CN106796242A - For the quantitative method and system with detection of selectivity of allergen - Google Patents

For the quantitative method and system with detection of selectivity of allergen Download PDF

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CN106796242A
CN106796242A CN201580054874.8A CN201580054874A CN106796242A CN 106796242 A CN106796242 A CN 106796242A CN 201580054874 A CN201580054874 A CN 201580054874A CN 106796242 A CN106796242 A CN 106796242A
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gly
glu
leu
ser
gln
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T·J·阿曼
B·W·谢弗
R·C·希尔
G·单
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Corteva Agriscience LLC
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    • G01N30/00Investigating or analysing materials by separation into components using adsorption, absorption or similar phenomena or using ion-exchange, e.g. chromatography or field flow fractionation
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Abstract

The present invention relates to such method and system, it identifies candidate feature peptide by bioinformatics research, for carrying out quantitative Multi-way analysis to the complex proteins sample from plant, plant part and/or food product using mass spectrum.There is provided the purposes and method that are selected using bioinformatics means for quantitative candidate feature peptide.Additionally provide comprising chromatogram and mass spectrographic system, for using selected feature peptide.

Description

For the quantitative method and system with detection of selectivity of allergen
Priority request
This application claims the rights and interests of the applying date of following U.S. Provisional Patent Application:It is entitled that August in 2014 is submitted on the 11st “Methods and Systems for Selective Quantitation and Detection of Allergens The sequence number 62/035,744 of Including GLY M 1 ";In entitled " the Methods and of submission on the 11st of August in 2014 Systems for Selective Quantitation and Detection of Allergens Including GLY M 3 " sequence number 62/035,731;In entitled " the Methods and Systems for of submission on the 11st of August in 2014 The U.S. of Selective Quantitation and Detection of Allergens Including GLY M 4 " is special Sharp patent application serial numbers 62/035,768;In entitled " the Methods and Systems for of submission on the 11st of August in 2014 The U.S. of Selective Quantitation and Detection of Allergens Including GLY M 5 " is special Sharp patent application serial numbers 62/035,800;Entitled " the Methods and Systems for of submission on the 11st of August in 2014 Selective Quantitation and Detection of Allergens Including GLY M 6 GI The sequence number 62/035,858 of SUBUNIT ";Entitled " the Methods and Systems for of submission on the 11st of August in 2014 Selective Quantitation and Detection of Allergens Including GLY M 6 G2 The sequence number 62/035,876 of SUBUNIT ";In entitled " the Methods and Systems for of submission on the 11st of August in 2014 Selective Quantitation and Detection of Allergens Including GLY M 6 G3 The sequence number 62/035,920 of SUBUNIT ";Entitled " the Methods and Systems for of submission on the 13rd of August in 2014 Selective Quantitation and Detection of Allergens Including GLY M 6 G4 The sequence number 62/036,926 of SUBUNIT ";And the Serial No. 62/035,944 submitted to for 11st in August in 2014 “Methods and Systems for Selective Quantitation and Detection of Allergens The Precursor of Including GLY M 6 ", the disclosure content of each application is incorporated herein by reference in their entirety.
Background
The method that this area is presently preferably used to analyze gene expression in plants includes technology (such as PCR based on DNA And/or RT-PCR);Use reporter gene;Southern traces;And immunochemistry.These methods have various shortcomings.Planting Detect that known and potential allergen is an important topic of public safety in thing, plant part and/or food.
Although mass spectrum is previously disclosed, existing means are limited, are quantified with sensitive without selection.Still Need for the selection, sensitive quantitative of known in plant, plant part and/or food and/or potential allergen High throughput method.
It is open
The present invention relates to the use of bioinformatics research to identify candidate feature peptide, for using mass spectrography to from plant The complex proteins sample of thing, plant part and/or food carries out the method and system of quantitative multiplex analysis.Given birth to there is provided using Thing Informatics Method selection candidate feature peptide is used for quantitative purposes and method.Additionally provide including chromatogram and mass spectrographic system, For the feature peptide selected by utilization.
In one aspect, there is provided selection candidate feature peptide is used for the quantitative known allergen from the sample based on plant With the method for potential allergen.The method includes:
A () is based on the potential allergen of homological identification with least one known allergenic proteins sequence;
B () carries out the sequence alignment of at least one known allergen and the potential allergen of identification in step (a);
C () is based on the sequence alignment and selects consensus sequence or representative series;
D () is based on coming the consensus sequence of selection or the sequence alignment and computer of representative series in comfortable step (c) and disappears Change the conservative region or domain of data, it is determined that multiple candidate feature peptides;With
E () is based on the measurement (measurements) of the feature peptide, described in the quantitative sample based on plant The amount of at least one known allergen and potential allergen.
In one embodiment, the quantification steps use column chromatography and mass spectrum.In another embodiment, it is quantitative Step includes measuring the multiple candidate feature peptide using high-resolution accurate mass mass spectrum (HRAM MS).In another implementation In scheme, quantification steps include being calculated from mass spectrum the corresponding peak heights or peak area of candidate feature peptide.In another embodiment In, quantification steps include being compared data and the data of low fragmentation mode from mass spectrographic fragmentation mode high.
In one embodiment, at least one known allergen includes at least one allergic effect being selected from the group It is former:Gly m 1, Gly m 3, Gly m 4, Gly m 5 (beta-conglycinin), (glycinin) Gly of Gly m 6 m 6 (the soybean ball eggs of 6 (glycinin) G3, Gly m of (glycinin) G2, Gly m, 6 (glycinin) G4, Gly m 6 Precursor in vain), Kunitz trypsin inhibitors 1, Kunitz trypsin inhibitors 3, Gly m Bd 28 K, Gly m Bd 30 K, Gly m 8 (2S albumin), agglutinin and lipoxygenase.In another embodiment, at least one known allergen Including Gly m 1, Gly m 3, Gly m 4, Gly m 5 (beta-conglycinin), Gly m 6 (glycinin) Gl, Gly (the soybean balls of 66 (glycinin) G4 or Gly m of (glycinin) G3, Gly m of m 6 (glycinin) G2, Gly m 6 Albumen) precursor.
In another embodiment, the consensus sequence or representative series of step (c) are included for Gly m 1 SEQ ID NO:12nd, 28,29,30,31,32,33,34 or 35.In another embodiment, the consensus sequence of step (c) or Representative series include SEQ ID NO for Gly m1:12nd, 28 or 29.In another embodiment, step (c) Consensus sequence or representative series include SEQ ID NO for Gly m 3:13rd, 38,39 or 40.In another embodiment party In case, the consensus sequence or representative series of step (c) include SEQ ID NO for Gly m 3:13 or 38.Another In individual embodiment, the consensus sequence or representative series of step (c) include SEQ ID NO for Gly m 4:14、42、 43rd, 44,45,46,47,48,49,50 or 51.In another embodiment, the consensus sequence or representative series of step (c) SEQ ID NO are included for Gly m 4:14 or 42.In another embodiment, the consensus sequence of step (c) or generation Table sequence includes SEQ ID NO for Gly m 5:15、61、62、63、64、65、66、67、68、69、70、71、72、 73 or 74.In another embodiment, the sequence or representative series of consensus sequence step (c) are wrapped for Gly m 5 The NO of ID containing SEQ:15 or 61.In another embodiment, the consensus sequence or representative series of step (c) are for Gly m SEQ ID NO are included for 6 G1:16 or 95.In another embodiment, the consensus sequence or representative series of step (c) SEQ ID NO are included for the G2 of Gly m 6:17 or 107.In another embodiment, the consensus sequence of step (c) Or representative series include SEQ ID NO for the G3 of Gly m 6:18.In another embodiment, step (c) is total to There are sequence or representative series for the G4 of Gly m 6 comprising SEQ ID NO:19th, 130,131,132,133 or 134. In another embodiment, the consensus sequence or representative series of step (c) include SEQ ID for the G4 of Gly m 6 NO:19 or 130.In another embodiment, the consensus sequence or representative series of step (c) are for Gly m6 precursors Comprising SEQ ID NO:20.
In one embodiment, for Gly m 1, potential allergen is comprising selected from SEQ ID NO:12 and 30-35 At least one sequence.In another embodiment, for Gly m 3, potential allergen is comprising selected from SEQ ID NO:13 With at least one sequence of 39-40.In another embodiment, for Gly m4, potential allergen is comprising selected from SEQ ID NO:At least one sequence of 14 and 43-51.In another embodiment, for Gly m5, potential allergen is included Selected from SEQ ID NO:At least one sequence of 15 and 62-74.In another embodiment, it is potential for the G1 of Gly m 6 Allergen comprising be selected from SEQ ID NO:16 and 95 at least one sequence.In another embodiment, for Gly m 6 G2, potential allergen is comprising selected from SEQ ID NO:17 and 107 at least one sequence.In another embodiment, it is right In the G4 of Gly m 6, potential allergen is comprising selected from SEQ ID NO:At least one sequence of 19 and 131-134.
In another embodiment, for Gly m 1, candidate feature peptide is comprising selected from SEQ ID NO:1st, 36 and 37 At least one sequence.In another embodiment, for Gly m 1, candidate feature peptide is comprising selected from SEQ ID NO:36 Hes 37 at least one sequence.In another embodiment, for Gly m 3, candidate feature peptide is comprising selected from SEQ ID NO:2 At least one sequence with 41.In another embodiment, for Gly m 3, candidate feature peptide includes SEQ ID NO:41. In another embodiment, for Gly m 4, candidate feature peptide is comprising selected from SEQ ID NO:At least one sequence of 52-57 Row.In another embodiment, for Gly m 4, candidate feature peptide includes SEQ ID NO:52-57.In another implementation In scheme, for Gly m5, candidate feature peptide is comprising selected from SEQ ID NO:At least one sequence of 3 and 75-94.At another In embodiment, for Gly m5, candidate feature peptide includes SEQ ID NO:75-94.In another embodiment, for The G1 of Gly m 6, candidate feature peptide is comprising selected from SEQ ID NO:At least one sequence of 96-106.In another embodiment In, for Gly m 6G1, candidate feature peptide includes SEQ ID NO:96-106.In another embodiment, for Gly m 6 G2, candidate feature peptide is comprising selected from SEQ ID NO:At least one sequence of 4 and 108-120.In another embodiment, For the G2 of Gly m 6, candidate feature peptide includes SEQ ID NO:108-120.In another embodiment, for Gly m 6 G3, candidate feature peptide is comprising selected from SEQ ID NO:At least one sequence of 5 and 121-129.In another embodiment, it is right In the G3 of Gly m 6, candidate feature peptide includes SEQ ID NO:121-129.In another embodiment, for Gly m 6 G4, candidate feature peptide is comprising selected from SEQ ID NO:At least one sequence of 135-156 and 58.In another embodiment, For the G4 of Gly m 6, candidate feature peptide includes SEQ ID NO:135-156 and 58.In another embodiment, for Gly M6 precursors, candidate feature peptide is comprising selected from SEQ ID NO:6th, 59 and 60 at least one sequence.In another embodiment, For Gly m6 precursors, candidate feature peptide includes SEQ ID NO:59 and 60.In another embodiment, the sample based on plant Part of the product comprising soya seeds or soya seeds.
On the other hand, there is provided there is known amino acid sequence for quantitative one or more in the sample based on plant The system of the target protein of row.The system includes:
A () is used to be extracted from the sample based on plant the high flux means of protein;
B () is used for the processing module of the protein extracted with least one protease digestion;
C () is used for the separation module of isolated peptides in a single step;
D () is used to be the selecting module of at least one known allergen and the multiple feature peptides of potential allergen selection; With
E () is used to measure the mass spectrum of the multiple feature peptide.
In one embodiment, separation module includes column chromatography.In another embodiment, column chromatography includes liquid Phase column chromatography.In another embodiment, mass spectrum includes high-resolution accurate mass mass spectrum (HRAM MS).In another reality In applying scheme, selecting module using provided herein is method.
In one embodiment, one or more purpose with known amino acid sequence in the sample based on plant Protein includes potential allergen.In another embodiment, for Gly m1, potential allergen is comprising selected from SEQ ID NO:At least one sequence of 12 and 30-35.In another embodiment, for Gly m 3, potential allergen is included Selected from SEQ ID NO:At least one of 13 and 39-40 sequence.In another embodiment, for Gly m 4, potentially Allergen is comprising selected from SEQ ID NO:At least one sequence of 14 and 43-51.In another embodiment, for Gly M5, potential allergen is comprising selected from SEQ ID NO:At least one sequence of 15 and 62-74.In another embodiment, For the G1 of Gly m 6, potential allergen is comprising selected from SEQ ID NO:16 and 95 at least one sequence.In another reality Apply in scheme, for the G2 of Gly m 6, potential allergen is comprising selected from SEQ ID NO:17 and 107 at least one sequence. In another embodiment, for the G4 of Gly m 6, potential allergen is comprising selected from SEQ ID NO:19 and 131-134's At least one sequence.
In another embodiment, for Gly m 1, feature peptide is comprising selected from SEQ ID NO:1st, 36 and 37 at least One sequence.In another embodiment, for Gly m 1, feature peptide includes SEQ ID NO:36 and 37.In another reality Apply in scheme, for Gly m 3, feature peptide is comprising selected from SEQ ID NO:2 and 41 at least one sequence.In another implementation In scheme, for Gly m 3, the SEQ ID NO that feature peptide is included:41.In another embodiment, it is special for Gly m 4 Peptide is levied comprising selected from SEQ ID NO:At least one sequence of 52-57.In another embodiment, for Gly m 4, feature Peptide includes SEQ ID NO:52-57.In another embodiment, for Gly m5, feature peptide is comprising selected from SEQ ID NO: At least one sequence of 75-94.In another embodiment, for Gly m5, feature peptide includes SEQ ID NO:75-94. In another embodiment, for the G1 of Gly m 6, feature peptide is comprising selected from SEQ ID NO:At least one sequence of 96-106 Row.In another embodiment, for the G1 of Gly m 6, feature peptide includes SEQ ID NO:96-106.In another implementation In scheme, for the G2 of Gly m 6, feature peptide is comprising selected from SEQ ID NO:At least one sequence of 4 and 108-120.Another In individual embodiment, for the G2 of Gly m 6, feature peptide includes SEQ ID NO:108-120.In another embodiment, it is right In the G3 of Gly m 6, feature peptide is comprising selected from SEQ ID NO:At least one sequence of 5 and 121-129.In another embodiment party In case, for the G3 of Gly m 6, feature peptide includes SEQ ID NO:121-129.In another embodiment, for Gly m 6 G4, feature peptide is comprising selected from SEQ ID NO:At least one sequence of 135-156 and 58.In another embodiment, it is right In the G4 of Gly m 6, feature peptide includes SEQ ID NO:135-156 and 58.In another embodiment, before for Gly m6 Body, feature peptide is comprising selected from SEQ ID NO:6th, 59 and 60 at least one sequence.In another embodiment, for Gly M6 precursors, feature peptide includes SEQ ID NO:59 and 60.In another embodiment, the sample based on plant includes Soybean Species The part of son or soya seeds.
On the other hand, there is provided quantitative at least one change with known amino acid sequence in the sample based on plant Answer the high throughput method of former and homologous potential allergen.The method include using provided herein is system.
Brief description of the drawings
Fig. 1 shows the delegate analysis workflow of method disclosed herein and system.
Fig. 2A -2C show the feature peptide for selecting:SEQ ID NO:1 SYPSNATCPR;SEQ ID NO:36 ALGILNLNR;With SEQ ID NO:The representative SRM LC-MS/MS of 37 NLQL1LNSCGR;Tryptose from Gly m 1 The soybean sample chromatogram of enzymic digestion.
Fig. 2 D show representational SRM LC-MS/MS reference colours spectrogram -500ng/mL synthetic peptide SEQ ID NO:1 SYPSNATCPR natural abundances peptide and heavy label peptide are changed.
Sequence alignment between the potential homologue of Fig. 2 E display Gly m1 and Gly m1.
Fig. 3 A show the selected feature peptide SEQ ID of the soybean sample chromatogram of the Trypsin Induced from Gly m 3 NO:The representative SRM LC-MS/MS of 2 YMVIQGEPGAVIR.
Fig. 3 B show representational SRM LC-MS/MS reference colours spectrogram -500ng/mL synthetic peptide SEQ ID NO:2 YMVIQGEPGAVIR natural abundances peptide and heavy label peptide are changed.
Sequence alignment between Fig. 3 C display Gly m 3 and the potential homologue of Gly m 3.
Fig. 4 A-4F show the representative SRM LC-MS/MS for following selected feature peptides:SEQ ID NO:52 MVVFTFEDEINSPVAPATLYK;SEQ ID NO:53 ALDSFK;SEQ ID NO:54 SVENVEGNGGPGTIK;SEQ ID NO:55 ITFLEDGETK;SEQ ID NO:56 FVLHK;With SEQ ID NO:57 AIEAYLLAHPDYN;From Gly m 4 Trypsin Induced soybean sample chromatogram.
Sequence alignment between the potential homologue of Fig. 4 G display Gly m4 and Gly m4.
Fig. 5 A-5U show the representative SRM LC-MS/MS of following selected feature peptides:SEQ ID NO:3 NILEASYDTK;SEQ ID NO:75 CNLLK;SEQ ID NO:76 EEDEDEQPRPIPFPRPQPR;SEQ ID NO:77 EEQEWPR;SEQ ID NO:78 QFPFPRPPHQK;SEQ ID NO:79 ESEESEDSELR;SEQ ID NO:80 NPFLFGSNR;SEQ ID NO:81 FETLFK;SEQ ID NO:82 SPQLQNLR;SEQ ID NO:83 LQSGDALR;SEQ ID NO:84 VPSGTTYYVVNPDNNENLR;SEQ ID NO:85 FESFFLSSTEAQQSYLQGFSR;SEQ ID NO:86 FEEINK;SEQ ID NO:87 VLFSR;SEQ ID NO:88 TISSEDKPFNLR;SEQ ID NO:89 DP1YSNK;SEQ ID NO:90 FFEITPEK;SEQ ID NO:91 AIVILVINEGDANIELVGLK;SEQ ID NO:92 EQQQEQQQEEQPLEVR;SEQ ID NO:93 NFLAGSQDNVISQ1PSQVQELAFPGSAQAVEK;With SEQ ID NO: 94ESYFVDAQPK;The soybean sample chromatogram of the Trypsin Induced from Gly m5.
Fig. 5 V show representational SRM LC-MS/MS reference colours spectrogram -500ng/mL synthetic peptide SEQ ID NO:3 The peptide conversion of NILEASYDTK natural abundances peptide and heavy label.
Sequence alignment between Fig. 5 W display Gly m 5 and the potential homologue of Gly m 5.
Fig. 6 A-6K show the representative SRM LC-MS/MS of the feature peptide of lower column selection:SEQ ID NO:96 LVFSLCFLLFSGCCFAFSSR;SEQ ID NO:97 EQPQQNECQIQK;SEQ ID NO:98 RPSYTNGPQEIYIQQGK;SEQ ID NO:99 HQQENENEGGSILSGFTLEFLEHAFSVDK;SEQ ID NO:100 HCQRPR;SEQ ID NO:101 HNIGQTSSPDIYNPQAGSVTTATSLDFPALSWLR;SEQ ID NO:102 ALIQVVNCNGER;SEQ ID NO:The VFDGELQEGR of expression vector 103;SEQ ID NO:104 TNDTPMIGTLAGANSLLNALPEEVIQHTFNLK;SEQ ID NO:105 NNNPFK;With SEQ ID NO:106 FLVPPQESQK;The soybean sample chromatogram of the Trypsin Induced from Gly m 6G1.
Sequence alignment between the potential homologue of the G1 of 6 G1 and Gly m of Fig. 6 L display Gly m 6.
Fig. 7 A-7N show the representative SRM LC-MS/MS of following selected feature peptide:SEQ ID NO:4 VTAPAMR;SEQ ID NO:108 LVLSLCFLLFSGCFALR;SEQ ID NO:109 EQAQQNECQIQK;SEQ ID NO: 110 RPSYTNGPQEIYIQQGNGIFGMIFPGCPSTYQEPQESQQR;SEQ ID NO:111 SQRPQDR;SEQ ID NO: 112 QQEEENEGSNILSGFAPEFLK;SEQ ID NO:113 EAFGVNMQIVR;SEQ ID NO:114 KPQQEEDDDDEEEQPQCVETDK;SEQ ID NO:115 LSAQYGSLR;SEQ ID NO:116 NAMFVPHYTLNANSIIYALNGR;SEQ ID NO:117 ALVQVVNCNGER;SEQ ID NO:118 VFDGELQEGGVLIVPQNFAVAAK;SEQ ID NO:119 TNDRPSIGNLAGANSLLNALPEE-VIQHTFNLK;And SEQ ID NO:120 NNNPFSFLVPPQESQR;The chromatogram of the soybean sample of the Trypsin Induced from the G2 of Gly m 6.
Fig. 7 O show representational SRM LC-MS/MS reference colours spectrogram -500ng/mL synthetic peptide SEQ ID NO:4 VTAPAMR natural abundances peptide and heavy label peptide are changed.
Sequence alignment between the potential homologue of the G2 of 6 G2 and Gly m of Fig. 7 P display Gly m 6.
Fig. 8 A-8J show the representative SRM LC-MS/MS of following selected feature peptides:SEQ ID NO:5 NNNPFSFLVPPK:SEQ ID NO:121 LVLSLCFLLFSGCCFAFSFR;SEQ ID NO:122 EQPQQNECQIQR; SEQ ID NO:123 QQEEENEGGSILSGFAPEFLEHAFVVDR;SEQ ID NO:124 LQGENEEEEK;SEQ ID NO:125 GGLSVISPPTEEQQQRPEEEEKPDCDEK;SEQ ID NO:126 HCQSQSR;SEQ ID NO:127 LSAQFGSLR;SEQ ID NO:128 VFDGELQEGQVLIVPQNFAVAAR;With SEQ ID NO:129 TNDRPSIGNLAGANSLLNALPEEVIQQTFNLR;The soybean sample chromatogram of the Trypsin Induced from the G3 of Gly m 6 Figure.
Fig. 8 K show representational SRM LC-MS/MS reference colours spectrogram -500ng/mL synthetic peptide SEQ ID NO:5 NNNPFSFLVPPK natural abundances peptide and heavy label peptide are changed.
Fig. 9 A-9X show the representative SRM LC-MS/MS of following selected feature peptides:SEQ ID NO:6 ADFYNPK;SEQ ID NO:135 LNECQLNNLNALEPDHR;SEQ ID NO:136 CAGVTVSK;SEQ ID NO:137 LTLNR;SEQ ID NO:138 MIIIAQGK;SEQ ID NO:139 GALGVAIPGCPETFEEPQEQSNR;SEQ ID NO: 140 QQLQDSHQK;SEQ ID NO:141 VFYLAGNPDIEYPETMQQQQQQK;SEQ ID NO:142 QGQHQQEEEEEGGSVLSGFSK;SEQ ID NO:143 HFLAQSFNTNEDIAEK;SEQ ID NO: 144QIVTVEGGLSVISPK;SEQ ID NO:145 WQEQQDEDEDEDEDDEDEQIPSHPPR;SEQ ID NO:146 RPSHGK;SEQ ID NO:147 EQDEDEDEDEDKPRPSRPSQGK;SEQ ID NO:148 QEEPR;SEQ ID NO: 149NGVEENICTLK;SEQ ID NO:150 LHENIARPSR;SEQ ID NO:151 ISTLNSLTLPALR;SEQ ID NO:152 QFQLSAQYVVLYK;SEQ ID NO:153 NGIYSPHWNLNANSVIYVTR;SEQ ID NO:154 DVFR; SEQ ID NO:155 AIPSEVLAHSYNLR;SEQ ID NO:156 QSQVSELK;With SEQ ID NO:58 YEGNWGPLVNPESQQGSPR, the soybean sample chromatogram of the Trypsin Induced from the G4 of Gly m 6.
