10 15 Pro Gln Gly His Ala Gly Ala Gly Gly Pro Pro Gly Pro Pro Gly Ile 20 25 30 Asn Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala 35 40 45 <210> 752 <211> 54 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 752 Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly 1 5 10 15 Pro Gln Gly His Ala Gly Ala Gly Gly Pro Pro Gly Pro Pro Gly Ile 20 25 30 Asn Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro 35 40 45 Gly Ala Pro Gly Leu Met 50 <210> 753 <211> 55 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 753 Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly 1 5 10 15 Pro Gln Gly His Ala Gly Ala Gly Gly Pro Pro Gly Pro Pro Gly Ile 20 25 30 Asn Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro 35 40 45 Gly Ala Pro Gly Leu Met Gly 50 55 <210> 754 <211> 56 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 754 Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly 1 5 10 15 Pro Gln Gly His Ala Gly Ala Gly Gly Pro Pro Gly Pro Pro Gly Ile 20 25 30 Asn Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro 35 40 45 Gly Ala Pro Gly Leu Met Gly Ala 50 55 <210> 755 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 755 Gly Ser Gln Gly Glu Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly 1 5 10 15 Pro Arg Gly Gln Pro Gly Val Met 20 <210> 756 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 756 Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly 1 5 10 15 Pro Ala <210> 757 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 757 Gly Val Pro Gly Gly Pro Gly Met Arg Gly Met Pro Gly Ser Pro Gly 1 5 10 15 Gly Pro Gly Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser Gln 20 25 30 <210> 758 <211> 51 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 758 Gly Val Pro Gly Gly Pro Gly Met Arg Gly Met Pro Gly Ser Pro Gly 1 5 10 15 Gly Pro Gly Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly Glu 20 25 30 Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln Pro 35 40 45 Gly Val Met 50 <210> 759 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 759 Gly Tyr Pro Gly Pro Ala Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly 1 5 10 15 Thr <210> 760 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 760 Gly Tyr Pro Gly Pro Ala Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly 1 5 10 15 Thr Ser <210> 761 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 761 Gly Tyr Pro Gly Pro Ala Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly 1 5 10 15 Thr Ser Gly His 20 <210> 762 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 762 Gly Tyr Pro Gly Pro Ala Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly 1 5 10 15 Thr Ser Gly His Pro Gly 20 <210> 763 <211> 54 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 763 Gly Tyr Pro Gly Pro Ala Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly 1 5 10 15 Thr Ser Gly His Pro Gly Ser Pro Gly Ser Pro Gly Tyr Gln Gly Pro 20 25 30 Pro Gly Glu Pro Gly Gln Ala Gly Pro Ser Gly Pro Pro Gly Pro Pro 35 40 45 Gly Ala Ile Gly Pro Ser 50 <210> 764 <211> 14 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 764 His Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn 1 5 10 <210> 765 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 765 His Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser 1 5 10 15 Pro Gly <210> 766 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 766 His Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser 1 5 10 15 Pro Gly Gly Lys Gly Glu Met Gly 20 <210> 767 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 767 His Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser 1 5 10 15 Pro Gly Gly Lys Gly Glu Met Gly Pro Ala 20 25 <210> 768 <211> 38 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 768 His Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser 1 5 10 15 Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala Pro 20 25 30 Gly Leu Met Gly Ala Arg 35 <210> 769 <211> 35 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 769 His Pro Gly Ser Pro Gly Ser Pro Gly Tyr Gln Gly Pro Pro Gly Glu 1 5 10 15 Pro Gly Gln Ala Gly Pro Ser Gly Pro Pro Gly Pro Pro Gly Ala Ile 20 25 30 Gly Pro Ser 35 <210> 770 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 770 His Arg Gly Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala 1 5 10 15 Pro Gly Leu Lys Gly Glu Asn 20 <210> 771 <211> 38 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 771 His Arg Gly Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala 1 5 10 15 Pro Gly Leu Lys Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro 20 25 30 Gly Pro Met Gly Pro Arg 35 <210> 772 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 772 Ile Gly Pro Ser Gly Pro Ala Gly Lys Asp Gly Glu Ser Gly Arg Pro 1 5 10 15 Gly Arg Pro Gly Glu Arg Gly Leu Pro Gly Pro Pro Gly Ile Lys 20 25 30 <210> 773 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 773 Ile Lys Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly 1 5 10 <210> 774 <211> 14 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 774 Ile Lys Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys 1 5 10 <210> 775 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 775 Ile Pro Gly Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Pro Gly Pro 1 5 10 15 Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg 20 25 <210> 776 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 776 Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe Asp Gly Arg 1 5 10 15 Asn <210> 777 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 777 Lys Asp Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg Gly Leu 1 5 10 15 Pro Gly Pro Pro Gly Ile Lys 20 <210> 778 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 778 Lys Asp Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg Gly Leu 1 5 10 15 Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala 20 25 <210> 779 <211> 32 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 779 Lys Asp Gly Ser Pro Gly Glu Pro Gly Ala Asn Gly Leu Pro Gly Ala 1 5 10 15 Ala Gly Glu Arg Gly Ala Pro Gly Phe Arg Gly Pro Ala Gly Pro Asn 20 25 30 <210> 780 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 780 Lys Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met 1 5 10 15 Gly Pro Arg <210> 781 <211> 13 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 781 Lys Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys 1 5 10 <210> 782 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 782 Lys Pro Gly Pro Pro Gly Ser Gln Gly Glu Ser Gly Arg Pro Gly Pro 1 5 10 15 Pro Gly Pro Ser Gly Pro Arg 20 <210> 783 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 783 Lys Pro Gly Pro Pro Gly Ser Gln Gly Glu Ser Gly Arg Pro Gly Pro 1 5 10 15 Pro Gly Pro Ser Gly Pro Arg Gly Gln Pro Gly Val Met 20 25 <210> 784 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 784 Leu Lys Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro 1 5 10 15 Met Gly Pro Arg 20 <210> 785 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 785 Leu Met Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala 1 5 10 15 Pro Gly Leu Arg 20 <210> 786 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 786 Leu Pro Gly Ala Ala Gly Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser 1 5 10 15 Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr Ala 20 25 <210> 787 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 787 Leu Pro Gly Ala Ala Gly Glu Arg Gly Ala Pro Gly Phe Arg Gly Pro 1 5 10 15 Ala Gly Pro Asn 20 <210> 788 <211> 8 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 788 Leu Pro Gly Pro Pro Gly Ile Lys 1 5 <210> 789 <211> 11 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 789 Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala 1 5 10 <210> 790 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 790 Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala Gly Ile Pro Gly Phe 1 5 10 15 Pro Gly Met Lys 20 <210> 791 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 791 Met Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro 1 5 10 15 Gly Leu Arg <210> 792 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 792 Met Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro 1 5 10 15 Gly Leu Arg Gly Gly Ala Gly Glu Pro Gly Lys Asn 20 25 <210> 793 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 793 Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met Gly Ala Arg 1 5 10 15 Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg 20 25 30 <210> 794 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 794 Met Gly Pro Arg Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro 1 5 10 15 Gly Ala Ala Gly Ala Arg 20 <210> 795 <211> 41 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 795 Met Pro Gly Ser Pro Gly Gly Pro Gly Ser Asp Gly Lys Pro Gly Pro 1 5 10 15 Pro Gly Ser Gln Gly Glu Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser 20 25 30 Gly Pro Arg Gly Gln Pro Gly Val Met 35 40 <210> 796 <211> 44 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 796 Met Arg Gly Met Pro Gly Ser Pro Gly Gly Pro Gly Ser Asp Gly Lys 1 5 10 15 Pro Gly Pro Pro Gly Ser Gln Gly Glu Ser Gly Arg Pro Gly Pro Pro 20 25 30 Gly Pro Ser Gly Pro Arg Gly Gln Pro Gly Val Met 35 40 <210> 797 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 797 Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro 1 5 10 15 Pro Gly Thr Ala 20 <210> 798 <211> 35 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 798 Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro 1 5 10 15 Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val 20 25 30 Gly Pro Ala 35 <210> 799 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 799 Asn Gly Ala Pro Gly Pro Met Gly Pro Arg Gly Ala Pro Gly Glu 1 5 10 15 <210> 800 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 800 Asn Gly Ala Pro Gly Pro Met Gly Pro Arg Gly Ala Pro Gly Glu Arg 1 5 10 15 Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala Arg 20 25 <210> 801 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 801 Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys Gly Glu Asn 1 5 10 15 Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly Pro Arg 20 25 30 <210> 802 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 802 Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly Pro Gly 1 5 10 15 Gly Asp <210> 803 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 803 Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly Pro Arg 1 5 10 15 <210> 804 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 804 Asn Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro 1 5 10 15 Gly Ala Pro Gly Leu Met 20 <210> 805 <211> 40 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 805 Asn Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro 1 5 10 15 Gly Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly 20 25 30 Ala Asn Gly Ala Pro Gly Leu Arg 35 40 <210> 806 <211> 11 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 806 Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met 1 5 10 <210> 807 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 807 Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met Gly 1 5 10 <210> 808 <211> 11 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 808 Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys 1 5 10 <210> 809 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 809 Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly 1 5 10 <210> 810 <211> 14 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 810 Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg 1 5 10 <210> 811 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 811 Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly 1 5 10 15 <210> 812 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 812 Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe 1 5 10 15 <210> 813 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 813 Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe 1 5 10 15 Asp Gly <210> 814 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 814 Pro Ala Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe 1 5 10 15 Asp Gly Arg Asn 20 <210> 815 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 815 Pro Ala Gly Lys Asp Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly Glu 1 5 10 15 Arg Gly Leu Pro Gly Pro Pro Gly Ile Lys 20 25 <210> 816 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 816 Pro Gly Ala Ala Gly Glu Arg Gly Ala Pro Gly Phe Arg Gly Pro Ala 1 5 10 15 Gly Pro Asn <210> 817 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 817 Pro Gly Ala Asn Gly Leu Pro Gly Ala Ala Gly Glu Arg Gly Ala Pro 1 5 10 15 <210> 818 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 818 Pro Gly Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Pro Gly Pro Ala 1 5 10 15 Gly Ala Asn Gly Ala Pro Gly Leu Arg 20 25 <210> 819 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 819 Pro Gly Glu Pro Gly Pro Lys Gly Asp Ala Gly Ala Pro Gly Ala Pro 1 5 10 15 Gly Gly Lys Gly Asp Ala Gly Ala Pro Gly Glu 20 25 <210> 820 <211> 13 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 820 Pro Gly Glu Arg Gly Leu Pro Gly Pro Gly Ile Lys 1 5 10 <210> 821 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 821 Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala Arg 1 5 10 15 <210> 822 <211> 9 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 822 Pro Gly Phe Pro Gly Met Lys Gly His 1 5 <210> 823 <211> 10 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 823 Pro Gly Phe Pro Gly Met Lys Gly His Arg 1 5 10 <210> 824 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 824 Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe 1 5 10 <210> 825 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 825 Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe Asp Gly Arg 1 5 10 15 <210> 826 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 826 Pro Gly Leu Met Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn 1 5 10 15 Gly Ala Pro Gly Leu 20 <210> 827 <211> 41 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 827 Pro Gly Leu Pro Gly Ala Ala Gly Ala Arg Gly Asn Asp Gly Ala Arg 1 5 10 15 Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr Ala Gly 20 25 30 Phe Pro Gly Ser Pro Gly Ala Lys Gly 35 40 <210> 828 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 828 Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly Gly Ala 1 5 10 15 Gly Glu Pro Gly Lys Asn 20 <210> 829 <211> 14 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 829 Pro Gly Pro Ala Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly 1 5 10 <210> 830 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 830 Pro Gly Pro Ala Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Thr Ser 1 5 10 15 <210> 831 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 831 Pro Gly Pro Ala Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Thr Ser 1 5 10 15 Gly <210> 832 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 832 Pro Gly Pro Ala Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Thr Ser 1 5 10 15 Gly His <210> 833 <211> 42 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 833 Pro Gly Pro Ala Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Thr Ser 1 5 10 15 Gly His Pro