Sequence alignment between the potential homologue of the G4 of 6 G4 and Gly m of Fig. 9 Y display Gly m 6.
Figure 10 A, 10B and 10C show the representative SRM LC-MS/MS of following selected feature peptide:SEQ ID NO:6 ADFYNPK, SEQ ID NO:59 GALQCKPGCPETFEEPQEQSNR and SEQ ID NO:60 LQSPDDER;From Gly m6 The soybean sample chromatogram of the Trypsin Induced of precursor.
Specific embodiment
Enabling can optionally detect that target protein and the sensitive multiple assay of measurement target protein level have Important meaning.At present, the technology of related protein expression detection depends critically upon traditional immunochemical technique, how should One challenge is become to the data volume that each sample requirement in the technology is produced.
Soybean is the trade product for being worth number in terms of 1,000,000,000 dollars, and this is because it balances protein, starch, oil composition --- By weight 2:2:1.Many seeds, including soybean, some contained protein are allergen and ANFs.Therefore someone Worry, in the soybean varieties of genetic modification, compared with the kind developed by traditional breeding method, allergen level is potentially possible to be changed Become.Allergen level so far in crop is entirely almost by immunoassay, such as enzyme linked immunosorbent assay (ELISA) Or IgE- Western blottings etc. are measured (ELISA);However, the problem of these methods is limited sensitivity and specificity, and become The property changed is high.
Recently, the albumen that people are expressed method of the exploitation based on LC-MS/MS with the quantitative several plant in single analysis Matter generates interest.The analysis carried out using these " feature peptides " is included by several high degree of specificity of quantitative objective protein Digestion fragment tracks protein expression level.This can generally use with associated with Selective reaction monitoring (SRM) tandem mass spectrum Liquid chromatography is completed.There is provided herein improved multiple LC-MS/MS method and systems, it is caused in transgenosis and non-turn Several allergen proteins of simultaneous quantitative are possibly realized in transgenic soybean.Provided herein is method and system just include the degree of accuracy, essence Exactness, linear, test limit and quantitative limit etc. are in the interior analysis figure of merit (analytical figures of merit), and bag Sample throughput, transferability and ease for use is included to be verified in other interior Considerations.Multiplex pattern can be used (multiplexing format) quantifies allergen, and can for example one day (twenty four hours) window (from field to The numerical value of measurement) in harvest sample, treatment and analysis/quantitative from field.Additionally, the sample preparation of the method and system for being provided Scale can amplify to realize high flux completely, therefore, it is possible to analyze hundreds of samples in single batch.
Representational soybean allergen includes such as Gly m 1, Gly m 3, Gly m 4, Gly m 5 (β-companion's soybean ball Albumen), (glycinin) G2, the Gly m 6 of Gly m 6 (glycinin) G1, Gly m 6) G3, (the soybean ball eggs of Gly m 6 G4 in vain), Gly m 6 (glycinin) precursor, Gly m 6 (glycinin) G4 precursors, Kunitz trypsin inhibitors 1, Kunitz trypsin inhibitor 3, Gly m Bd 28 K, Gly m Bd 30 K, Gly m 8 (2S albumin), agglutinin And lipoxygenase.
Representational wheat allergens include such as factor Ⅰ (Tri a12), (Tri of wheat lipid transfer protein 1 A14), agglutinin isolectin 1 (Tri a18), ω -5 gliadins-seed storage protein (Tri a19), the molten egg of wheat alcohol (Tri a20 in vain;NCBI accession number M10092, M11073, M11074, M11075, M11076, K03074 and K03075), sulphur oxygen Also albumen (Tri a25), high molecular weight glutenin (Tri a26), low molecular weight glutenin (Tri a36), and α-purine Thionine (purothionin) (Tri a37).
Representational corn allergen includes such as corn lipid transfer proteins (LTP) (Zea m14) and thioredoxin (Zea m25)。
Representational corn allergen includes, for example, paddy rice factor Ⅰ A (Ory s12).
In some embodiments, the method and system for being provided uses the liquid chromatogram (LC- for being coupled to tandem mass spectrum MS/MS) the protein expression level of the different allergens of 16 kinds from soybean of detection.In some embodiments, the side Method and system can analyze single allergen, or analyze every kind of allergen with the combination of other oroteins to carry out resurvey more It is fixed, for the qualitative and quantitative analysis in plant substrates.
In some embodiments, the Mass Spectrometer Method for quantitative study can be by enterprising in triple quadrupole mass spectrometer Row Selective reaction monitoring is realized.Using such instrument and equipment, to the initial of the object ion (peptide) of formation in source Quality is selected, and then dissociate the precursor ion in the collision area of MS, followed by the quality of specific product (son) ion is selected And counting.In some embodiments, the Mass Spectrometer Method for quantitative study can have been come using Selective reaction monitoring (SRM) Into.Using certain types of instrument and equipment, the initial mass selection of the object ion formed in source, then at mass spectrograph (MS) Collision area in dissociate precursor (protein) ion, followed by the quality selection of specific product (peptide) ion and count. In some embodiments, the counting of unit interval can provide the peak area of integrable, can therefrom determine analyte amount or Concentration.In some embodiments, what is carried out on the mass spectrograph with HRAM abilities quantitative uses high-resolution accurate mass (HRAM) monitoring can include but is not limited to mixing quadrupole-flight time, quadrupole-track trap, ion trap-track trap or quadrupole- Ion trap-track trap (three grid) mass spectrograph.Using certain types of instrument and equipment, peptide does not suffer from fragmentation condition, but as complete Whole peptide is measured using full scan or targeting scan pattern (such as selected ion monitoring pattern or SIM).Can be by being each Specific analyte produces extraction chromatography of ions figure to determine the peak area of integrable, and can calculate the amount of analyte or dense Degree.The high-resolution and accurate mass property of data cause high degree of specificity and the spirit of target analytes (protein and/or peptide) Quick ion signal is possibly realized.
Unless otherwise indicated, the following term used in the application, including in specification and claims, with following The definition for being given.It has to be noticed that as used in specification and appended, singulative " ", " one " and " being somebody's turn to do " includes plural referents, unless the context clearly indicates otherwise.
As used herein, term " biology limitation " refer to limit genetic modification plant or its inhereditary material move to it is specified Region.The term includes physics, physicochemical, biology limitation, and other forms prevented genetic modification The limitation of survival, diffusion or breeding of the plant in natural environment or Artificial Growth condition.
As used herein, term " complex proteins sample " is used to distinguish the protein example of sample and purifying.Complicated egg White sample contains multiple proteins, and can in addition contain other pollutants.
As used herein, generic term " mass spectrum " or " MS " refer to any suitable mass spectrometry method, device or configuration, bag Include such as electron spray ionisation (ESI), substance assistant laser desorpted/ionization (MALDI) MS, MALDI- flight time (TOF) MS, big Air pressure (AP) MALDI MS, vacuum MALDI MS or its combination.Mass spectrometric apparatus are by measuring molecule by one group of magnetic field and electric field Flight path measure the molecular weight (as the function of the mass-to-charge ratio of molecule) of molecule.Mass-to-charge ratio is in the electronic of charged particle Widely used physical quantity in mechanics.The mass-to-charge ratio of particular peptide can a priori be calculated by those skilled in the art.With difference Two particles of mass-to-charge ratio will not be moved in identical path in a vacuum when by identical electric field and magnetic field.
Mass spectrometer is made up of three modules:Ion gun, sample molecule is separated into ion by it;Mass analyzer, it leads to Applying electromagnetic field is crossed to classify ion according to quality;And detector, the value of the amount of its measurement indicant, and therefore provide Data for calculating the abundance that every kind of ion is present.The technology can apply to qualitative and quantitative.These include that identification is unknown Compound, determines the isotopics of element in molecule, and its structure, and quantitative sample are determined by observing compound fragmentation The amount of middle compound.
The detailed overview of mass spectrometry method and device can find in below with reference to document, and these are incorporated by reference into this Text:Can and Annan (1997) Overview of peptide and protein analysis by mass Spectrometry. Current Protocols in Molecular Biology, Ausubel et al. volume, New are embodied in York:Wiley,p.10.21.1-10.21.27;Paterson and Aebersold (1995) Electrophoresis 16: 1791-1814;Patterson(1998)Protein identification and characterization by mass Spectrometry. Current Protocols in Molecular Biology, Ausubel et al. volume, New are embodied in York:Wiley,p.10.22.1-10.22.24;With Domon and Aebersold (2006) Science 312 (5771):212- 17。
As the term is employed herein, when there is two or more target proteins and/or peptide in same sample, albumen Matter and/or peptide are " multiple ".
As it is used herein, " plant trait " can refer to any single features or quantifiable measurement of plant.
As used herein, the short polymerization for being linked in sequence and being formed that phrase " peptide " or " peptide " can refer to a-amino acid to determine Thing.Peptide can also be produced by with protease digestion polypeptide such as protein.
As it is used herein, phrase " protein " can refer to by being arranged in straight chain and by contiguous amino acid residues The organic compound of the Amino acid profile that the peptide bond between carboxyl and amino links together.Amino acid sequence in protein by The sequence definition of gene, the sequence of gene is with genetic code encoding.Generally, genetic code specifies 20 standard amino acids, but In some organisms, genetic code may include selenocysteine, in some archeobacterias, it may include pyrrolysine.It is logical The residue being frequently observed in protein is acted on by posttranslational modification and is modified by sulphation, and posttranslational modification effect can be in the albumen Matter is occurred before cell use, or is occurred as the part of controlling mechanism.Residue of protein can also be according to this area skill Technology familiar to art personnel is modified by design.As used herein, term " protein " is covered comprising naturally occurring The straight chain of amino acid, synthesizing amino acid, the amino acid of modification or any or all combinations of the above.
As it is used herein, term " single injection " refers to the initial step in the operation of MS or LC-MS devices.Work as albumen When quality sample is introduced into device in single injection, the whole sample is introduced in a single step.
As used herein, phrase " feature peptide " refers to mark (small peptide) sequence of specified protein.Any protein can be with Contain average 10 to 100 kinds of features peptide.Usual feature peptide has at least one in following standard:Examined easily by mass spectrography Survey;Can be predicted and stably from liquid chromatogram (LC) post wash-out;It is enriched with by RPLC (RP-HPLC);Well Ionization;Good fragmentation;Or the combination of above-mentioned person.Easily by the peptide of mass spectrum standard measure generally with least in following standard Kind:Be readily synthesized, can by it is highly purified (>97%)≤20% acetonitrile, is dissolved in, low non-specific binding is anti-oxidant, anti-conjunction Into rear modification, hydrophobicity or hydrophobicity index >=10 and≤40.Hydrophobicity index can be according to Krokhin, Molecular and Cellular Proteomics 3 (2004) 908 are calculated, and it is incorporated herein by reference.Known hydrophobicity index less than 10 or Peptide more than 40 may repeatably be separated or eluted by RP-HPLC posts.
As used herein, term " stacking " refers to depositing for multiple heterologous polynucleotides for being incorporated into Plant Genome .
Tandem mass spectrum:In tandem mass spectrum, the parent ion produced from target molecule can be filtered in a mass spectrometer, and Parent ion is then fractured to produce one or more daughter ions, daughter ion to be then analyzed (inspection in second mass spectrum program Survey and/or quantitative)).In some embodiments, the use of tandem mass spectrum is excluded.In these embodiments, provided Tandem mass spectrum is not used in method and system.Therefore, parent ion is neither produced in these embodiments nor produces daughter ion.
As used herein, term " genetically modified plants " can refer to the plant comprising heterologous polynucleotide in its genome Thing.Generally, heterologous polynucleotide stable integration is in genome so that polynucleotides are delivered to subsequent generation.Heterologous multinuclear Thuja acid can be incorporated into genome either individually or as a part for recombinant expression cassettes." transgenosis " is used to include herein Any such cell, cell line, callus, tissue, plant part or plant, its genotype is by the presence of heterologous nucleic acids Change, including initially so change those genetically modified plants and from initial genetically modified plants pass through sexual hybridization or nothing Sexual reproduction and the genetically modified plants that generate.
Any plant that useful plant part is provided can be processed in an embodiment of the present invention.Example includes providing The plant of flower, water fruits and vegetables and cereal.
As used herein, phrase " plant " includes dicotyledon and monocotyledon.The example of dicotyledon includes Tobacco, arabidopsis, soybean, tomato, pawpaw, Canola, sunflower, cotton, clover, potato, grape, pigeonpea, pea, rue Tongue, chick-pea, beet, rape, watermelon, muskmelon, pepper, peanut, pumpkin, radish, spinach, pumpkin, broccoli, cabbage, Hu Luo Fore-telling, cauliflower, celery, Chinese cabbage, cucumber, eggplant and lettuce.Monocotyledonous example include corn, paddy rice, wheat, sugarcane, Barley, rye, sorghum, orchid, bamboo, banana, cattail, lily, oat, onion, millet and triticale.The example of fruit includes Banana, pineapple, orange, grape, grape fruit, watermelon, muskmelon, apple, peach, pears, Kiwi berry, mango, nectarine, guava, persimmon, Avocado, lemon, fig, and berry.Colored example include babysbreath, carnation, dahlia, narcissus, fish pelargonium, African Chrysanthemum, Lily, orchid, tree peony, cicely (Queen Anne ' s lace), rose, toad's-mouth or other flower arrangements or decoration flower, potted flower And bouquet.
The specificity that identification single protein is allowed from complex sample in mass spectrometry method is unique, because identification Target protein only needs the sequence of target protein.Compared with the multiplex of other forms, the unique distinction of mass spectrography is energy Enough using the total length of the primary amino acid sequences of protein come the unique mark type of the primary amino acid sequences of targeting protein Part, so as to almost eliminate non-specific detection.In some embodiments of the present invention, using uniquely identifying target protein The target protein that the proteolytic fragments of matter or a histone proteolytie fragrnent come in detection of complex protein example.
In some embodiments, disclosed method can be by single mass spectral analysis come quantitative complex proteins sample In multiple proteins or determine its ratio, rather than repeatedly measuring every kind of target protein respectively, then single result is converged Weave into a sample result.
In some embodiments, the present disclosure also provides the side that can be used for development and utilization transgene plant technology Method.Specifically, disclosed method can be used for maintaining the genotype experience successive generation of genetically modified plants.Additionally, being disclosed herein Some embodiments of method can be used to provide to the high throughput analysis of non-transgenic plant as described below:The non-transgenic Plant is in the risk by the transgenosis pollution from neighbouring plant (such as by cross-pollination).By these embodiment party Case, can promote and/or complete the biological limitation of transgenosis.In other embodiments, method disclosed herein can be used for High flux mode screens the result of Plant Transformation program, and the transformant of desired expression characteristic is shown to identify
Mass-to-charge ratio can be determined using quadrupole analyzer.For example, in " quadrupole " or " quadrupole ion trap " instrument, vibration Ion in radiofrequency field is subject to and applies DC potentials between the electrodes, the amplitude of RF signals and the proportional power of m/z.Can To select voltage and amplitude so that the ion only with specific m/z can advance the total length of quadrupole rod, and every other ion It is deflected.Therefore, quadrupole instrument can serve as " mass filter " and " mass detector " of the ion in injection instrument.
Collision induced dissociation (" CID ") is generally used for producing the daughter ion for further detection.In CID, parent ion Energy is obtained by being collided with inert gas (such as argon gas), and it is then broken by being referred to as the process of " unimolecule decomposition " Split.Enough energy must be stored in parent ion so that some keys in ion are broken because energy increases.
Mass spectrograph generally provides the user ion scan;Each m/z i.e. in given range (such as 10 to 1200amu) Relative abundance.The result of analyte determination, i.e. mass spectrum, can be by dividing in many methods known in the art and primary sample Analyse the amount association of thing.For example, in view of sampling and analysing parameter is carefully controlled, can by the relative abundance of given ion with The table that the relative abundance is converted into the absolute magnitude of initial molecule is compared.Or, molecule mark can be run together with sample Accurate (for example, internal standard and external standard), and standard curve is built based on the ion produced from those standards.Using this standard curve, The relative abundance of given ion can be converted into the absolute magnitude of initial molecule.It is many other for by the presence of ion or amount with it is former The presence of beginning molecule or the associated method of amount are known to a person of ordinary skill in the art.
The selection of ionization method can be based on analyte to be measured, sample type, detector type, the positive to negative mould Selection of formula etc. determines.Ion can be produced using various methods, including but not limited to:Electron ionization, chemi-ionization, quickly Atom bombardment, field desorption and substance assistant laser desorpted ionized (MALDI), Protein-based tumor biomarker (SELDI), desorption Electro-spray ionization (DESI), photon ionization, electro-spray ionization and inductively coupled plasma.Electro-spray ionization refers to this The method of sample, wherein making solution by one section of short capillary, the end of pipe applies positive or negative current potential high.Reach pipe end Solution is evaporated the jet or spraying of (atomization) into very small solution droplets in solvent vapour.The spray of this drop crosses steaming Hair room, vaporization chamber is heated to prevent condensation and evaporation solvent.As drop diminishes, ammeter surface charge density increases, until this The time of sample arrives:Natural repulsion between identical charges causes ion and neutral molecule to be released.
The effluent of LC can directly and automatically (that is, " online ") is injected into electrospray device.In some embodiment party In case, the protein included in LC effluents is first by electro-spray ionization into parent ion.
A variety of mass analyzers can be used for liquid chromatograph mass spectrography (LC-MS).Exemplary quality analysis device bag Include but be not limited to single quadrupole rod, triple quadrupole bar, ion trap, TOF (flight time) and quadrupole rod flight time (Q-TOF).
Four-electrode quality analyzer can be made up of 4 poles being set parallel to each other.In quadrupole mass spectrometer (QMS), Quadrupole rod is the responsible part based on mass-to-charge ratio (m/z) filtered sample ion in instrument.It is being applied on bar based on ion Oscillating electric field in track stability, ion is separated in quadrupole.
Ion trap is the combination in electric field or magnetic field, can capture the ion in certain region of vacuum system or pipe.In operation During the quantum state of ion, ion trap can be used in mass spectrum.
Time-of-flight mass spectrometry (TOFMS) (TOFMS) is a kind of mass spectrometry method, wherein determining the matter lotus of ion by time measurement Than.The electric field acceleration that ion passes through known strength.The acceleration cause ion have and any other ion with identical charges Identical kinetic energy.The speed of ion depends on mass-to-charge ratio.The detector that measurement particle then reaches known distance apart is spent Time.This time will depend on the mass-to-charge ratio (speed that heavier particle reaches is lower) of particle.From this time and The experiment parameter known, can obtain the mass-to-charge ratio of ion.
In some embodiments, the particular instrument for being used by the method and/or system that are provided can include fragmentation high Pattern and low fragmentation mode (or alternatively, non-fragmentation mode).Such different mode can include mixed sweep high-energy and Low energy acquisition methods are producing high-resolution qualitative data.In some embodiments, high-resolution qualitative data can be wrapped Include product data collection (such as the data obtained from product ion (fragment ion) under fragmentation mode high) and preceding volumetric data set (example The data obtained from precursor ion (non-fragmentation of ions) such as under low fragmentation or non-fragmentation mode).
In some embodiments, the method and/or system for being provided use mass spectrograph, and mass spectrograph is including can be used to select The filter of step, can be used for the fragmentation device of fragmentation step, and/or can be used for obtain and/or mass spectrum foundation step in One or more mass analyzers.
Filter and/or mass analyzer can include quadrupole.Selection step and/or obtaining step and/or mass spectrum wound Build step and may involve the use of resolution quadrupole (resolving quadrupole).Additionally or alternatively, filter may include two Dimension or three-dimensional ion trap or flight time (ToF) mass analyzer.One or more mass analyzers can include or can be with Further include following one or more:TOF and/or ion cyclotron resonance mass analyzer and/or Orbitrap mass analyser and/or two dimension or three-dimensional ion trap.
Filtering by means of the selection based on mass-to-charge ratio (m/z) can be by using the matter that can be based on m/z selection ions Contents analyzer (such as quadrupole rod) is realized;Or transmit m/z scopes wide, the m/z according to ion separates ion, then by from The m/z value selection target ions of son.The example of the latter is the TOF combined with timing ion selector.Institute The method and/or system of offer may include to use chromatographic technique, such as liquid chromatogram (LC), separate and/or separate and be a kind of or many Target protein is planted, is such as separated from two or more in multiple proteins and/or separated.The method can be wrapped further Include the elution time of measurement target protein and/or the elution time of measurement is compared with expected elution time.
Additionally or alternatively, it is possible to use ionic mobility technology separates target protein, and it can use Ion transfer Cell is carried out.Furthermore it is possible to by the order or time of ion mobility drift come selection target protein.The method can be with Including measure proteins of interest matter drift time and/or by the drift time of measurement with expection drift time be compared.
In some embodiments, the method and/or system for being provided are unmarked, wherein quantitatively can be by comparing Target precursors between injection and each sample between or area is realized under the peak intensity or mass spectra peak of product m/z values.At some In embodiment, it is possible to use internal standard standardizes to tackle any of correlation analysis error.It is another unmarked quantitative Method, spectrogram counts (spectral counting), including the fragment obtained to each given peptide with nonredundancy or redundant fashion Ionic spectrum or the number of scanning are sued for peace.Then the related peptide mass spectrum of every kind of protein is added, so as to provide every kind of protein The measurement of number is scanned, it is proportional to the abundance of the protein.Then can be compared between sample/injection.
In some embodiments, ion gun is selected from:(1) electro-spray ionization (" ESI ") ion gun;(2) air press polish Ionization (" APPI ") ion gun;(3) APCI (" APCI ") ion gun;(4) it is substance assistant laser desorpted ionized (" MALDI ") ion gun;(5) laser desorption ionisation (" LDI ") ion gun;(6) atmospheric pressure ionization (" API ") ion gun;(7) silicon On desorption ionization (" DIOS ") ion gun;(8) electron bombardment (" E1 ") ion gun;(9) chemi-ionization (" CI ") ion gun; (10) FI (" F1 ") ion gun;(11) field desorption (" FD ") ion gun;(12) inductively coupled plasma (" ICP ") ion Source;(13) fast atom bombardment (" FAB ") ion gun;(14) liquid SIMS (" LSIMS ") ion gun;(15) desorb Electro-spray ionization (" DESI ") ion gun;(16) isotopic ion of nickel -63 source;(17) atmospheric pressure matrix assisted laser desorption electricity Luxuriant component;(18) thermojet ion gun.
In some embodiments, the method and/or system for being provided include being configured as performing computer program element Device and/or control system, the computer program element includes for making computing device for realizing methods described The computer readable program code means of process.
In some embodiments, the method and/or system for being provided scan work(using alternate low energy and high-energy Can be with liquid chromatogram separating plant extract combination.The information list of target protein, including but not limited to precursor can be provided The m/z of ion, the m/z of product ion, retention time, ion mobility drift time and mobility change rate.Separated in LC Cheng Zhong, and when target ion is eluted in mass spectrograph (and when detect low energy precursor ion or detect high-energy product from When son or activation retention time window), so the mass analyzer and/or system of method can select the narrow m/z scopes (to have Alterable and changeable width), by ion transport to air chamber.Therefore, it can significantly increase signal to noise ratio for target egg White matter is quantified.
In some embodiments, when the chromatogram when target target protein will be eluted in mass spectrometer ion source retains Between, the method and/or the mass analyzer of system for being provided can select narrow m/z scopes according to target precursor example, and (having can Change and changeable width).Then by these selected ion-transfers to can be by fragmentation mode high and low fragmentation mould Replace and repeat the Instrument Level that switching carrys out disassociated ions between formula (or non-fragmentation mode), before sample under the fragmentation mode high Body ion is substantially fragmented into product ion, the sample precursor ion substantially not fragmentation under the low fragmentation mode.Generally Obtain high-resolution, accurate mass spectrum in both modes, and at the end of experiment, by its chromatographic elution time and The fitting tightness degree of other optional physicochemical properties recognizes related precursor and product ion.With target target protein phase The precursor ion of pass or the signal intensity of product ion can be used to determine the amount of protein in plant extracts.
It will be understood by those skilled in the art that there may be some changes on the basis of disclosed in being provided.Therefore, be given Following examples for the purpose of illustrating the invention, and should not be construed as to the present invention or claim scope limitation.
Embodiment
Embodiment 1
The method and system for being provided is used to determine the endogenous soybean allergen protein in soya seeds, including Gly m 1, Gly m 3, Gly m 4, Gly m 5 (beta-conglycinin), Gly m 6, Kunitz trypsin inhibitors 1, Kunitz trypsin inhibitors 3, K the and Gly m 8 (2S albumin) of Gly m Bd 28 K, Gly m Bd 30.By 100 ± The soybean seed representative of 0.5mg grindings twice and is dried with hexane degreasing, is then used and is contained 5M urea, 2M thiocarbamides, 50mM Tris The Extraction buffer of pH 8.0 and 65mM DTT is extracted.By sample ultrasonically treated 30 minutes in a water bath, it is vortexed 1 minute, ultrasound Process other 30 minutes, and 4 DEG C with>3,000rpm is centrifuged 10 minutes.
Collect aqueous supernatant and diluted so that endogenous soybean allergen protein concentration reaches calibration with Extraction buffer Critical field.Will dilute extract at 95 DEG C with additional 1M Tris pH 8.0,0.5M DTT and deionized water are together Denaturation 20 minutes, then refrigerates 10 minutes at 4 DEG C.The extract of denaturation was incubated at 37 DEG C with 0.5mg/mL trypsase Night (~15 hours).Digestion reaction formic acid water (50/50v/v) be quenched and 4 DEG C with>3,000rpm is centrifuged minute.Will digestion A aliquot of extract be transferred in automatic sampler bottle, and analyze liquid chromatogram together with calibration standard items and connect Same positive ionization electrospray (ESI) tandem mass spectrum (LC-MS/MS) is analyzed.The calibration standard items of feature peptide are made as listed in table 1 It is standby.
In this embodiment, the test limit (LOD) and quantitative limit (LOQ) of endogenous soybean allergen are listed in table 2, wherein LOD and LOQ represent protein concentration (ng/mg).
(such as the Analyst Bioanalytical for LC-MS/MS are soft from feature peptide quantitative for the concentration of allergen Part) calculate, and by other method validations including enzyme linked immunosorbent assay (ELISA) (ELISA).Compared using statistical analysis and come from The calculating concentration of the allergen of different samples, as a result shows the good uniformity between sample.
Embodiment 2
The homologous of several Gly m1 is identified in interior public database from including NCBI, Phytozome and UniProt Protein sequence.To sequence (the SEQ ID NO for identifying:12 and 29-35) analyzed using bioinformatics tools, to identify Sequence homology and consensus sequence between available protein sequence are constituted (referring to Fig. 2 E).Specifically, this is directed to use with Vector NTI Align X compare instrument, and the instrument performs CLUSTAL W types and compares.From the analysis, it may be determined that altogether There are sequence and/or representative series.
Once selection determines consensus sequence and/or representative series, by its on computers (in silico) disappear Change, the candidate feature fragments of peptides for being detected by LC-MS and being measured is treated in generation.According to provided herein is unique method, based on available Protein sequence between conservative select feature peptide so that selected feature peptide can be used in common sequence number According to quantitative protein isoforms all or as much as possible in the protein sequence identified in storehouse.Therefore, selected feature The quantitative of peptide can not only measure Gly m 1 itself, can also measure the potential allergen with the very high homologies of Gly m 1.
Soybean seed representative is ground to form into fine powder, with hexane degreasing twice, and buffer solution (such as 5M urine is determined with suitable Element, 2M thiocarbamides, 50mM Tris (pH 8.0), 65mM DTT) extract.Sample is ultrasonically treated extracting albumen in buffer solution Matter.The protein dilution that will be extracted, denaturation, then by adding trypsase protease and incubation 15-20 hours at 37 DEG C Carry out proteolytic digestion.Digestion reaction is acidified with formic acid (pH=1-2), and is analyzed using LC-MS/MS.
Selected feature peptide can be used for Gly m 1 (being combined individually or with other oroteins in multiple assay pattern) Qualitative and quantitative analysis.In this embodiment, three kinds of feature peptides (SEQ ID NO are have selected from all peptide possibilities: 1SYPSNATCPR;SEQ ID NO:36 ALGILNLNR;With SEQ ID NO:37 NLQLILNSCGR), the generation of these feature peptides Table quantitative display is in fig 1 and 2.Fig. 2A -2C.It is SEQ ID NO:1 SYPSNATCPR has synthesized poly saccharide peptide standard product for quantitative With qualitative analysis (referring to Fig. 2 D).Synthetic peptide can be directly as the analysis normative reference of quantification of protein.
Embodiment 3
The several same of Gly m 3 is identified in interior public database from including NCBI, Phytozome and UniProt Source protein matter sequence.Sequence (the SEQ ID NO analyzed and identified out using bioinformatics tools:13,39 and 40) with identify can Sequence homology and consensus sequence between protein sequence are constituted (referring to Fig. 3 C).Specifically, this includes using Vector NTI Align X compare instrument, and the instrument performs CLUSTAL W types and compares.From the analysis, it may be determined that altogether There are sequence and/or representative series.
Once selection determines consensus sequence and/or representative series, it is carried out to be digested on computer and is treated with generation The candidate feature fragments of peptides for being detected by LC-MS and being measured.According to provided herein is unique method, based on available protein sequence Conservative selection feature peptide between row so that selected feature peptide can be used for being identified in common sequence database Protein sequence in quantitative all or protein isoforms as much as possible.Therefore, the quantitative of selected feature peptide not only may be used To measure Gly m 3 itself, and the potential allergen with the very high homologies of Gly m 3 can be measured.
Soybean seed representative is ground to form into fine powder, with hexane degreasing twice, and buffer solution (such as 5M urine is determined with suitable Element, 2M thiocarbamides, 50mM Tris (pH 8.0), 65mM DTT) extract.Sample is ultrasonically treated extracting albumen in buffer solution Matter.The protein dilution that will be extracted, denaturation, then by adding trypsase protease and incubation 15-20 hours at 37 DEG C Carry out proteolytic digestion.Digestion reaction is acidified with formic acid (pH=1-2), and is analyzed using LC-MS/MS.
Selected feature peptide can be used for Gly m 3 (being combined individually or with other oroteins in multiple assay pattern) Qualitative and quantitative analysis.In this embodiment, two feature peptides (SEQ ID NO are have selected from all peptide possibilities:2 YMVIQGEPGAVIR;With SEQ ID NO:41 GPGGVTVK), and SEQ ID NO:The representativeness of 2YMVIQGEPGAVIR is determined Amount is shown in Fig. 3 A.It is SEQ ID NO:2 YMVIQGEPGAVIR have synthesized poly saccharide peptide standard product for qualitatively and quantitatively analysis (ginseng See Fig. 3 B).Synthetic peptide can be directly as the analysis normative reference of quantification of protein.
Embodiment 4
The several homologous of Gly m4 is identified in interior public database from including NCBI, Phytozome and UniProt Protein sequence.Sequence (the SEQ ID NO analyzed and identified out using bioinformatics tools:14 and 43-51) it is available to identify Protein sequence between sequence homology and consensus sequence constitute (referring to Fig. 4 G).Specifically, this is directed to use with Vector NTI Align X compare instrument, and the instrument performs CLUSTAL W types and compares.From the analysis, it may be determined that consensus sequence And/or representative series.
Once selection determines consensus sequence and/or representative series, it is carried out to be digested on computer and is treated with generation The candidate feature fragments of peptides for being detected by LC-MS and being measured.According to provided herein is unique method, based on available protein sequence Conservative selection feature peptide between row so that selected feature peptide can be used for being identified in common sequence database Protein sequence in quantitative all or protein isoforms as much as possible.Therefore, selected feature peptide it is quantitative not only Gly m 4 itself can be measured, but also the potential allergen with the very high homologies of Gly m 4 can be measured.
Soybean seed representative is ground to form into fine powder, with hexane degreasing twice, and buffer solution (such as 5M urine is determined with suitable Element, 2M thiocarbamides, 50mM Tris (pH 8.0), 65mM DTT) extract.Sample is ultrasonically treated extracting albumen in buffer solution Matter.The protein dilution that will be extracted, denaturation, then by adding trypsase protease and incubation 15-20 hours at 37 DEG C Carry out proteolytic digestion.Digestion reaction is acidified with formic acid (pH=1-2), and is analyzed using LC-MS/MS.
Selected feature peptide can be used for Gly m4 (being combined individually or with other oroteins in multiple assay pattern) Qualitative and quantitative analysis.In this embodiment, several feature peptides (SEQ ID NO are selected from all peptide possibilities:52 MGVFTFEDEINSPVAPATLYK;SEQ ID NO:53 ALDSFK;SEQ ID NO:54 SVENVEGNGGPGTIK;SEQ ID NO:55 ITFLEDGETK;SEQ ID NO:56 FVLHK;With SEQ ID NO:57 AIEAYLLAHPDYN), and these are special The representative quantitative display of peptide is levied in Fig. 4 A-4F.Synthetic peptide can be directly as the analysis normative reference of quantification of protein.
Embodiment 5
The several homologous of Gly m5 is identified in interior public database from including NCBI, Phytozome and UniProt Protein sequence.Sequence (the SEQ ID NO analyzed and identified out using bioinformatics tools:15 and 62-74) it is available to identify Protein sequence between sequence homology and consensus sequence constitute (referring to Fig. 5 W).Specifically, this is directed to use with Vector NTI Align X compare instrument, and the instrument performs CLUSTAL W types and compares.From the analysis, it may be determined that consensus sequence And/or representative series.
Once selection determines consensus sequence and/or representative series, it is carried out to be digested on computer and is treated with generation The candidate feature fragments of peptides for being detected by LC-MS and being measured.According to provided herein is unique method, based on available protein sequence Conservative selection feature peptide between row so that selected feature peptide can be used for being identified in common sequence database Protein sequence in quantitative all or protein isoforms as much as possible.Therefore, selected feature peptide it is quantitative not only Gly m 5 itself can be measured, the potential allergen with the very high homologies of Gly m 5 can also be measured.
Soybean seed representative is ground to form into fine powder, with hexane degreasing twice, and buffer solution (such as 5M urine is determined with suitable Element, 2M thiocarbamides, 50mM Tris (pH 8.0), 65mM DTT) extract.Sample is ultrasonically treated extracting albumen in buffer solution Matter.The protein dilution that will be extracted, denaturation, then by adding trypsase protease and incubation 15-20 hours at 37 DEG C Carry out proteolytic digestion.Digestion reaction is acidified with formic acid (pH=1-2), and is analyzed using LC-MS/MS.
Selected feature peptide can be used for Gly m 5 (being combined individually or with other oroteins in multiple assay pattern) Qualitative and quantitative analysis.In this embodiment, several feature peptides (SEQ ID NO are have selected from all peptide possibilities:3 NILEASYDTK;SEQ ID NO:75 CNLLK;SEQ ID NO:76 EEDEDEQPRPIPFPRPQPR;SEQ ID NO:77 EEQEWPR;SEQ ID NO:78 QFPFPRPPHQK;SEQ ID NO:79 ESEESEDSELR;SEQ ID NO:80 NPFLFGSNR;SEQ ID NO:81 FETLFK;SEQ ID NO:82 SPQLQNLR;SEQ ID NO:83 LQSGDALR;SEQ ID NO:84 VPSGTTYYVVNPDNNENLR;SEQ ID NO:85 FESFFLSSTEAQQSYLQGFSR;SEQ ID NO:86 FEEINK;SEQ ID NO:87 VLFSR;SEQ ID NO:88 TISSEDKPFNLR;SEQ ID NO:89 DPIYSNK;SEQ ID NO:90 FFEITPEK;SEQ ID NO:91 AIVILVINEGDANIELVGLK;SEQ ID NO:92 EQQQEQQQEEQPLEVR;SEQ ID NO:93 NFLAGSQDNVISQIPSQVQELAFPGSAQAVEK;With SEQ ID NO:94 ESYFVDAQPK), the representative quantitative display of these feature peptides is in 5A-5U.It is SEQ ID NO:3 NILEASYDTK synthesize Poly saccharide peptide standard product is used for qualitatively and quantitatively analysis (referring to Fig. 5 V).Synthetic peptide can be directly as the analysis of quantification of protein with reference to mark It is accurate.
Embodiment 6
At least the two of the G1 of Gly m 6 is identified in interior public database from including NCBI, Phytozome and UniProt Individual homologous protein sequence.Sequence (the SEQ ID NO analyzed and identified out using bioinformatics tools:16 and 95), to identify Sequence homology and consensus sequence between available protein sequence are constituted (referring to Fig. 6 L).Specifically, this is directed to use with Vector NTI Align X compare instrument, and the instrument performs CLUSTAL W types and compares.From the analysis, it may be determined that altogether There are sequence and/or representative series.
Once selection determines consensus sequence and/or representative series, it is carried out to be digested on computer and is treated with generation The candidate feature fragments of peptides for being detected by LC-MS and being measured.According to provided herein is unique method, based on available protein sequence Conservative selection feature peptide between row so that selected feature peptide can be used for being identified in common sequence database Protein sequence in quantitative all or protein isoforms as much as possible.Therefore, the quantitative of selected feature peptide not only may be used To measure the G1 of Gly m 6 in itself, but also the potential allergen with the G1 very high homologies of Gly m 6 can be measured.
Soybean seed representative is ground to form into fine powder, with hexane degreasing twice, and buffer solution (such as 5M urine is determined with suitable Element, 2M thiocarbamides, 50mM Tris (pH 8.0), 65mM DTT) extract.Sample is ultrasonically treated extracting albumen in buffer solution Matter.The protein dilution that will be extracted, denaturation, then by adding trypsase protease and incubation 15-20 hours at 37 DEG C Carry out proteolytic digestion.Digestion reaction is acidified with formic acid (pH=1-2), and is analyzed using LC-MS/MS.
Selected feature peptide can be used for the Gl of Gly m 6 (individually or in multiple assay pattern with other oroteins group Close) qualitative and quantitative analysis.In this embodiment, several feature peptides (SEQ ID NO are have selected from all peptide possibilities: 96 LVFSLCFLLFSGCCFAFSSR;SEQ ID NO:97 EQPQQNECQIQK;SEQ ID NO:98 RPSYTNGPQEIYIQQGK;SEQ ID NO:99 HQQEEENEGGSILSGFTLEFLEHAFSVDK;SEQ ID NO:100 HCQRPR;SEQ ID NO:101 HNIGQTSSPDIYNPQAGSVTTATSLDFPALSWLR;SEQ ID NO:102 ALIQVVNCNGER;SEQ ID NO:103 VFDGELQEGR;SEQ ID NO:104 TNDTPMIGTLAGANSLLNALPEEVIQHTFNLK;SEQ ID NO:105 NNNPFK;With SEQ ID NO:106 FLVPPQESQK), the representative quantitative display of these mark peptides is in 6A-6K.Synthetic peptide can be directly as quantification of protein Analysis normative reference.
Embodiment 7
At least the two of the G2 of Gly m 6 is identified in interior public database from including NCBI, Phytozome and UniProt Individual homologous protein sequence.Sequence (the SEQ ID NO analyzed and identified out using bioinformatics tools:17 and 107) with identify Can be constituted (referring to Fig. 7 P) with the sequence homology between protein sequence and consensus sequence.Specifically, this is directed to use with Vector NTI Align X compare instrument, and the instrument performs CLUSTAL W types and compares.From the analysis, it may be determined that consensus sequence And/or representative series.
Once selection determines consensus sequence and/or representative series, it is carried out to be digested on computer and is treated with generation The candidate feature fragments of peptides for being detected by LC-MS and being measured.According to provided herein is unique method, based on available protein sequence Conservative selection feature peptide between row so that selected feature peptide can be used for being identified in common sequence database Protein sequence in quantitative all or protein isoforms as much as possible.Therefore, the quantitative of selected feature peptide not only may be used To measure the G2 of Gly m 6 in itself, but also the potential allergen with the G2 very high homologies of Gly m 6 can be measured.
Soybean seed representative is ground to form into fine powder, with hexane degreasing twice, and buffer solution (such as 5M urine is determined with suitable Element, 2M thiocarbamides, 50mM Tris (pH 8.0), 65mM DTT) extract.Sample is ultrasonically treated extracting albumen in buffer solution Matter.The protein dilution that will be extracted, denaturation, then by adding trypsase protease and incubation 15-20 hours at 37 DEG C Carry out proteolytic digestion.Digestion reaction is acidified with formic acid (pH=1-2), and is analyzed using LC-MS/MS.
Selected feature peptide can be used for the G2 of Gly m 6 (individually or in multiple assay pattern with other oroteins group Close) qualitative and quantitative analysis.In this embodiment, several feature peptides (SEQ ID NO are have selected from all peptide possibilities:4 VTAPAMR;SEQ ID NO:108 LVLSLCFLLFSGCFALR;SEQ ID NO:109 EQAQQNECQIQK;SEQ ID NO: 110 RPSYTNGPQEIYIQQGNGIFGMIFPGCPSTYQEPQESQQR;SEQ ID NO:111 SQRPQDR;SEQ ID NO: 112 QQEEENEGSNILSGFAPEFLK;SEQ ID NO:113 EAFGVNMQIVR;SEQ ID NO:114 KPQQEEDDDDEEEQPQCVETDK;SEQ ID NO:115 LSAQYGSLR;SEQ ID NO:116 NAMFVPHYTLNANSIIYALNGR;SEQ ID NO:117 ALVQVVNCNGER;SEQ ID NO:118 VFDGELQEGGVLIVPQNFAVAAK;SEQ ID NO:119 TNDRPSIGNLAGANSLLNALPEE-VIQHTFNLK;And SEQ ID NO:120 NNNPFSFLVPPQESQR), and these feature peptides representative quantitative display in Fig. 7 A-7N.It is SEQ ID NO:4VTAPAMR synthesis poly saccharide peptide standard products are used for qualitatively and quantitatively analysis (referring to Fig. 7 O).Synthetic peptide can be directly as albumen The quantitative analysis normative reference of matter.
Embodiment 8
The G3 sequences of Gly m 6 from database identification are digested in a computer to treat by LC-MS detections and measure to produce Candidate feature fragments of peptides.According to provided herein is unique method, based between available protein sequence conservative choosing Select feature peptide so that selected feature peptide can be used for quantitative in the protein sequence identified in common sequence database Protein isoforms all or as much as possible.The quantitative of selected feature peptide can not only measure the G3 of Gly m 6 in itself, And potential allergen with the G3 very high homologies of Gly m 6 can be measured.
Soybean seed representative is ground to form into fine powder, with hexane degreasing twice, and buffer solution (such as 5M urine is determined with suitable Element, 2M thiocarbamides, 50mM Tris (pH 8.0), 65mM DTT) extract.Sample is ultrasonically treated extracting albumen in buffer solution Matter.The protein dilution that will be extracted, denaturation, then by adding trypsase protease and incubation 15-20 hours at 37 DEG C Carry out proteolytic digestion.Digestion reaction is acidified with formic acid (pH=1-2), and is analyzed using LC-MS/MS.
Selected feature peptide can be individually or with multiplexed assay formats other protein combination be used for Gly m 6 The qualitative and quantitative analysis of G3.In this embodiment, several feature peptides (SEQ ID NO are have selected from all peptide possibilities:5 NNNPFSFLVPPK;SEQ ID NO:121 LVLSLCFLLFSGCCFAFSFR;SEQ ID NO:122 EQPQQNECQIQR; SEQ ID NO:123 QQEEENEGGSILSGFAPEFLEHAFVVDR;SEQ ID NO:124 LQGENEEEEK;SEQ ID NO:125 GGLSVISPPTEEQQQRPEEEEKPDCDEK;SEQ ID NO:126 HCQSQSR;SEQ ID NO:127 LSAQFGSLR;SEQ ID NO:128 VFDGELQEGQVLIVPQNFAVAAR;With SEQ ID NO:129 TNDRPSIGNLAGANSLLNALPEEVIQQTFNLR), and these feature peptides representative quantitative display in Fig. 8 A-8J.For SEQ ID NO:5 NNNPFSFLVPPK synthesis poly saccharide peptide standard products are used for qualitatively and quantitatively analysis (referring to Fig. 8 K).Synthetic peptide can be straight Connect as the analysis normative reference of quantification of protein.
Embodiment 9
Identify several G4's of Gly m 6 in interior public database from including NCBI, Phytozome and UniProt Homologous protein sequence.Sequence (the SEQ ID NO analyzed and identified out using bioinformatics tools:19 and 131-134) with mirror Sequence homology and consensus sequence between fixed available protein sequence are constituted (referring to Fig. 9 Y).Specifically, this is directed to use with Vector NTI Align X compare instrument, and the instrument performs CLUSTAL W types and compares.From the analysis, it may be determined that altogether There are sequence and/or representative series.
Once selection determines consensus sequence and/or representative series, it is carried out to be digested on computer and is treated with generation The candidate feature fragments of peptides for being detected by LC-MS and being measured.According to provided herein is unique method, based on available protein sequence Conservative selection feature peptide between row so that selected feature peptide can be used for being identified in common sequence database Protein sequence in quantitative all or protein isoforms as much as possible.Therefore, selected feature peptide it is quantitative not only The G4 of Gly m 6 can be measured in itself, the potential allergen with the G4 very high homologies of Gly m 6 can also be measured.
Soybean seed representative is ground to form into fine powder, with hexane degreasing twice, and buffer solution (such as 5M urine is determined with suitable Element, 2M thiocarbamides, 50mM Tris (pH 8.0), 65mM DTT) extract.Sample is ultrasonically treated extracting albumen in buffer solution Matter.The protein dilution that will be extracted, denaturation, then by adding trypsase protease and incubation 15-20 hours at 37 DEG C Carry out proteolytic digestion.Digestion reaction is acidified with formic acid (pH=1-2), and is analyzed using LC-MS/MS.
Selected feature peptide can be individually or with multiplexed assay formats other protein combination be used for Gly m 6 The qualitative and quantitative analysis of G4.In this embodiment, several feature peptides (SEQ ID NO are have selected from all peptide possibilities:6 ADFYNPK;SEQ ID NO:135 LNECQLNNLNALEPDHR;SEQ ID NO:136 CAGVTVSK;SEQ ID NO:137 LTLNR;SEQ ID NO:138 MIIIAQGK;SEQ ID NO:139 GALGVAIPGCPETFEEPQEQSNR;SEQ ID NO: 140 QQLQDSHQK;SEQ ID NO:141 VFYLAGNPDIEYPETMQQQQQQK;SEQ ID NO:142 QGQHQQEEEEEGGSVLSGFSK;SEQ ID NO:143 HFLAQSFNTNEDIAEK;SEQ ID NO:144 QIVTVEGGLSVISPK;SEQ ID NO:145 WQEQQDEDEDEDEDDEDEQIPSHPPR;SEQ ID NO:146 RPSHGK;SEQ ID NO:147 EQDEDEDEDEDKPRPSRPSQGK;SEQ ID NO:148 QEEPR;SEQ ID NO:149 NGVEENICTLK;SEQ ID NO:150 LHENIARPSR;SEQ ID NO:151 ISTLNSLTLPALR;SEQ ID NO: 152 QFQLSAQYVVLYK;SEQ ID NO:153 NGIYSPHWNLNANSVIYVTR;SEQ ID NO:154 DVFR;SEQ ID NO:155 AIPSEVLAHSYNLR;SEQ ID NO:156 QSQVSELK;With SEQ ID NO:58 YEGNWGPLVNPESQQGSPR), the representativeness of these signature peptides is quantitatively shown in Fig. 9 A-9X.Synthetic peptide can be directly as egg The quantitative analysis normative reference of white matter.