Gly Ser Pro Gly Ser Pro Gly Tyr Gln Gly Pro Pro Gly 20 25 30 Glu Pro Gly Gln Ala Gly Pro Ser Gly Pro 35 40 <210> 834 <211> 57 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 834 Pro Gly Pro Ala Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Thr Ser 1 5 10 15 Gly His Pro Gly Ser Pro Gly Ser Pro Gly Tyr Gln Gly Pro Pro Gly 20 25 30 Glu Pro Gly Gln Ala Gly Pro Ser Gly Pro Pro Gly Pro Pro Gly Ala 35 40 45 Ile Gly Pro Ser Gly Pro Ala Gly Lys 50 55 <210> 835 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 835 Pro Gly Pro Met Gly Pro Arg Gly Ala Pro Gly Glu Arg Gly Arg Pro 1 5 10 15 Gly Leu Pro Gly Ala Ala Gly Ala Arg 20 25 <210> 836 <211> 10 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 836 Pro Gly Pro Pro Gly Ala Ile Gly Pro Ser 1 5 10 <210> 837 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 837 Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala Gly Ile Pro Gly Phe Pro 1 5 10 15 Gly Met Lys <210> 838 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 838 Pro Gly Pro Pro Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro 1 5 10 15 Gly Ala Lys <210> 839 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 839 Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln Pro Gly Val Met 1 5 10 15 <210> 840 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 840 Pro Gly Arg Pro Gly Glu Arg Gly Leu Pro Gly Pro Pro Gly Ile Lys 1 5 10 15 <210> 841 <211> 34 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 841 Pro Gly Ser Asp Gly Lys Pro Gly Pro Gly Ser Gln Gly Glu Ser 1 5 10 15 Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln Pro Gly 20 25 30 Val Met <210> 842 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 842 Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln 1 5 10 15 Gly His Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly 20 25 30 Ser <210> 843 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 843 Pro Pro Gly Ala Ile Gly Pro Ser Gly Pro Ala Gly Lys Asp Gly Glu 1 5 10 15 Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg 20 25 <210> 844 <211> 35 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 844 Pro Pro Gly Ala Ile Gly Pro Ser Gly Pro Ala Gly Lys Asp Gly Glu 1 5 10 15 Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg Gly Leu Pro Gly Pro Pro 20 25 30 Gly Ile Lys 35 <210> 845 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 845 Pro Pro Gly Glu Pro Gly Gln Ala Gly Pro Ser Gly Pro Pro Gly Pro 1 5 10 15 Pro Gly Ala Ile Gly Pro Ser 20 <210> 846 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 846 Pro Pro Gly Glu Pro Gly Gln Ala Gly Pro Ser Gly Pro Pro Gly Pro 1 5 10 15 Pro Gly Ala Ile Gly Pro Ser Gly Pro Ala Gly Lys Asp 20 25 <210> 847 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 847 Pro Pro Gly Ile Lys Gly Pro Ala Gly Ile Pro Gly Phe Pro Gly Met 1 5 10 15 Lys <210> 848 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 848 Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro 1 5 10 15 Ala Gly Ile Pro Gly Ala Pro Gly Leu Met 20 25 <210> 849 <211> 14 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 849 Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg 1 5 10 <210> 850 <211> 11 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 850 Pro Pro Gly Pro Pro Gly Ala Ile Gly Pro Ser 1 5 10 <210> 851 <211> 38 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 851 Pro Pro Gly Pro Pro Gly Ala Ile Gly Pro Ser Gly Pro Ala Gly Lys 1 5 10 15 Asp Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg Gly Leu Pro 20 25 30 Gly Pro Pro Gly Ile Lys 35 <210> 852 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 852 Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly Lys Gly Glu 1 5 10 15 Met Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met 20 25 <210> 853 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 853 Pro Pro Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala 1 5 10 15 Lys Gly Glu Val Gly Pro Ala 20 <210> 854 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 854 Pro Pro Gly Ser Gln Gly Glu Ser Gly Arg Pro Gly Pro Pro Gly Pro 1 5 10 15 Ser Gly Pro Arg Gly Gln Pro Gly Val Met 20 25 <210> 855 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 855 Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu 1 5 10 15 Val Gly Pro Ala 20 <210> 856 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 856 Pro Gln Gly His Ala Gly Ala Gly Gly Pro Pro Gly Pro Pro Gly Ile 1 5 10 15 Asn <210> 857 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 857 Pro Ser Gly Pro Ala Gly Lys Asp Gly Glu Ser Gly Arg Pro Gly Arg 1 5 10 15 Pro Gly Glu Arg Gly Leu Pro Gly Pro Pro Gly Ile Lys 20 25 <210> 858 <211> 14 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 858 Pro Ser Gly Pro Pro Gly Pro Pro Gly Ala Ile Gly Pro Ser 1 5 10 <210> 859 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 859 Gln Ala Gly Pro Ser Gly Pro Pro Gly Pro Pro Gly Ala Ile Gly Pro 1 5 10 15 Ser <210> 860 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 860 Gln Gly Pro Pro Gly Glu Pro Gly Gln Ala Gly Pro Ser Gly Pro Pro 1 5 10 15 Gly Pro Pro Gly Ala Ile Gly Pro Ser Gly Pro Ala Gly Lys Asp 20 25 30 <210> 861 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 861 Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro 1 5 10 15 Pro Gly Pro Pro Gly Ile Asn 20 <210> 862 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 862 Arg Gly Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro 1 5 10 15 Gly Leu Lys Gly Glu Asn 20 <210> 863 <211> 10 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 863 Arg Gly Leu Pro Gly Pro Pro Gly Ile Lys 1 5 10 <210> 864 <211> 13 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 864 Arg Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala 1 5 10 <210> 865 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 865 Arg Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala Gly Ile Pro 1 5 10 15 Gly Phe Pro Gly Met Lys 20 <210> 866 <211> 43 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 866 Arg Gly Met Pro Gly Ser Pro Gly Gly Pro Gly Ser Asp Gly Lys Pro 1 5 10 15 Gly Pro Pro Gly Ser Gln Gly Glu Ser Gly Arg Pro Gly Pro Pro Gly 20 25 30 Pro Ser Gly Pro Arg Gly Gln Pro Gly Val Met 35 40 <210> 867 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 867 Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro 1 5 10 15 Gly Pro Pro Gly Thr Ala 20 <210> 868 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 868 Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro 1 5 10 15 Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys 20 25 30 <210> 869 <211> 37 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 869 Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro 1 5 10 15 Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly 20 25 30 Glu Val Gly Pro Ala 35 <210> 870 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 870 Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu 1 5 10 15 <210> 871 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 871 Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg 1 5 10 15 <210> 872 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 872 Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg 1 5 10 15 Gly <210> 873 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 873 Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg 1 5 10 15 Gly Gly Ala Gly Glu Pro Gly Lys Asn 20 25 <210> 874 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 874 Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg 1 5 10 15 Gly Gly Ala Gly Glu Pro Gly Lys Asn Gly Ala Lys 20 25 <210> 875 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 875 Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr Ala 1 5 10 15 Gly Phe Pro Gly Ser Pro Gly Ala Lys 20 25 <210> 876 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 876 Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr Ala 1 5 10 15 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala 20 25 30 <210> 877 <211> 14 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 877 Arg Pro Gly Glu Arg Gly Leu Pro Gly Pro Gly Ile Lys 1 5 10 <210> 878 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 878 Arg Pro Gly Glu Arg Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro 1 5 10 15 Ala <210> 879 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 879 Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala Arg Gly Asn Asp Gly Ala 1 5 10 15 Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro 20 25 <210> 880 <211> 32 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 880 Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala Arg Gly Asn Asp Gly Ala 1 5 10 15 Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr Ala 20 25 30 <210> 881 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 881 Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln Pro Gly Val 1 5 10 15 Met <210> 882 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 882 Arg Pro Gly Arg Pro Gly Glu Arg Gly Leu Pro Gly Pro Pro Gly Ile 1 5 10 15 Lys <210> 883 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 883 Arg Pro Gly Arg Pro Gly Glu Arg Gly Leu Pro Gly Pro Pro Gly Ile 1 5 10 15 Lys Gly Pro Ala 20 <210> 884 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 884 Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly Glu Ser Gly Arg 1 5 10 15 Pro Gly Pro Pro Gly Pro Ser 20 <210> 885 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 885 Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly Glu Ser Gly Arg 1 5 10 15 Pro Gly Pro Pro Gly Pro Ser Gly 20 <210> 886 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 886 Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly Glu Ser Gly Arg 1 5 10 15 Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg 20 25 <210> 887 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 887 Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly Glu Ser Gly Arg 1 5 10 15 Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly 20 25 <210> 888 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 888 Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly Glu Ser Gly Arg 1 5 10 15 Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln Pro Gly 20 25 30 <210> 889 <211> 32 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 889 Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly Glu Ser Gly Arg 1 5 10 15 Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln Pro Gly Val Met 20 25 30 <210> 890 <211> 40 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 890 Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly Glu Ser Gly Arg 1 5 10 15 Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln Pro Gly Val Met 20 25 30 Gly Phe Pro Gly Pro Lys Gly Asn 35 40 <210> 891 <211> 14 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 891 Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr Ala 1 5 10 <210> 892 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 892 Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr Ala Gly Phe 1 5 10 15 Pro Gly Ser Pro Gly Ala Lys 20 <210> 893 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 893 Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr Ala Gly Phe 1 5 10 15 Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala 20 25 <210> 894 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 894 Ser Gly Pro Ala Gly Lys Asp Gly Glu Ser Gly Arg Pro Gly Arg Pro 1 5 10 15 Gly Glu Arg Gly Leu Pro Gly Pro Pro Gly Ile Lys 20 25 <210> 895 <211> 13 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 895 Ser Gly Pro Pro Gly Pro Pro Gly Ala Ile Gly Pro Ser 1 5 10 <210> 896 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 896 Ser Gly Pro Pro Gly Pro Pro Gly Ala Ile Gly Pro Ser Gly Pro Ala 1 5 10 15 Gly Lys Asp <210> 897 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 897 Ser Gly Pro Pro Gly Pro Pro Gly Ala Ile Gly Pro Ser Gly Pro Ala 1 5 10 15 Gly Lys Asp Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg 20 25 30 <210> 898 <211> 40 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 898 Ser Gly Pro Pro Gly Pro Pro Gly Ala Ile Gly Pro Ser Gly Pro Ala 1 5 10 15 Gly Lys Asp Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg Gly 20 25 30 Leu Pro Gly Pro Pro Gly Ile Lys 35 40 <210> 899 <211> 43 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 899 Ser Gly Pro Pro Gly Pro Pro Gly Ala Ile Gly Pro Ser Gly Pro Ala 1 5 10 15 Gly Lys Asp Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg Gly 20 25 30 Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala 35 40 <210> 900 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 900 Ser Gly Pro Arg Gly Gln Pro Gly Val Met Gly Phe Pro Gly Pro Lys 1 5 10 15 Gly Asn <210> 901 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 901 Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln Pro 1 5 10 15 Gly Val Met <210> 902 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 902 Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln Pro 1 5 10 15 Gly Val Met Gly Phe Pro Gly Pro Lys Gly Asn 20 25 <210> 903 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 903 Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg Gly Leu Pro Gly Pro Pro 1 5 10 15 <210> 904 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 904 Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg Gly Leu Pro Gly Pro Pro 1 5 10 15 Gly <210> 905 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 905 Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg Gly Leu Pro Gly Pro Pro 1 5 10 15 Gly Ile Lys <210> 906 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 906 Ser Gly Arg Pro Gly Arg Pro Gly Glu Arg Gly Leu Pro Gly Pro Pro 1 5 10 15 Gly Ile Lys Gly Pro Ala 20 <210> 907 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 907 Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly His 1 5 10 15 Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn 20 25 <210> 908 <211> 35 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 908 Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly His 1 5 10 15 Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro 20 25 30 Gly Gly Lys 35 <210> 909 <211> 41 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 909 Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly His 1 5 10 15 Ala Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro 20 25 30 Gly Gly Lys Gly Glu Met Gly Pro Ala 35 40 <210> 910 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 910 Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser 1 5 10 15 Asn Gly Ala Pro Gly 20 <210> 911 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 911 Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser 1 5 10 15 Asn Gly Ala Pro Gly Gln 20 <210> 912 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 912 Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser 1 5 10 15 Asn Gly Ala Pro Gly Gln Arg Gly Glu 20 25 <210> 913 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 913 Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser 1 5 10 15 Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly 20 25 <210> 914 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 914 Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser 1 5 10 15 Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln 20 25 <210> 915 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 915 Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser 1 5 10 15 Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly 20 25 30 <210> 916 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 916 Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser 1 5 10 15 Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly His 20 25 30 <210> 917 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 917 Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser 1 5 10 15 Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala 20 25 30 Gly <210> 918 <211> 44 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 918 Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser 1 5 10 15 Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala 20 25 30 Gly Ala Gln Gly Pro Pro Gly Pro Pro Gly Ile Asn 35 40 <210> 919 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 919 Ser Pro Gly Glu Pro Gly Ala Asn Gly Leu Pro Gly Ala Ala Gly Glu 1 5 10 15 Arg Gly Ala Pro Gly Phe Arg Gly Pro Ala Gly Pro Asn 20 25 <210> 920 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 920 Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala 1 5 10 15 Pro Gly Leu Met 20 <210> 921 <211> 22 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 921 Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala 1 5 10 15 Pro Gly Leu Met Gly Ala 20 <210> 922 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 922 Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala 1 5 10 15 Pro Gly Leu Met Gly Ala Arg 20 <210> 923 <211> 32 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 923 Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly Ile Pro Gly Ala 1 5 10 15 Pro Gly Leu Met Gly Ala Arg Gly Pro Pro Gly Pro Ala Gly Ala Asn 20 25 30 <210> 924 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 924 Ser Pro Gly Gly Pro Gly Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser 1 5 10 15 Gln Gly Glu Ser Gly Arg Pro Gly Pro Pro Gly 20 25 <210> 925 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 925 Ser Pro Gly Gly Pro Gly Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser 1 5 10 15 Gln Gly Glu Ser Gly Arg Pro Gly Pro Pro Gly Pro 20 25 <210> 926 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 926 Ser Pro Gly Gly Pro Gly Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser 1 5 10 15 Gln Gly Glu Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser 20 25 <210> 927 <211> 32 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 927 Ser Pro Gly Gly Pro Gly Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser 1 5 10 15 Gln Gly Glu Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg 20 25 30 <210> 928 <211> 33 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 928 Ser Pro Gly Gly Pro Gly Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser 1 5 10 15 Gln Gly Glu Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg 20 25 30 Gly <210> 929 <211> 38 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 929 Ser Pro Gly Gly Pro Gly Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser 1 5 10 15 Gln Gly Glu Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg 20 25 30 Gly Gln Pro Gly Val Met 35 <210> 930 <211> 46 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 930 Ser Pro Gly Gly Pro Gly Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser 1 5 10 15 Gln Gly Glu Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg 20 25 30 Gly Gln Pro Gly Val Met Gly Phe Pro Gly Pro Lys Gly Asn 35 40 45 <210> 931 <211> 27 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 931 Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro 1 5 10 15 Gln Gly His Ala Gly Ala Gln Gly Pro Pro Gly 20 25 <210> 932 <211> 32 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 932 Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro 1 5 10 15 Gln Gly His Ala Gly Ala Gly Pro Pro Gly Pro Pro Gly Ile Asn 20 25 30 <210> 933 <211> 36 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 933 Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro 1 5 10 15 Gln Gly His Ala Gly Ala Gly Pro Pro Gly Pro Pro Gly Ile Asn 20 25 30 Gly Ser Pro Gly 35 <210> 934 <211> 38 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 934 Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro 1 5 10 15 Gln Gly His Ala Gly Ala Gly Pro Pro Gly Pro Pro Gly Ile Asn 20 25 30 Gly Ser Pro Gly Gly Lys 35 <210> 935 <211> 42 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 935 Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro 1 5 10 15 Gln Gly His Ala Gly Ala Gly Pro Pro Gly Pro Pro Gly Ile Asn 20 25 30 Gly Ser Pro Gly Gly Lys Gly Glu Met Gly 35 40 <210> 936 <211> 44 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 936 Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly Pro 1 5 10 15 Gln Gly His Ala Gly Ala Gly Pro Pro Gly Pro Pro Gly Ile Asn 20 25 30 Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala 35 40 <210> 937 <211> 32 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 937 Ser Pro Gly Ser Pro Gly Tyr Gln Gly Pro Pro Gly Glu Pro Gly Gln 1 5 10 15 Ala Gly Pro Ser Gly Pro Pro Gly Pro Pro Gly Ala Ile Gly Pro Ser 20 25 30 <210> 938 <211> 29 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 938 Ser Pro Gly Tyr Gln Gly Pro Pro Gly Glu Pro Gly Gln Ala Gly Pro 1 5 10 15 Ser Gly Pro Pro Gly Pro Pro Gly Ala Ile Gly Pro Ser 20 25 <210> 939 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 939 Ser Gln Gly Glu Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro 1 5 10 15 Arg Gly Gln Pro Gly Val Met 20 <210> 940 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 940 Ser Gln Gly Glu Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro 1 5 10 15 Arg Gly Gln Pro Gly Val Met Gly Phe Pro Gly Pro Lys Gly Asn 20 25 30 <210> 941 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 941 Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro 1 5 10 15 Ala <210> 942 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 942 Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro 1 5 10 15 Ala Gly <210> 943 <211> 21 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 943 Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro 1 5 10 15 Ala Gly Ser Pro Gly 20 <210> 944 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 944 Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro 1 5 10 15 Ala Gly Ser Pro Gly Ser Asn 20 <210> 945 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 945 Thr Gly Ala Pro Gly Leu Lys Gly Glu Asn Gly Leu Pro Gly Glu Asn 1 5 10 15 Gly Ala Pro Gly Pro Met Gly Pro Arg 20 25 <210> 946 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 946 Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly Pro Gly Gly Asp 1 5 10 15 <210> 947 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 947 Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg 1 5 10 15 Gly Glu Pro Gly Pro Gln Gly 20 <210> 948 <211> 42 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 948 Gly His Pro Gly Ser Pro Gly Ser Pro Gly Tyr Gln Gly Pro Pro Gly 1 5 10 15 Glu Pro Gly Gln Ala Gly Pro Ser Gly Pro Pro Gly Pro Pro Gly Ala 20 25 30 Ile Gly Pro Ser Gly Pro Ala Gly Lys Asp 35 40 <210> 949 <211> 35 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 949 Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu 20 25 30 Val Gly Pro 35 <210> 950 <211> 50 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 950 Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly 1 5 10 15 Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly Lys 20 25 30 Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly Pro Gly 35 40 45 Gly Asp 50 <210> 951 <211> 46 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 951 Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg Gly Glu Pro Gly 1 5 10 15 Pro Gln Gly His Ala Gly Ala Gly Gly Pro Pro Gly Pro Pro Gly Ile 20 25 30 Asn Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro Ala Gly 35 40 45 <210> 952 <211> 32 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 952 Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu 20 25 30 <210> 953 <211> 43 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 953 Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu 20 25 30 Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly 35 40 <210> 954 <211> 31 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 954 Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn Gly Glu Arg 1 5 10 15 Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly Lys Asn 20 25 30 <210> 955 <211> 39 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 955 Gly Thr Ser Gly His Pro Gly Ser Pro Gly Ser Pro Gly Tyr Gln Gly 1 5 10 15 Pro Pro Gly Glu Pro Gly Gln Ala Gly Pro Ser Gly Pro Pro Gly Pro 20 25 30 Pro Gly Ala Ile Gly Pro Ser 35 <210> 956 <211> 45 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 956 Gly His Pro Gly Ser Pro Gly Ser Pro Gly Tyr Gln Gly Pro Pro Gly 1 5 10 15 Glu Pro Gly Gln Ala Gly Pro Ser Gly Pro Pro Gly Pro Pro Gly Ala 20 25 30 Ile Gly Pro Ser Gly Pro Ala Gly Lys Asp Gly Glu Ser 35 40 45 <210> 957 <211> 47 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 957 Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu 20 25 30 Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln 35 40 45 <210> 958 <211> 13 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 958 Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala 1 5 10 <210> 959 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 959 Gly Ala Pro Gly Leu Arg Gly Gly Ala Gly Glu Pro Gly Lys Asn 1 5 10 15 <210> 960 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 960 Gly Ile Pro Gly Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Gly 1 5 10 15 Pro Ala Gly Ala 20 <210> 961 <211> 26 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 961 Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala Gly 1 5 10 15 Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln 20 25 <210> 962 <211> 13 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 962 Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys Asn 1 5 10 <210> 963 <211> 18 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 963 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 1 5 10 15 Gln Arg <210> 964 <211> 57 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 964 Gly Tyr Pro Gly Pro Ala Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly 1 5 10 15 Thr Ser Gly His Pro Gly Ser Pro Gly Ser Pro Gly Tyr Gln Gly Pro 20 25 30 Pro Gly Glu Pro Gly Gln Ala Gly Pro Ser Gly Pro Pro Gly Pro Pro 35 40 45 Gly Ala Ile Gly Pro Ser Gly Pro Ala 50 55 <210> 965 <211> 45 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 965 Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys Gly Glu Asn Gly 1 5 10 15 Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly Pro Arg Gly Ala 20 25 30 Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala 35 40 45 <210> 966 <211> 40 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 966 Gly Gly Ala Gly Glu Pro Gly Lys Asn Gly Ala Lys Gly Glu Pro Gly 1 5 10 15 Pro Arg Gly Glu Arg Gly Glu Ala Gly Ile Pro Gly Val Pro Gly Ala 20 25 30 Lys Gly Glu Asp Gly Lys Asp Gly 35 40 <210> 967 <211> 48 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 967 Gly Gly Ala Gly Glu Pro Gly Lys Asn Gly Ala Lys Gly Glu Pro Gly 1 5 10 15 Pro Arg Gly Glu Arg Gly Glu Ala Gly Ile Pro Gly Val Pro Gly Ala 20 25 30 Lys Gly Glu Asp Gly Lys Asp Gly Ser Pro Gly Glu Pro Gly Ala Asn 35 40 45 <210> 968 <211> 36 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 968 Gly His Arg Gly Phe Asp Gly Arg Asn Gly Glu Lys Gly Glu Thr Gly 1 5 10 15 Ala Pro Gly Leu Lys Gly Glu Asn Gly Leu Pro Gly Glu Asn Gly Ala 20 25 30 Pro Gly Pro Met 35 <210> 969 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 969 Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr Ala Gly Phe Pro 1 5 10 15 Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala 20 25 <210> 970 <211> 32 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 970 Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly Pro Pro Gly Thr 1 5 10 15 Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu Val Gly Pro Ala 20 25 30 <210> 971 <211> 28 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 971 Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly 20 25 <210> 972 <211> 19 <212> PRT <213> Artificial Sequence <220> <223> Synthetic sequence <400> 972 Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly 1 5 10 15 Pro Pro Gly <210> 973 <211> 4893 <212> DNA <213> Artificial Sequence <220> <223> Plasmid <400> 973 ggatccttca gtaatgtctt gtttcttttg ttgcagtggt gagccatttt gacttcgtga 60 aagtttcttt agaatagttg tttccagagg ccaaacattc cacccgtagt aaagtgcaag 120 cgtaggaaga ccaagactgg cataaatcag gtataagtgt cgagcactgg caggtgatct 180 tctgaaagtt tctactagca gataagatcc agtagtcatg catatggcaa caatgtaccg 240 tgtggatcta agaacgcgtc ctactaacct tcgcattcgt tggtccagtt tgttgttatc 300 gatcaacgtg acaaggttgt cgattccgcg taagcatgca tacccaagga cgcctgttgc 360 aattccaagt gagccagttc caacaatctt tgtaatatta gagcacttca ttgtgttgcg 420 cttgaaagta aaatgcgaac aaattaagag ataatctcga aaccgcgact tcaaacgcca 480 atatgatgtg cggcacacaa taagcgttca tatccgctgg gtgactttct cgctttaaaa 540 aattatccga aaaaattttc tagagtgttg ttactttata cttccggctc gtataatacg 600 acaaggtgta aggaggacta aaccatggct aaactcacct ctgctgttcc agtcctgact 660 gctcgtgatg ttgctggtgc tgttgagttc tggactgata ggctcggttt ctcccgtgac 720 ttcgtagagg acgactttgc cggtgttgta cgtgacgacg ttaccctgtt catctccgca 780 gttcaggacc aggttgtgcc agacaacact ctggcatggg tatgggttcg tggtctggac 840 gaactgtacg ctgagtggtc tgaggtcgtg tctaccaact tccgtgatgc atctggtcca 900 gctatgaccg agatcggtga acagccctgg ggtcgtgagt ttgcactgcg tgatccagct 960 ggtaactgcg tgcatttcgt cgcagaagag caggactaac aattgacacc ttacgattat 1020 ttagagagta tttattagtt ttattgtatg tatacggatg ttttattatc tatttatgcc 1080 cttatattct gtaactatcc aaaagtccta tcttatcaag ccagcaatct atgtccgcga 1140 acgtcaacta aaaataagct ttttatgctc ttctctcttt ttttcccttc ggtataatta 1200 taccttgcat ccacagattc tcctgccaaa ttttgcataa tcctttacaa catggctata 1260 tgggagcact tagcgccctc caaaacccat attgcctacg catgtatagg tgttttttcc 1320 acaatatttt ctctgtgctc tctttttatt aaagagaagc tctatatcgg agaagcttct 1380 gtggccgtta tattcggcct tatcgtggga ccacattgcc tgaattggtt tgccccggaa 1440 gattggggaa acttggatct gattacctta gctgcagaaa agggtaccac tgagcgtcag 1500 accccgtaga aaagatcaaa ggatcttctt gagatccttt ttttctgcgc gtaatctgct 1560 gcttgcaaac aaaaaaacca ccgctaccag cggtggtttg tttgccggat caagagctac 1620 caactctttt tccgaaggta actggcttca gcagagcgca gataccaaat actgttcttc 1680 tagtgtagcc gtagttaggc caccacttca agaactctgt agcaccgcct acatacctcg 1740 ctctgctaat cctgttacca gtggctgctg ccagtggcga taagtcgtgt cttaccgggt 1800 tggacccaag acgatagtta ccggataagg cgcagcggtc gggctgaacg gggggttcgt 1860 gcacacagcc cagcttggag cgaacgacct acaccgaact gagataccta cagcgtgagc 1920 tatgagaaag cgccacgctt cccgaaggga gaaaggcgga caggtatccg gtaagcggca 1980 gggtcggaac aggagagcgc acgagggagc ttccaggggg aaacgcctgg tatctttata 2040 gtcctgtcgg gtttcgccac ctctgacttg agcgtcgatt tttgtgatgc tcgtcagggg 2100 ggcggagcct atggaaaaac gccagcaacg cggccttttt acggttcctg gccttttgct 2160 ggccttttgc tcacatgtat ttaaataatg tatctaaacg caaactccga gctggaaaaa 2220 tgttaccggc gatgcgcgga