Embodiment 10
Gly m6 precursors are digested the candidate feature fragments of peptides for producing and treating to be detected by LC-MS and measured on computers. According to provided herein is unique method, based between available protein sequence conservative select feature peptide so that it is selected The feature peptide for going out can be used for quantitative all or as much as possible in the protein sequence identified in common sequence database Protein isoforms.Therefore, the quantitative of selected feature peptide can not only measure the precursors of Gly m 6 in itself, but also can be with Measurement and the potential allergen of the precursor very high homologies of Gly m 6.
Soybean seed representative is ground to form into fine powder, with hexane degreasing twice, and buffer solution (such as 5M urine is determined with suitable Element, 2M thiocarbamides, 50mM Tris (pH 8.0), 65mM DTT) extract.Sample is ultrasonically treated extracting albumen in buffer solution Matter.The protein dilution that will be extracted, denaturation, then by adding trypsase protease and incubation 15-20 hours at 37 DEG C Carry out proteolytic digestion.Digestion reaction is acidified with formic acid (pH=1-2), and is analyzed using LC-MS/MS.
Selected feature peptide can be individually or with multiplexed assay formats other protein combination be used for Gly m 6 before The qualitative and quantitative analysis of body.In this embodiment, three kinds of feature peptides (SEQ ID NO are have selected from all peptide possibilities:6 ADFYNPK,SEQ ID NO:59 GALQCKPGCPETFEEPQEQSNR and SEQ ID NO:60 LQSPDDER), these features The representative quantitative display of peptide is in Figure 10 B and 10C.Synthetic peptide can be directly as the analysis normative reference of quantification of protein.
Sequence table
SEQ ID NO:The example feature peptide of 1 Gly m 1
SYPSNATCPR
SEQ ID NO:The example feature peptide of 2 Gly m 3
YMVIQGEPGAVIR
SEQ ID NO:The example feature peptide of 3 Gly m 5 (beta-conglycinin)
NILEASYDTK
SEQ ID NO:The example feature peptide of 4 Gly m 6 (glycinin) G2
VTAPAMR
SEQ ID NO:The example feature peptide of 5 Gly m 6 (glycinin) G3
NNNPFSFLVPPK
SEQ ID NO:The example feature peptide of 6 Gly m 6 (glycinin) precursors
ADFYNPK
SEQ ID NO:The example feature peptide of 7 Kunitz trypsin inhibitors 1
GGGIEVDSTGK
SEQ ID NO:The example feature peptide of 8 Kunitz trypsin inhibitors 3
GIGTIISSPYR
SEQ ID NO:The example feature peptide of the K of 9 Gly m Bd 28
NKPQFLAGAASLLR
SEQ ID NO:The example feature peptide of the K of 10 Gly m Bd 30
GVITQVK
SEQ ID NO:The example feature peptide of 11 Gly m 8 (2S albumin)
IMENQSEELEEK
SEQ ID NO:The ABA54898.1 of 12 Gly m 1 [MW=12482.64Da]
MGSKVVASVALLLSINILFISMVSSSSHYDPQPQPSHVTALITRPSCPDLSICLNILGGSLGTVDDCCA LIGGLGDIEAIVCLCIQLRALGILNLNRNLQLILNSCGRSYPSNATCPRT
SEQ ID NO:The CAA11755.1 of 13 Gly m 3 [MW=14100.07Da]
MSWQAYVDDHLLCGIEGNHLTHAAIIGQDGSVWLQSTDFPQFKPEEITAI MNDFNEPGSLAPTGLYLGGTKYMVIQGEPGAVIRGKKGPGGVTVKKTGAALIIGIYDEPMTPGQCNMVVERLGDYLI DQGY
SEQ ID NO:The P26987 of 14 Gly m 4 [MW=16771.81Da]
MGVFTFEDEINSPVAPATLYKALVTDADNVIPKALDSFKSVENVEGNGGPGTIKKITFLEDGETKFVLH KIESIDEANLGYSYSVVGGAALPDTAEKITFDSKLVAGPNGGSAGKLTVKYETKGDAEPNQDELKTGKAKADALFKA IEAYLLAHPDYN
SEQ ID NO:15 Gly m 5 (beta-conglycinin) 121281 [MW=70293.13Da]
MMRARFPLLLLGLVFLASVSVSFGIAYWEKENPKHNKCLQSCNSERDSYRNQACHARCNLLKVEKEECE EGEIPRPRPRPQHPEREPQQPGEKEEDEDEQPRPIPFPRPQPRQEEEHEQREEQEWPRKEEKRGEKGSEEEDEDEDE EQDERQFPFPRPPHQKEERNEEEDEDEEQQRESEESEDSELRRHKNKNPFLFGSNRFETLFKNQYGRIRVLQRFNQR SPQLQNLRDYRILEFNSKPNTLLLPNHADADYLIVILNGTAILSLVNNDDRDSYRLQSGDALRVPSGTTYYVVNPDN NENLRLITLAIPVNKPGRFESFFLSSTEAQQSYLQGFSRNILEASYDTKFEEINKVLFSREEGQQQGEQRLQESVIV EISKEQIRALSKRAKSSSRKTISSEDKPFNLRSRDPIYSNKLGKFFEITPEKNPQLRDLDIFLSIVDMNEGALLLPH FNSKAIVILVINEGDANIELVGLKEQQQEQQQEEQPLEVRKYRAELSEQDIFVIPAGYPVVVNATSNLNFFAIGINA ENNQRNFLAGSQDNVISQIPSQVQELAFPGSAQAVEKLLKNQRESYFVDAQPKKKEEGNKGRKGPLSSILRAFY
SEQ ID NO:The glycinin G1 121276 [MW=55706.34Da] of 16 Gly m 6
MAKLVFSLCFLLFSGCCFAFSSREQPQQNECQIQKLNALKPDNRIESEGGLIETWNPNNKPFQCAGVAL SRCTLNRNALRRPSYTNGPQEIYIQQGKGIFGMIYPGCPSTFEEPQQPQQRGQSSRPQDRHQKIYNFREGDLIAVPT GVAWWMYNNEDTPVVAVSIIDTNSLENQLDQMPRRFYLAGNQEQEFLKYQQEQGGHQSQKGKHQQEEENEGGSILSG FTLEFLEHAFSVDKQIAKNLQGENEGEDKGAIVTVKGGLSVIKPPTDEQQQRPQEEEEEEEDEKPQCKGKDKHCQRP RGSQSKSRRNGIDETICTMRLRHNIGQTSSPDIYNPQAGSVTTATSLDFPALSWLRLSAEFGSLRKNAMFVPHYNLN ANSIIYALNGRALIQVVNCNGERVFDGELQEGRVLIVPQNFVVAARSQSDNFEYVSFKTNDTPMIGTLAGANSLLNA LPEEVIQHTFNLKSQQARQIKNNNPFKFLVPPQESQKRAVA
SEQ ID NO:The glycinin G2 121277 [MW=54390.76Da] of 17 Gly m 6
MAKLVLSLCFLLFSGCFALREQAQQNECQIQKLNALKPDNRIESEGGFIETWNPNNKPFQCAGVALSRCTLNRNALR RPSYTNGPQEIYIQQGNGIFGMIFPGCPSTYQEPQESQQRGRSQRPQDRHQKVHRFREGDLIAVPTGVAWWMYNNED TPVVAVSIIDTNSLENQLDQMPRRFYLAGNQEQEFLKYQQQQQGGSQSQKGKQQEEENEGSNILSGFAPEFLKEAFG VNMQIVRNLQGENEEEDSGAIVTVKGGLRVTAPAMRKPQQEEDDDDEEEQPQCVETDKGCQRQSKRSRNGIDETICT MRLRQNIGQNSSPDIYNPQAGSITTATSLDFPALWLLKLSAQYGSLRKNAMFVPHYTLNANSIIYALNGRALVQVVN CNGERVFDGELQEG GVLIVPQNFAVAAKSQSDNFEYVSFKTNDRPSIGNLAGANSLLNALPEEVIQHTFNLKSQQA RQVKNNNPFSFLVPPQESQRRAVA
SEQ ID NO:The glycinin G3 121278 [MW=54241.73Da] of 18 Gly m 6
MAKLVLSLCFLLFSGCCFAFSFREQPQQNECQIQRLNALKPDNRIESEGGFIETWNPNNKPFQCAGVAL SRCTLNRNALRRPSYTNAPQEIYIQQGSGIFGMIFPGCPSTFEEPQQKGQSSRPQDRHQKIYHFREGDLIAVPTGFA YWMYNNEDTPVVAVSLIDTNSFQNQLDQMPRRFYLAGNQEQEFLQYQPQKQQGGTQSQKGKRQQEEENEGGSILSGF APEFLEHAFVVDRQIVRKLQGENEEEEKGAIVTVKGGLSVISPPTEEQQQRPEEEEKPDCDEKDKHCQSQSRNGIDE TICTMRLRHNIGQTSSPDIFNPQAGSITTATSLDFPALSWLKLSAQFGSLRKNAMFVPHYNLNANSIIYALNGRALV QVVNCNGERVFDGELQEGQVLIVPQNFAVAARSQSDNFEYVSFKTNDRPSIGNLAGANSLLNALPEEVIQQTFNLRR QQARQVKNNNPFSFLVPPKESQRRVVA
SEQ ID NO:The glycinin G4 121279 [MW=63587.16Da] of 19 Gly m 6
MGKPFTLSLSSLCLLLLSSACFAISSSKLNECQLNNLNALEPDHRVESEGGLIQTWNSQHPELKCAGVT VSKLTLNRNGLHSPSYSPYPRMIIIAQGKGALGVAIPGCPETFEEPQEQSNRRGSRSQKQQLQDSHQKIRHFNEGDV LVIPPSVPYWTYNTGDEPVVAISLLDTSNFNNQLDQTPRVFYLAGNPDIEYPETMQQQQQQKSHGGRKQGQHQQEEE EEGGSVLSGFSKHFLAQSFNTNEDIAEKLESPDDERKQIVTVEGGLSVISPKWQEQQDEDEDEDEDDEDEQIPSHPP RRPSHGKREQDEDEDEDEDKPRPSRPSQGKRNKTGQDEDEDEDEDQPRKSREWRSKKTQPRRPRQEEPRERGCETRN GVEENICTLKLHENIARPSRADFYNPKAGRISTLNSLTLPALRQFQLSAQYVVLYKNGIYSPHWNLNANSVIYVTRG QGKVRVVNCQGNAVFDGELRRGQLLVVPQNFVVAEQAGEQGFEYIVFKTHHNAVTSYLKDVFRAIPSEVLAHSYNLR QSQVSELKYEGNWGPLVNPESQQGSPRVKVA
SEQ ID NO:The glycinin precursors 75221455 [MW=63876.47Da] of 20 Gly m 6
MGKPFTLSLSSLCLLLLSSACFAISSSKLNECQLNNLNALEPDHRVEFEGGLIQTWNSQHPELKCAGVT VSKLTLNRNGLHLPSYSPYPRMIIIAQGKGALQCKPGCPETFEEPQEQSNRRGSRSQKQQLQDSHQKIRHFNEGDVL VIPPGVPYWTYNTGDEPVVAISLLDTSNFNNQLDQTPRVFYLAGNPDIEYPETMQQQQQQKSHGGRKQGQHQQEEEE EGGSVLSGFSKHFLAQSFNTNEDIAEKLQSPDDERKQIVTVEGGLSVISPKWQEQQDEDEDEDEDDEDEQIPSHPPR RPSHGKREQDEDEDEDEDKPRPSRPSQGKREQDQDQDEDEDEDEDQPRKSREWRSKKTQPRRPRQEEPRERGCETRN GVEENICTLKLHENIARPSRADFYNPKAGRISTLNSLTLPALRQFQLSAQYVVLYKNGIYSPHWNLNANSVIYVTRG QGKVRVVNCQGNAVFDGELRRGQLLVVPQNFVVAEQAGEQGFEYIVFKTHHNAVTSYLKDVFRAIPSEVLAHSYNLR QSQVSELKYEGNWGPLVNPESQQGSPRVKVA
SEQ ID NO:21 Gly m Bd 28K 12697782 [MW=52944.36Da]
MGNKTTLLLLLFVLCHGVATTTMAFHDDEGGDKKSPKSLFLMSNSTRVFKTDAGEMRVLKSHGGRIFYR HMHIGFISMEPKSLFVPQYLDSNLIIFIRRGEAKLGFIYDDELAERRLKTGDLYMIPSGSAFYLVNIGEGQRLHVIC SIDPSTSLGLETFQSFYIGGGANSHSVLSGFEPAILETAFNESRTVVEEIFSKELDGPIMFVDDSHAPSLWTKFLQL KKDDKEQQLKKMMQDQEEDEEEKQTSRSWRKLLETVFGKVNEKIENKDTAGSPASYNLYDDKKADFKNAYGWSKALH GGEYPPLSEPDIGVLLVKLSAGSMLAPHVNPISDEYTIVLSGYGELHIGYPNGSRAMKTKIKQGDVFVVPRYFPFCQ VASRDGPLEFFGFSTSARKNKPQFLAGAASLLRTLMGPELSAAFGVSEDTLRRAVDAQHEAVILPSAWAAPPENAGK LKMEEEPNAIRSFANDVVMDVF
SEQ ID NO:22 Gly m Bd 30K 84371705 [MW=42757.81Da]
MGFLVLLLFSLLGLSSSSSISTHRSILDLDLTKFTTQKQVSSLFQLWKSEHGRVYHNHEEEAKRLEIFK NNLNYIRDMNANRKSPHSHRLGLNKFADITPQEFSKKYLQAPKDVSQQIKMANKKMKKEQYSCDHPPASWDWRKKGV ITQVKYQGGCGSGWAFSATGAIEAAHAIATGDLVSLSEQELVDCVEESEGCYNGWHYQSFEWVLEHGGIATDDDYPY RAKEGRCKANKIQDKVTIDGYETLIMSDESTESETEQAFLSAILEQPISVSIDAKDFHLYTGGIYDGENCTSPYGIN HFVLLVGYGSADGVDYWIAKNSWGEDWGEDGYIWIQRNTGNLLGVCGMNYFASYPTKEESETLVSARVKGHRRVDHS PL
SEQ ID NO:23 KTI 1 125722 [MW=22545.94Da]
MKSTIFFALFLVCAFTISYLPSATAQFVLDTDDDPLQNGGTYYMLPVMRGKGGGIEVDSTGKEICPLTV VQSPNELDKGIGLVFTSPLHALFIAERYPLSIKFGSFAVITLCAGMPTEWAIVEREGLQAVKLAARDTVDGWFNIER VSREYNDYKLVFCPQQAEDNKCEDIGIQIDDDGIRRLVLSKNKPLVVQFQKFRSSTA
SEQ ID NO:24 KTI 3 125020 [MW=24005.29Da]
MKSTIFFLFLFCAFTTSYLPSAIADFVLDNEGNPLENGGTYYILSDITAFGGIRAAPTGNERCPLTVVQ SRNELDKGIGTIISSPYRIRFIAEGHPLSLKFDSFAVIMLCVGIPTEWSVVEDLPEGPAVKIGENKDAMDGWFRLER VSDDEFNNYKLVFCPQQAEDDKCGDIGISIDHDDGTRRLVVSKNKPLVVQFQKLDKESLAKKNHGLSRSE
SEQ ID NO:25 Gly m 8 (2S albumin) NP_001238443 [MW=18459.97Da]
MTKFTILLISLLFCIAHTCSASKWQHQQDSCRKQLQGVNLTPCEKHIMEKIQGRGDDDDDDDDDNHILR TMRGRINYIRRNEGKDEDEEEEGHMQKCCTEMSELRSPKCQCKALQKIMENQSEELEEKQKKKMEKELINLATMCRF GPMIQCDLSSDD
SEQ ID NO:26 agglutinin ADC94422 [MW=30186.22Da]
MATSNFSIVLSLSLAFFLVLLTKANSTNTVSFTVSKFSPRQQNLIFQGDAAISPSGVLRLTKVDSIDVPTTGSLGRA LYATPIQIWDSETGKVASWATSFKFKVFSPNKTADGLAFFLAPVGSKPQSKGGFLGLFNSDSKNKSVQTVAVEFDTY YNAKWDPANRHIGIDVNSIKSVKTASWGLANGQIAQILITYDADTSLLVASLIHPSRKTSYILSETVSLKSNLPEWV NIGFSATTGLNKGFVETHDVFSWSFASKLSDGSTSDTLDLPSFLLNEAI
SEQ ID NO:27 LOX CAA39604 [MW=96817.14Da]
MFGIFDKGQKIKGTVVLMPKNVLDFNAITSIGKGGVIDTATGILGQGVSLVGGVIDTATSFLGRNISMQ LISATQTDGSGNGKVGKEVYLEKHLPTLPTLGARQDAFSIFFEWDASFGIPGAFYIKNFMTDEFFLVSVKLEDIPNH GTIEFVCNSWVYNFRSYKKNRIFFVNDTYLPSATPAPLLKYRKEELEVLRGDGTGKRKDFDRIYDYDVYNDLGNPDG GDPRPILGGSSIYPYPRRVRTGRERTRTDPNSEKPGEVYVPRDENFGHLKSSDFLTYGIKSLSHDVIPLFKSAIFQL RVTSSEFESFEDVRSLYEGGIKLPTDILSQISPLPALKEIFRTDGENVLQFPPPHVAKVSKSGWMTDEEFAREVIAG VNPNVIRRLQEFPPKSTLDPTLYGDQTSTITKEQLEINMGGVTVEEALSTQRLFILDYQDAFIPYLTRINSLPTAKA YATRTILFLKDDGTLKPLAIELSKPHPDGDNLGPESIVVLPATEGVDSTIWLLAKAHVIVNDSGYHQLVSHWLNTHA VMEPFAIATNRHLSVLHPIYKLLYPHYRDTININGLARQSLINADGIIEKSFLPGKYSIEMSSSVYKNWVFTDQALP ADLVKRGLAIEDPSAPHGLRLVIEDYPYAVDGLEIWDAIKTWVHEYVSLYYPTDAAVQQDTELQAWWKEAVEKGHGD LKEKPWWPKMQTTEDLIQSCSIIVWTASALHAAVNFGQYPYGGLILNRPTLARRFIPAEGTPEYDEMVKNPQKAYLR TITPKFETLIDLSVIEILSRHASDEIYLGERETPNWTTDKKALEAFKRFGSKLTGIEGKINARNSDPSLRNRTGPVQ LPYTLLHRSSEEGLTFKGIPNSISI
SEQ ID NO:The consensus sequences of 28 Gly m 1
MGSKVVASVALLLSINILFISMVSSSSHYDPPQPSYVTALITRPSCPDLSICLNILGGSLGTVDDCCAL IGGLGDIEAIVCLCIQLRALGILNLNRNLQLILNACGRSYPSNATCPRT
SEQ ID NO:The consensus sequence #2 of 29 Gly m 1
MGSKVVASVALLLSINILFISMVSSSSHYDPQPQPSHVTALITRPSCPDLSICLNILGGSLGTVDDCCA LIGGLGDIEAIVCLCIQLRALGILNLNRNLQLILNACGRSYPSNATCPRT
SEQ ID NO:30 Gly m 1 Ping AAB34755.1 42aa
ALITRPSXPDLSIXLNILGGSLGTVDDXXALIGGLXDXXAIV
SEQ ID NO:31 Gly m 1 Ping ABA54897.1 134aa
MGSKVVASVALLLSINILFISMVSSSSHYDPPPPPCYVPAPLTPPPSLSPPPSLSPPPPSGPSCPDLSV CLNILDGSPADDCCALIADLVDLEASVCLCIQLRVLGIVNLDLNLQLILNACGPSYPSNATCPRT
SEQ ID NO:32 Gly m 1 Eric ABA54899 118aa
GSKVVASVALLLSINILFISMVSSSSHYDPQPQPSHVTALITRPSCPDLSICLNILGGSLGTVDDCCALIGGLGDIE AIVCLCIQLRALGILNLNRNLQLILNSC GRSYPSNATCPRT
SEQ ID NO:33 Gly m 1 Glyma15g13740.1BLAST 120aa
MGSKVVAYVALLLSINILFISMVSSSSHYDPQPQPSYVTALITRPSCPDLSVCLNILGGYLGTVDDCCA LIGGLGDIEATVCLCIQLRALGILNLNRNLQLILNACGPSYPSNATCPRT
SEQ ID NO:34 Gly m 1 Glyma15g13770.1BLAST 130aa
MGSKVVASVALLLSINILFISMVSSSSHYDPPPPPCYVPAPFTPPPPSLSPPPPSGPSCPDLSVCLNIL DGSPADDCCALIADLVDLEASVCLCIQLRVLGIVNLDLNLQLILNACGPSYPSNATCPRT
SEQ ID NO:35 Gly m 1 Glyma15g13750.1BLAST 120aa
MGSKVVASVALLLSINILFISMVSSSSHYDPPPQPSYVTALITRPSCPDLSICLNILGGSLGTVDDCCA LIGGLGDIEAIVCLCIQLRALGILNLNRNLQLILNSCGRSYPSNATCPRT
SEQ ID NO:36 ALGILNLNR
SEQ ID NO:37 NLQLILNSCGR
SEQ ID NO:The consensus sequences of 38 Gly m 3
MSWQAYVDDHLLCGIEGNHLTHAAIIGQDGSVWAQSTDFPQFKPEEITAIMNDFNEPGSLAPTGLYLGG TKYMVIQGEPGAVIRGKKGPGGVTVKKTGAALIIGIYDEPMTPGQCNMVVERLGDYLIDQGY
SEQ ID NO:39 Gly m 3 Ping ABU97472.1 131aa
MSWQAYVDDHLLCEIEGNHLTHAAIIGQDGSVWAQSTNFPQFKPEEITAINNDFNEPGSLAPTGLYIGG TKYMVIQGEPGAVIRGKKGPGGVTVKKTGAALIIGIYDEPMTPGQCNMVVERLGDYLIDQGL
SEQ ID NO:40 Gly m 3 Ping O65809.1 131aa
MSWQAYVDDHLLCDIEGNHLTHAAIIGQDGSVWAQSTDFPQFKPEEITAIMNDFNEPGSLAPTGLYLGG TKYMVIQGEPGAVIRGKKGPGGVTVKKTGAALIIGIYDEPMTPGQCNMVVERPGDYLIDQGY
SEQ ID NO:41 GPGGVTVK
SEQ ID NO:The consensus sequences of 42 Gly m 4
MGVFTFEDETTSPVAPATLYKALVTDADNVIPKAVDAFKSVENVEGNGGPGTIKKITFVEDGETKFVLH KIEAIDEANLGYSYSVVGGAGLPDTVEKITFEAKLAAGANGGSAGKLTVKYQTKGDAQPNQDELKSGKAKADALFKA VEAYLLANPDYN
SEQ ID NO:43 Gly m 4 Glyma07g37240.1 BLAST 165aa
MGVFTFEDEINSPVAPATLYKALVTDADNVIPKALDSFKSVENVEGNGGPGTIKKITFLEADVNEWIDG ETKFVLHKIESIDEANLGYSYSVVGGAALPDTAEKITFDSKLVAGPNGGSAGKLTVKYETKGDAEPNQDELKTGKAK ADALFKAIEAYLLAHPDYN
SEQ ID NO:44 Gly m 4 Glyma17g03365.1 BLAST 159aa
MGIFTFEDEITSPVAPATLYKALVTDADNIIPKALDSFKSVENVEGNGGPGTIKKITFVEDGETKFVLH KIEAVDEANLGYSYSVVGGAALPDTAEKITFHSKLAAGPNGGSAGKLTVEYQTKGDAQPNQDQLKTGKAKADALFKA IEAYLLANPDYN
SEQ ID NO:45 Gly m 4 Glyma07g37240.3 BLAST 147aa
MGVFTFEDEINSPVAPATLYKALDSFKSVENVEGNGGPGTIKKITFLEDGETKFVLHKIESIDEANLGY SYSVVGGAALPDTAEKITFDSKLVAGPNGGSAGKLTVKYETKGDAEPNQDELKTGKAKADALFKAIEAYLLAHPDYN
SEQ ID NO:46 Gly m 4 Glyma07g37270.2 BLAST 159aa
MGVFTFEDEINSPVAPATLYKALVTDADNVIPKALDSFKSVENVEGNGGPGTIKKITFLEDGETKFVLH KIEAIDEANLGYSYSVVGGDGLPDTVEKITFECKLAAGANGGSAGKLTVKYQTKGDAQPNQDDLKIGKAKSDALFKA VEAYLLAHPDYN
SEQ ID NO:47 Gly m 4 Glyma07g37270.1 BLAST 159aa
MGVFTFEDETTSPVAPATLYKALVTDADNVIPKAVDAFRSVENVEGNGGPGTIKKITFLEDGETKFVLH KIEAIDEANLGYSYSVVGGDGLPDTVEKITFECKLAAGANGGSAGKLTVKYQTKGDAQPNQDDLKIGKAKSDALFKA VEAYLLAHPDYN
SEQ ID NO:48 Gly m 4 Glyma17g03360.1 BLAST 159aa
MGVFTFEDETTSPVAPATLYKALVTDADNVIPKAVDAFRSVENLEGNGGPGTIKKITFVEDGESKFVLH KIESVDEANLGYSYSVVGGVGLPDTVEKITFECKLAAGANGGSAGKLTVKYQTKGDAQPNPDDLKIGKVKSDALFKA VEAYLLANPHYN
SEQ ID NO:49 Gly m 4 Glyma17g03350.1 BLAST 159aa
MGIFTFEDETTSPVAPATLYKALVTDADNVIPKAVEAFRSVENLEGNGGPGTIKKITFVEDGESKFVLH KIESVDEANLGYSYSVVGGVGLPDTVEKITFECKLAAGANGGSAGKLTVKYQTKGDAQPNPDDLKIGKVKSDALFKA VEAYLLANPHYN
SEQ ID NO:50 Gly m 4 Glyma09g04510.1 BLAST 159aa
MGVFTFEDETTSTVAPARLYKALVKDADNLVPKAVEAIKSVEIVEGNGGPGTIKKLTFVEDGQTKYVLHKVEAIDEA NWGYNYSVVGGVGLPDTVEKIS FEAKLVADPNGGSIAKITVKYQTKGDANPSEEELKSGKAKGDALFKALEGYVLA NPDYN
SEQ ID NO:51 Gly m 4 Glyma15g15590.1BLAST 159aa
MGVFTFEDETTSTVAPARLYKALVKDADNLVPKAVEAIKSVEIVEGNGGPGTIKKLTFVEDGQTKYVLH KVEAIDEANWGYNYSVVGGVGLPDTVEKISFEAKLVEGASGGSIAKITVKYQTKGDVNPSEEELKSGKAKGDALFKA LEGYVLANPDYN
SEQ ID NO:52 MGVFTFEDEINSPVAPATLYK
SEQ ID NO:53 ALDSFK
SEQ ID NO:54 SVENVEGNGGPGTIK
SEQ ID NO:55 ITFLEDGETK
SEQ ID NO:56 FVLHK
SEQ ID NO:57 AIEAYLLAHPDYN
SEQ ID NO:The consensus sequences of 61 Gly m 5
MMRARFPLLLLGVVFLASVSVSFGIAYWEKQNPSHNKCLQSCNSEKDSYRNQACHARCNLLKVEEEEEC EEGQIPRPRPQHPERERQQHGEKEEDEGEQPRPFPFPRPRQPHQEEEHEQKEEHEWHRKEEKHGGKGSEEEQDEREH PRPHQPHQKEEEKHEWQHKQEKHQGKESEEEEEDQDEDEEQDKESQESEGSESQREPRRHKNKNPFHFNSKRFQTLF KNQYGHVRVLQRFNKRSQQLQNLRDYRILEFNSKPNTLLLPHHADADYLIVILNGTAILTLVNNDDRDSYNLQSGDA LRVPAGTTYYVVNPDNDENLRMITLAIPVNKPGRFESFFLSSTQAQQSYLQGFSKNILEASYDTKFEEINKVLFGRE EGQQQGEERLQESVIVEISKKQIRELSKRAKSSSRKTISSEDKPFNLRSRDPIYSNKLGKLFEITPEKNPQLRDLDV FLSVVDMNEGALLLPHFNSKAIVVLVINEGDANIELVGIKEQQQRQQQEEQPLEVRKYRAELSEQDIFVIPAGYPVV VNATSNLNFFAFGINAENNQRNFLAGSKDNVISQIPSQVQELAFPGSAKDIENLIKSQSESYFVDAQPQQKEEGNKG RKGPLSSILRAFY
SEQ ID NO:62 Gly m 5 ABH09130BLAST 600aa
MFGIVYWEKQNPSHNKCLRSCNSEKDSYRNQACHARCNLLKVEEEEECEEGQIPRPRPQHPERERQQHGEKEEDEGE QPRPFPFPRPRQPHQEEEHEQKEEHEWHRKEEKHGGKGSEEEQDEREHPRPHQPHQKEEEKHEWQHKQEKHQGKESE EEEEDQDEDEGQDKESQESEGSESQREPRRHKNKNPFHFNSKRFQTLFKNQYGHVRVLQRFNKRSQQLQNLRDYRIL EFNSKPNTLLSPNHADADYLIVILNGTAILTLVNNDDRDSYNLQSGDALRVPAGTTYYVVNPDNDENLRMITLAIPV NKPGRFESFFLSSTQAQQSYLQGFSKNILEASYDTKFEEIN KVLFGREEGQQQGEERLQESVIVEISKKQIRELSK HAKPSSRKTISSEDKPFNLRSRDPIYSNKLGKLFEITPEKNPQLRDLDVFLSVVDMNEGALFLPHFNSKAIVVLVIN EGEANIELVGIKEQQQRQQQEEQPLEVRKYRAELSEQDIFVIPAGYPVVVNATSDLNFFAFGINAENNQRNFLAGSK DNVISQIPSQVQELAFPGSAKDIENLIKSQSESYFVDAQPQQKEEGNKGRKGPLSSILRAFY
SEQ ID NO:63 Gly m 5 BAA74452 BLAST 559aa
VEEEEECEEGQIPRPRPQHPERERQQHGEKEEDEGEQPRPFPFPRPRQPHQEEEHEQKEEHEWHRKEEK HGGKGSEEEQDEREHPRPHQPHQKEEEKHEWQHKQEKHQGKESEEEEEDQDEDEEQDKESQESEGSESQREPRRHKN KNPFHFNSKRFQTLFKNQYGHVRVLQRFNKRSQQLQNLRDYRILEFNSKPNTLLLPHHADADYLIVILNGTAILTLV NNDDRDSYNLQSGDALRVPAGTTYYVVNPDNDENLRMITLAIPVNKPGRFESFFLSSTQAQQSYLQGFSKNILEASY DTKFEEINKVLFGREEGQQQGEERLQESVIVEISKKQIRELSKHAKSSSRKTISSEDKPFNLRSRDPIYSNKLGKLF EITPEKNPQLRDLDVFLSVVDMNEGALFLPHFNSKAIVVLVINEGEANIELVGIKEQQQRQQQEEQPLEVRKYRAEL SEQDIFVIPAGYPVVVNATSDLNFFAFGINAENNQRNFLAGSKDNVISQIPSQVQELAFPGSAKDIENLIKSQSESY FVDAQPQQKEEGNKGRKGPLSSILRAFY
SEQ ID NO:64 Gly m 5 BAC78524 BLAST 621aa
MMRARFPLLLLGVVFLASVSVSFGIAYWEKQNPSHNKCLRSCNSEKDSYRNQACHARCNLLKVEEEEEC EEGQIPRPRPQHPERERQQHGEKEEDEGEQPRPFPFPRPRQPRQEEEHEQKEEHEWHRKEEKHGGKGSEEEQDEREH PRPHQPHQKEEEKHEWQHKQEKHQGKESEEEEEDQDEDEEQDKESQESEGSESQREPRRHKNKNPFHFNSKRFQTLF KNQYGHVRVLQRFNKRSQQLQNLRDYRILEFNSKPNTLLLPHHADADYLIVILNGTAILTLVNNDDRDSYNLQSGDA LRVPAGTTYYVVNPDNDENLRMITLAIPVNKPGRFESFFLSSTQAQQSYLQGFSKNILEASYDTKFEEINKVLFGRE EGQQQGEERLQESVIVEISKKQIRELSKHAKSSSRKTISSEDKPFNLRSRDPIYSNKLGKLFEITPEKNPQLRDLDV FLSVVDMNEGALFLPHFNSKAIVVLVINEGEANIELVGIKEQQQRQQQEEQPLEVRKYRAELSEQDIFVIPAGYPVV VNATSDLNFFAFGINAENNQRNFLAGSKDNVISQIPSQVQELAFPGSAKDIENLIKSQSESYFVDAQPQQKEEGNKG RKGPLSSILRAFY
SEQ ID NO:65 Gly m 5 Glyma20g28460.1 BLAST 440aa
MMRVRFPLLVLLGTVFLASVCVSLKVREDENNPFYLRSSNSFQTLFENQNGRIRLLQRFNKRSPQLENLRDYRIVQF QSKPNTILLPHHADADFLLFVLSGRAILTLVNNDDRDSYNLHPGDAQRIPAGTTYYLVNPHDHQNLKIIKLAIPVNK PGRYDDFFLSSTQAQQSYLQGFSHNILETSFHSEFEEINRVLFGEEEEQRQQEGVIVELSKEQIRQLSRRAKSSSRK TISSEDEPFNLRSRNPIYSNNFGKFFEITPEKNPQLRDLDIFLSSVDINEGALLLPHFNSKAIVILVINEGDANIEL VGIKEQQQKQKQEEEPLEVQRYRAELSEDDVFVIPAAYPFVVNATSNLNFLAFGINAENNQRNFLAGEKDNVVRQIE RQVQELAFPGSAQDVERLLKKQR ESYFVDAQPQQKEEGSKGRKGPFPSILGALY
SEQ ID NO:66 Gly m 5 Ping AAB23463 439aa
MMRVRFPLLVLLGTVFLASVCVSLKVREDENNPFYFRSSNSFQTLFENQNVRIRLLQRFNKRSPQLENL RDYRIVQFQSKPNTILLPHHADADFLLFVLSGRAILTLVNNDDRDSYNLHPGDAQRIPAGTTYYLVNPHDHQNLKII KLAIPVNKPGRYDDFFLSSTQAQQSYLQGFSHNILETSFHSEFEEINRVLFGEEEEQRQQEGVIVELSKEQIRQLSR RAKSSSRKTISSEDEPFNLRSRNPIYSNNFGKFFEITPEKNPQLRDLDIFLSSVDINEGALLLPHFNSKAIVILVIN EGDANIELVGIKEQQQKQKQEEEPLEVQRYRAELSEDDVFVIPAAYPFVVNATSNLNFLAFGINAENNQRNFLAGEK DNVVRQIERQVQELAFPGSAQDVERLLKKQRESYFVDAQPQQKEEGSKGRKGPFPSILGALY
SEQ ID NO:67 Gly m 5 Glyma20g28650.1 BLAST 606aa
MMRARFPLLLLGLVFLASVSVSFGIAYWEKENPKHNKCLQSCNSERDSYRNQACHARCNLLKVEKEECE EGEIPRPRPRPQHPEREPQQPGEKEEDEDEQPRPIPFPRPQPRQEEEHEQREEQEWPRKEEKRGEKGSEEEDEDEDE EQDERQFPFPRPPHQKEERKQEEDEDEEQQRESEESEDSELRRHKNKNPFLFGSNRFETLFKNQYGRIRVLQRFNQR SPQLQNLRDYRILEFNSKPNTLLLPNHADADYLIVILNGTAILSLVNNDDRDSYRLQSGDALRVPSGTTYYVVNPDN NENLRLITLAIPVNKPGRFESFFLSSTEAQQSYLQGFSRNILEASYDTKFEEINKVLFSREEGQQQGEQRLQESVIV EISKEQIRALSKRAKSSSRKTISSEDKPFNLRSRDPIYSNKLGKFFEITPEKNPQLRDLDIFLSIVDMNEGALLLPH FNSKAIVILVINEGDANIELVGLKEQQQEQQQEEQPLEVRKYRAELSEQDIFVIPAGYPVVVNATSNLNFFAIGINA ENNQRNFLAGSQDNVISQIPSQVQELAFPGSAQAVEKLLKNQRESYFVDAQPKKKEEGNKGRKGPLSSILRAFY
SEQ ID NO:68 Gly m 5 Glyma20g28660.1 BLAST 606aa
MMRARFPLLLLGLVFLASVSVSFGIAYWEKENPKHNKCLQSCNSERDSYRNQACHARCNLLKVEKEECE EGEIPRPRPRPQHPEREPQQPGEKEEDEDEQPRPIPFPRPQPRQEEEHEQREEQEWPRKEEKRGEKGSEEEDEDEDE EQDERQFPFPRPPHQKEERKQEEDEDEEQQRESEESEDSELRRHKNKNPFLFGSNRFETLFKNQYGRIRVLQRFNQR SPQLQNLRDYRILEFNSKPNTLLLPNHADADYLIVILNGTAILSLVNNDDRDSYRLQSGDALRVPSGTTYYVVNPDN NENLRLITLAIPVNKPGRFESFFLSSTEAQQSYLQGFSRNILEASYDTKFEEINKVLFSREEGQQQGEQRLQESVIV EISKEQIRALSKRAKSSSRKTISSEDKPFNLRSRDPIYSNKLGKFFEITPEKNPQLRDLDIFLSIVDMNEGALLLPH FNSKAIVILVINEGDANIELVGLKEQQQEQQQEEQPLEVRKYRAELSEQDIFVIPAGYPVVVNATSNLNFFAIGINA ENNQRNFLAGSQDNVISQIPSQVQELAFPGSAQAVEKLLKNQRESYFVDAQPKKKEEGNKGRKGPLSSILRAFY
SEQ ID NO:69 Gly m 5 Glyma20g28650.2 BLAST 543aa
MMRARFPLLLLGLVFLASVSVSFGIAYWEKENPKHNKCLQSCNSERDSYRNQACHARCNLLKVEKEECE EGEIPRPRPRPQHPEREPQQPGEKEEDEDEQPRPIPFPRPQPRQEEEHEQREEQEWPRKEEKRGEKGSEEEDEDEDE EQDERQFPFPRPPHQKEERKQEEDEDEEQQRESEESEDSELRRHKNKNPFLFGSNRFETLFKNQYGRIRVLQRFNQR SPQLQNLRDYRILEFNSKPNTLLLPNHADADYLIVILNGTAILSLVNNDDRDSYRLQSGDALRVPSGTTYYVVNPDN NENLRLITLAIPVNKPGRFESFFLSSTEAQQSYLQGFSRNILEASYDTKFEEINKVLFSREEGQQQGEQRLQESVIV EISKEQIRALSKRAKSSSRKTISSEDKPFNLRSRDPIYSNKLGKFFEITPEKNPQLRDLDIFLSIVDMNEGALLLPH FNSKAIVILVINEGDANIELVGLKEQQQEQQQEEQPLEVRKYRAELSEQDIFVIPAGYPVVVNATSNLNFFAIGINA ENNQRNFLAGI
SEQ ID NO:70 Gly m 5 Ping AAA33947 218aa
SKRAKSSSRKTISSEDKPFNLGSRDPIYSKKLGKFFEITPEKNPQLRDLDIFLSIVDMNEGALLLPHFN SKAIVILVINEGDANIELVGLKEQQQEQQQEEQPLEVRKYRAELSEQDIFVIPAGYPVVVNATSNLNFFAIGINAEN NQRNFLAGSQDNVISQIPSQVQELAFPGSAQAVEKLLKNQRESYFVDAQPNEKEEGNKGRKGPLSSILRAFY
SEQ ID NO:71 Gly m 5 NP_001237316 BLAST 621aa
MMRARFPLLLLGVVFLASVSVSFGIAYWEKQNPSHNKCLRSCNSEKDSYRNQACHARCNLLKVEEEEEC EEGQIPRPRPQHPERERQQHGEKEEDEGEQPRPFPFPRPRQPRQEGEHEQKEEHEWHRKEEKHGGKGSEEEQDGREH PRPHQPHQKEEEKHEWQHKQEKHQGKESEEEEEDQDEDEEQDKESQESEGSESQREPRRHKNKNPFHFNSKRFQTLF KNQYGHVRVLQRFNKRSQQLQNLRDYRILEFNSKPNTLLLPHHADADYLIVILNGTAILTLVNNDDRDSYNLQSGDA LRVPAGTTYYVVNPDNDENLRMITLAIPVNKPGRFESFFLSSTQAQQSYLQGFSKNILEASYDTKFEEINKVLFGRE EGQQQGEERLQESVIVEISKKQIRELSKRAKSSSRKTISSEDKPFNLRSRDPIYSNKLGKLFEITPEKNPQLRDLDV FLSVVDMNEGALFLPHFNSKAIVVLVINEGEANIELVGIKEQQQRQQQEEQPLEVRKYRAELSEQDIFVIPAGYPVV VNATSDLNFFAFGINAENNQRNFLAGSKDNVISQIPSQVQELAFLGSAKDIENLIKSQSESYFVDAQPQQKEEGNKG RKGPLSSILRAFY
SEQ ID NO:72 Gly m 5 BAE02726 BLAST 621aa
MMRARFPLLLLGVVFLASVSVSFGIAYWEKQNPSHNKCLRSCNSEKDSYRNQACHARCNLLKVEEEEECEEGQIPRP RPQHPERERQQHGEKEEDEGEQPRPFPFPRPRQPHQEEEHEQKEEHEWHRKEEKHGGKGSEEEQDEREHPRPHQPHQ KEEEKHEWQHKQEKHQGKESEEEEEDQDEDEEQDKESQESEGSESQREPRRHKNKNPFHFNSKRFQTLFKNQYGHVR VLQRFNKRSQQLQNLRDYRILEFNSKPNTLLLPHHADADYLIVILNGTAILTLVNNDDRDSYNLQSGDALRVPAGTT YYVVNPDNDENLRMITLAIPVNKPGRFESFFLSSTQAQQSYLQGFSKNILEASYDTKFEEINKVLFGREEGQQQGEE RLQESVIVEISKKQIRELSKHAKSSSRKTISSEDKPFNLRSRDPIYSNKLGKLFEITPEKNPQLRDLDVFLSVVDMN EGALFLPHFNSKAIVVLVINEGEANIELVGIKEQQQRQQQEEQPLEVRKYRAELSEQDIFVIPAGYPVVVNATSDLN FFAFGINAENNQRN FLAGSKDNVISQIPSQVQELAFPGSAKDIENLIKSQSESYFVDAQPQQKEEGNKGRKGPLSS ILRAFY
SEQ ID NO:73 Gly m 5 Ping AAB01374 639aa
MMRARFPLLLLGVVFLASVSVSFGIAYWEKQNPSHNKCLRSCNSEKDSYRNQACHARCNLLKVEEEEEC EEGQIPRPRPQHPERERQQHGEKEEDEGEQPRPFPFPRPRQPHQEEEHEQKEEHEWHRKEEKHGGKGSEEEQDEREH PRPHQPHQKEEEKHEWQHKQEKHQGKESEEEEEDQDEDEEQDKESQESEGSESQREPRRHKNKNPFHFNSKRFQTLF KNQYGHVRVLQRFNKRSQQLQNLRDYRILEFNSKPNTLLLPHHADADYLIVILNGTAILTLVNNDDRDSYNLQSGDA LRVPAGTTFYVVNPDNDENLRMIAGTTFYVVNPDNDENLRMITLAIPVNKPGRFESFFLSSTQAQQSYLQGFSKNIL EASYDTKFEEINKVLFGREEGQQQGEERLQESVIVEISKKQIRELSKHAKSSSRKTISSEDKPFNLGSRDPIYSNKL GKLFEITQRNPQLRDLDVFLSVVDMNEGALFLPHFNSKAIVVLVINEGEANIELVGIKEQQQRQQQEEQPLEVRKYR AELSEQDIFVIPAGYPVMVNATSDLNFFAFGINAENNQRNFLAGSKDNVISQIPSQVQELAFPRSAKDIENLIKSQS ESYFVDAQPQQKEEGNKGRKGPLSSILRAFY
SEQ ID NO:74 Gly m 5 Glyma10g39150.1 BLAST 622aa
MMRARFPLLLLGVVFLASVSVSFGIAYWEKQNPSHNKCLRSCNSEKDSYRNQACHARCNLLKVEEEEEC EEGQIPRPRPQHPERERQQHGEKEEDEGEQPRPFPFPRPRQPHQEEEHEQKEEHEWHRKEEKHGGKGSEEEQDEREH PRPHQPHQKEEEKHEWQHKQEKHQGKESEEEEEDQDEDEEQDKESQESEGSESQREPRRHKNKNPFHFNSKRFQTLF KNQYGHVRVLQRFNKRSQQLQNLRDYRILEFNSKPNTLLLPHHADADYLIVILNGTAILTLVNNDDRDSYNLQSGDA LRVPAGTTYYVVNPDNDENLRMITLAIPVNKPGRFESFFLSSTQAQQSYLQGFSKNILEASYDTKFEEINKVLFGRE EGQQQGEERLQESVIVEISKKQIRELSKHAKSSSRKTISSEDKPFNLRSRDPIYSNKLGKLFEITPEKNPQLRDLDV FLSVVDMNEGALFLPHFNSKAIVVLVINEGEANIELVGIKEQQQRQQQEEQPLEVRKYRAELSEQDIFVIPAGYPVV VNATSDLNFFAFGINAENNQRNFLAGSKDNVISQIPSQVQELAFPGSAKDIENLIKSQSESYFVDAQPQQKEEGNKG RKGPLSSILRAFY
SEQ ID NO:75 CNLLK
SEQ ID NO:76 EEDEDEQPRPIPFPRPQPR
SEQ ID NO:77 EEQEWPR
SEQ ID NO:78 QFPFPRPPHQK
SEQ ID NO:79 ESEESEDSELR
SEQ ID NO:80 NPFLFGSNR
SEQ ID NO:81 FETLFK
SEQ ID NO:82 SPQLQNLR
SEQ ID NO:83 LQSGDALR
SEQ ID NO:84 VPSGTTYYVVNPDNNENLR
SEQ ID NO:85 FESFFLSSTEAQQSYLQGFSR
SEQ ID NO:86 FEEINK
SEQ ID NO:87 VLFSR
SEQ ID NO:88 TISSEDKPFNLR
SEQ ID NO:89 DPIYSNK
SEQ ID NO:90 FFEITPEK
SEQ ID NO:91 AIVILVINEGDANIELVGLK
SEQ ID NO:92 EQQQEQQQEEQPLEVR
SEQ ID NO:93 NFLAGSQDNVISQIPSQVQELAFPGSAQAVEK
SEQ ID NO:94 ESYFVDAQPK
SEQ ID NO:95 Gly m 6 G1 Ping CAA26723.1 495aa
MAKLVFSLCFLLFSGCCFAFSSREQPQQNECQIQKLNALKPGNRIESEGGLIETWNPNNKPFQCAGVAL SRCTLNRNALRRPSYTNGPQEIYIQQGKGIFGMIYPGCSSTFEEPQQPQQRGQSSRPQDRHQKIYNSREGDLIAVPT GVAWWMYNNEDTPVVAVSIIDTNSLENQLDQMPRRFYLAGNQEQEFLKYQQEQGGHQSQKGKHQQEEENEGGSILSG FTLEFLEHAFSVDKQIAKNLQGENEGEDKGAIVTVKGGLSVIKPPTDEQQQRPQEEEEEEEDEKPQCKGKDKHCQRP RGSQSKSRRNGIDETICTMRLRHNIGQTSSPDIYNPQAGSVTTATSLDFPALSWLRLSAGFGSLRKNAMFVPHYNLN ANSIIYALNGRALIQVVNCNGERVFDGELQEGRVLIVPQNFVVAARSQSDNFEYVSFKTNDTPMIGTLAGANSLLNA LPEEVIQHTFNLKSQQARQIKNNNPFKFLVPPQESQKRAVA
SEQ ID NO:96 LVFSLCFLLFSGCCFAFSSR
SEQ ID NO:97 EQPQQNECQIQK
SEQ ID NO:98 RPSYTNGPQEIYIQQGK
SEQ ID NO:99 HQQEEENEGGSILSGFTLEFLEHAFSVDK
SEQ ID NO:100 HCQRPR
SEQ ID NO:101 HNIGQTSSPDIYNPQAGSVTTATSLDFPALSWLR
SEQ ID NO:102 ALIQVVNCNGER
SEQ ID NO:103 VFDGELQEGR
SEQ ID NO:104 TNDTPMIGTLAGANSLLNALPEEVIQHTFNLK
SEQ ID NO:105 NNNPFK
SEQ ID NO:106 FLVPPQESQK
SEQ ID NO:107 Gly m 6 G2 Ping CAA26575.1 485aa
MAKLVLSLCFLLFSGCFALREQAQQNECQIQKLNALKPGNRIESEGGFIETWNPNNKPFQCAGVALSRC TLNRNALRRPSYTNGPQEIYIQQGNGIFGMIFPGCPSTYQEPQESQQRGRSQRPQDRHQKVHRFREGDLIAVPTGVA WWMYNNEDTPVVAVSIIDTNSLENQLDQMPRRFYLAGNQEQEFLKYQQQQQGGSQSQKGKQQEEENEGSNILSGFAP EFLKEAFGVNMQIVRNLQGENEEEDSGAIVTVKGGLRVTAPAMRKPQQEEDDDDEEEQPQCVETDKGCQRQSKRSRN GIDETICTMRLRQNIGQNSSPDIYNPQAGSITTATSLDFPALWLLKLSAQYGSLRKNAMFVPHYTLNANSIIYALNG RALVQVVNCNGERVFDGELQEGGVLIVPQNFAVAAKSQSDNFEYVSFKTNDRPSIGNLAGANSLLNALPEEVIQHTF NLKSQQARQVKNNNPFSFLVPPQESQRRAVA
SEQ ID NO:108 LVLSLCFLLFSGCFALR
SEQ ID NO:109 EQAQQNECQIQK
SEQ ID NO:110 RPSYTNGPQEIYIQQGNGIFGMIFPGCPSTYQEPQESQQR
SEQ ID NO:111 SQRPQDR
SEQ ID NO:112 QQEEENEGSNILSGFAPEFLK
SEQ ID NO:113 EAFGVNMQIVR
SEQ ID NO:114 KPQQEEDDDDEEEQPQCVETDK
SEQ ID NO:115 LSAQYGSLR
SEQ ID NO:116 NAMFVPHYTLNANSIIYALNGR
SEQ ID NO:117 ALVQVVNCNGER
SEQ ID NO:118 VFDGELQEGGVLIVPQNFAVAAK
SEQ ID NO:119 TNDRPSIGNLAGANSLLNALPEEVIQHTFNLK
SEQ ID NO:120 NNNPFSFLVPPQESQR
The feature peptide of the G3 of Gly m 6
SEQ ID NO:121 LVLSLCFLLFSGCCFAFSFR
SEQ ID NO:122 EQPQQNECQIQR
SEQ ID NO:123 QQEEENEGGSILSGFAPEFLEHAFVVDR
SEQ ID NO:124 LQGENEEEEK