caatttagag gcggcgatca agaaacacct gctgggcgag 2280 cagtctggag cacagtcttc gatgggcccg agatcccacc gcgttcctgg gtaccgggac 2340 gtgaggcagc gcgacatcca tcaaatatac caggcgccaa ccgagtgtct cggaaaacag 2400 cttctggata tcttccgctg gcggcgcaac gacgaataat agtccctgga ggtgacggaa 2460 tatatatgtg tggagggtaa atctgacagg gtgtagcaaa ggtaatattt tcctaaaaca 2520 tgcaatcggc tgccccgcaa cgggaaaaag aatgactttg gcactcttca ccagagtggg 2580 gtgtcccgct cgtgtgtgca aataggctcc cactggtcac cccggatttt gcagaaaaac 2640 agcaagttcc ggggtgtctc actggtgtcc gccaataaga ggagccggca ggcacggagt 2700 ttacatcaag ctgtctccga tacactcgac taccatccgg gtctctcaga gaggggaatg 2760 gcactataaa taccgcctcc ttgcgctctc tgccttcatc aatcaaatca tgtacaggaa 2820 cttaataatt gctactgccc ttacttgcgg tgcatacagt gcctacgtgc cttccgaacc 2880 atggagcaca ctgacacctg atgctagcct tgaaagtgcc ctcaaagatt actcacaaac 2940 ttttggaata gctattagt ccttagatgc cgacaagatt aagagagacg tcaaatctgg 3000 tgttgctgtt ggaggtttag caggctaccc tggtcccgca gggcccccag gtccgccggg 3060 tccgcccgga acatcaggtc atcccggaag ccctggttca ccaggttatc agggaccgcc 3120 cggagagcct ggacaagctg gtccctccgg accccctggt ccaccaggtg ctattggacc 3180 aagtggtcct gccggaaaag acggtgaatc cggtagacct ggtagacccg gcgaaagggg 3240 tttaccaggt cctcccggaa ttaagggtcc agccggtata cccggttttc ctgggatgaa 3300 gggtcacaga ggatttgatg gtagaaacgg agagaaaggc gaaaccggtg ctcccggact 3360 gaagggtgaa aacggtcttc ctggtgagaa cggcgctcct ggacctatgg gtccacgtgg 3420 tgctccagga gaaagaggca gaccaggatt gcctggtgca gctggtgcta gaggtaacga 3480 tggtgcccgt ggttccgatg gacaacccgg gccacccggc cctccaggta ccgctggatt 3540 tcctggaagc cctggtgcta agggggaggt tggtccggct ggtagtcccg gaagtaacgg 3600 tgccccaggt caaagaggcg aaccaggccc tcagggtcac gcaggagcac agggaccgcc 3660 tggtcctcct ggtattaatg gttcgcctgg aggaaaaggt gaaatggggc ccgcaggaat 3720 ccccggtgcg cctggtctta tgggtgccag gggtcctcca ggcccggccg gtgcaaatgg 3780 tgctcccgga ttacgaggag gagctggtga acctggtaaa aacggtgcca aaggagaacc 3840 aggtcctcgt ggagagcgtg gtgaagctgg cattcccggt gtgcctggtg caaaaggtga 3900 ggacggtaag gacggttccc ctggtgagcc aggtgcgaac ggactgccag gtgcagccgg 3960 agagcgagga gctccaggat tcaggggacc agccggtcct aacggcattc ctggtgaaaa 4020 agggcccgcc ggtgaaaggg gagctcccgg tccagcaggc cctcgtggag cagctggtga 4080 gcctggacgt gacggtgtcc caggagggcc aggtatgagg ggtatgcccg ggtcccctgg 4140 cggtcctgga tcggatggaa aaccagggcc accaggttcg cagggtgaaa gcggacgtcc 4200 aggcccaccc ggcccttcag gtccaagggg tcagcctggt gtcatgggtt tccccggtcc 4260 aaagggtaat gacggagcac cgggtaaaaa tggtgaacgt ggtggcccag gtggtccagg 4320 accccaaggt ccaccaggaa aaaacggtga gacaggtcct caaggacctc caggacctac 4380 cggtcctgga ggagataagg gagatacggg accgccagga cctcaaggat tgcaaggttt 4440 gcctggtaca ggaggccctc ccggagaaaa tggtaagcct ggagagccag gaccaaaagg 4500 cgatgctgga gccccaggtg cacccggagg taagggagac gccggtgctc cgggtgagcg 4560 tggtcctccg gcaattgctg gtattggtgg agaaaaggcc ggcggtttcg ctccatatta 4620 tggttaatca agaggatgtc agaatgccat ttgcctgaga gatgcaggct tcatttttga 4680 tactttttta tttgtaacct atatagtata ggattttttt tgtcattttg tttcttctcg 4740 tacgagcttg ctcctgatca gcctatctcg cagctgatga atatcttgtg gtaggggttt 4800 gggaaaatca ttcgagtttg atgtttttct tggtatttcc cactcctctt cagagtacag 4860 aagattaagt gagacgttcg tttgtgctcc gga 4893 <210> 974 <211> 6038 <212> DNA <213> Artificial Sequence <220> <223> Plasmid <400> 974 gatccttcag taatgtcttg tttcttttgt tgcagtggtg agccattttg acttcgtgaa 60 agtttcttta gaatagttgt ttccagaggc caaacattcc acccgtagta aagtgcaagc 120 gtaggaagac caagactggc ataaatcagg tataagtgtc gagcactggc aggtgatctt 180 ctgaaagttt ctactagcag ataagatcca gtagtcatgc atatggcaac aatgtaccgt 240 gtggatctaa gaacgcgtcc tactaacctt cgcattcgtt ggtccagttt gttgttatcg 300 atcaacgtga caaggttgtc gattccgcgt aagcatgcat acccaaggac gcctgttgca 360 attccaagtg agccagttcc aacaatcttt gtaatattag agcacttcat tgtgttgcgc 420 ttgaaagtaa aatgcgaaca aattaagaga taatctcgaa accgcgactt caaacgccaa 480 tatgatgtgc ggcacacaat aagcgttcat atccgctggg tgactttctc gctttaaaaa 540 attatccgaa aaaattttcc tctagaatga ctactttaga tgacaccgct tacagatata 600 gaacttcagt ccctggtgac gcagaggcaa tcgaagcttt ggacggatct tttacgactg 660 ataccgtttt tagagttacc gccactggtg atggtttcac attgagagaa gtgccagttg 720 atccacctct tactaaagtt ttccgggatg atgagtcaga tgacgagagc gacgatggtg 780 aagatggcga tcctgattcc agaacattcg tagcttatgg tgacgacggt gacttggctg 840 gatttgtggt agtttcctat agtggttgga atcgtaggct gactgtcgaa gatattgaag 900 tggcacccga gcatagggga cacggcgttg gtagagcctt gatgggactg gcaacagagt 960 tcgctagaga gcgtggtgca ggacacctgt ggctagaagt cacaaatgtg aacgctccag 1020 caatccatgc ttaccgtaga atgggtttta ctttgtgtgg tcttgacaca gctttatacg 1080 acggaacagc ttccgacggt gaacaagcct tgtacatgtc tatgccatgc ccttagtaaa 1140 attgacacct tacgattatt tagagagtat ttattagttt tattgtatgt atacggatgt 1200 tttattatct atttatgccc ttatattctg taactatcca aaagtcctat cttatcaagc 1260 cagcaatcta tgtccgcgaa cgtcaactaa aaataagctt tttatgctgt tctctctttt 1320 tttcccttcg gtataattat accttgcatc cacagattct cctgccaaat tttgcataat 1380 cctttacaac atggctatat gggagcactt agcgccctcc aaaacccata ttgcctacgc 1440 atgtataggt gttttttcca caatattttc tctgtgctct ctttttatta aagagaagct 1500 ctatatcgga gaagcttctg tggccgttat attcggcctt atcgtgggac cacattgcct 1560 gaattggttt gccccggaag attggggaaa cttggatctg attaccttag ctgcattacc 1620 aatgcttaat cagtgaggca cctatctcag cgatctgtct atttcgttca tccatagttg 1680 cctgactccc cgtcgtgtag ataactacga tacgggaggg cttaccatct ggccccagcg 1740 ctgcgatgat accgcgagaa ccacgctcac cggctccgga tttatcagca ataaaccagc 1800 cagccggaag ggccgagcgc agaagtggtc ctgcaacttt atccgcctcc atccagtcta 1860 ttaattgttg ccgggaagct agagtaagta gttcgccagt taatagtttg cgcaacgttg 1920 ttgccatcgc tacaggcatc gtggtgtcac gctcgtcgtt tggtatggct tcattcagct 1980 ccggttccca acgatcaagg cgagttacat gatcccccat gttgtgcaaa aaagcggtta 2040 gctccttcgg tcctccgatc gttgtcagaa gtaagttggc cgcagtgtta tcactcatgg 2100 ttatggcagc actgcataat tctcttactg tcatgccatc cgtaagatgc ttttctgtga 2160 ctggtgagta ctcaaccaag tcattctgag aatagtgtat gcggcgaccg agttgctctt 2220 gcccggcgtc aatacgggat aataccgcgc cacatagcag aactttaaaa gtgctcatca 2280 ttggaaaacg ttcttcgggg cgaaaactct caaggatctt accgctgttg agatccagtt 2340 cgatgtaacc cactcgtgca cccaactgat cttcagcatc ttttactttc accagcgttt 2400 ctgggtgagc aaaaacagga aggcaaaatg ccgcaaaaaa gggaataagg gcgacacgga 2460 aatgttgaat actcatattc ttcctttttt aatattattg aagcatttat cagggttatt 2520 gtctcatgag cggatacata tttgaatgta tttagaaaaa taaacaaata ggggtcagtg 2580 ttacaaccaa ttaaccaatt ctgaaaggaa gaatctgcag gaaaagggta ccactgagcg 2640 tcagaccccg tagaaaagat caaaggatct tcttgagatc ctttttttct gcgcgtaatc 2700 tgctgcttgc aaacaaaaaa accaccgcta ccagcggtgg tttgtttgcc ggatcaagag 2760 ctaccaactc tttttccgaa ggtaactggc ttcagcagag cgcagatacc aaatactgtt 2820 cttctagtgt agccgtagtt aggccaccac ttcaagaact ctgtagcacc gcctacatac 2880 ctcgctctgc taatcctgtt accagtggct gctgccagtg gcgataagtc gtgtcttacc 2940 gggttggacc caagacgata gttaccggat aaggcgcagc ggtcgggctg aacggggggt 3000 tcgtgcacac agcccagctt ggagcgaacg acctacaccg aactgagata cctacagcgt 3060 gagctatgag aaagcgccac gcttcccgaa gggagaaagg cggacaggta tccggtaagc 3120 ggcagggtcg gaacaggaga gcgcacgagg gagcttccag ggggaaacgc ctggtatctt 3180 tatagtcctg tcgggtttcg ccacctctga cttgagcgtc gatttttgtg atgctcgtca 3240 ggggggcgga gcctatggaa aaacgccagc aacgcggcct ttttacggtt cctggccttt 3300 tgctggcctt ttgctcacat gtatttaaat aatgtatcta aacgcaaact ccgagctgga 3360 aaaatgttac cggcgatgcg cggacaattt agaggcggcg atcaagaaac acctgctggg 3420 cgagcagtct ggagcacagt cttcgatggg cccgagatcc caccgcgttc ctgggtaccg 3480 ggacgtgagg cagcgcgaca tccatcaaat ataccaggcg ccaaccgagt gtctcggaaa 3540 acagcttctg gatatcttcc gctggcggcg caacgacgaa taatagtccc tggaggtgac 3600 ggaatatata tgtgtggagg gtaaatctga cagggtgtag caaaggtaat attttcctaa 3660 aacatgcaat cggctgcccc gcaacgggaa aaagaatgac tttggcactc ttcaccagag 3720 tggggtgtcc cgctcgtgtg tgcaaatagg ctcccactgg tcaccccgga ttttgcagaa 3780 aaacagcaag ttccggggtg tctcactggt gtccgccaat aagaggagcc ggcaggcacg 3840 gagtttacat caagctgtct ccgatacact cgactaccat ccgggtctct cagagagggg 3900 aatggcacta taaataccgc ctccttgcgc tctctgcctt catcaatcaa atcatgtaca 3960 ggaacttaat aattgctact gcccttactt gcggtgcata cagtgcctac gtgccttccg 4020 aaccatggag cacactgaca cctgatgcta gccttgaaag tgccctcaaa gattactcac 4080 aaacttttgg aatagctatt aagtccttag atgccgacaa gattaagaga gacgtcaaat 4140 ctggtgttgc tgttggaggt ttagcaggct accctggtcc cgcagggccc ccaggtccgc 4200 cgggtccgcc cggaacatca ggtcatcccg gaagccctgg ttcaccaggt tatcagggac 4260 cgcccggaga gcctggacaa gctggtccct ccggaccccc tggtccacca ggtgctattg 4320 gaccaagtgg tcctgccgga aaagacggtg aatccggtag acctggtaga cccggcgaaa 4380 ggggtttacc aggtcctccc ggaattaagg gtccagccgg tatacccggt tttcctggga 4440 tgaagggtca cagaggattt gatggtagaa acggagagaa aggcgaaacc ggtgctcccg 4500 gactgaaggg tgaaaacggt cttcctggtg agaacggcgc tcctggacct atgggtccac 4560 gtggtgctcc aggagaaaga ggcagaccag gattgcctgg tgcagctggt gctagaggta 4620 acgatggtgc ccgtggttcc gatggacaac ccgggccacc cggccctcca ggtaccgctg 4680 gatttcctgg aagccctggt gctaaggggg aggttggtcc ggctggtagt cccggaagta 4740 acggtgcccc aggtcaaaga ggcgaaccag gccctcaggg tcacgcagga gcacagggac 4800 cgcctggtcc tcctggtatt aatggttcgc ctggaggaaa aggtgaaatg gggcccgcag 4860 gaatccccgg tgcgcctggt cttatgggtg ccaggggtcc tccaggcccg gccggtgcaa 4920 atggtgctcc cggattacga ggaggagctg gtgaacctgg taaaaacggt gccaaaggag 4980 aaccaggtcc tcgtggagag cgtggtgaag ctggcattcc cggtgtgcct ggtgcaaaag 5040 gtgaggacgg taaggacggt tcccctggtg agccaggtgc gaacggactg ccaggtgcag 5100 ccggagagcg aggagctcca ggattcaggg gaccagccgg tcctaacggc attcctggtg 5160 aaaaagggcc cgccggtgaa aggggagctc ccggtccagc aggccctcgt ggagcagctg 5220 gtgagcctgg acgtgacggt gtcccaggag ggccaggtat gaggggtatg cccgggtccc 5280 ctggcggtcc tggatcggat ggaaaaccag ggccaccagg ttcgcagggt gaaagcggac 5340 gtccaggccc acccggccct tcaggtccaa ggggtcagcc tggtgtcatg ggtttccccg 5400 gtccaaaggg taatgacgga gcaccgggta aaaatggtga acgtggtggc ccaggtggtc 5460 caggacccca aggtccacca ggaaaaaacg gtgagacagg tcctcaagga cctccaggac 5520 ctaccggtcc tggaggagat aagggagata cgggaccgcc aggacctcaa ggattgcaag 5580 gtttgcctgg tacaggaggc cctcccggag aaaatggtaa gcctggagag ccaggaccaa 5640 aaggcgatgc tggagcccca ggtgcacccg gaggtaaggg agacgccggt gctccgggtg 5700 agcgtggtcc tccggcaatt gctggtattg gtggagaaaa ggccggcggt ttcgctccat 5760 attatggtta atcaagagga tgtcagaatg ccatttgcct gagagatgca ggcttcattt 5820 ttgatacttt tttatttgta acctatatag tataggattt tttttgtcat tttgtttctt 5880 ctcgtacgag cttgctcctg atcagcctat ctcgcagctg atgaatatct tgtggtaggg 5940 gtttgggaaa atcattcgag tttgatgttt ttcttggtat ttcccactcc tcttcagagt 6000 acagaagatt aagtgagacg ttcgtttgtg ctccggag 6038 <210> 975 <211> 59 <212> DNA <213> Artificial Sequence <220> <223> Primer <400> 975 cttgcgctct ctgccttcat caatcaaatc atgtacagga acttaataat tgctactgc 59 <210> 976 <211> 30 <212> DNA <213> Artificial Sequence <220> <223> Primer <400> 976 tctcttaatc ttgtcggcat ctaaggactt 30 <210> 977 <211> 108 <212> DNA <213> Artificial Sequence <220> <223> Primer <400> 977 gcaaatggca ttctgacatc ctcttgatta accataatat ggagcgaaac cgccggcctt 60 ttctccacca ataccagcaa ttgccggagg accacgctca cccggagc 108 <210> 978 <211> 1463 <212> PRT <213> Artificial Sequence <220> <223> Col1A1, described by Accession No. NP_001029211.1 <400> 978 Met Phe Ser Phe Val Asp Leu Arg Leu Leu Leu Leu Leu Leu Ala Ala Thr 1 5 10 15 Ala Leu Leu Thr His Gly Gln Glu Glu Gly Gln Glu Glu Gly Gln Glu 20 25 30 Glu Asp Ile Pro Val Thr Cys Val Gln Asn Gly Leu Arg Tyr His 35 40 45 Asp Arg Asp Val Trp Lys Pro Val Pro Cys Gln Ile Cys Val Cys Asp 50 55 60 Asn Gly Asn Val Leu Cys Asp Asp Val Ile Cys Asp Glu Leu Lys Asp 65 70 75 80 Cys Pro Asn Ala Lys Val Pro Thr Asp Glu Cys Cys Pro Val Cys Pro 85 90 95 Glu Gly Gln Glu Ser Pro Thr Asp Gin Glu Thr Thr Gly Val Glu Gly 100 105 110 Pro Lys Gly Asp Thr Gly Pro Arg Gly Pro Arg Gly Pro Ala Gly Pro 115 120 125 Pro Gly Arg Asp Gly Ile Pro Gly Gln Pro Gly Leu Pro Gly Pro Pro 130 135 140 Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Leu Gly Gly Asn Phe Ala 145 150 155 160 Pro Gln Leu Ser Tyr Gly Tyr Asp Glu Lys Ser Thr Gly Ile Ser Val 165 170 175 Pro Gly Pro Met Gly Pro Ser Gly Pro Arg Gly Leu Pro Gly Pro Pro 180 185 190 Gly Ala Pro Gly Pro Gln Gly Phe Gln Gly Pro Pro Gly Glu Pro Gly 195 200 205 Glu Pro Gly Ala Ser Gly Pro Met Gly Pro Arg Gly Pro Pro Gly Pro 210 215 220 Pro Gly Lys Asn Gly Asp Asp Gly Glu Ala Gly Lys Pro Gly Arg Pro 225 230 235 240 Gly Glu Arg Gly Pro Pro Gly Pro Gln Gly Ala Arg Gly Leu Pro Gly 245 250 255 Thr Ala Gly Leu Pro Gly Met Lys Gly His Arg Gly Phe Ser Gly Leu 260 265 270 Asp Gly Ala Lys Gly Asp Ala Gly Pro Ala Gly Pro Lys Gly Glu Pro 275 280 285 Gly Ser Pro Gly Glu Asn Gly Ala Pro Gly Gln Met Gly Pro Arg Gly 290 295 300 Leu Pro Gly Glu Arg Gly Arg Pro Gly Ala Pro Gly Pro Ala Gly Ala 305 310 315 320 Arg Gly Asn Asp Gly Ala Thr Gly Ala Ala Gly Pro Pro Gly Pro Thr 325 330 335 Gly Pro Ala Gly Pro Pro Gly Phe Pro Gly Ala Val Gly Ala Lys Gly 340 345 350 Glu Gly Gly Pro Gln Gly Pro Arg Gly Ser Glu Gly Pro Gln Gly Val 355 360 365 Arg Gly Glu Pro Gly Pro Pro Gly Pro Ala Gly Ala Ala Gly Pro Ala 370 375 380 Gly Asn Pro Gly Ala Asp Gly Gln Pro Gly Ala Lys Gly Ala Asn Gly 385 390 395 400 Ala Pro Gly Ile Ala Gly Ala Pro Gly Phe Pro Gly Ala Arg Gly Pro 405 410 415 Ser Gly Pro Gln Gly Pro Ser Gly Pro Pro Gly Pro Lys Gly Asn Ser 420 425 430 Gly Glu Pro Gly Ala Pro Gly Ser Lys Gly Asp Thr Gly Ala Lys Gly 435 440 445 Glu Pro Gly Pro Thr Gly Ile Gln Gly Pro Gly Pro Ala Gly Glu 450 455 460 Glu Gly Lys Arg Gly Ala Arg Gly Glu Pro Gly Pro Ala Gly Leu Pro 465 470 475 480 Gly Pro Pro Gly Glu Arg Gly Gly Pro Gly Ser Arg Gly Phe Pro Gly 485 490 495 Ala Asp Gly Val Ala Gly Pro Lys Gly Pro Ala Gly Glu Arg Gly Ala 500 505 510 Pro Gly Pro Ala Gly Pro Lys Gly Ser Pro Gly Glu Ala Gly Arg Pro 515 520 525 Gly Glu Ala Gly Leu Pro Gly Ala Lys Gly Leu Thr Gly Ser Pro Gly 530 535 540 Ser Pro Gly Pro Asp Gly Lys Thr Gly Pro Pro Gly Pro Ala Gly Gln 545 550 555 560 Asp Gly Arg Pro Gly Pro Pro Gly Pro Pro Gly Ala Arg Gly Gln Ala 565 570 575 Gly Val Met Gly Phe Pro Gly Pro Lys Gly Ala Ala Gly Glu Pro Gly 580 585 590 Lys Ala Gly Glu Arg Gly Val Pro Gly Pro Pro Gly Ala Val Gly Pro 595 600 605 Ala Gly Lys Asp Gly Glu Ala Gly Ala Gln Gly Pro Pro Gly Pro Ala 610 615 620 Gly Pro Ala Gly Glu Arg Gly Glu Gln Gly Pro Ala Gly Ser Pro Gly 625 630 635 640 Phe Gln Gly Leu Pro Gly Pro Ala Gly Pro Pro Gly Glu Ala Gly Lys 645 650 655 Pro Gly Glu Gln Gly Val Pro Gly Asp Leu Gly Ala Pro Gly Pro Ser 660 665 670 Gly Ala Arg Gly Glu Arg Gly Phe Pro Gly Glu Arg Gly Val Gln Gly 675 680 685 Pro Pro Gly Pro Ala Gly Pro Arg Gly Ala Asn Gly Ala Pro Gly Asn 690 695 700 Asp Gly Ala Lys Gly Asp Ala Gly Ala Pro Gly Ala Pro Gly Ser Gln 705 710 715 720 Gly Ala Pro Gly Leu Gln Gly Met Pro Gly Glu Arg Gly Ala Ala Gly 725 730 735 Leu Pro Gly Pro Lys Gly Asp Arg Gly Asp Ala Gly Pro Lys Gly Ala 740 745 750 Asp Gly Ala Pro Gly Lys Asp Gly Val Arg Gly Leu Thr Gly Pro Ile 755 760 765 Gly Pro Pro Gly Pro Ala Gly Ala Pro Gly Asp Lys Gly Glu Ala Gly 770 775 780 Pro Ser Gly Pro Ala Gly Pro Thr Gly Ala Arg Gly Ala Pro Gly Asp 785 790 795 800 Arg Gly Glu Pro Gly Pro Pro Gly Pro Ala Gly Phe Ala Gly Pro Pro 805 810 815 Gly Ala Asp Gly Gln Pro Gly Ala Lys Gly Glu Pro Gly Asp Ala Gly 820 825 830 Ala Lys Gly Asp Ala Gly Pro Pro Gly Pro Ala Gly Pro Ala Gly Pro 835 840 845 Pro Gly Pro Ile Gly Asn Val Gly Ala Pro Gly Pro Lys Gly Ala Arg 850 855 860 Gly Ser Ala Gly Pro Pro Gly Ala Thr Gly Phe Pro Gly Ala Ala Gly 865 870 875 880 Arg Val Gly Pro Pro Gly Pro Ser Gly Asn Ala Gly Pro Pro Gly Pro 885 890 895 Pro Gly Pro Ala Gly Lys Glu Gly Ser Lys Gly Pro Arg Gly Glu Thr 900 905 910 Gly Pro Ala Gly Arg Pro Gly Glu Val Gly Pro Pro Gly Pro Pro Gly 915 920 925 Pro Ala Gly Glu Lys Gly Ala Pro Gly Ala Asp Gly Pro Ala Gly Ala 930 935 940 Pro Gly Thr Pro Gly Pro Gln Gly Ile Ala Gly Gln Arg Gly Val Val 945 950 955 960 Gly Leu Pro Gly Gln Arg Gly Glu Arg Gly Phe Pro Gly Leu Pro Gly 965 970 975 Pro Ser Gly Glu Pro Gly Lys Gln Gly Pro Ser Gly Ala Ser Gly Glu 980 985 990 Arg Gly Pro Pro Gly Pro Met Gly Pro Pro Gly Leu Ala Gly Pro Pro 995 1000 1005 Gly Glu Ser Gly Arg Glu Gly Ala Pro Gly Ala Glu Gly Ser Pro 1010 1015 1020 Gly Arg Asp Gly Ser Pro Gly Ala Lys Gly Asp Arg Gly Glu Thr 1025 1030 1035 Gly Pro Ala Gly Pro Pro Gly Ala Pro Gly Ala Pro Gly Ala Pro 1040 1045 1050 Gly Pro Val Gly Pro Ala Gly Lys Ser Gly Asp Arg Gly Glu Thr 1055 1060 1065 Gly Pro Ala Gly Pro Ala Gly Pro Ile Gly Pro Val Gly Ala Arg 1070 1075 1080 Gly Pro Ala Gly Pro Gln Gly Pro Arg Gly Asp Lys Gly Glu Thr 1085 1090 1095 Gly Glu Gln Gly Asp Arg Gly Ile Lys Gly His Arg Gly Phe Ser 1100 1105 1110 Gly Leu Gln Gly Pro Pro Gly Pro Pro Gly Ser Pro Gly Glu Gln 1115 1120 1125 Gly Pro Ser Gly Ala Ser Gly Pro Ala Gly Pro Arg Gly Pro Pro 1130 1135 1140 Gly Ser Ala Gly Ser Pro Gly Lys Asp Gly Leu Asn Gly Leu Pro 1145 1150 1155 Gly Pro Ile Gly Pro Pro Gly Pro Arg Gly Arg Thr Gly Asp Ala 1160 1165 1170 Gly Pro Ala Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Pro Pro 1175 1180 1185 Gly Pro Pro Ser Gly Gly Tyr Asp Leu Ser Phe Leu Pro Gln Pro 1190 1195 1200 Pro Gln Glu Lys Ala His Asp Gly Gly Arg Tyr Tyr Arg Ala Asp 1205 1210 1215 Asp Ala Asn Val Val Arg Asp Arg Asp Leu Glu Val Asp Thr Thr 1220 1225 1230 Leu Lys Ser Leu Ser Gln Gln Ile Glu Asn Ile Arg Ser Pro Glu 1235 1240 1245 Gly Ser Arg Lys Asn Pro Ala Arg Thr Cys Arg Asp Leu Lys Met 1250 1255 1260 Cys His Ser Asp Trp Lys Ser Gly Glu Tyr Trp Ile Asp Pro Asn 1265 1270 1275 Gln Gly Cys Asn Leu Asp Ala Ile Lys Val Phe Cys Asn Met Glu 1280 1285 1290 Thr Gly Glu Thr Cys Val Tyr Pro Thr Gln Pro Ser Val Ala Gln 1295 1300 1305 Lys Asn Trp Tyr Ile Ser Lys Asn Pro Lys Glu Lys Arg His Val 1310 1315 1320 Trp Tyr Gly Glu Ser Met Thr Gly Gly Phe Gln Phe Glu Tyr Gly 1325 1330 1335 Gly Gln Gly Ser Asp Pro Ala Asp Val Ala Ile Gln Leu Thr Phe 1340 1345 1350 Leu Arg Leu Met Ser Thr Glu Ala Ser Gln Asn Ile Thr Tyr His 1355 1360 1365 Cys Lys Asn Ser Val Ala Tyr Met Asp Gln Gln Thr Gly Asn Leu 1370 1375 1380 Lys Lys Ala Leu Leu Leu Gln Gly Ser Asn Glu Ile Glu Ile Arg 1385 1390 1395 Ala Glu Gly Asn Ser Arg Phe Thr Tyr Ser Val Thr Tyr Asp Gly 1400 1405 1410 Cys Thr Ser His Thr Gly Ala Trp Gly Lys Thr Val Ile Glu Tyr 1415 1420 1425 Lys Thr Thr Lys Thr Ser Arg Leu Pro Ile Ile Asp Val Ala Pro 1430 1435 1440 Leu Asp Val Gly Ala Pro Asp Gln Glu Phe Gly Phe Asp Val Gly 1445 1450 1455 Pro Ala Cys Phe Leu 1460 <210> 979 <211> 1364 <212> PRT <213> Artificial Sequence <220> <223> Col1A2, described by Accession No. NP_776945.1 <400> 979 Met Leu Ser Phe Val Asp Thr Arg Thr Leu Leu Leu Leu Leu Ala Val Thr 1 5 10 15 Ser Cys Leu Ala Thr Cys Gln Ser Leu Gln Glu Ala Thr Ala Arg Lys 20 25 30 Gly Pro Ser Gly Asp Arg Gly Pro Arg Gly Glu Arg Gly Pro Pro Gly 35 40 45 Pro Pro Gly Arg Asp Gly Asp Asp Gly Ile Pro Gly Pro Pro Gly Pro 50 55 60 Pro Gly Pro Pro Gly Pro Pro Gly Leu Gly Gly Asn Phe Ala Ala Gln 65 70 75 80 Phe Asp Ala Lys Gly Gly Gly Pro Gly Pro Met Gly Leu Met Gly Pro 85 90 95 Arg Gly Pro Pro Gly Ala Ser Gly Ala Pro Gly Pro Gln Gly Phe Gln 100 105 110 Gly Pro Pro Gly Glu Pro Gly Glu Pro Gly Gln Thr Gly Pro Ala Gly 115 120 125 Ala Arg Gly Pro Pro Gly Pro Pro Gly Lys Ala Gly Glu Asp Gly His 130 135 140 Pro Gly Lys Pro Gly Arg Pro Gly Glu Arg Gly Val Val Gly Pro Gln 145 150 155 160 Gly Ala Arg Gly Phe Pro Gly Thr Pro Gly Leu Pro Gly Phe Lys Gly 165 170 175 Ile Arg Gly His Asn Gly Leu Asp Gly Leu Lys Gly Gln Pro Gly Ala 180 185 190 Pro Gly Val Lys Gly Glu Pro Gly Ala Pro Gly Glu Asn Gly Thr Pro 195 200 205 Gly Gln Thr Gly Ala Arg Gly Leu Pro Gly Glu Arg Gly Arg Val Gly 210 215 220 Ala Pro Gly Pro Ala Gly Ala Arg Gly Ser Asp Gly Ser Val Gly Pro 225 230 235 240 Val Gly Pro Ala Gly Pro Ile Gly Ser Ala Gly Pro Pro Gly Phe Pro 245 250 255 Gly Ala Pro Gly Pro Lys Gly Glu Leu Gly Pro Val Gly Asn Pro Gly 260 265 270 Pro Ala Gly Pro Ala Gly Pro Arg Gly Glu Val Gly Leu Pro Gly Leu 275 280 285 Ser Gly Pro Val Gly Pro Pro Gly Asn Pro Gly Ala Asn Gly Leu Pro 290 295 300 Gly Ala Lys Gly Ala Ala Gly Leu Pro Gly Val Ala Gly Ala Pro Gly 305 310 315 320 Leu Pro Gly Pro Arg Gly Ile Pro Gly Pro Val Gly Ala Ala Gly Ala 325 330 335 Thr Gly Ala Arg Gly Leu Val Gly Glu Pro Gly Pro Ala Gly Ser Lys 340 345 350 Gly Glu Ser Gly Asn Lys Gly Glu Pro Gly Ala Val Gly Gln Pro Gly 355 360 365 Pro Pro Gly Pro Ser Gly Glu Glu Gly Lys Arg Gly Ser Thr Gly Glu 370 375 380 Ile Gly Pro Ala Gly Pro Pro Gly Pro Pro Gly Leu Arg Gly Asn Pro 385 390 395 400 Gly Ser Arg Gly Leu Pro Gly Ala Asp Gly Arg Ala Gly Val Met Gly 405 410 415 Pro Ala Gly Ser Arg Gly Ala Thr Gly Pro Ala Gly Val Arg Gly Pro 420 425 430 Asn Gly Asp Ser Gly Arg Pro Gly Glu Pro Gly Leu Met Gly Pro Arg 435 440 445 Gly Phe Pro Gly Ser Pro Gly Asn Ile Gly Pro Ala Gly Lys Glu Gly 450 455 460 Pro Val Gly Leu Pro Gly Ile Asp Gly Arg Pro Gly Pro Ile Gly Pro 465 470 475 480 Ala Gly Ala Arg Gly Glu Pro Gly Asn Ile Gly Phe Pro Gly Pro Lys 485 490 495 Gly Pro Ser Gly Asp Pro Gly Lys Ala Gly Glu Lys Gly His Ala Gly 500 505 510 Leu Ala Gly Ala Arg Gly Ala Pro Gly Pro Asp Gly Asn Asn Gly Ala 515 520 525 Gln Gly Pro Pro Gly Leu Gln Gly Val Gln Gly Gly Lys Gly Glu Gln 530 535 540 Gly Pro Ala Gly Pro Pro Gly Phe Gln Gly Leu Pro Gly Pro Ala Gly 545 550 555 560 Thr Ala Gly Glu Ala Gly Lys Pro Gly Glu Arg Gly Ile Pro Gly Glu 565 570 575 Phe Gly Leu Pro Gly Pro Ala Gly Ala Arg Gly Glu Arg Gly Pro Pro 580 585 590 Gly Glu Ser Gly Ala Ala Gly Pro Thr Gly Pro Ile Gly Ser Arg Gly 595 600 605 Pro Ser Gly Pro Pro Gly Pro Asp Gly Asn Lys Gly Glu Pro Gly Val 610 615 620 Val Gly Ala Pro Gly Thr Ala Gly Pro Ser Gly Pro Ser Gly Leu Pro 625 630 635 640 Gly Glu Arg Gly Ala Ala Gly Ile Pro Gly Gly Lys Gly Glu Lys Gly 645 650 655 Glu Thr Gly Leu Arg Gly Asp Ile Gly Ser Pro Gly Arg Asp Gly Ala 660 665 670 Arg Gly Ala Pro Gly Ala Ile Gly Ala Pro Gly Pro Ala Gly Ala Asn 675 680 685 Gly Asp Arg Gly Glu Ala Gly Pro Ala Gly Pro Ala Gly Pro Ala Gly 690 695 700 Pro Arg Gly Ser Pro Gly Glu Arg Gly Glu Val Gly Pro Ala Gly Pro 705 710 715 720 Asn Gly Phe Ala Gly Pro Ala Gly Ala Ala Gly Gln Pro Gly Ala Lys 725 730 735 Gly Glu Arg Gly Thr Lys Gly Pro Lys Gly Glu Asn Gly Pro Val Gly 740 745 750 Pro Thr Gly Pro Val Gly Ala Ala Gly Pro Ser Gly Pro Asn Gly Pro 755 760 765 Pro Gly Pro Ala Gly Ser Arg Gly Asp Gly Gly Pro Pro Gly Ala Thr 770 775 780 Gly Phe Pro Gly Ala Ala Gly Arg Thr Gly Pro Pro Gly Pro Ser Gly 785 790 795 800 Ile Ser Gly Pro Pro Gly Pro Pro Gly Pro Ala Gly Lys Glu Gly Leu 805 810 815 Arg Gly Pro Arg Gly Asp Gin Gly Pro Val Gly Arg Ser Gly Glu Thr 820 825 830 Gly Ala Ser Gly Pro Pro Gly Phe Val Gly Glu Lys Gly Pro Ser Gly 835 840 845 Glu Pro Gly Thr Ala Gly Pro Pro Gly Thr Pro Gly Pro Gln Gly Leu 850 855 860 Leu Gly Ala Pro Gly Phe Leu Gly Leu Pro Gly Ser Arg Gly Glu Arg 865 870 875 880 Gly Leu Pro Gly Val Ala Gly Ser Val Gly Glu Pro Gly Pro Leu Gly 885 890 895 Ile Ala Gly Pro Pro Gly Ala Arg Gly Pro Pro Gly Asn Val Gly Asn 900 905 910 Pro Gly Val Asn Gly Ala Pro Gly Glu Ala Gly Arg Asp Gly Asn Pro 915 920 925 Gly Asn Asp Gly Pro Pro Gly Arg Asp Gly Gln Pro Gly His Lys Gly 930 935 940 Glu Arg Gly Tyr Pro Gly Asn Ala Gly Pro Val Gly Ala Ala Gly Ala 945 950 955 960 Pro Gly Pro Gln Gly Pro Val Gly Pro Val Gly Lys His Gly Asn Arg 965 970 975 Gly Glu Pro Gly Pro Ala Gly Ala Val Gly Pro Ala Gly Ala Val Gly 980 985 990 Pro Arg Gly Pro Ser Gly Pro Gln Gly Ile Arg Gly Asp Lys Gly Glu 995 1000 1005 Pro Gly Asp Lys Gly Pro Arg Gly Leu Pro Gly Leu Lys Gly His 1010 1015 1020 Asn Gly Leu Gln Gly Leu Pro Gly Leu Ala Gly His His Gly Asp 1025 1030 1035 Gln Gly Ala Pro Gly Ala Val Gly Pro Ala Gly Pro Arg Gly Pro 1040 1045 1050 Ala Gly Pro Ser Gly Pro Ala Gly Lys Asp Gly Arg Ile Gly Gln 1055 1060 1065 Pro Gly Ala Val Gly Pro Ala Gly Ile Arg Gly Ser Gln Gly Ser 1070 1075 1080 Gln Gly Pro Ala Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Pro 1085 1090 1095 Pro Gly Pro Ser Gly Gly Gly Tyr Glu Phe Gly Phe Asp Gly Asp 1100 1105 1110 Phe Tyr Arg Ala Asp Gln Pro Arg Ser Pro Thr Ser Leu Arg Pro 1115 1120 1125 Lys Asp Tyr Glu Val Asp Ala Thr Leu Lys Ser Leu Asn Asn Gln 1130 1135 1140 Ile Glu Thr Leu Leu Thr Pro Glu Gly Ser Arg Lys Asn Pro Ala 1145 1150 1155 Arg Thr Cys Arg Asp Leu Arg Leu Ser His Pro Glu Trp Ser Ser 1160 1165 1170 Gly Tyr Tyr Trp Ile Asp Pro Asn Gin Gly Cys Thr Met Asp Ala 1175 1180 1185 Ile Lys Val Tyr Cys Asp Phe Ser Thr Gly Glu Thr Cys Ile Arg 1190 1195 1200 Ala Gln Pro Glu Asp Ile Pro Val Lys Asn Trp Tyr Arg Asn Ser 1205 1210 1215 Lys Ala Lys Lys His Val Trp Val Gly Glu Thr Ile Asn Gly Gly 1220 1225 1230 Thr Gln Phe Glu Tyr Asn Val Glu Gly Val Thr Thr Lys Glu Met 1235 1240 1245 Ala Thr Gln Leu Ala Phe Met Arg Leu Leu Ala Asn His Ala Ser 1250 1255 1260 Gln Asn Ile Thr Tyr His Cys Lys Asn Ser Ile Ala Tyr Met Asp 1265 1270 1275 Glu Glu Thr Gly Asn Leu Lys Lys Ala Val Ile Leu Gln Gly Ser 1280 1285 1290 Asn Asp Val Glu Leu Val Ala Glu Gly Asn Ser Arg Phe Thr Tyr 1295 1300 1305 Thr Val Leu Val Asp Gly Cys Ser Lys Lys Thr Asn Glu Trp Gln 1310 1315 1320 Lys Thr Ile Ile Glu Tyr Lys Thr Asn Lys Pro Ser Arg Leu Pro 1325 1330 1335 Ile Leu Asp Ile Ala Pro Leu Asp Ile Gly Gly Ala Asp Gln Glu 1340 1345 1350 Ile Arg Leu Asn Ile Gly Pro Val Cys Phe Lys 1355 1360 <210> 980 <211> 1466 <212> PRT <213> Artificial Sequence <220> <223> Col3A1, described by Accession No. NP_001070299.1 <400> 980 Met Met Ser Phe Val Gln Lys Gly Thr Trp Leu Leu Phe Ala Leu Leu 1 5 10 15 His Pro Thr Val Ile Leu Ala Gln Gln Glu Ala Val Asp Gly Gly Cys 20 25 30 Ser His Leu Gly Gln Ser Tyr Ala Asp Arg Asp Val Trp Lys Pro Glu 35 40 45 Pro Cys Gln Ile Cys Val Cys Asp Ser Gly Ser Val Leu Cys Asp Asp 50 55 60 Ile Ile Cys Asp Asp Gln Glu Leu Asp Cys Pro Asn Pro Glu Ile Pro 65 70 75 80 Phe Gly Glu Cys Cys Ala Val Cys Pro Gln Pro Pro Thr Ala Pro Thr 85 90 95 Arg Pro Pro Asn Gly Gln Gly Pro Gln Gly Pro Lys Gly Asp Pro Gly 100 105 110 Pro Pro Gly Ile Pro Gly Arg Asn Gly Asp Pro Gly Pro Pro Gly Ser 115 120 125 Pro Gly Ser Pro Gly Ser Pro Gly Pro Pro Gly Ile Cys Glu Ser Cys 130 135 140 Pro Thr Gly Gly Gln Asn Tyr Ser Pro Gln Tyr Glu Ala Tyr Asp Val 145 150 155 160 Lys Ser Gly Val Ala Gly Gly Gly Ile Ala Gly Tyr Pro Gly Pro Ala 165 170 175 Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Thr Ser Gly His Pro Gly 180 185 190 Ala Pro Gly Ala Pro Gly Tyr Gln Gly Pro Pro Gly Glu Pro Gly Gln 195 200 205 Ala Gly Pro Ala Gly Pro Pro Gly Pro Pro Gly Ala Ile Gly Pro Ser 210 215 220 Gly Pro Ala Gly Lys Asp Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly 225 230 235 240 Glu Arg Gly Phe Pro Gly Pro Pro Gly Met Lys Gly Pro Ala Gly Met 245 250 255 Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe Asp Gly Arg Asn 260 265 270 Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys Gly Glu Asn Gly 275 280 285 Val Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly Pro Arg Gly Ala 290 295 300 Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala Arg 305 310 315 320 Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly 325 330 335 Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu 340 345 350 Val Gly Pro Ala Gly Ser Pro Gly Ser Ser Gly Ala Pro Gly Gln Arg 355 360 365 Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Pro Gly Pro Pro Gly 370 375 380 Pro Pro Gly Ser Asn Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro 385 390 395 400 Ala Gly Ile Pro Gly Ala Pro Gly Leu Ile Gly Ala Arg Gly Pro Pro 405 410 415 Gly Pro Pro Gly Thr Asn Gly Val Pro Gly Gln Arg Gly Ala Ala Gly 420 425 430 Glu Pro Gly Lys Asn Gly Ala Lys Gly Asp Pro Gly Pro Arg Gly Glu 435 440 445 Arg Gly Glu Ala Gly Ser Pro Gly Ile Ala Gly Pro Lys Gly Glu Asp 450 455 460 Gly Lys Asp Gly Ser Pro Gly Glu Pro Gly Ala Asn Gly Leu Pro Gly 465 470 475 480 Ala Ala Gly Glu Arg Gly Val Pro Gly Phe Arg Gly Pro Ala Gly Ala 485 490 495 Asn Gly Leu Pro Gly Glu Lys Gly Pro Pro Gly Asp Arg Gly Gly Pro 500 505 510 Gly Pro Ala Gly Pro Arg Gly Val Ala Gly Glu Pro Gly Arg Asp Gly 515 520 525 Leu Pro Gly Gly Pro Gly Leu Arg Gly Ile Pro Gly Ser Pro Gly Gly 530 535 540 Pro Gly Ser Asp Gly Lys Pro Gly Pro Gly Ser Gln Gly Glu Thr 545 550 555 560 Gly Arg Pro Gly Pro Pro Gly Ser Pro Gly Pro Arg Gly Gln Pro Gly 565 570 575 Val Met Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys 580 585 590 Asn Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Ala 595 600 605 Gly Lys Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly 610 615 620 Pro Ser Gly Asp Lys Gly Asp Thr Gly Pro Pro Gly Pro Gln Gly Leu 625 630 635 640 Gln Gly Leu Pro Gly Thr Ser Gly Pro Pro Gly Glu Asn Gly Lys Pro 645 650 655 Gly Glu Pro Gly Pro Lys Gly Glu Ala Gly Ala Pro Gly Ile Pro Gly 660 665 670 Gly Lys Gly Asp Ser Gly Ala Pro Gly Glu Arg Gly Pro Pro Gly Ala 675 680 685 Gly Gly Pro Pro Gly Pro Arg Gly Gly Ala Gly Pro Pro Gly Pro Glu 690 695 700 Gly Gly Lys Gly Ala Ala Gly Pro Pro Gly Pro Pro Gly Ser Ala Gly 705 710 715 720 Thr Pro Gly Leu Gln Gly Met Pro Gly Glu Arg Gly Gly Pro Gly Gly 725 730 735 Pro Gly Pro Lys Gly Asp Lys Gly Glu Pro Gly Ser Ser Gly Val Asp 740 745 750 Gly Ala Pro Gly Lys Asp Gly Pro Arg Gly Pro Thr Gly Pro Ile Gly 755 760 765 Pro Pro Gly Pro Ala Gly Gln Pro Gly Asp Lys Gly Glu Ser Gly Ala 770 775 780 Pro Gly Val Pro Gly Ile Ala Gly Pro Arg Gly Gly Pro Gly Glu Arg 785 790 795 800 Gly Glu Gln Gly Pro Pro Gly Pro Ala Gly Phe Pro Gly Ala Pro Gly 805 810 815 Gln Asn Gly Glu Pro Gly Ala Lys Gly Glu Arg Gly Ala Pro Gly Glu 820 825 830 Lys Gly Glu Gly Gly Pro Pro Gly Ala Ala Gly Pro Ala Gly Gly Ser 835 840 845 Gly Pro Ala Gly Pro Pro Gly Pro Gln Gly Val Lys Gly Glu Arg Gly 850 855 860 Ser Pro Gly Gly Pro Gly Ala Ala Gly Phe Pro Gly Gly Arg Gly Pro 865 870 875 880 Pro Gly Pro Pro Gly Ser Asn Gly Asn Pro Gly Pro Pro Gly Ser Ser 885 890 895 Gly Ala Pro Gly Lys Asp Gly Pro Pro Gly Pro Pro Gly Ser Asn Gly 900 905 910 Ala Pro Gly Ser Pro Gly Ile Ser Gly Pro Lys Gly Asp Ser Gly Pro 915 920 925 Pro Gly Glu Arg Gly Ala Pro Gly Pro Gln Gly Pro Pro Gly Ala Pro 930 935 940 Gly Pro Leu Gly Ile Ala Gly Leu Thr Gly Ala Arg Gly Leu Ala Gly 945 950 955 960 Pro Pro Gly Met Pro Gly Ala Arg Gly Ser Pro Gly Pro Gln Gly Ile 965 970 975 Lys Gly Glu Asn Gly Lys Pro Gly Pro Ser Gly Gln Asn Gly Glu Arg 980 985 990 Gly Pro Pro Gly Pro Gln Gly Leu Pro Gly Leu Ala Gly Thr Ala Gly 995 1000 1005 Glu Pro Gly Arg Asp Gly Asn Pro Gly Ser Asp Gly Leu Pro Gly 1010 1015 1020 Arg Asp Gly Ala Pro Gly Ala Lys Gly Asp Arg Gly Glu Asn Gly 1025 1030 1035 Ser Pro Gly Ala Pro Gly Ala Pro Gly His Pro Gly Pro Pro Gly 1040 1045 1050 Pro Val Gly Pro Ala Gly Lys Ser Gly Asp Arg Gly Glu Thr Gly 1055 1060 1065 Pro Ala Gly Pro Ser Gly Ala Pro Gly Pro Ala Gly Ser Arg Gly 1070 1075 1080 Pro Pro Gly