SEQ ID NO:125 GGLSVISPPTEEQQQRPEEEEKPDCDEK
SEQ ID NO:126 HCQSQSR
SEQ ID NO:127 LSAQFGSLR
SEQ ID NO:128 VFDGELQEGQVLIVPQNFAVAAR
SEQ ID NO:129 TNDRPSIGNLAGANSLLNALPEEVIQQTFNLR
SEQ ID NO:The G4 consensus sequences of 130 Gly m 6
MGKPFTLSLSSLCLLLLSSACFAISSSKLNECQLNNLNALEPDHRVESEGGLIQTWNSQHPELKCAGVT VSKLTLNRNGLHLPSYSPYPRMIIIAQGKGALGVAIPGCPETFEEPQEQSNRRGSRSQKQQLQDSHQKIRHFNEGDV LVIPPGVPYWTYNTGDEPVVAISLLDTSNFNNQLDQTPRVFYLAGNPDIEYPETMQQQQQQKSHGGRKQGQHQQEEE EEGGSVLSGFSKHFLAQSFNTNEDIAEKLQSPDDERKQIVTVEGGLSVISPKWQEQQDEDEDEDEDDEDEQIPSHP
SEQ ID NO:131 Gly m 6 G4 Ping CAA60533.1 563aa
MGKPFTLSLSSLCLLLLSSACFAISSSKLNECQLNNLNALEPDHRVESEGG LIQTWNSQHPELKCAGVTVSKLTLNRNGLHLPSYSPYPRMIIIAQGKGALGVAIPGCPETFEEPQEQSNRRGSRSQK QQLQDSHQKIRHFNEGDVLVIPPGVPYWTYNTGDEPVVAISLLDTSNFNNQLDQTPRVFYLAGNPDIEYPETMQQQQ QQKSHGGRKQGQHQQEEEEEGGSVLSGFSKHFLAQSFNTNEDIAEKLQSPDDERKQIVTVEGGLSVISPKWQEQQDE DEDEDEDDEDEQIPSHPPRRPSHGKREQDEDEDEDEDKPRPSRPSHGKREQDQDQDEDEDEDEDQPRKSREWRSKKT QPRRPRQEEPRERGCETRNGVEENICTLKLHENIARPSRADFYNPKAGRISTLNSLTLPALRQFQLSAQYVVLYKNG IYSPHWNLNANSVIYVTRGQGKVRVVNCQGNAVFDGELRRGQLLVVPQNFVVAEQAGEQGFEYIVFKTHHNAVTSYL KDVFRAIPSEVLAHSYNLRQSQVSELKYEGNWGPLVNPESQQGSPRVKVA
SEQ ID NO:132 Gly m 6 G4 UniProt Q9SB11 G4 563aa
MGKPFTLSLSSLCLLLLSSACFAISSSKLNECQLNNLNALEPDHRVESEGGLIQTWNSQHPELKCAGVT VSKLTLNRNGLHLPSYSPYPRMIIIAQGKGALGVAIPGCPETFEEPQEQSNRRGSRSQKQQLQDSHQKIRHFNEGDV LVIPPGVPYWTYNTGDEPVVAISLLDTSNFNNQLDQTPRVFYLAGNPDIEYPETMQQQQQQKSHGGRKQGQHQQEEE EEGGSVLSGFSKHFLAQSFNTNEDIAEKLQSPDDERKQIVTVEGGLSVISPKWQEQQDEDEDEDEDDEDEQIPSHPP RRPSHGKREQDEDEDEDEDKPRPSRPSQGKREQDQDQDEDEDEDEDQPRKSREWRSKKTQPRRPRQEEPRERGCETR NGVEENICTLKLHENIARPSRADFYNPKAGRISTLNSLTLPALRQFQLSAQYVVLYKNGIYSPHWNLNANSVIYVTR GQGKVRVVNCQGNAVFDGELRRGQLLVVPQNFVVAEQAGEQGFEYIVFKTHHNAVTSYLKDVFRAIPSEVLAHSYNL RQSQVSELKYEGNWGPLVNPESQQGSPRVKVA
SEQ ID NO:133 Gly m 6 G4 Ping CAA55977.1 517aa
MGKPFFTLSLSSLCLLLLSSACFAITSSKFNECQLNNLNALEPDHRVESEGGLIETWNSQHPELQCAGV TVSKRTLNRNGLHLPSYSPYPQMIIVVQGKGAIGFAFPGCPETFEKPQQQSSRRGSRSQQQLQDSHQKIRHFNEGDV LVIPPGVPYWTYNTGDEPVVAISLLDTSNFNNQLDQNPRVFYLAGNPDIEHPETMQQQQQQKSHGGRKQGQHQQQEE EGGSVLSGFSKHFLAQSFNTNEDTAEKLRSPDDERKQIVTVEGGLSVISPKWQEQEDEDEDEDEEYEQTPSYPPRRP SHGKHEDDEDEDEEEDQPRPDHPPQRPSRPEQQEPRGRGCQTRNGVEENICTMKLHENIARPSRADFYNPKAGRIST LNSLTLPALRQFGLSAQYVVLYRNGIYSPHWNLNANSVIYVTRGKGRVRVVNCQGNAVFDGELRRGQLLVVPQNFVV AEQGGEQGLEYVVFKTHHNAVSSYIKDVFRAIPSEVLSNSYNLGQSQVRQLKYQGNSGPLVNP
SEQ ID NO:134 Gly m 6 G4 Ping AAA33964.1 516aa
MGKPFFTLSLSSLCLLLLSSACFAITSSKFNECQLNNLNALEPDHRVESEGGLIETWNSQHPELQCAGV TVSKRTLNRNGSHLPSYLPYPQMIIVVQGKGAIGFAFPGCPETFEKPQQQSSRRGSRSQQQLQDSHQKIRHFNEGDV LVIPLGVPYWTYNTGDEPVVAISPLDTSNFNNQLDQNPRVFYLAGNPDIEHPETMQQQQQQKSHGGRKQGQHRQQEE EGGSVLSGFSKHFLAQSFNTNEDTAEKLRSPDDERKQIVTVEGGLSVISPKWQEQEDEDEDEDEEYGRTPSYPPRRP SHGKHEDDEDEDEEEDQPRPDHPPQRPSRPEQQEPRGRGCQTRNGVEENICTMKLHENIARPSRADFYNPKAGRIST LNSLTLPALRQFGLSAQYVVLYRNGIYSPDWNLNANSVTMTRGKGRVRVVNCQGNAVFDGELRRGQLLVVPQNPAVA EQGGEQGLEYVVFKTHHNAVSSYIKDVFRVIPSEVLSNSYNLGQSQVRQLKYQGNSGPLVNP
SEQ ID NO:135 LNECQLNNLNALEPDHR
SEQ ID NO:136 CAGVTVSK
SEQ ID NO:137 LTLNR
SEQ ID NO:138 MIIIAQGK
SEQ ID NO:139 GALGVAIPGCPETFEEPQEQSNR
SEQ ID NO:140 QQLQDSHQK
SEQ ID NO:141 VFYLAGNPDIEYPETMQQQQQQK
SEQ ID NO:142 QGQHQQEEEEEGGSVLSGFSK
SEQ ID NO:143 HFLAQSFNTNEDIAEK
SEQ ID NO:144 QIVTVEGGLSVISPK
SEQ ID NO:145 WQEQQDEDEDEDEDDEDEQIPSHPPR
SEQ ID NO:146 RPSHGK
SEQ ID NO:147 EQDEDEDEDEDKPRPSRPSQGK
SEQ ID NO:148 QEEPR
SEQ ID NO:149 NGVEENICTLK
SEQ ID NO:150 LHENIARPSR
SEQ ID NO:151 ISTLNSLTLPALR
SEQ ID NO:152 QFQLSAQYVVLYK
SEQ ID NO:153 NGIYSPHWNLNANSVIYVTR
SEQ ID NO:154 DVFR
SEQ ID NO:155 AIPSEVLAHSYNLR
SEQ ID NO:156 QSQVSELK
SEQ ID NO:58 YEGNWGPLVNPESQQGSPR
The feature peptide of the precursors of Gly m 6
SEQ ID NO:59 GALQCKPGCPETFEEPQEQSNR
SEQ ID NO:60 LQSPDDER
Sequence table
<110>TJ Oman
BW Schaefers
RC Xi Er
G is mono-
<120>For the quantitative method and system with detection of selectivity of allergen
<130> 2971-12517.1PC (76259-WO-PCT)
<160> 156
<170> PatentIn version 3.5
<210> 1
<211> 10
<212> PRT
<213>Artificial sequence
<220>
<223>The example feature peptide of Gly m 1
<400> 1
Ser Tyr Pro Ser Asn Ala Thr Cys Pro Arg
1 5 10
<210> 2
<211> 13
<212> PRT
<213>Manually
<220>
<223>The example feature peptide of Gly m 3
<400> 2
Tyr Met Val Ile Gln Gly Glu Pro Gly Ala Val Ile Arg
1 5 10
<210> 3
<211> 10
<212> PRT
<213>Manually
<220>
<223>The example feature peptide of Gly m 5 (beta- conglycinins)
<400> 3
Asn Ile Leu Glu Ala Ser Tyr Asp Thr Lys
1 5 10
<210> 4
<211> 7
<212> PRT
<213>Manually
<220>
<223>The example feature peptide of Gly m 6 (glycinin) G2
<400> 4
Val Thr Ala Pro Ala Met Arg
1 5
<210> 5
<211> 12
<212> PRT
<213>Manually
<220>
<223>The example feature peptide of Gly m 6 (glycinin) G3
<400> 5
Asn Asn Asn Pro Phe Ser Phe Leu Val Pro Pro Lys
1 5 10
<210> 6
<211> 7
<212> PRT
<213>Manually
<220>
<223>The example feature peptide of Gly m 6 (glycinin) precursor
<400> 6
Ala Asp Phe Tyr Asn Pro Lys
1 5
<210> 7
<211> 11
<212> PRT
<213>Manually
<220>
<223>The example feature peptide of Kunitz trypsin inhibitors 1
<400> 7
Gly Gly Gly Ile Glu Val Asp Ser Thr Gly Lys
1 5 10
<210> 8
<211> 11
<212> PRT
<213>Manually
<220>
<223>The example feature peptide of Kunitz trypsin inhibitors 3
<400> 8
Gly Ile Gly Thr Ile Ile Ser Ser Pro Tyr Arg
1 5 10
<210> 9
<211> 14
<212> PRT
<213>Manually
<220>
<223>The example feature peptide of the K of Gly m Bd 28
<400> 9
Asn Lys Pro Gln Phe Leu Ala Gly Ala Ala Ser Leu Leu Arg
1 5 10
<210> 10
<211> 7
<212> PRT
<213>Manually
<220>
<223>The example feature peptide of the K of Gly m Bd 30
<400> 10
Gly Val Ile Thr Gln Val Lys
1 5
<210> 11
<211> 12
<212> PRT
<213>Manually
<220>
<223>The example feature peptide of Gly m 8 (2S albumin)
<400> 11
Ile Met Glu Asn Gln Ser Glu Glu Leu Glu Glu Lys
1 5 10
<210> 12
<211> 119
<212> PRT
<213>Manually
<220>
<223> Gly m 1 ABA54898.1 [MW= 12482.64 Da]
<400> 12
Met Gly Ser Lys Val Val Ala Ser Val Ala Leu Leu Leu Ser Ile Asn
1 5 10 15
Ile Leu Phe Ile Ser Met Val Ser Ser Ser Ser His Tyr Asp Pro Gln
20 25 30
Pro Gln Pro Ser His Val Thr Ala Leu Ile Thr Arg Pro Ser Cys Pro
35 40 45
Asp Leu Ser Ile Cys Leu Asn Ile Leu Gly Gly Ser Leu Gly Thr Val
50 55 60
Asp Asp Cys Cys Ala Leu Ile Gly Gly Leu Gly Asp Ile Glu Ala Ile
65 70 75 80
Val Cys Leu Cys Ile Gln Leu Arg Ala Leu Gly Ile Leu Asn Leu Asn
85 90 95
Arg Asn Leu Gln Leu Ile Leu Asn Ser Cys Gly Arg Ser Tyr Pro Ser
100 105 110
Asn Ala Thr Cys Pro Arg Thr
115
<210> 13
<211> 131
<212> PRT
<213>Manually
<220>
<223> Gly m 3 CAA11755.1 [MW= 14100.07 Da]
<400> 13
Met Ser Trp Gln Ala Tyr Val Asp Asp His Leu Leu Cys Gly Ile Glu
1 5 10 15
Gly Asn His Leu Thr His Ala Ala Ile Ile Gly Gln Asp Gly Ser Val
20 25 30
Trp Leu Gln Ser Thr Asp Phe Pro Gln Phe Lys Pro Glu Glu Ile Thr
35 40 45
Ala Ile Met Asn Asp Phe Asn Glu Pro Gly Ser Leu Ala Pro Thr Gly
50 55 60
Leu Tyr Leu Gly Gly Thr Lys Tyr Met Val Ile Gln Gly Glu Pro Gly
65 70 75 80
Ala Val Ile Arg Gly Lys Lys Gly Pro Gly Gly Val Thr Val Lys Lys
85 90 95
Thr Gly Ala Ala Leu Ile Ile Gly Ile Tyr Asp Glu Pro Met Thr Pro
100 105 110
Gly Gln Cys Asn Met Val Val Glu Arg Leu Gly Asp Tyr Leu Ile Asp
115 120 125
Gln Gly Tyr
130
<210> 14
<211> 158
<212> PRT
<213>Manually
<220>
<223> Gly m 4 P26987 [MW= 16771.81 Da]
<400> 14
Met Gly Val Phe Thr Phe Glu Asp Glu Ile Asn Ser Pro Val Ala Pro
1 5 10 15
Ala Thr Leu Tyr Lys Ala Leu Val Thr Asp Ala Asp Asn Val Ile Pro
20 25 30
Lys Ala Leu Asp Ser Phe Lys Ser Val Glu Asn Val Glu Gly Asn Gly
35 40 45
Gly Pro Gly Thr Ile Lys Lys Ile Thr Phe Leu Glu Asp Gly Glu Thr
50 55 60
Lys Phe Val Leu His Lys Ile Glu Ser Ile Asp Glu Ala Asn Leu Gly
65 70 75 80
Tyr Ser Tyr Ser Val Val Gly Gly Ala Ala Leu Pro Asp Thr Ala Glu
85 90 95
Lys Ile Thr Phe Asp Ser Lys Leu Val Ala Gly Pro Asn Gly Gly Ser
100 105 110
Ala Gly Lys Leu Thr Val Lys Tyr Glu Thr Lys Gly Asp Ala Glu Pro
115 120 125
Asn Gln Asp Glu Leu Lys Thr Gly Lys Ala Lys Ala Asp Ala Leu Phe
130 135 140
Lys Ala Ile Glu Ala Tyr Leu Leu Ala His Pro Asp Tyr Asn
145 150 155
<210> 15
<211> 605
<212> PRT
<213>Manually
<220>
<223>Gly m 5 (beta- conglycinins) 121281 [Da of MW=70293.13]
<400> 15
Met Met Arg Ala Arg Phe Pro Leu Leu Leu Leu Gly Leu Val Phe Leu
1 5 10 15
Ala Ser Val Ser Val Ser Phe Gly Ile Ala Tyr Trp Glu Lys Glu Asn
20 25 30
Pro Lys His Asn Lys Cys Leu Gln Ser Cys Asn Ser Glu Arg Asp Ser
35 40 45
Tyr Arg Asn Gln Ala Cys His Ala Arg Cys Asn Leu Leu Lys Val Glu
50 55 60
Lys Glu Glu Cys Glu Glu Gly Glu Ile Pro Arg Pro Arg Pro Arg Pro
65 70 75 80
Gln His Pro Glu Arg Glu Pro Gln Gln Pro Gly Glu Lys Glu Glu Asp
85 90 95
Glu Asp Glu Gln Pro Arg Pro Ile Pro Phe Pro Arg Pro Gln Pro Arg
100 105 110
Gln Glu Glu Glu His Glu Gln Arg Glu Glu Gln Glu Trp Pro Arg Lys
115 120 125
Glu Glu Lys Arg Gly Glu Lys Gly Ser Glu Glu Glu Asp Glu Asp Glu
130 135 140
Asp Glu Glu Gln Asp Glu Arg Gln Phe Pro Phe Pro Arg Pro Pro His
145 150 155 160
Gln Lys Glu Glu Arg Asn Glu Glu Glu Asp Glu Asp Glu Glu Gln Gln
165 170 175
Arg Glu Ser Glu Glu Ser Glu Asp Ser Glu Leu Arg Arg His Lys Asn
180 185 190
Lys Asn Pro Phe Leu Phe Gly Ser Asn Arg Phe Glu Thr Leu Phe Lys
195 200 205
Asn Gln Tyr Gly Arg Ile Arg Val Leu Gln Arg Phe Asn Gln Arg Ser
210 215 220
Pro Gln Leu Gln Asn Leu Arg Asp Tyr Arg Ile Leu Glu Phe Asn Ser
225 230 235 240
Lys Pro Asn Thr Leu Leu Leu Pro Asn His Ala Asp Ala Asp Tyr Leu
245 250 255
Ile Val Ile Leu Asn Gly Thr Ala Ile Leu Ser Leu Val Asn Asn Asp
260 265 270
Asp Arg Asp Ser Tyr Arg Leu Gln Ser Gly Asp Ala Leu Arg Val Pro
275 280 285
Ser Gly Thr Thr Tyr Tyr Val Val Asn Pro Asp Asn Asn Glu Asn Leu
290 295 300
Arg Leu Ile Thr Leu Ala Ile Pro Val Asn Lys Pro Gly Arg Phe Glu
305 310 315 320
Ser Phe Phe Leu Ser Ser Thr Glu Ala Gln Gln Ser Tyr Leu Gln Gly
325 330 335
Phe Ser Arg Asn Ile Leu Glu Ala Ser Tyr Asp Thr Lys Phe Glu Glu
340 345 350
Ile Asn Lys Val Leu Phe Ser Arg Glu Glu Gly Gln Gln Gln Gly Glu
355 360 365
Gln Arg Leu Gln Glu Ser Val Ile Val Glu Ile Ser Lys Glu Gln Ile
370 375 380
Arg Ala Leu Ser Lys Arg Ala Lys Ser Ser Ser Arg Lys Thr Ile Ser
385 390 395 400
Ser Glu Asp Lys Pro Phe Asn Leu Arg Ser Arg Asp Pro Ile Tyr Ser
405 410 415
Asn Lys Leu Gly Lys Phe Phe Glu Ile Thr Pro Glu Lys Asn Pro Gln
420 425 430
Leu Arg Asp Leu Asp Ile Phe Leu Ser Ile Val Asp Met Asn Glu Gly
435 440 445
Ala Leu Leu Leu Pro His Phe Asn Ser Lys Ala Ile Val Ile Leu Val
450 455 460
Ile Asn Glu Gly Asp Ala Asn Ile Glu Leu Val Gly Leu Lys Glu Gln
465 470 475 480
Gln Gln Glu Gln Gln Gln Glu Glu Gln Pro Leu Glu Val Arg Lys Tyr
485 490 495
Arg Ala Glu Leu Ser Glu Gln Asp Ile Phe Val Ile Pro Ala Gly Tyr
500 505 510
Pro Val Val Val Asn Ala Thr Ser Asn Leu Asn Phe Phe Ala Ile Gly
515 520 525
Ile Asn Ala Glu Asn Asn Gln Arg Asn Phe Leu Ala Gly Ser Gln Asp
530 535 540
Asn Val Ile Ser Gln Ile Pro Ser Gln Val Gln Glu Leu Ala Phe Pro
545 550 555 560
Gly Ser Ala Gln Ala Val Glu Lys Leu Leu Lys Asn Gln Arg Glu Ser
565 570 575
Tyr Phe Val Asp Ala Gln Pro Lys Lys Lys Glu Glu Gly Asn Lys Gly
580 585 590
Arg Lys Gly Pro Leu Ser Ser Ile Leu Arg Ala Phe Tyr
595 600 605
<210> 16
<211> 495
<212> PRT
<213>Manually
<220>
<223>The glycinin G1 121276 [Da of MW=55706.34] of Gly m 6
<400> 16
Met Ala Lys Leu Val Phe Ser Leu Cys Phe Leu Leu Phe Ser Gly Cys
1 5 10 15
Cys Phe Ala Phe Ser Ser Arg Glu Gln Pro Gln Gln Asn Glu Cys Gln
20 25 30
Ile Gln Lys Leu Asn Ala Leu Lys Pro Asp Asn Arg Ile Glu Ser Glu
35 40 45
Gly Gly Leu Ile Glu Thr Trp Asn Pro Asn Asn Lys Pro Phe Gln Cys
50 55 60
Ala Gly Val Ala Leu Ser Arg Cys Thr Leu Asn Arg Asn Ala Leu Arg
65 70 75 80
Arg Pro Ser Tyr Thr Asn Gly Pro Gln Glu Ile Tyr Ile Gln Gln Gly
85 90 95
Lys Gly Ile Phe Gly Met Ile Tyr Pro Gly Cys Pro Ser Thr Phe Glu
100 105 110
Glu Pro Gln Gln Pro Gln Gln Arg Gly Gln Ser Ser Arg Pro Gln Asp
115 120 125
Arg His Gln Lys Ile Tyr Asn Phe Arg Glu Gly Asp Leu Ile Ala Val
130 135 140
Pro Thr Gly Val Ala Trp Trp Met Tyr Asn Asn Glu Asp Thr Pro Val
145 150 155 160
Val Ala Val Ser Ile Ile Asp Thr Asn Ser Leu Glu Asn Gln Leu Asp
165 170 175
Gln Met Pro Arg Arg Phe Tyr Leu Ala Gly Asn Gln Glu Gln Glu Phe
180 185 190
Leu Lys Tyr Gln Gln Glu Gln Gly Gly His Gln Ser Gln Lys Gly Lys
195 200 205
His Gln Gln Glu Glu Glu Asn Glu Gly Gly Ser Ile Leu Ser Gly Phe
210 215 220
Thr Leu Glu Phe Leu Glu His Ala Phe Ser Val Asp Lys Gln Ile Ala
225 230 235 240
Lys Asn Leu Gln Gly Glu Asn Glu Gly Glu Asp Lys Gly Ala Ile Val
245 250 255
Thr Val Lys Gly Gly Leu Ser Val Ile Lys Pro Pro Thr Asp Glu Gln
260 265 270
Gln Gln Arg Pro Gln Glu Glu Glu Glu Glu Glu Glu Asp Glu Lys Pro
275 280 285
Gln Cys Lys Gly Lys Asp Lys His Cys Gln Arg Pro Arg Gly Ser Gln
290 295 300
Ser Lys Ser Arg Arg Asn Gly Ile Asp Glu Thr Ile Cys Thr Met Arg
305 310 315 320
Leu Arg His Asn Ile Gly Gln Thr Ser Ser Pro Asp Ile Tyr Asn Pro
325 330 335
Gln Ala Gly Ser Val Thr Thr Ala Thr Ser Leu Asp Phe Pro Ala Leu
340 345 350
Ser Trp Leu Arg Leu Ser Ala Glu Phe Gly Ser Leu Arg Lys Asn Ala
355 360 365
Met Phe Val Pro His Tyr Asn Leu Asn Ala Asn Ser Ile Ile Tyr Ala
370 375 380
Leu Asn Gly Arg Ala Leu Ile Gln Val Val Asn Cys Asn Gly Glu Arg
385 390 395 400
Val Phe Asp Gly Glu Leu Gln Glu Gly Arg Val Leu Ile Val Pro Gln
405 410 415
Asn Phe Val Val Ala Ala Arg Ser Gln Ser Asp Asn Phe Glu Tyr Val
420 425 430
Ser Phe Lys Thr Asn Asp Thr Pro Met Ile Gly Thr Leu Ala Gly Ala
435 440 445
Asn Ser Leu Leu Asn Ala Leu Pro Glu Glu Val Ile Gln His Thr Phe
450 455 460
Asn Leu Lys Ser Gln Gln Ala Arg Gln Ile Lys Asn Asn Asn Pro Phe
465 470 475 480
Lys Phe Leu Val Pro Pro Gln Glu Ser Gln Lys Arg Ala Val Ala
485 490 495
<210> 17
<211> 485
<212> PRT
<213>Manually
<220>
<223>The glycinin G2 121277 [Da of MW=54390.76] of Gly m 6
<400> 17
Met Ala Lys Leu Val Leu Ser Leu Cys Phe Leu Leu Phe Ser Gly Cys
1 5 10 15
Phe Ala Leu Arg Glu Gln Ala Gln Gln Asn Glu Cys Gln Ile Gln Lys
20 25 30
Leu Asn Ala Leu Lys Pro Asp Asn Arg Ile Glu Ser Glu Gly Gly Phe
35 40 45
Ile Glu Thr Trp Asn Pro Asn Asn Lys Pro Phe Gln Cys Ala Gly Val
50 55 60
Ala Leu Ser Arg Cys Thr Leu Asn Arg Asn Ala Leu Arg Arg Pro Ser
65 70 75 80
Tyr Thr Asn Gly Pro Gln Glu Ile Tyr Ile Gln Gln Gly Asn Gly Ile
85 90 95
Phe Gly Met Ile Phe Pro Gly Cys Pro Ser Thr Tyr Gln Glu Pro Gln
100 105 110
Glu Ser Gln Gln Arg Gly Arg Ser Gln Arg Pro Gln Asp Arg His Gln
115 120 125
Lys Val His Arg Phe Arg Glu Gly Asp Leu Ile Ala Val Pro Thr Gly
130 135 140
Val Ala Trp Trp Met Tyr Asn Asn Glu Asp Thr Pro Val Val Ala Val
145 150 155 160
Ser Ile Ile Asp Thr Asn Ser Leu Glu Asn Gln Leu Asp Gln Met Pro
165 170 175
Arg Arg Phe Tyr Leu Ala Gly Asn Gln Glu Gln Glu Phe Leu Lys Tyr
180 185 190
Gln Gln Gln Gln Gln Gly Gly Ser Gln Ser Gln Lys Gly Lys Gln Gln
195 200 205
Glu Glu Glu Asn Glu Gly Ser Asn Ile Leu Ser Gly Phe Ala Pro Glu
210 215 220
Phe Leu Lys Glu Ala Phe Gly Val Asn Met Gln Ile Val Arg Asn Leu
225 230 235 240
Gln Gly Glu Asn Glu Glu Glu Asp Ser Gly Ala Ile Val Thr Val Lys
245 250 255
Gly Gly Leu Arg Val Thr Ala Pro Ala Met Arg Lys Pro Gln Gln Glu
260 265 270
Glu Asp Asp Asp Asp Glu Glu Glu Gln Pro Gln Cys Val Glu Thr Asp
275 280 285
Lys Gly Cys Gln Arg Gln Ser Lys Arg Ser Arg Asn Gly Ile Asp Glu
290 295 300
Thr Ile Cys Thr Met Arg Leu Arg Gln Asn Ile Gly Gln Asn Ser Ser
305 310 315 320
Pro Asp Ile Tyr Asn Pro Gln Ala Gly Ser Ile Thr Thr Ala Thr Ser
325 330 335
Leu Asp Phe Pro Ala Leu Trp Leu Leu Lys Leu Ser Ala Gln Tyr Gly
340 345 350
Ser Leu Arg Lys Asn Ala Met Phe Val Pro His Tyr Thr Leu Asn Ala
355 360 365
Asn Ser Ile Ile Tyr Ala Leu Asn Gly Arg Ala Leu Val Gln Val Val
370 375 380
Asn Cys Asn Gly Glu Arg Val Phe Asp Gly Glu Leu Gln Glu Gly Gly
385 390 395 400
Val Leu Ile Val Pro Gln Asn Phe Ala Val Ala Ala Lys Ser Gln Ser
405 410 415
Asp Asn Phe Glu Tyr Val Ser Phe Lys Thr Asn Asp Arg Pro Ser Ile
420 425 430
Gly Asn Leu Ala Gly Ala Asn Ser Leu Leu Asn Ala Leu Pro Glu Glu
435 440 445
Val Ile Gln His Thr Phe Asn Leu Lys Ser Gln Gln Ala Arg Gln Val
450 455 460
Lys Asn Asn Asn Pro Phe Ser Phe Leu Val Pro Pro Gln Glu Ser Gln
465 470 475 480
Arg Arg Ala Val Ala
485
<210> 18
<211> 481
<212> PRT
<213>Manually
<220>
<223>The glycinin G3 121278 [Da of MW=54241.73] of Gly m 6
<400> 18
Met Ala Lys Leu Val Leu Ser Leu Cys Phe Leu Leu Phe Ser Gly Cys
1 5 10 15
Cys Phe Ala Phe Ser Phe Arg Glu Gln Pro Gln Gln Asn Glu Cys Gln
20 25 30
Ile Gln Arg Leu Asn Ala Leu Lys Pro Asp Asn Arg Ile Glu Ser Glu
35 40 45
Gly Gly Phe Ile Glu Thr Trp Asn Pro Asn Asn Lys Pro Phe Gln Cys
50 55 60
Ala Gly Val Ala Leu Ser Arg Cys Thr Leu Asn Arg Asn Ala Leu Arg
65 70 75 80
Arg Pro Ser Tyr Thr Asn Ala Pro Gln Glu Ile Tyr Ile Gln Gln Gly
85 90 95
Ser Gly Ile Phe Gly Met Ile Phe Pro Gly Cys Pro Ser Thr Phe Glu
100 105 110
Glu Pro Gln Gln Lys Gly Gln Ser Ser Arg Pro Gln Asp Arg His Gln
115 120 125
Lys Ile Tyr His Phe Arg Glu Gly Asp Leu Ile Ala Val Pro Thr Gly
130 135 140
Phe Ala Tyr Trp Met Tyr Asn Asn Glu Asp Thr Pro Val Val Ala Val
145 150 155 160
Ser Leu Ile Asp Thr Asn Ser Phe Gln Asn Gln Leu Asp Gln Met Pro
165 170 175
Arg Arg Phe Tyr Leu Ala Gly Asn Gln Glu Gln Glu Phe Leu Gln Tyr
180 185 190
Gln Pro Gln Lys Gln Gln Gly Gly Thr Gln Ser Gln Lys Gly Lys Arg
195 200 205
Gln Gln Glu Glu Glu Asn Glu Gly Gly Ser Ile Leu Ser Gly Phe Ala
210 215 220
Pro Glu Phe Leu Glu His Ala Phe Val Val Asp Arg Gln Ile Val Arg
225 230 235 240
Lys Leu Gln Gly Glu Asn Glu Glu Glu Glu Lys Gly Ala Ile Val Thr
245 250 255
Val Lys Gly Gly Leu Ser Val Ile Ser Pro Pro Thr Glu Glu Gln Gln
260 265 270
Gln Arg Pro Glu Glu Glu Glu Lys Pro Asp Cys Asp Glu Lys Asp Lys
275 280 285
His Cys Gln Ser Gln Ser Arg Asn Gly Ile Asp Glu Thr Ile Cys Thr
290 295 300
Met Arg Leu Arg His Asn Ile Gly Gln Thr Ser Ser Pro Asp Ile Phe
305 310 315 320
Asn Pro Gln Ala Gly Ser Ile Thr Thr Ala Thr Ser Leu Asp Phe Pro
325 330 335
Ala Leu Ser Trp Leu Lys Leu Ser Ala Gln Phe Gly Ser Leu Arg Lys
340 345 350
Asn Ala Met Phe Val Pro His Tyr Asn Leu Asn Ala Asn Ser Ile Ile
355 360 365
Tyr Ala Leu Asn Gly Arg Ala Leu Val Gln Val Val Asn Cys Asn Gly
370 375 380
Glu Arg Val Phe Asp Gly Glu Leu Gln Glu Gly Gln Val Leu Ile Val
385 390 395 400
Pro Gln Asn Phe Ala Val Ala Ala Arg Ser Gln Ser Asp Asn Phe Glu
405 410 415
Tyr Val Ser Phe Lys Thr Asn Asp Arg Pro Ser Ile Gly Asn Leu Ala
420 425 430
Gly Ala Asn Ser Leu Leu Asn Ala Leu Pro Glu Glu Val Ile Gln Gln
435 440 445
Thr Phe Asn Leu Arg Arg Gln Gln Ala Arg Gln Val Lys Asn Asn Asn
450 455 460
Pro Phe Ser Phe Leu Val Pro Pro Lys Glu Ser Gln Arg Arg Val Val
465 470 475 480
Ala
<210> 19
<211> 562
<212> PRT
<213>Manually
<220>
<223>The glycinin G4 121279 [Da of MW=63587.16] of Gly m 6
<400> 19
Met Gly Lys Pro Phe Thr Leu Ser Leu Ser Ser Leu Cys Leu Leu Leu
1 5 10 15
Leu Ser Ser Ala Cys Phe Ala Ile Ser Ser Ser Lys Leu Asn Glu Cys
20 25 30
Gln Leu Asn Asn Leu Asn Ala Leu Glu Pro Asp His Arg Val Glu Ser
35 40 45
Glu Gly Gly Leu Ile Gln Thr Trp Asn Ser Gln His Pro Glu Leu Lys
50 55 60
Cys Ala Gly Val Thr Val Ser Lys Leu Thr Leu Asn Arg Asn Gly Leu
65 70 75 80
His Ser Pro Ser Tyr Ser Pro Tyr Pro Arg Met Ile Ile Ile Ala Gln
85 90 95
Gly Lys Gly Ala Leu Gly Val Ala Ile Pro Gly Cys Pro Glu Thr Phe
100 105 110
Glu Glu Pro Gln Glu Gln Ser Asn Arg Arg Gly Ser Arg Ser Gln Lys
115 120 125
Gln Gln Leu Gln Asp Ser His Gln Lys Ile Arg His Phe Asn Glu Gly
130 135 140
Asp Val Leu Val Ile Pro Pro Ser Val Pro Tyr Trp Thr Tyr Asn Thr
145 150 155 160
Gly Asp Glu Pro Val Val Ala Ile Ser Leu Leu Asp Thr Ser Asn Phe
165 170 175
Asn Asn Gln Leu Asp Gln Thr Pro Arg Val Phe Tyr Leu Ala Gly Asn
180 185 190
Pro Asp Ile Glu Tyr Pro Glu Thr Met Gln Gln Gln Gln Gln Gln Lys
195 200 205
Ser His Gly Gly Arg Lys Gln Gly Gln His Gln Gln Glu Glu Glu Glu
210 215 220
Glu Gly Gly Ser Val Leu Ser Gly Phe Ser Lys His Phe Leu Ala Gln
225 230 235 240
Ser Phe Asn Thr Asn Glu Asp Ile Ala Glu Lys Leu Glu Ser Pro Asp
245 250 255
Asp Glu Arg Lys Gln Ile Val Thr Val Glu Gly Gly Leu Ser Val Ile
260 265 270
Ser Pro Lys Trp Gln Glu Gln Gln Asp Glu Asp Glu Asp Glu Asp Glu
275 280 285
Asp Asp Glu Asp Glu Gln Ile Pro Ser His Pro Pro Arg Arg Pro Ser
290 295 300
His Gly Lys Arg Glu Gln Asp Glu Asp Glu Asp Glu Asp Glu Asp Lys
305 310 315 320
Pro Arg Pro Ser Arg Pro Ser Gln Gly Lys Arg Asn Lys Thr Gly Gln
325 330 335
Asp Glu Asp Glu Asp Glu Asp Glu Asp Gln Pro Arg Lys Ser Arg Glu
340 345 350
Trp Arg Ser Lys Lys Thr Gln Pro Arg Arg Pro Arg Gln Glu Glu Pro
355 360 365
Arg Glu Arg Gly Cys Glu Thr Arg Asn Gly Val Glu Glu Asn Ile Cys
370 375 380
Thr Leu Lys Leu His Glu Asn Ile Ala Arg Pro Ser Arg Ala Asp Phe
385 390 395 400
Tyr Asn Pro Lys Ala Gly Arg Ile Ser Thr Leu Asn Ser Leu Thr Leu
405 410 415
Pro Ala Leu Arg Gln Phe Gln Leu Ser Ala Gln Tyr Val Val Leu Tyr
420 425 430
Lys Asn Gly Ile Tyr Ser Pro His Trp Asn Leu Asn Ala Asn Ser Val
435 440 445
Ile Tyr Val Thr Arg Gly Gln Gly Lys Val Arg Val Val Asn Cys Gln
450 455 460
Gly Asn Ala Val Phe Asp Gly Glu Leu Arg Arg Gly Gln Leu Leu Val
465 470 475 480
Val Pro Gln Asn Phe Val Val Ala Glu Gln Ala Gly Glu Gln Gly Phe
485 490 495
Glu Tyr Ile Val Phe Lys Thr His His Asn Ala Val Thr Ser Tyr Leu
500 505 510
Lys Asp Val Phe Arg Ala Ile Pro Ser Glu Val Leu Ala His Ser Tyr
515 520 525
Asn Leu Arg Gln Ser Gln Val Ser Glu Leu Lys Tyr Glu Gly Asn Trp
530 535 540
Gly Pro Leu Val Asn Pro Glu Ser Gln Gln Gly Ser Pro Arg Val Lys
545 550 555 560
Val Ala
<210> 20
<211> 562
<212> PRT
<213>Manually
<220>
<223>The glycinin precursors 75221455 [Da of MW=63876.47] of Gly m 6
<400> 20
Met Gly Lys Pro Phe Thr Leu Ser Leu Ser Ser Leu Cys Leu Leu Leu
1 5 10 15
Leu Ser Ser Ala Cys Phe Ala Ile Ser Ser Ser Lys Leu Asn Glu Cys
20 25 30
Gln Leu Asn Asn Leu Asn Ala Leu Glu Pro Asp His Arg Val Glu Phe
35 40 45
Glu Gly Gly Leu Ile Gln Thr Trp Asn Ser Gln His Pro Glu Leu Lys
50 55 60
Cys Ala Gly Val Thr Val Ser Lys Leu Thr Leu Asn Arg Asn Gly Leu
65 70 75 80
His Leu Pro Ser Tyr Ser Pro Tyr Pro Arg Met Ile Ile Ile Ala Gln
85 90 95
Gly Lys Gly Ala Leu Gln Cys Lys Pro Gly Cys Pro Glu Thr Phe Glu
100 105 110
Glu Pro Gln Glu Gln Ser Asn Arg Arg Gly Ser Arg Ser Gln Lys Gln
115 120 125
Gln Leu Gln Asp Ser His Gln Lys Ile Arg His Phe Asn Glu Gly Asp
130 135 140
Val Leu Val Ile Pro Pro Gly Val Pro Tyr Trp Thr Tyr Asn Thr Gly
145 150 155 160
Asp Glu Pro Val Val Ala Ile Ser Leu Leu Asp Thr Ser Asn Phe Asn
165 170 175
Asn Gln Leu Asp Gln Thr Pro Arg Val Phe Tyr Leu Ala Gly Asn Pro
180 185 190
Asp Ile Glu Tyr Pro Glu Thr Met Gln Gln Gln Gln Gln Gln Lys Ser
195 200 205
His Gly Gly Arg Lys Gln Gly Gln His Gln Gln Glu Glu Glu Glu Glu
210 215 220
Gly Gly Ser Val Leu Ser Gly Phe Ser Lys His Phe Leu Ala Gln Ser
225 230 235 240
Phe Asn Thr Asn Glu Asp Ile Ala Glu Lys Leu Gln Ser Pro Asp Asp
245 250 255
Glu Arg Lys Gln Ile Val Thr Val Glu Gly Gly Leu Ser Val Ile Ser
260 265 270
Pro Lys Trp Gln Glu Gln Gln Asp Glu Asp Glu Asp Glu Asp Glu Asp
275 280 285
Asp Glu Asp Glu Gln Ile Pro Ser His Pro Pro Arg Arg Pro Ser His
290 295 300
Gly Lys Arg Glu Gln Asp Glu Asp Glu Asp Glu Asp Glu Asp Lys Pro
305 310 315 320
Arg Pro Ser Arg Pro Ser Gln Gly Lys Arg Glu Gln Asp Gln Asp Gln
325 330 335
Asp Glu Asp Glu Asp Glu Asp Glu Asp Gln Pro Arg Lys Ser Arg Glu
340 345 350
Trp Arg Ser Lys Lys Thr Gln Pro Arg Arg Pro Arg Gln Glu Glu Pro
355 360 365
Arg Glu Arg Gly Cys Glu Thr Arg Asn Gly Val Glu Glu Asn Ile Cys
370 375 380
Thr Leu Lys Leu His Glu Asn Ile Ala Arg Pro Ser Arg Ala Asp Phe
385 390 395 400
Tyr Asn Pro Lys Ala Gly Arg Ile Ser Thr Leu Asn Ser Leu Thr Leu
405 410 415
Pro Ala Leu Arg Gln Phe Gln Leu Ser Ala Gln Tyr Val Val Leu Tyr
420 425 430
Lys Asn Gly Ile Tyr Ser Pro His Trp Asn Leu Asn Ala Asn Ser Val
435 440 445
Ile Tyr Val Thr Arg Gly Gln Gly Lys Val Arg Val Val Asn Cys Gln
450 455 460
Gly Asn Ala Val Phe Asp Gly Glu Leu Arg Arg Gly Gln Leu Leu Val
465 470 475 480
Val Pro Gln Asn Phe Val Val Ala Glu Gln Ala Gly Glu Gln Gly Phe
485 490 495
Glu Tyr Ile Val Phe Lys Thr His His Asn Ala Val Thr Ser Tyr Leu
500 505 510
Lys Asp Val Phe Arg Ala Ile Pro Ser Glu Val Leu Ala His Ser Tyr
515 520 525
Asn Leu Arg Gln Ser Gln Val Ser Glu Leu Lys Tyr Glu Gly Asn Trp
530 535 540
Gly Pro Leu Val Asn Pro Glu Ser Gln Gln Gly Ser Pro Arg Val Lys
545 550 555 560
Val Ala
<210> 21
<211> 476
<212> PRT
<213>Manually
<220>
<223> Gly m Bd 28K 12697782 [MW= 52944.36 Da]
<400> 21
Met Gly Asn Lys Thr Thr Leu Leu Leu Leu Leu Phe Val Leu Cys His
1 5 10 15
Gly Val Ala Thr Thr Thr Met Ala Phe His Asp Asp Glu Gly Gly Asp
20 25 30
Lys Lys Ser Pro Lys Ser Leu Phe Leu Met Ser Asn Ser Thr Arg Val
35 40 45
Phe Lys Thr Asp Ala Gly Glu Met Arg Val Leu Lys Ser His Gly Gly
50 55 60
Arg Ile Phe Tyr Arg His Met His Ile Gly Phe Ile Ser Met Glu Pro
65 70 75 80
Lys Ser Leu Phe Val Pro Gln Tyr Leu Asp Ser Asn Leu Ile Ile Phe
85 90 95
Ile Arg Arg Gly Glu Ala Lys Leu Gly Phe Ile Tyr Asp Asp Glu Leu
100 105 110
Ala Glu Arg Arg Leu Lys Thr Gly Asp Leu Tyr Met Ile Pro Ser Gly
115 120 125
Ser Ala Phe Tyr Leu Val Asn Ile Gly Glu Gly Gln Arg Leu His Val
130 135 140
Ile Cys Ser Ile Asp Pro Ser Thr Ser Leu Gly Leu Glu Thr Phe Gln
145 150 155 160
Ser Phe Tyr Ile Gly Gly Gly Ala Asn Ser His Ser Val Leu Ser Gly
165 170 175
Phe Glu Pro Ala Ile Leu Glu Thr Ala Phe Asn Glu Ser Arg Thr Val
180 185 190
Val Glu Glu Ile Phe Ser Lys Glu Leu Asp Gly Pro Ile Met Phe Val
195 200 205
Asp Asp Ser His Ala Pro Ser Leu Trp Thr Lys Phe Leu Gln Leu Lys
210 215 220
Lys Asp Asp Lys Glu Gln Gln Leu Lys Lys Met Met Gln Asp Gln Glu