Pro Gln Gly Pro Arg Gly Asp Lys Gly Glu Thr Gly 1085 1090 1095 Glu Arg Gly Ala Met Gly Ile Lys Gly His Arg Gly Phe Pro Gly 1100 1105 1110 Asn Pro Gly Ala Pro Gly Ser Pro Gly Pro Ala Gly His Gln Gly 1115 1120 1125 Ala Val Gly Ser Pro Gly Pro Ala Gly Pro Arg Gly Pro Val Gly 1130 1135 1140 Pro Ser Gly Pro Pro Gly Lys Asp Gly Ala Ser Gly His Pro Gly 1145 1150 1155 Pro Ile Gly Pro Pro Gly Pro Arg Gly Asn Arg Gly Glu Arg Gly 1160 1165 1170 Ser Glu Gly Ser Pro Gly His Pro Gly Gln Pro Gly Pro Pro Gly 1175 1180 1185 Pro Pro Gly Ala Pro Gly Pro Cys Cys Gly Ala Gly Gly Val Ala 1190 1195 1200 Ala Ile Ala Gly Val Gly Ala Glu Lys Ala Gly Gly Phe Ala Pro 1205 1210 1215 Tyr Tyr Gly Asp Glu Pro Ile Asp Phe Lys Ile Asn Thr Asp Glu 1220 1225 1230 Ile Met Thr Ser Leu Lys Ser Val Asn Gly Gln Ile Glu Ser Leu 1235 1240 1245 Ile Ser Pro Asp Gly Ser Arg Lys Asn Pro Ala Arg Asn Cys Arg 1250 1255 1260 Asp Leu Lys Phe Cys His Pro Glu Leu Gln Ser Gly Glu Tyr Trp 1265 1270 1275 Val Asp Pro Asn Gln Gly Cys Lys Leu Asp Ala Ile Lys Val Tyr 1280 1285 1290 Cys Asn Met Glu Thr Gly Glu Thr Cys Ile Ser Ala Ser Pro Leu 1295 1300 1305 Thr Ile Pro Gln Lys Asn Trp Trp Thr Asp Ser Gly Ala Glu Lys 1310 1315 1320 Lys His Val Trp Phe Gly Glu Ser Met Glu Gly Gly Phe Gln Phe 1325 1330 1335 Ser Tyr Gly Asn Pro Glu Leu Pro Glu Asp Val Leu Asp Val Gln 1340 1345 1350 Leu Ala Phe Leu Arg Leu Leu Ser Ser Arg Ala Ser Gln Asn Ile 1355 1360 1365 Thr Tyr His Cys Lys Asn Ser Ile Ala Tyr Met Asp His Ala Ser 1370 1375 1380 Gly Asn Val Lys Lys Ala Leu Lys Leu Met Gly Ser Asn Glu Gly 1385 1390 1395 Glu Phe Lys Ala Glu Gly Asn Ser Lys Phe Thr Tyr Thr Val Leu 1400 1405 1410 Glu Asp Gly Cys Thr Lys His Thr Gly Glu Trp Gly Lys Thr Val 1415 1420 1425 Phe Gln Tyr Gln Thr Arg Lys Ala Val Arg Leu Pro Ile Val Asp 1430 1435 1440 Ile Ala Pro Tyr Asp Ile Gly Gly Pro Asp Gln Glu Phe Gly Ala 1445 1450 1455 Asp Ile Gly Pro Val Cys Phe Leu 1460 1465 <210> 981 <211> 87 <212> DNA <213> Artificial Sequence <220> <223> Primer <400> 981 aagtccttag atgccgacaa gattaagaga gacgtcaaat ctggtgttgc tgttggaggt 60 ttagcaggct accctggtcc cgcaggg 87 <210> 982 <211> 1466 <212> PRT <213> Artificial Sequence <220> <223> Human COL3A1, described by Accession No. P02461.4 <400> 982 Met Met Ser Phe Val Gln Lys Gly Ser Trp Leu Leu Leu Ala Leu Leu 1 5 10 15 His Pro Thr Ile Ile Leu Ala Gln Gln Glu Ala Val Glu Gly Gly Cys 20 25 30 Ser His Leu Gly Gln Ser Tyr Ala Asp Arg Asp Val Trp Lys Pro Glu 35 40 45 Pro Cys Gln Ile Cys Val Cys Asp Ser Gly Ser Val Leu Cys Asp Asp 50 55 60 Ile Ile Cys Asp Asp Gln Glu Leu Asp Cys Pro Asn Pro Glu Ile Pro 65 70 75 80 Phe Gly Glu Cys Cys Ala Val Cys Pro Gln Pro Pro Thr Ala Pro Thr 85 90 95 Arg Pro Pro Asn Gly Gln Gly Pro Gln Gly Pro Lys Gly Asp Pro Gly 100 105 110 Pro Pro Gly Ile Pro Gly Arg Asn Gly Asp Pro Gly Ile Pro Gly Gln 115 120 125 Pro Gly Ser Pro Gly Ser Pro Gly Pro Pro Gly Ile Cys Glu Ser Cys 130 135 140 Pro Thr Gly Pro Gln Asn Tyr Ser Pro Gln Tyr Asp Ser Tyr Asp Val 145 150 155 160 Lys Ser Gly Val Ala Val Gly Gly Leu Ala Gly Tyr Pro Gly Pro Ala 165 170 175 Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Thr Ser Gly His Pro Gly 180 185 190 Ser Pro Gly Ser Pro Gly Tyr Gln Gly Pro Pro Gly Glu Pro Gly Gln 195 200 205 Ala Gly Pro Ser Gly Pro Pro Gly Pro Pro Gly Ala Ile Gly Pro Ser 210 215 220 Gly Pro Ala Gly Lys Asp Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly 225 230 235 240 Glu Arg Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala Gly Ile 245 250 255 Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe Asp Gly Arg Asn 260 265 270 Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys Gly Glu Asn Gly 275 280 285 Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly Pro Arg Gly Ala 290 295 300 Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala Arg 305 310 315 320 Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly 325 330 335 Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu 340 345 350 Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg 355 360 365 Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro Gly 370 375 380 Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro 385 390 395 400 Ala Gly Ile Pro Gly Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Pro 405 410 415 Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly Gly Ala Gly 420 425 430 Glu Pro Gly Lys Asn Gly Ala Lys Gly Glu Pro Gly Pro Arg Gly Glu 435 440 445 Arg Gly Glu Ala Gly Ile Pro Gly Val Pro Gly Ala Lys Gly Glu Asp 450 455 460 Gly Lys Asp Gly Ser Pro Gly Glu Pro Gly Ala Asn Gly Leu Pro Gly 465 470 475 480 Ala Ala Gly Glu Arg Gly Ala Pro Gly Phe Arg Gly Pro Ala Gly Pro 485 490 495 Asn Gly Ile Pro Gly Glu Lys Gly Pro Ala Gly Glu Arg Gly Ala Pro 500 505 510 Gly Pro Ala Gly Pro Arg Gly Ala Ala Gly Glu Pro Gly Arg Asp Gly 515 520 525 Val Pro Gly Gly Pro Gly Met Arg Gly Met Pro Gly Ser Pro Gly Gly 530 535 540 Pro Gly Ser Asp Gly Lys Pro Gly Pro Gly Ser Gln Gly Glu Ser 545 550 555 560 Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln Pro Gly 565 570 575 Val Met Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys 580 585 590 Asn Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro 595 600 605 Gly Lys Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly 610 615 620 Pro Gly Gly Asp Lys Gly Asp Thr Gly Pro Pro Gly Pro Gln Gly Leu 625 630 635 640 Gln Gly Leu Pro Gly Thr Gly Gly Pro Pro Gly Glu Asn Gly Lys Pro 645 650 655 Gly Glu Pro Gly Pro Lys Gly Asp Ala Gly Ala Pro Gly Ala Pro Gly 660 665 670 Gly Lys Gly Asp Ala Gly Ala Pro Gly Glu Arg Gly Pro Pro Gly Leu 675 680 685 Ala Gly Ala Pro Gly Leu Arg Gly Gly Ala Gly Pro Pro Gly Pro Glu 690 695 700 Gly Gly Lys Gly Ala Ala Gly Pro Pro Gly Pro Pro Gly Ala Ala Gly 705 710 715 720 Thr Pro Gly Leu Gln Gly Met Pro Gly Glu Arg Gly Gly Leu Gly Ser 725 730 735 Pro Gly Pro Lys Gly Asp Lys Gly Glu Pro Gly Gly Pro Gly Ala Asp 740 745 750 Gly Val Pro Gly Lys Asp Gly Pro Arg Gly Pro Thr Gly Pro Ile Gly 755 760 765 Pro Pro Gly Pro Ala Gly Gln Pro Gly Asp Lys Gly Glu Gly Gly Ala 770 775 780 Pro Gly Leu Pro Gly Ile Ala Gly Pro Arg Gly Ser Pro Gly Glu Arg 785 790 795 800 Gly Glu Thr Gly Pro Pro Gly Pro Ala Gly Phe Pro Gly Ala Pro Gly 805 810 815 Gln Asn Gly Glu Pro Gly Gly Lys Gly Glu Arg Gly Ala Pro Gly Glu 820 825 830 Lys Gly Glu Gly Gly Pro Pro Gly Val Ala Gly Pro Pro Gly Gly Ser 835 840 845 Gly Pro Ala Gly Pro Pro Gly Pro Gln Gly Val Lys Gly Glu Arg Gly 850 855 860 Ser Pro Gly Gly Pro Gly Ala Ala Gly Phe Pro Gly Ala Arg Gly Leu 865 870 875 880 Pro Gly Pro Pro Gly Ser Asn Gly Asn Pro Gly Pro Pro Gly Pro Ser 885 890 895 Gly Ser Pro Gly Lys Asp Gly Pro Pro Gly Pro Ala Gly Asn Thr Gly 900 905 910 Ala Pro Gly Ser Pro Gly Val Ser Gly Pro Lys Gly Asp Ala Gly Gln 915 920 925 Pro Gly Glu Lys Gly Ser Pro Gly Ala Gln Gly Pro Pro Gly Ala Pro 930 935 940 Gly Pro Leu Gly Ile Ala Gly Ile Thr Gly Ala Arg Gly Leu Ala Gly 945 950 955 960 Pro Pro Gly Met Pro Gly Pro Arg Gly Ser Pro Gly Pro Gln Gly Val 965 970 975 Lys Gly Glu Ser Gly Lys Pro Gly Ala Asn Gly Leu Ser Gly Glu Arg 980 985 990 Gly Pro Pro Gly Pro Gln Gly Leu Pro Gly Leu Ala Gly Thr Ala Gly 995 1000 1005 Glu Pro Gly Arg Asp Gly Asn Pro Gly Ser Asp Gly Leu Pro Gly 1010 1015 1020 Arg Asp Gly Ser Pro Gly Gly Lys Gly Asp Arg Gly Glu Asn Gly 1025 1030 1035 Ser Pro Gly Ala Pro Gly Ala Pro Gly His Pro Gly Pro Pro Gly 1040 1045 1050 Pro Val Gly Pro Ala Gly Lys Ser Gly Asp Arg Gly Glu Ser Gly 1055 1060 1065 Pro Ala Gly Pro Ala Gly Ala Pro Gly Pro Ala Gly Ser Arg Gly 1070 1075 1080 Ala Pro Gly Pro Gln Gly Pro Arg Gly Asp Lys Gly Glu Thr Gly 1085 1090 1095 Glu Arg Gly Ala Ala Gly Ile Lys Gly His Arg Gly Phe Pro Gly 1100 1105 1110 Asn Pro Gly Ala Pro Gly Ser Pro Gly Pro Ala Gly Gln Gln Gly 1115 1120 1125 Ala Ile Gly Ser Pro Gly Pro Ala Gly Pro Arg Gly Pro Val Gly 1130 1135 1140 Pro Ser Gly Pro Pro Gly Lys Asp Gly Thr Ser Gly His Pro Gly 1145 1150 1155 Pro Ile Gly Pro Pro Gly Pro Arg Gly Asn Arg Gly Glu Arg Gly 1160 1165 1170 Ser Glu Gly Ser Pro Gly His Pro Gly Gln Pro Gly Pro Pro Gly 1175 1180 1185 Pro Pro Gly Ala Pro Gly Pro Cys Cys Gly Gly Val Gly Ala Ala 1190 1195 1200 Ala Ile Ala Gly Ile Gly Gly Glu Lys Ala Gly Gly Phe Ala Pro 1205 1210 1215 Tyr Tyr Gly Asp Glu Pro Met Asp Phe Lys Ile Asn Thr Asp Glu 1220 1225 1230 Ile Met Thr Ser Leu Lys Ser Val Asn Gly Gln Ile Glu Ser Leu 1235 1240 1245 Ile Ser Pro Asp Gly Ser Arg Lys Asn Pro Ala Arg Asn Cys Arg 1250 1255 1260 Asp Leu Lys Phe Cys His Pro Glu Leu Lys Ser Gly Glu Tyr Trp 1265 1270 1275 Val Asp Pro Asn Gln Gly Cys Lys Leu Asp Ala Ile Lys Val Phe 1280 1285 1290 Cys Asn Met Glu Thr Gly Glu Thr Cys Ile Ser Ala Asn Pro Leu 1295 1300 1305 Asn Val Pro Arg Lys His Trp Trp Thr Asp Ser Ser Ala Glu Lys 1310 1315 1320 Lys His Val Trp Phe Gly Glu Ser Met Asp Gly Gly Phe Gln Phe 1325 1330 1335 Ser Tyr Gly Asn Pro Glu Leu Pro Glu Asp Val Leu Asp Val His 1340 1345 1350 Leu Ala Phe Leu Arg Leu Leu Ser Ser Arg Ala Ser Gln Asn Ile 1355 1360 1365 Thr Tyr His Cys Lys Asn Ser Ile Ala Tyr Met Asp Gln Ala Ser 1370 1375 1380 Gly Asn Val Lys Lys Ala Leu Lys Leu Met Gly Ser Asn Glu Gly 1385 1390 1395 Glu Phe Lys Ala Glu Gly Asn Ser Lys Phe Thr Tyr Thr Val Leu 1400 1405 1410 Glu Asp Gly Cys Thr Lys His Thr Gly Glu Trp Ser Lys Thr Val 1415 1420 1425 Phe Glu Tyr Arg Thr Arg Lys Ala Val Arg Leu Pro Ile Val Asp 1430 1435 1440 Ile Ala Pro Tyr Asp Ile Gly Gly Pro Asp Gln Glu Phe Gly Val 1445 1450 1455 Asp Val Gly Pro Val Cys Phe Leu 1460 1465 <210> 983 <211> 5053 <212> DNA <213> Artificial Sequence <220> <223> Primer <400> 983 ggatccttca gtaatgtctt gtttcttttg ttgcagtggt gagccatttt gacttcgtga 60 aagtttcttt agaatagttg tttccagagg ccaaacattc cacccgtagt aaagtgcaag 120 cgtaggaaga ccaagactgg cataaatcag gtataagtgt cgagcactgg caggtgatct 180 tctgaaagtt tctactagca gataagatcc agtagtcatg catatggcaa caatgtaccg 240 tgtggatcta agaacgcgtc ctactaacct tcgcattcgt tggtccagtt tgttgttatc 300 gatcaacgtg acaaggttgt cgattccgcg taagcatgca tacccaagga cgcctgttgc 360 aattccaagt gagccagttc caacaatctt tgtaatatta gagcacttca ttgtgttgcg 420 cttgaaagta aaatgcgaac aaattaagag ataatctcga aaccgcgact tcaaacgcca 480 atatgatgtg cggcacacaa taagcgttca tatccgctgg gtgactttct cgctttaaaa 540 aattatccga aaaaattttc ctctagaatg actactttag atgacaccgc ttacagatat 600 agaacttcag tccctggtga cgcagaggca atcgaagctt tggacggatc ttttacgact 660 gataccgttt ttagagttac cgccactggt gatggtttca cattgagaga agtgccagtt 720 gatccacctc tactaaagt tttcccggat gatgagtcag atgacgagag cgacgatggt 780 gaagatggcg atcctgattc cagaacattc gtagcttatg gtgacgacgg tgacttggct 840 ggatttgtgg tagtttccta tagtggttgg aatcgtaggc tgactgtcga agatattgaa 900 gtggcacccg agcatagggg acacggcgtt ggtagagcct tgatgggact ggcaacagag 960 ttcgctagag agcgtggtgc aggacacctg tggctagaag tcacaaatgt gaacgctcca 1020 gcaatccatg cttaccgtag aatgggtttt actttgtgtg gtcttgacac agctttatac 1080 gacggaacag cttccgacgg tgaacaagcc ttgtacatgt ctatgccatg cccttagtaa 1140 aattgacacc ttacgattat ttagagagta tttattagtt ttattgtatg tatacggatg 1200 ttttattatc tatttatgcc cttatattct gtaactatcc aaaagtccta tcttatcaag 1260 ccagcaatct atgtccgcga acgtcaacta aaaataagct ttttatgctg ttctctcttt 1320 ttttcccttc ggtataatta taccttgcat ccacagattc tcctgccaaa ttttgcataa 1380 tcctttacaa catggctata tgggagcact tagcgccctc caaaacccat attgcctacg 1440 catgtatagg tgttttttcc acaatatttt ctctgtgctc tctttttatt aaagagaagc 1500 tctatatcgg agaagcttct gtggccgtta tattcggcct tatcgtggga ccacattgcc 1560 tgaattggtt tgccccggaa gattggggaa acttggatct gattacctta gctgcattac 1620 caatgcttaa tcagtgaggc acctatctca gcgatctgtc tatttcgttc atccatagtt 1680 gcctgactcc ccgtcgtgta gataactacg atacgggagg gcttaccatc tggccccagc 1740 gctgcgatga taccgcgaga accacgctca ccggctccgg atttatcagc aataaaccag 1800 ccagccggaa gggccgagcg cagaagtggt cctgcaactt tatccgcctc catccagtct 1860 attaattgtt gccgggaagc tagagtaagt agttcgccag ttaatagttt gcgcaacgtt 1920 gttgccatcg ctacaggcat cgtggtgtca cgctcgtcgt ttggtatggc ttcattcagc 1980 tccggttccc aacgatcaag gcgagttaca tgatccccca tgttgtgcaa aaaagcggtt 2040 agctccttcg gtcctccgat cgttgtcaga agtaagttgg ccgcagtgtt atcactcatg 2100 gttatggcag cactgcataa ttctcttact gtcatgccat ccgtaagatg cttttctgtg 2160 actggtgagt actcaaccaa gtcattctga gaatagtgta tgcggcgacc gagttgctct 2220 tgcccggcgt caatacggga taataccgcg ccacatagca gaactttaaa agtgctcatc 2280 attggaaaac gttcttcggg gcgaaaactc tcaaggatct taccgctgtt gagatccagt 2340 tcgatgtaac ccactcgtgc acccaactga tcttcagcat cttttacttt caccagcgtt 2400 tctgggtgag caaaaacagg aaggcaaaat gccgcaaaaa agggaataag ggcgacacgg 2460 aaatgttgaa tactcatatt cttccttttt caatattatt gaagcattta tcagggttat 2520 tgtctcatga gcggatacat atttgaatgt atttagaaaa ataaacaaat aggggtcagt 2580 gttacaacca attaaccaat tctgaaagga agaatctgca ggaaaagggt accactgagc 2640 gtcagacccc gtagaaaaga tcaaaggatc ttcttgagat cctttttttc tgcgcgtaat 2700 ctgctgcttg caaacaaaaa aaccaccgct accagcggtg gtttgtttgc cggatcaaga 2760 gctaccaact ctttttccga aggtaactgg cttcagcaga gcgcagatac caaatactgt 2820 tcttctagtg tagccgtagt taggccacca cttcaagaac tctgtagcac cgcctacata 2880 cctcgctctg ctaatcctgt taccagtggc tgctgccagt ggcgataagt cgtgtcttac 2940 cgggttggac ccaagacgat agttaccgga taaggcgcag cggtcgggct gaacgggggg 3000 ttcgtgcaca cagcccagct tggagcgaac gacctacacc gaactgagat acctacagcg 3060 tgagctatga gaaagcgcca cgcttcccga agggagaaag gcggacaggt atccggtaag 3120 cggcagggtc ggaacaggag agcgcacgag ggagcttcca gggggaaacg cctggtatct 3180 ttatagtcct gtcgggtttc gccacctctg acttgagcgt cgatttttgt gatgctcgtc 3240 aggggggcgg agcctatgga aaaacgccag caacgcggcc tttttacggt tcctggcctt 3300 ttgctggcct tttgctcaca tgtatttaaa taatgtatct aaacgcaaac tccgagctgg 3360 aaaaatgtta ccggcgatgc gcggacaatt tagaggcggc gatcaagaaa cacctgctgg 3420 gcgagcagtc tggagcacag tcttcgatgg gcccgagatc ccaccgcgtt cctgggtacc 3480 gggacgtgag gcagcgcgac atccatcaaa tataccaggc gccaaccgag tgtctcggaa 3540 aacagcttct ggatatcttc cgctggcggc gcaacgacga ataatagtcc ctggaggtga 3600 cggaatatat atgtgtggag ggtaaatctg acagggtgta gcaaaggtaa tattttccta 3660 aaacatgcaa tcggctgccc cgcaacggga aaaagaatga ctttggcact cttcaccaga 3720 gtggggtgtc ccgctcgtgt gtgcaaatag gctcccactg gtcaccccgg attttgcaga 3780 aaaacagcaa gttccggggt gtctcactgg tgtccgccaa taagaggagc cggcaggcac 3840 ggagtttaca tcaagctgtc tccgatacac tcgactacca tccgggtctc tcagagaggg 3900 gaatggcact ataaataccg cctccttgcg ctctctgcct tcatcaatca aatcatgctg 3960 aggactcgaa ttcgacctct gttgcctctt tgttggacga accattcacc ggtgtcttgt 4020 acttaaaggg cagtggtatc actgaagact tccagtccct aaagggtaag aagatcggtt 4080 acgttggtga cttcggtaag atccaaatcg atgaattgac caagcactac ggtatgaagc 4140 cagaagacta caccgccgtc agatgtggta tgaatgtcgc caagtacatc atcgaaggta 4200 agattgatgc cggtattggt atcgaatgta tgcaacaagt cgaattggaa gagtacttgg 4260 ccaagcaagg cagaccagct tctgatgcta aaatgttgag aattgacaag ttggcttgct 4320 tgggttgctg ttgcttctgt accgttcttt acatctgcaa cgatgaattt ttgaagaaga 4380 accctgaaaa ggtcagaaag ttcttgaaag ccatcaagaa ggcaaccgac tacgttctag 4440 ccgaccctgt gaaggcttgg aaagaataca tcgacttcaa gcctcaattg aacaacgatc 4500 tatcctacaa gcaataccaa agatgttacg cttacttctc ttcatctttg tacaatgttc 4560 accgtgactg gaagaaggtt accggttacg gtaagagatt agccatcttg ccaccagact 4620 atgtctcgaa ctacactaat gaatacttgt cctggccaga accagaagag gtttctgatc 4680 ctttggaagc tcaaagattg atggctattc atcaagaaaa atgcagacag gaaggtactt 4740 tcaagagatt ggctcttcca gcttaagcgg ccgcgagtcg tgagtaatca agaggatgtc 4800 agaatgccat ttgcctgaga gatgcaggct tcatttttga tactttttta tttgtaacct 4860 atatagtata ggattttttt tgtcattttg tttcttctcg tacgagcttg ctcctgatca 4920 gcctatctcg cagctgatga atatcttgtg gtaggggttt gggaaaatca ttcgagtttg 4980 atgtttttct tggtatttcc cactcctctt cagagtacag aagattaagt gagacgttcg 5040 tttgtgctcc gga 5053 <210> 984 <211> 6696 <212> DNA <213> Artificial Sequence <220> <223> Primer <400> 984 aagagaagct ctatatcgga gaagcttctg tggccgttat attcggcctt atcgtgggac 60 cacattgcct gaattggttt gccccggaag attggggaaa cttggatctg attaccttag 120 ctgcagaaaa gggtaccact gagcgtcaga ccccgtagaa aagatcaaag gatcttcttg 180 agatcctttt tttctgcgcg taatctgctg cttgcaaaca aaaaaaccac cgctaccagc 240 ggtggtttgt ttgccggatc aagagctacc aactcttttt ccgaaggtaa ctggcttcag 300 cagagcgcag ataccaaata ctgttcttct agtgtagccg tagttaggcc accacttcaa 360 gaactctgta gcaccgccta catacctcgc tctgctaatc ctgttaccag tggctgctgc 420 cagtggcgat aagtcgtgtc ttaccgggtt ggacccaaga cgatagttac cggataaggc 480 gcagcggtcg ggctgaacgg ggggttcgtg cacacagccc agcttggagc gaacgaccta 540 caccgaactg agatacctac agcgtgagct atgagaaagc gccacgcttc ccgaagggag 600 aaaggcggac aggtatccgg taagcggcag ggtcggaaca ggagagcgca cgagggagct 660 tccaggggga aacgcctggt atctttatag tcctgtcggg tttcgccacc tctgacttga 720 gcgtcgattt ttgtgatgct cgtcaggggg gcggagccta tggaaaaacg ccagcaacgc 780 ggccttttta cggttcctgg ccttttgctg gccttttgct cacatgtatt taaataatgt 840 atctaaacgc aaactccgag ctggaaaaat gttaccggcg atgcgcggac aatttagagg 900 cggcgatcaa gaaacacctg ctgggcgagc agtctggagc acagtcttcg atgggcccga 960 gatccccaccg cgttcctggg taccgggacg tgaggcagcg cgacatccat caaatatacc 1020 aggcgccaac cgagtgtctc ggaaaacagc ttctggatat cttccgctgg cggcgcaacg 1080 acgaataata gtccctggag gtgacggaat atatatgtgt ggagggtaaa tctgacaggg 1140 tgtagcaaag gtaatatttt cctaaaacat gcaatcggct gccccgcaac gggaaaaaga 1200 atgactttgg cactcttcac cagagtgggg tgtcccgctc gtgtgtgcaa ataggctccc 1260 actggtcacc ccggattttg cagaaaaaca gcaagttccg gggtgtctca ctggtgtccg 1320 ccaataagag gagccggcag gcacggagtt tacatcaagc tgtctccgat acactcgact 1380 accatccggg tctctcagag aggggaatgg cactataaat accgcctcct tgcgctctct 1440 gccttcatca atcaaatcat gtacaggaac ttaataattg ctactgccct tacttgcggt 1500 gcatacagtg cctacgtgcc ttccgaacca tggagcacac tgacacctga tgctagcctt 1560 gaaagtgccc tcaaagatta ctcacaaact tttggaatag ctataagtc cttagatgcc 1620 gacaagatta agagagacgt caaatctggt gttgctggag gaggtattgc aggctaccct 1680 ggtcccgcag ggcccccagg tccgccgggt ccgcccggaa catcaggtca tcccggagcc 1740 cctggtgcac caggttatca gggaccgccc ggagagcctg gacaagctgg tcccgctgga 1800 ccccctggtc caccaggtgc tattggacca agtggtcctg ccggaaaaga cggtgaatcc 1860 ggtagacctg gtagacccgg cgaaaggggt ttcccaggtc ctcccggaat gaagggtcca 1920 gccggtatgc ccggttttcc tgggatgaag ggtcacagag gatttgatgg tagaaacgga 1980 gagaaaggcg aaaccggtgc tcccggactg aagggtgaaa acggtgtccc tggtgagaac 2040 ggcgctcctg gacctatggg tccacgtggt gctccaggag aaagaggcag accaggattg 2100 cctggtgcag ctggtgctag aggtaacgat ggtgcccgtg gttccgatgg acaacccggg 2160 ccacccggcc ctccaggtac cgctggattt cctggaagcc ctggtgctaa gggggaggtt 2220 ggtccggctg gtagtcccgg aagtagcggt gccccaggtc aaagaggcga accaggccct 2280 cagggtcacg caggagcacc tggaccgcct ggtcctcctg gttcgaatgg ttcgcctgga 2340 ggaaaaggtg aaatggggcc cgcaggaatc cccggtgcgc ctggtcttat tggtgccagg 2400 ggtcctccag gcccgccagg tacaaatggt gtacccggac agcgaggagc agctggtgaa 2460 cctggtaaaa acggtgccaa aggagatcca ggtcctcgtg gagagcgtgg tgaagctggc 2520 tctcccggta tcgccggtcc aaaaggtgag gacggtaagg acggttcccc tggtgagcca 2580 ggtgcgaacg gactgccagg tgcagccgga gagcgaggag tcccaggatt caggggacca 2640 gccggtgcta acggcttgcc tggtgaaaaa gggccccctg gtgatagggg aggacccggt 2700 ccagcaggcc ctcgtggagt tgctggtgag cctggacgtg acggtttacc aggagggcca 2760 ggtttgaggg gtattcccgg gtcccctggc ggtcctggat cggatggaaa accagggcca 2820 ccaggttcgc agggtgaaac aggacgtcca ggcccacccg gctcacctgg tccaaggggt 2880 cagcctggtg tcatgggttt ccccggtcca aagggtaatg acggagcacc gggtaaaaat 2940 ggtgaacgtg gtggcccagg tggtccagga ccccaaggtc cagctggaaa aaacggtgag 3000 acaggtcctc aaggacctcc aggacctacc ggtcctagcg gagataaggg agatacggga 3060 ccgccaggac ctcaaggatt gcaaggtttg cctggtacat ctggccctcc cggagaaaat 3120 ggtaagcctg gagagccagg accaaaaggc gaagctggag ccccaggtat ccccggaggt 3180 aagggagact caggtgctcc gggtgagcgt ggtcctccgg gtgccggtgg tccacctgga 3240 cctagaggtg gtgccgggcc gccaggtcct gaaggtggta aaggtgctgc tggtccaccg 3300 ggaccgcctg gctctgctgg tactcctggc ttgcagggaa tgccaggaga gagaggtgga 3360 cctggaggtc ccggtccgaa gggtgataaa ggggagccag gatcatccgg tgttgacggc 3420 gcacctggta aagacggacc aaggggacca acgggtccaa tcggaccacc aggacccgct 3480 ggccagccag gagataaagg cgagtccgga gcacccggtg ttcctggtat agctggaccc 3540 aggggtggtc ccggtgaaag aggtgaacag ggcccaccgg gtcccgccgg tttccctggc 3600 gcccctggtc aaaatggaga accaggtgca aagggcgaga gaggagcccc aggagaaaag 3660 ggtgagggag gaccacccgg tgctgccggt ccagctgggg gttcaggtcc tgctggacca 3720 ccaggtccac agggcgttaa aggtgagaga ggaagtccag gtggtcctgg agctgctgga 3780 ttcccaggtg gccgtggacc tcctggtccc cctggatcga atggtaatcc tggtccgcca 3840 ggtagttcgg gtgctcctgg gaaggacggt ccacctggcc ccccaggtag taacggtgca 3900 cctggtagtc caggtatatc cggacctaaa ggagattccg gtccaccagg cgaaagaggg 3960 gccccaggcc cacagggtcc accaggagcc cccggtcctc tgggtattgc tggtcttact 4020 ggtgcacgtg gactggccgg tccacccgga atgcctggag caagaggttc acctggacca 4080 caaggtatta aaggagagaa cggtaaacct ggaccttccg gtcaaaacgg agagcgggga 4140 cccccaggcc cccaaggtct gccaggacta gctggtaccg caggggaacc aggaagagat 4200 ggaaatccag gttcagacgg actacccggt agagatggtg caccgggggc caagggcgac 4260 aggggtgaga atggatctcc tggtgcgcca ggggcaccag gccacccagg tcccccaggt 4320 cctgtgggcc ctgctggaaa gtcaggtgac aggggagaga caggcccggc tggtccatct 4380 ggcgcacccg gaccagctgg ttccagaggc ccacctggtc cgcaaggccc tagaggtgac 4440 aagggagaga ctggagaacg aggtgctatg ggtatcaagg gtcatagagg ttttccgggt 4500 aatcccggcg ccccaggttc tcctggtcca gctggccatc aaggtgcagt cggatcgccc 4560 ggcccagccg gtcccagggg ccctgttggt ccatccggtc ctccaggaaa ggatggtgct 4620 tctggacacc caggacctat cggacctccg ggtcctagag gtaatagagg agaacgtgga 4680 tccgagggta gtcctggtca ccctggtcaa cctggcccac cagggcctcc aggtgcaccc 4740 ggtccatgtt gtggtgcagg cggtgtggct gcaattgctg gtgtgggtgc tgaaaaggcc 4800 ggcggtttcg ctccatatta tggtgatgaa ccgattgatt ttaagatcaa tactgacgaa 4860 atcatgactt ccttaaagtc cgttaatggt caaattgagt ctctaatctc cccagatggt 4920 tcacgtaaaa atcctgctag aaattgtaga gatttgaagt tttgtcaccc cgagttgcag 4980 tccggtgagt actgggtgga ccccaatcaa ggttgtaagt tagacgctat taaagtttac 5040 tgcaatatgg agacaggaga aacttgcatc agcgcttaat caagaggatg tcagaatgcc 5100 atttgcctga gagatgcagg cttcattttt gatacttttt tatttgtaac ctatatagta 5160 taggattttt tttgtcattt tgtttcttct cgtacgagct tgctcctgat cagcctatct 5220 cgcagctgat gaatatcttg tggtaggggt ttgggaaaat cattcgagtt tgatgttttt 5280 cttggtattt cccactcctc ttcagagtac agaagattaa gtgagacgtt cgtttgtgct 5340 ccggaggatc cttcagtaat gtcttgtttc ttttgttgca gtggtgagcc attttgactt 5400 cgtgaaagtt tctttagaat agttgtttcc agaggccaaa cattccaccc gtagtaaagt 5460 gcaagcgtag gaagccaag actggcataa atcaggtata agtgtcgagc actggcaggt 5520 gatcttctga aagtttctac tagcagataa gatccagtag tcatgcatat ggcaacaatg 5580 taccgtgtgg atctaagaac gcgtcctact aaccttcgca ttcgttggtc cagtttgttg 5640 ttatcgatca acgtgacaag gttgtcgatt ccgcgtaagc atgcataccc aaggacgcct 5700 gttgcaattc caagtgagcc agttccaaca atctttgtaa tattagagca cttcattgtg 5760 ttgcgcttga aagtaaaatg cgaacaaatt aagagataat ctcgaaaccg cgacttcaaa 5820 cgccaatatg atgtgcggca cacaataagc gttcatatcc gctgggtgac tttctcgctt 5880 taaaaaatta tccgaaaaaa ttttctagag tgttgttact ttatacttcc ggctcgtata 5940 atacgacaag gtgtaaggag gactaaacca tggctaaact cacctctgct gttccagtcc 6000 tgactgctcg tgatgttgct ggtgctgttg agttctggac tgataggctc ggtttctccc 6060 gtgacttcgt agaggacgac tttgccggtg ttgtacgtga cgacgttacc ctgttcatct 6120 ccgcagttca ggaccaggtt gtgccagaca acactctggc atgggtatgg gttcgtggtc 6180 tggacgaact gtacgctgag tggtctgagg tcgtgtctac caacttccgt gatgcatctg 6240 gtccagctat gaccgagatc ggtgaacagc cctggggtcg tgagtttgca ctgcgtgatc 6300 cagctggtaa ctgcgtgcat ttcgtcgcag aagagcagga ctaacaattg acaccttacg 6360 attatttaga gagtatttat tagttttatt gtatgtatac ggatgtttta ttatctattt 6420 atgcccttat attctgtaac tatccaaaag tcctatctta tcaagccagc aatctatgtc 6480 cgcgaacgtc aactaaaaat aagcttttta tgctcttctc tctttttttc ccttcggtat 6540 aattatacct tgcatccaca gattctcctg ccaaattttg cataatcctt tacaacatgg 6600 ctatatggga gcacttagcg ccctccaaaa cccatattgc ctacgcatgt ataggtgttt 6660 tttccacaat attttctctg tgctctcttt ttatta 6696 <210> 985 <211> 6420 <212> DNA <213> Artificial Sequence <220> <223> Primer <400> 985 caggtcctga aggtggtaaa ggtgctgctg gtccaccggg accgcctggc gccgctggta 60 ctcctggctt gcagggaatg ccaggagaga gaggtggatt aggaagcccc ggtccgaagg 120 gtgataaagg ggagccagga ggacctggtg ctgacggcgt tcctggtaaa gacggaccaa 180 ggggaccaac gggtccaatc ggaccaccag gacccgctgg ccagccagga gataaaggcg 240 agggaggagc acccggttta cctggtatag ctggacccag gggttccccc ggtgaaagag 300 gtgaaacagg cccaccgggt cccgccggtt tccctggcgc ccctggtcaa aatggagaac 360 caggtggcaa gggcgagaga ggagccccag gagaaaaggg tgagggagga ccacccggtg 420 tcgccggtcc acctgggggt tcaggtcctg ctggaccacc aggtccacag ggcgttaaag 480 gtgagagagg aagtccaggt ggtcctggag ctgctggatt cccaggtgct cgtggacttc 540 ctggtccccc tggatcgaat ggtaatcctg gtccgccagg tccatcgggt agccctggga 600 aggacggtcc acctggcccc gctggtaaca caggtgcacc tggtagtcca ggtgtgtccg 660 gacctaaagg agatgctggt cagccaggcg aaaaagggag cccaggcgca cagggtccac 720 caggagcccc cggtcctctg ggtattgctg gtattactgg tgcacgtgga ctggccggtc 780 cacccggaat gcctggacct agaggttcac ctggaccaca aggtgtcaaa ggagagagcg 840 gtaaacctgg agccaacggt ctttcaggag agcggggacc cccaggcccc caaggtctgc 900 caggactagc tggtaccgca ggggaaccag gaagagatgg aaatccaggt tcagacggac 960 tacccggtag agatggtagc ccggggggaa agggcgacag gggtgagaat ggatctcctg 1020 gtgcgccagg ggcaccaggc cacccaggtc ccccaggtcc tgtgggccct gctggaaagt 1080 caggtgacag gggagagagc ggcccggctg gtccagccgg cgcacccgga ccagctggtt 1140 ccagaggcgc acctggtccg caaggcccta gaggtgacaa gggagagact ggagaacgag 1200 gtgctgctgg tatcaagggt catagaggtt ttccgggtaa tcccggcgcc ccaggttctc 1260 ctggtccagc tggccagcaa ggtgcaattg gatcgcccgg cccagccggt cccaggggcc 1320 ctgttggtcc atccggtcct ccaggaaagg atggtacatc tggacaccca ggacctatcg 1380 gacctccggg tcctagaggt aatagaggag aacgtggatc cgagggtagt cctggtcacc 1440 ctggtcaacc tggcccacca gggcctccag gtgcacccgg tccatgttgt ggtggagttg 1500 gtgccgctgc aattgctggt attggtggtg aaaaggccta atcaagagga tgtcagaatg 1560 ccatttgcct gagagatgca ggcttcattt ttgatacttt tttatttgta acctatatag 1620 tataggattt tttttgtcat tttgtttctt ctcgtacgag cttgctcctg atcagcctat 1680 ctcgcagctg atgaatatct tgtggtaggg gtttgggaaa atcattcgag tttgatgttt 1740 ttcttggtat ttcccactcc tcttcagagt acagaagatt aagtgagacg ttcgtttgtg 1800 ctccggagga tccttcagta atgtcttgtt tcttttgttg cagtggtgag ccattttgac 1860 ttcgtgaaag tttctttaga atagttgttt ccagaggcca aacattccac ccgtagtaaa 1920 gtgcaagcgt aggaagcca agactggcat aaatcaggta taagtgtcga gcactggcag 1980 gtgatcttct gaaagtttct actagcagat aagatccagt agtcatgcat atggcaacaa 2040 tgtaccgtgt ggatctaaga acgcgtccta ctaaccttcg cattcgttgg tccagtttgt 2100 tgttatcgat caacgtgaca aggttgtcga ttccgcgtaa gcatgcatac ccaaggacgc 2160 ctgttgcaat tccaagtgag ccagttccaa caatctttgt aatattagag cacttcattg 2220 tgttgcgctt gaaagtaaaa tgcgaacaaa ttaagagata atctcgaaac cgcgacttca 2280 aacgccaata tgatgtgcgg cacacaataa gcgttcatat ccgctgggtg actttctcgc 2340 tttaaaaaat tatccgaaaa aattttctag agtgttgtta ctttatactt ccggctcgta 2400 taatacgaca aggtgtaagg aggactaaac catggctaaa ctcacctctg ctgttccagt 2460 cctgactgct cgtgatgttg ctggtgctgt tgagttctgg actgataggc tcggtttctc 2520 ccgtgacttc gtagaggacg actttgccgg tgttgtacgt gacgacgtta ccctgttcat 2580 ctccgcagtt caggaccagg ttgtgccaga caacactctg gcatgggtat gggttcgtgg 2640 tctggacgaa ctgtacgctg agtggtctga ggtcgtgtct accaacttcc gtgatgcatc 2700 tggtccagct atgaccgaga tcggtgaaca gccctggggt cgtgagtttg cactgcgtga 2760 tccagctggt aactgcgtgc atttcgtcgc agaagagcag gactaacaat tgacacctta 2820 cgattattta gagagtattt attagtttta ttgtatgtat acggatgttt tattatctat 2880 ttatgccctt atattctgta actatccaaa agtcctatct tatcaagcca gcaatctatg 2940 tccgcgaacg tcaactaaaa ataagctttt tatgctcttc tctctttttt tcccttcggt 3000 ataattatac cttgcatcca cagattctcc tgccaaattt tgcataatcc tttacaacat 3060 ggctatatgg gagcacttag cgccctccaa aacccatatt gcctacgcat gtataggtgt 3120 tttttccaca atattttctc tgtgctctct ttttattaaa gagaagctct atatcggaga 3180 agcttctgtg gccgttatat tcggccttat cgtgggacca cattgcctga attggtttgc 3240 cccggaagat tggggaaact tggatctgat taccttagct gcagaaaagg gtaccactga 3300 gcgtcagacc ccgtagaaaa gatcaaagga tcttcttgag atcctttttt tctgcgcgta 3360 atctgctgct tgcaaacaaa aaaaccaccg ctaccagcgg tggtttgttt gccggatcaa 3420 gagctaccaa ctctttttcc gaaggtaact ggcttcagca gagcgcagat accaaatact 3480 gttcttctag tgtagccgta gttaggccac cacttcaaga actctgtagc accgcctaca 3540 tacctcgctc tgctaatcct gttaccagtg gctgctgcca gtggcgataa gtcgtgtctt 3600 accgggttgg acccaagacg atagttaccg gataaggcgc agcggtcggg ctgaacgggg 3660 ggttcgtgca cacagcccag cttggagcga acgacctaca ccgaactgag atacctacag 3720 cgtgagctat gagaaagcgc cacgcttccc gaagggagaa aggcggacag gtatccggta 3780 agcggcaggg tcggaacagg agagcgcacg agggagcttc cagggggaaa cgcctggtat 3840 ctttatagtc ctgtcgggtt tcgccacctc tgacttgagc gtcgattttt gtgatgctcg 3900 tcaggggggc ggagcctatg gaaaaacgcc agcaacgcgg cctttttacg gttcctggcc 3960 ttttgctggc cttttgctca catgtattta aataatgtat ctaaacgcaa actccgagct 4020 ggaaaaatgt taccggcgat gcgcggacaa tttagaggcg gcgatcaaga aacacctgct 4080 gggcgagcag tctggagcac agtcttcgat gggcccgaga tcccaccgcg ttcctgggta 4140 ccgggacgtg aggcagcgcg acatccatca aatataccag gcgccaaccg agtgtctcgg 4200 aaaacagctt ctggatatct tccgctggcg gcgcaacgac gaataatagt ccctggaggt 4260 gacggaatat atatgtgtgg agggtaaatc tgacagggtg tagcaaaggt aatattttcc 4320 taaaacatgc aatcggctgc cccgcaacgg gaaaaagaat gactttggca ctcttcacca 4380 gagtggggtg tcccgctcgt gtgtgcaaat aggctcccac tggtcacccc ggattttgca 4440 gaaaaacagc aagttccggg gtgtctcact ggtgtccgcc aataagagga gccggcaggc 4500 acggagttta catcaagctg tctccgatac actcgactac catccgggtc tctcagagag 4560 gggaatggca ctataaatac cgcctccttg cgctctctgc cttcatcaat caaatcatgt 4620 acaggaactt aataattgct actgccctta cttgcggtgc atacagtgcc tacgtgcctt 4680 ccgaaccatg gagcacactg acacctgatg ctagccttga aagtgccctc aaagattact 4740 cacaaacttt tggaatagct attaagtcct tagatgccga caagattaag agagacgtca 4800 aatctggtgt tgctgttgga ggtttagcag gctaccctgg tcccgcaggg cccccaggtc 4860 cgccgggtcc gcccggaaca tcaggtcatc ccggaagccc tggttcacca ggttatcagg 4920 gaccgcccgg agagcctgga caagctggtc cctccggacc ccctggtcca ccaggtgcta 4980 ttggaccaag tggtcctgcc ggaaaagacg gtgaatccgg tagacctggt agacccggcg 5040 aaaggggttt accaggtcct cccggaatta agggtccagc cggtataccc ggttttcctg 5100 ggatgaaggg tcacagagga tttgatggta gaaacggaga gaaaggcgaa accggtgctc 5160 ccggactgaa gggtgaaaac ggtcttcctg gtgagaacgg cgctcctgga cctatgggtc 5220 cacgtggtgc tccaggagaa agaggcagac caggattgcc tggtgcagct ggtgctagag 5280 gtaacgatgg tgcccgtggt tccgatggac aacccgggcc acccggccct ccaggtaccg 5340 ctggatttcc tggaagccct ggtgctaagg gggaggttgg tccggctggt agtcccggaa 5400 gtaacggtgc cccaggtcaa agaggcgaac caggccctca gggtcacgca ggagcacagg 5460 gaccgcctgg tcctcctggt attaatggtt cgcctggagg aaaaggtgaa atggggcccg 5520 caggaatccc cggtgcgcct ggtcttatgg gtgccagggg tcctccaggc ccggccggtg 5580 caaatggtgc tcccggatta cgaggaggag ctggtgaacc tggtaaaaac ggtgccaaag 5640 gagaaccagg tcctcgtgga gagcgtggtg aagctggcat tcccggtgtg cctggtgcaa 5700 aaggtgagga cggtaaggac ggttcccctg gtgagccagg tgcgaacgga ctgccaggtg 5760 cagccggaga gcgaggagct ccaggattca ggggaccagc cggtcctaac ggcattcctg 5820 gtgaaaaagg gcccgccggt gaaaggggag ctcccggtcc agcaggccct cgtggagcag 5880 ctggtgagcc tggacgtgac ggtgtcccag gagggccagg tatgaggggt atgcccgggt 5940 cccctggcgg tcctggatcg gatggaaaac cagggccacc aggttcgcag ggtgaaagcg 6000 gacgtccagg cccacccggc ccttcaggtc caaggggtca gcctggtgtc atgggtttcc 6060 ccggtccaaa gggtaatgac ggagcaccgg gtaaaaatgg tgaacgtggt ggcccaggtg 6120 gtccaggacc ccaaggtcca ccaggaaaaa acggtgagac aggtcctcaa ggacctccag 6180 gacctaccgg tcctggagga gataagggag atacgggacc gccaggacct caaggattgc 6240 aaggtttgcc tggtacagga ggccctcccg gagaaaatgg taagcctgga gagccaggac 6300 caaaaggcga tgctggagcc ccaggtgcac ccggaggtaa gggagacgcc ggtgctccgg 6360 gtgagcgtgg tcctccgggt ttagctggtg cacctggatt gagaggtggt gccgggccgc 6420 <210> 986 <211> 546 <212> PRT <213> Artificial Sequence <220> <223> Collagen Fragment <400> 986 Asp Val Lys Ser Gly Val Ala Val Gly Gly Leu Ala Gly Tyr Pro Gly 1 5 10 15 Pro Ala Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Thr Ser Gly His 20 25 30 Pro Gly Ser Pro Gly Ser Pro Gly Tyr Gln Gly Pro Pro Gly Glu Pro 35 40 45 Gly Gln Ala Gly Pro Ser Gly Pro Pro Gly Pro Pro Gly Ala Ile Gly 50 55 60 Pro Ser Gly Pro Ala Gly Lys Asp Gly Glu Ser Gly Arg Pro Gly Arg 65 70 75 80 Pro Gly Glu Arg Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala 85 90 95 Gly Ile Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe Asp Gly 100 105 110 Arg Asn Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys Gly Glu 115 120 125 Asn Gly Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly Pro Arg 130 135 140 Gly Ala Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly 145 150 155 160 Ala Arg Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro 165 170 175 Pro Gly Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys 180 185 190 Gly Glu Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly 195 200 205 Gln Arg Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro 210 215 220 Pro Gly Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly Lys Gly Glu Met 225 230 235 240 Gly Pro Ala Gly Ile Pro Gly Ala Pro Gly Leu Met Gly Ala Arg Gly 245 250 255 Pro Pro Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly Gly 260 265 270 Ala Gly Glu Pro Gly Lys Asn Gly Ala Lys Gly Glu Pro Gly Pro Arg 275 280 285 Gly Glu Arg Gly Glu Ala Gly Ile Pro Gly Val Pro Gly Ala Lys Gly 290 295 300 Glu Asp Gly Lys Asp Gly Ser Pro Gly Glu Pro Gly Ala Asn Gly Leu 305 310 315 320 Pro Gly Ala Ala Gly Glu Arg Gly Ala Pro Gly Phe Arg Gly Pro Ala 325 330 335 Gly Pro Asn Gly Ile Pro Gly Glu Lys Gly Pro Ala Gly Glu Arg Gly 340 345 350 Ala Pro Gly Pro Ala Gly Pro Arg Gly Ala Ala Gly Glu Pro Gly Arg 355 360 365 Asp Gly Val Pro Gly Gly Pro Gly Met Arg Gly Met Pro Gly Ser Pro 370 375 380 Gly Gly Pro Gly Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly 385 390 395 400 Glu Ser Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln 405 410 415 Pro Gly Val Met Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro 420 425 430 Gly Lys Asn Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly 435 440 445 Pro Pro Gly Lys Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro 450 455 460 Thr Gly Pro Gly Gly Asp Lys Gly Asp Thr Gly Pro Pro Gly Pro Gln 465 470 475 480 Gly Leu Gln Gly Leu Pro Gly Thr Gly Gly Pro Pro Gly Glu Asn Gly 485 490 495 Lys Pro Gly Glu Pro Gly Pro Lys Gly Asp Ala Gly Ala Pro Gly Ala 500 505 510 Pro Gly Gly Lys Gly Asp Ala Gly Ala Pro Gly Glu Arg Gly Pro Pro 515 520 525 Ala Ile Ala Gly Ile Gly Gly Glu Lys Ala Gly Gly Phe Ala Pro Tyr 530 535 540 Tyr Gly 545

Claims (67)

A recombinant collagen fragment having a molecular weight of about 50 kDa and at least about 85% sequence homology to the amino acid sequence set forth in SEQ ID NO: 1. The recombinant collagen fragment of claim 1 , wherein the recombinant collagen fragment is not hydroxylated. The recombinant collagen fragment of claim 1 , wherein the recombinant collagen fragment is hydroxylated. The recombinant collagen fragment according to claim 3, wherein the collagen fragment has the amino acid sequence set forth in SEQ ID NO: 1. A recombinant collagen fragment comprising the amino acid sequence according to any one of SEQ ID NOs: 2 to 972. A composition comprising the recombinant collagen fragment of any one of claims 1 to 5. 7. The composition of claim 6, wherein the composition further comprises one or more peptides formed from hydrolysis of a collagen fragment having the amino acid sequence set forth in SEQ ID NO: 1. 8. The composition of claim 7, wherein at least one of the one or more peptides formed from hydrolysis of a collagen fragment having the amino acid sequence set forth in SEQ ID NO: 1 has an amino acid sequence according to one of SEQ ID NOs: 2-972. 9. The composition of any one of claims 6-8, further comprising a pharmaceutically acceptable or cosmetically acceptable excipient. A method for producing the recombinant collagen fragment of any one of claims 1 to 5, comprising producing the recombinant collagen fragment in a strain of genetically engineered yeast. 11. The method of claim 10, wherein the yeast is Pichia pastoris . 12. The method according to claim 10 or 11, wherein the yeast is transformed with a plasmid comprising the nucleic acid sequence set forth in SEQ ID NO: 973. 13. The method according to any one of claims 10 to 12, wherein the yeast is a yeast transformed with a plasmid comprising the nucleic acid sequence set forth in SEQ ID NO: 974. 14. The method according to any one of claims 10 to 13, comprising the steps of:
(i) fermenting the genetically engineered yeast in a fermentation broth;
(ii) recovering the recombinant collagen fragment secreted by the genetically engineered yeast from the fermentation broth; and
(iii) optionally, purifying the recombinant collagen fragment. 15. The method of claim 14, further comprising hydroxylating the recombinant collagen fragment ex vivo . A strain of yeast genetically engineered to produce the recombinant collagen fragment of any one of claims 1 to 5, wherein the strain of yeast comprises a vector comprising a DNA sequence encoding the recombinant collagen. 17. The strain of yeast according to claim 16, wherein the vector comprises a nucleic acid sequence comprising the DNA sequence set forth in SEQ ID NO:973. 18. The strain of yeast of claim 17, further comprising a second vector comprising a nucleic acid sequence comprising the DNA sequence set forth in SEQ ID NO:974. 19. The strain of yeast according to any one of claims 16 to 18, wherein the strain of yeast is Pichia pastoris . 6. A method of treating a dermatological condition comprising administering to a subject in need thereof an effective amount of the recombinant collagen fragment of any one of claims 1-5. 10. A method of treating a dermatological condition comprising administering to a subject in need thereof an effective amount of the composition of any one of claims 6-9. 22. The method of claim 21, wherein the dermatological condition is fine lines, wrinkles, dry skin, excessive pore size, skin abnormality, loss of elasticity, unwanted hair, thinning skin, purpura, actinic keratosis, pruritus, eczema, acne, rosacea, erythema , telangiectasia, actinic telangiectasia, skin cancer, or rhinitis. 23. The method of claim 21 or 22, wherein the composition is administered topically to a skin region. 24. The method of claim 23, wherein said skin region is the facial surface, scalp, neck, ears, shoulders, chest (breast) and/or decolletage (

), arm, hand, leg, stomach, hip, groin, back, foot, and combinations thereof. 6. A method of increasing collagen production in a cell, comprising administering to the cell an effective amount of the recombinant collagen fragment of any one of claims 1-5. 26. The method of claim 25, wherein the method increases the production of type I collagen. 27. The method of claim 25 or 26, wherein the method increases the production of type III collagen. 28. The method of any one of claims 25-27, wherein the cell is a fibroblast. 29. The method of any one of claims 25-28, wherein the cell is a cultured cell. 30. The method of any one of claims 25-29, wherein the fragment is formulated into a composition. 31. The method of any one of claims 25-30, wherein the fragment has the amino acid sequence set forth in SEQ ID NO: 1. For reducing the appearance of wrinkles, evening the skin tone, providing moisture, reducing the appearance of dark circles under the eyes, increasing the collagen content of the skin, increasing skin density, skin For improving firmness and elasticity, for improving the appearance of lines and wrinkles, for smoothing skin texture, for increasing skin radiance and radiance, for improving the appearance of sagging skin, for whitening skin, or 10. A skin care product comprising the composition of any one of claims 6-9 for use in any combination thereof. 10. A method of treating a wound in a human subject in need thereof, comprising applying the composition of any one of claims 6 to 9 to the wound of the subject, wherein applying said recombinant collagen fragment comprises human type I collagen. , inducing the production of human type III collagen or a combination thereof. 34. The method of claim 33, wherein the collagen fragment is topically applied to the wound. A recombinant collagen fragment having a molecular weight of about 50 kDa and at least about 85% sequence homology to the amino acid sequence set forth in SEQ ID NO: 986. 36. The recombinant collagen fragment of claim 35, wherein the recombinant collagen fragment is not hydroxylated. 36. The recombinant collagen fragment of claim 35, wherein the recombinant collagen fragment is hydroxylated. 38. The recombinant collagen fragment of claim 37, wherein the collagen fragment has the amino acid sequence set forth in SEQ ID NO: 986. 39. A composition comprising the recombinant collagen fragment of any one of claims 35-38. 40. The composition of claim 39, wherein the composition further comprises one or more peptides formed from hydrolysis of a collagen fragment having the amino acid sequence set forth in SEQ ID NO: 986. 41. The composition of claim 40, wherein at least one of said one or more peptides formed from hydrolysis of a collagen fragment having an amino acid sequence set forth in SEQ ID NO: 986 has an amino acid sequence according to one of SEQ ID NOs: 2-972. 42. The composition of any one of claims 39-41, further comprising a pharmaceutically acceptable or cosmetically acceptable excipient. 39. A method of producing the recombinant collagen fragment of any one of claims 35-38, comprising producing the recombinant collagen fragment in a strain of genetically engineered yeast. 44. The method of claim 43, wherein the yeast is Pichia pastoris . 45. The method of claim 43 or 44, wherein the yeast is transformed with a plasmid comprising the nucleic acid sequence set forth in SEQ ID NO:973. 46. The method of any one of claims 43-45, wherein the yeast is a yeast transformed with a plasmid comprising the nucleic acid sequence set forth in SEQ ID NO:974. 47. The method according to any one of claims 43 to 46, comprising the steps of:
(i) fermenting the genetically engineered yeast in a fermentation broth;
(ii) recovering the recombinant collagen fragment secreted by the genetically engineered yeast from the fermentation broth; and
(iii) optionally, purifying the recombinant collagen fragment. 48. The method of claim 47, further comprising hydroxylating the recombinant collagen fragment ex vivo . 39. A strain of yeast genetically engineered to produce the recombinant collagen fragment of any one of claims 35-38, wherein the strain of yeast comprises a vector comprising a DNA sequence encoding the recombinant collagen. 50. The strain of yeast according to claim 49, wherein the vector comprises a nucleic acid sequence comprising the DNA sequence set forth in SEQ ID NO:973. 51. The strain of yeast of claim 50, further comprising a second vector comprising a nucleic acid sequence comprising the DNA sequence set forth in SEQ ID NO:974. 52. The strain of yeast according to any one of claims 49 to 51, wherein the strain of yeast is Pichia pastoris . 39. A method of treating a dermatological condition comprising administering to a subject in need thereof an effective amount of the recombinant collagen fragment of any one of claims 35-38. 43. A method of treating a dermatological condition comprising administering to a subject in need thereof an effective amount of the composition of any one of claims 39-42. 55. The method of claim 54, wherein the dermatological condition is fine lines, wrinkles, dry skin, excessive pore size, skin discoloration, reduced elasticity, unwanted hair, thinning skin, purpura, actinic keratosis, pruritus, eczema, acne, rosacea, erythema , telangiectasia, actinic telangiectasia, skin cancer, or rhinitis. 55. The method of claim 53 or 54, wherein the composition is administered topically to a skin region. 57. The method of claim 56, wherein said skin region is the facial surface, scalp, neck, ears, shoulders, chest (including breast and/or décolletage), arms, hands, legs, stomach, buttocks, groin, back, feet and these selected from the group consisting of a combination of 39. A method of increasing collagen production in a cell comprising administering to the cell an effective amount of the recombinant collagen fragment of any one of claims 35-38. 59. The method of claim 58, wherein the method increases production of type I collagen. 60. The method of claim 58 or 59, wherein the method increases the production of type III collagen. 61. The method of any one of claims 58-60, wherein the cell is a fibroblast. 62. The method of any one of claims 58-61, wherein the cell is a cultured cell. 63. The method of any one of claims 58-62, wherein the fragment is formulated into a composition. 64. The method of any one of claims 58-63, wherein the fragment has the amino acid sequence set forth in SEQ ID NO: 986. For reducing the appearance of wrinkles, evening the skin tone, providing moisture, reducing the appearance of dark circles under the eyes, increasing the collagen content of the skin, increasing skin density, skin For improving firmness and elasticity, for improving the appearance of lines and wrinkles, for smoothing skin texture, for increasing skin radiance and radiance, for improving the appearance of sagging skin, for whitening skin, or 43. A skin care product comprising the composition of any one of claims 39-42 for use in any combination thereof. 43. A method of treating a wound in a human subject in need thereof comprising applying the composition of any one of claims 39 to 42 to the wound of the subject, wherein applying said recombinant collagen fragment comprises human type I collagen. , inducing the production of human type III collagen or a combination thereof. 67. The method of claim 66, wherein the collagen fragment is topically applied to the wound.

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