225 230 235 240
Glu Asp Glu Glu Glu Lys Gln Thr Ser Arg Ser Trp Arg Lys Leu Leu
245 250 255
Glu Thr Val Phe Gly Lys Val Asn Glu Lys Ile Glu Asn Lys Asp Thr
260 265 270
Ala Gly Ser Pro Ala Ser Tyr Asn Leu Tyr Asp Asp Lys Lys Ala Asp
275 280 285
Phe Lys Asn Ala Tyr Gly Trp Ser Lys Ala Leu His Gly Gly Glu Tyr
290 295 300
Pro Pro Leu Ser Glu Pro Asp Ile Gly Val Leu Leu Val Lys Leu Ser
305 310 315 320
Ala Gly Ser Met Leu Ala Pro His Val Asn Pro Ile Ser Asp Glu Tyr
325 330 335
Thr Ile Val Leu Ser Gly Tyr Gly Glu Leu His Ile Gly Tyr Pro Asn
340 345 350
Gly Ser Arg Ala Met Lys Thr Lys Ile Lys Gln Gly Asp Val Phe Val
355 360 365
Val Pro Arg Tyr Phe Pro Phe Cys Gln Val Ala Ser Arg Asp Gly Pro
370 375 380
Leu Glu Phe Phe Gly Phe Ser Thr Ser Ala Arg Lys Asn Lys Pro Gln
385 390 395 400
Phe Leu Ala Gly Ala Ala Ser Leu Leu Arg Thr Leu Met Gly Pro Glu
405 410 415
Leu Ser Ala Ala Phe Gly Val Ser Glu Asp Thr Leu Arg Arg Ala Val
420 425 430
Asp Ala Gln His Glu Ala Val Ile Leu Pro Ser Ala Trp Ala Ala Pro
435 440 445
Pro Glu Asn Ala Gly Lys Leu Lys Met Glu Glu Glu Pro Asn Ala Ile
450 455 460
Arg Ser Phe Ala Asn Asp Val Val Met Asp Val Phe
465 470 475
<210> 22
<211> 379
<212> PRT
<213>Manually
<220>
<223> Gly m Bd 30K 84371705 [MW= 42757.81 Da]
<400> 22
Met Gly Phe Leu Val Leu Leu Leu Phe Ser Leu Leu Gly Leu Ser Ser
1 5 10 15
Ser Ser Ser Ile Ser Thr His Arg Ser Ile Leu Asp Leu Asp Leu Thr
20 25 30
Lys Phe Thr Thr Gln Lys Gln Val Ser Ser Leu Phe Gln Leu Trp Lys
35 40 45
Ser Glu His Gly Arg Val Tyr His Asn His Glu Glu Glu Ala Lys Arg
50 55 60
Leu Glu Ile Phe Lys Asn Asn Leu Asn Tyr Ile Arg Asp Met Asn Ala
65 70 75 80
Asn Arg Lys Ser Pro His Ser His Arg Leu Gly Leu Asn Lys Phe Ala
85 90 95
Asp Ile Thr Pro Gln Glu Phe Ser Lys Lys Tyr Leu Gln Ala Pro Lys
100 105 110
Asp Val Ser Gln Gln Ile Lys Met Ala Asn Lys Lys Met Lys Lys Glu
115 120 125
Gln Tyr Ser Cys Asp His Pro Pro Ala Ser Trp Asp Trp Arg Lys Lys
130 135 140
Gly Val Ile Thr Gln Val Lys Tyr Gln Gly Gly Cys Gly Ser Gly Trp
145 150 155 160
Ala Phe Ser Ala Thr Gly Ala Ile Glu Ala Ala His Ala Ile Ala Thr
165 170 175
Gly Asp Leu Val Ser Leu Ser Glu Gln Glu Leu Val Asp Cys Val Glu
180 185 190
Glu Ser Glu Gly Cys Tyr Asn Gly Trp His Tyr Gln Ser Phe Glu Trp
195 200 205
Val Leu Glu His Gly Gly Ile Ala Thr Asp Asp Asp Tyr Pro Tyr Arg
210 215 220
Ala Lys Glu Gly Arg Cys Lys Ala Asn Lys Ile Gln Asp Lys Val Thr
225 230 235 240
Ile Asp Gly Tyr Glu Thr Leu Ile Met Ser Asp Glu Ser Thr Glu Ser
245 250 255
Glu Thr Glu Gln Ala Phe Leu Ser Ala Ile Leu Glu Gln Pro Ile Ser
260 265 270
Val Ser Ile Asp Ala Lys Asp Phe His Leu Tyr Thr Gly Gly Ile Tyr
275 280 285
Asp Gly Glu Asn Cys Thr Ser Pro Tyr Gly Ile Asn His Phe Val Leu
290 295 300
Leu Val Gly Tyr Gly Ser Ala Asp Gly Val Asp Tyr Trp Ile Ala Lys
305 310 315 320
Asn Ser Trp Gly Glu Asp Trp Gly Glu Asp Gly Tyr Ile Trp Ile Gln
325 330 335
Arg Asn Thr Gly Asn Leu Leu Gly Val Cys Gly Met Asn Tyr Phe Ala
340 345 350
Ser Tyr Pro Thr Lys Glu Glu Ser Glu Thr Leu Val Ser Ala Arg Val
355 360 365
Lys Gly His Arg Arg Val Asp His Ser Pro Leu
370 375
<210> 23
<211> 203
<212> PRT
<213>Manually
<220>
<223> KTI 1 125722 [MW= 22545.94 Da]
<400> 23
Met Lys Ser Thr Ile Phe Phe Ala Leu Phe Leu Val Cys Ala Phe Thr
1 5 10 15
Ile Ser Tyr Leu Pro Ser Ala Thr Ala Gln Phe Val Leu Asp Thr Asp
20 25 30
Asp Asp Pro Leu Gln Asn Gly Gly Thr Tyr Tyr Met Leu Pro Val Met
35 40 45
Arg Gly Lys Gly Gly Gly Ile Glu Val Asp Ser Thr Gly Lys Glu Ile
50 55 60
Cys Pro Leu Thr Val Val Gln Ser Pro Asn Glu Leu Asp Lys Gly Ile
65 70 75 80
Gly Leu Val Phe Thr Ser Pro Leu His Ala Leu Phe Ile Ala Glu Arg
85 90 95
Tyr Pro Leu Ser Ile Lys Phe Gly Ser Phe Ala Val Ile Thr Leu Cys
100 105 110
Ala Gly Met Pro Thr Glu Trp Ala Ile Val Glu Arg Glu Gly Leu Gln
115 120 125
Ala Val Lys Leu Ala Ala Arg Asp Thr Val Asp Gly Trp Phe Asn Ile
130 135 140
Glu Arg Val Ser Arg Glu Tyr Asn Asp Tyr Lys Leu Val Phe Cys Pro
145 150 155 160
Gln Gln Ala Glu Asp Asn Lys Cys Glu Asp Ile Gly Ile Gln Ile Asp
165 170 175
Asp Asp Gly Ile Arg Arg Leu Val Leu Ser Lys Asn Lys Pro Leu Val
180 185 190
Val Gln Phe Gln Lys Phe Arg Ser Ser Thr Ala
195 200
<210> 24
<211> 216
<212> PRT
<213>Manually
<220>
<223> KTI 3 125020 [ MW= 24005.29 Da]
<400> 24
Met Lys Ser Thr Ile Phe Phe Leu Phe Leu Phe Cys Ala Phe Thr Thr
1 5 10 15
Ser Tyr Leu Pro Ser Ala Ile Ala Asp Phe Val Leu Asp Asn Glu Gly
20 25 30
Asn Pro Leu Glu Asn Gly Gly Thr Tyr Tyr Ile Leu Ser Asp Ile Thr
35 40 45
Ala Phe Gly Gly Ile Arg Ala Ala Pro Thr Gly Asn Glu Arg Cys Pro
50 55 60
Leu Thr Val Val Gln Ser Arg Asn Glu Leu Asp Lys Gly Ile Gly Thr
65 70 75 80
Ile Ile Ser Ser Pro Tyr Arg Ile Arg Phe Ile Ala Glu Gly His Pro
85 90 95
Leu Ser Leu Lys Phe Asp Ser Phe Ala Val Ile Met Leu Cys Val Gly
100 105 110
Ile Pro Thr Glu Trp Ser Val Val Glu Asp Leu Pro Glu Gly Pro Ala
115 120 125
Val Lys Ile Gly Glu Asn Lys Asp Ala Met Asp Gly Trp Phe Arg Leu
130 135 140
Glu Arg Val Ser Asp Asp Glu Phe Asn Asn Tyr Lys Leu Val Phe Cys
145 150 155 160
Pro Gln Gln Ala Glu Asp Asp Lys Cys Gly Asp Ile Gly Ile Ser Ile
165 170 175
Asp His Asp Asp Gly Thr Arg Arg Leu Val Val Ser Lys Asn Lys Pro
180 185 190
Leu Val Val Gln Phe Gln Lys Leu Asp Lys Glu Ser Leu Ala Lys Lys
195 200 205
Asn His Gly Leu Ser Arg Ser Glu
210 215
<210> 25
<211> 158
<212> PRT
<213>Manually
<220>
<223>Gly m 8 (2S albumin) NP_001238443 [Da of MW=18459.97]
<400> 25
Met Thr Lys Phe Thr Ile Leu Leu Ile Ser Leu Leu Phe Cys Ile Ala
1 5 10 15
His Thr Cys Ser Ala Ser Lys Trp Gln His Gln Gln Asp Ser Cys Arg
20 25 30
Lys Gln Leu Gln Gly Val Asn Leu Thr Pro Cys Glu Lys His Ile Met
35 40 45
Glu Lys Ile Gln Gly Arg Gly Asp Asp Asp Asp Asp Asp Asp Asp Asp
50 55 60
Asn His Ile Leu Arg Thr Met Arg Gly Arg Ile Asn Tyr Ile Arg Arg
65 70 75 80
Asn Glu Gly Lys Asp Glu Asp Glu Glu Glu Glu Gly His Met Gln Lys
85 90 95
Cys Cys Thr Glu Met Ser Glu Leu Arg Ser Pro Lys Cys Gln Cys Lys
100 105 110
Ala Leu Gln Lys Ile Met Glu Asn Gln Ser Glu Glu Leu Glu Glu Lys
115 120 125
Gln Lys Lys Lys Met Glu Lys Glu Leu Ile Asn Leu Ala Thr Met Cys
130 135 140
Arg Phe Gly Pro Met Ile Gln Cys Asp Leu Ser Ser Asp Asp
145 150 155
<210> 26
<211> 280
<212> PRT
<213>Manually
<220>
<223>Agglutinin ADC94422 [Da of MW=30186.22]
<400> 26
Met Ala Thr Ser Asn Phe Ser Ile Val Leu Ser Leu Ser Leu Ala Phe
1 5 10 15
Phe Leu Val Leu Leu Thr Lys Ala Asn Ser Thr Asn Thr Val Ser Phe
20 25 30
Thr Val Ser Lys Phe Ser Pro Arg Gln Gln Asn Leu Ile Phe Gln Gly
35 40 45
Asp Ala Ala Ile Ser Pro Ser Gly Val Leu Arg Leu Thr Lys Val Asp
50 55 60
Ser Ile Asp Val Pro Thr Thr Gly Ser Leu Gly Arg Ala Leu Tyr Ala
65 70 75 80
Thr Pro Ile Gln Ile Trp Asp Ser Glu Thr Gly Lys Val Ala Ser Trp
85 90 95
Ala Thr Ser Phe Lys Phe Lys Val Phe Ser Pro Asn Lys Thr Ala Asp
100 105 110
Gly Leu Ala Phe Phe Leu Ala Pro Val Gly Ser Lys Pro Gln Ser Lys
115 120 125
Gly Gly Phe Leu Gly Leu Phe Asn Ser Asp Ser Lys Asn Lys Ser Val
130 135 140
Gln Thr Val Ala Val Glu Phe Asp Thr Tyr Tyr Asn Ala Lys Trp Asp
145 150 155 160
Pro Ala Asn Arg His Ile Gly Ile Asp Val Asn Ser Ile Lys Ser Val
165 170 175
Lys Thr Ala Ser Trp Gly Leu Ala Asn Gly Gln Ile Ala Gln Ile Leu
180 185 190
Ile Thr Tyr Asp Ala Asp Thr Ser Leu Leu Val Ala Ser Leu Ile His
195 200 205
Pro Ser Arg Lys Thr Ser Tyr Ile Leu Ser Glu Thr Val Ser Leu Lys
210 215 220
Ser Asn Leu Pro Glu Trp Val Asn Ile Gly Phe Ser Ala Thr Thr Gly
225 230 235 240
Leu Asn Lys Gly Phe Val Glu Thr His Asp Val Phe Ser Trp Ser Phe
245 250 255
Ala Ser Lys Leu Ser Asp Gly Ser Thr Ser Asp Thr Leu Asp Leu Pro
260 265 270
Ser Phe Leu Leu Asn Glu Ala Ile
275 280
<210> 27
<211> 864
<212> PRT
<213>Manually
<220>
<223>Lipoxygenase CAA39604 [Da of MW=96817.14]
<400> 27
Met Phe Gly Ile Phe Asp Lys Gly Gln Lys Ile Lys Gly Thr Val Val
1 5 10 15
Leu Met Pro Lys Asn Val Leu Asp Phe Asn Ala Ile Thr Ser Ile Gly
20 25 30
Lys Gly Gly Val Ile Asp Thr Ala Thr Gly Ile Leu Gly Gln Gly Val
35 40 45
Ser Leu Val Gly Gly Val Ile Asp Thr Ala Thr Ser Phe Leu Gly Arg
50 55 60
Asn Ile Ser Met Gln Leu Ile Ser Ala Thr Gln Thr Asp Gly Ser Gly
65 70 75 80
Asn Gly Lys Val Gly Lys Glu Val Tyr Leu Glu Lys His Leu Pro Thr
85 90 95
Leu Pro Thr Leu Gly Ala Arg Gln Asp Ala Phe Ser Ile Phe Phe Glu
100 105 110
Trp Asp Ala Ser Phe Gly Ile Pro Gly Ala Phe Tyr Ile Lys Asn Phe
115 120 125
Met Thr Asp Glu Phe Phe Leu Val Ser Val Lys Leu Glu Asp Ile Pro
130 135 140
Asn His Gly Thr Ile Glu Phe Val Cys Asn Ser Trp Val Tyr Asn Phe
145 150 155 160
Arg Ser Tyr Lys Lys Asn Arg Ile Phe Phe Val Asn Asp Thr Tyr Leu
165 170 175
Pro Ser Ala Thr Pro Ala Pro Leu Leu Lys Tyr Arg Lys Glu Glu Leu
180 185 190
Glu Val Leu Arg Gly Asp Gly Thr Gly Lys Arg Lys Asp Phe Asp Arg
195 200 205
Ile Tyr Asp Tyr Asp Val Tyr Asn Asp Leu Gly Asn Pro Asp Gly Gly
210 215 220
Asp Pro Arg Pro Ile Leu Gly Gly Ser Ser Ile Tyr Pro Tyr Pro Arg
225 230 235 240
Arg Val Arg Thr Gly Arg Glu Arg Thr Arg Thr Asp Pro Asn Ser Glu
245 250 255
Lys Pro Gly Glu Val Tyr Val Pro Arg Asp Glu Asn Phe Gly His Leu
260 265 270
Lys Ser Ser Asp Phe Leu Thr Tyr Gly Ile Lys Ser Leu Ser His Asp
275 280 285
Val Ile Pro Leu Phe Lys Ser Ala Ile Phe Gln Leu Arg Val Thr Ser
290 295 300
Ser Glu Phe Glu Ser Phe Glu Asp Val Arg Ser Leu Tyr Glu Gly Gly
305 310 315 320
Ile Lys Leu Pro Thr Asp Ile Leu Ser Gln Ile Ser Pro Leu Pro Ala
325 330 335
Leu Lys Glu Ile Phe Arg Thr Asp Gly Glu Asn Val Leu Gln Phe Pro
340 345 350
Pro Pro His Val Ala Lys Val Ser Lys Ser Gly Trp Met Thr Asp Glu
355 360 365
Glu Phe Ala Arg Glu Val Ile Ala Gly Val Asn Pro Asn Val Ile Arg
370 375 380
Arg Leu Gln Glu Phe Pro Pro Lys Ser Thr Leu Asp Pro Thr Leu Tyr
385 390 395 400
Gly Asp Gln Thr Ser Thr Ile Thr Lys Glu Gln Leu Glu Ile Asn Met
405 410 415
Gly Gly Val Thr Val Glu Glu Ala Leu Ser Thr Gln Arg Leu Phe Ile
420 425 430
Leu Asp Tyr Gln Asp Ala Phe Ile Pro Tyr Leu Thr Arg Ile Asn Ser
435 440 445
Leu Pro Thr Ala Lys Ala Tyr Ala Thr Arg Thr Ile Leu Phe Leu Lys
450 455 460
Asp Asp Gly Thr Leu Lys Pro Leu Ala Ile Glu Leu Ser Lys Pro His
465 470 475 480
Pro Asp Gly Asp Asn Leu Gly Pro Glu Ser Ile Val Val Leu Pro Ala
485 490 495
Thr Glu Gly Val Asp Ser Thr Ile Trp Leu Leu Ala Lys Ala His Val
500 505 510
Ile Val Asn Asp Ser Gly Tyr His Gln Leu Val Ser His Trp Leu Asn
515 520 525
Thr His Ala Val Met Glu Pro Phe Ala Ile Ala Thr Asn Arg His Leu
530 535 540
Ser Val Leu His Pro Ile Tyr Lys Leu Leu Tyr Pro His Tyr Arg Asp
545 550 555 560
Thr Ile Asn Ile Asn Gly Leu Ala Arg Gln Ser Leu Ile Asn Ala Asp
565 570 575
Gly Ile Ile Glu Lys Ser Phe Leu Pro Gly Lys Tyr Ser Ile Glu Met
580 585 590
Ser Ser Ser Val Tyr Lys Asn Trp Val Phe Thr Asp Gln Ala Leu Pro
595 600 605
Ala Asp Leu Val Lys Arg Gly Leu Ala Ile Glu Asp Pro Ser Ala Pro
610 615 620
His Gly Leu Arg Leu Val Ile Glu Asp Tyr Pro Tyr Ala Val Asp Gly
625 630 635 640
Leu Glu Ile Trp Asp Ala Ile Lys Thr Trp Val His Glu Tyr Val Ser
645 650 655
Leu Tyr Tyr Pro Thr Asp Ala Ala Val Gln Gln Asp Thr Glu Leu Gln
660 665 670
Ala Trp Trp Lys Glu Ala Val Glu Lys Gly His Gly Asp Leu Lys Glu
675 680 685
Lys Pro Trp Trp Pro Lys Met Gln Thr Thr Glu Asp Leu Ile Gln Ser
690 695 700
Cys Ser Ile Ile Val Trp Thr Ala Ser Ala Leu His Ala Ala Val Asn
705 710 715 720
Phe Gly Gln Tyr Pro Tyr Gly Gly Leu Ile Leu Asn Arg Pro Thr Leu
725 730 735
Ala Arg Arg Phe Ile Pro Ala Glu Gly Thr Pro Glu Tyr Asp Glu Met
740 745 750
Val Lys Asn Pro Gln Lys Ala Tyr Leu Arg Thr Ile Thr Pro Lys Phe
755 760 765
Glu Thr Leu Ile Asp Leu Ser Val Ile Glu Ile Leu Ser Arg His Ala
770 775 780
Ser Asp Glu Ile Tyr Leu Gly Glu Arg Glu Thr Pro Asn Trp Thr Thr
785 790 795 800
Asp Lys Lys Ala Leu Glu Ala Phe Lys Arg Phe Gly Ser Lys Leu Thr
805 810 815
Gly Ile Glu Gly Lys Ile Asn Ala Arg Asn Ser Asp Pro Ser Leu Arg
820 825 830
Asn Arg Thr Gly Pro Val Gln Leu Pro Tyr Thr Leu Leu His Arg Ser
835 840 845
Ser Glu Glu Gly Leu Thr Phe Lys Gly Ile Pro Asn Ser Ile Ser Ile
850 855 860
<210> 28
<211> 118
<212> PRT
<213>Manually
<220>
<223>The consensus sequences of Gly m 1
<400> 28
Met Gly Ser Lys Val Val Ala Ser Val Ala Leu Leu Leu Ser Ile Asn
1 5 10 15
Ile Leu Phe Ile Ser Met Val Ser Ser Ser Ser His Tyr Asp Pro Pro
20 25 30
Gln Pro Ser Tyr Val Thr Ala Leu Ile Thr Arg Pro Ser Cys Pro Asp
35 40 45
Leu Ser Ile Cys Leu Asn Ile Leu Gly Gly Ser Leu Gly Thr Val Asp
50 55 60
Asp Cys Cys Ala Leu Ile Gly Gly Leu Gly Asp Ile Glu Ala Ile Val
65 70 75 80
Cys Leu Cys Ile Gln Leu Arg Ala Leu Gly Ile Leu Asn Leu Asn Arg
85 90 95
Asn Leu Gln Leu Ile Leu Asn Ala Cys Gly Arg Ser Tyr Pro Ser Asn
100 105 110
Ala Thr Cys Pro Arg Thr
115
<210> 29
<211> 119
<212> PRT
<213>Manually
<220>
<223>The consensus sequence #2 of Gly m 1
<400> 29
Met Gly Ser Lys Val Val Ala Ser Val Ala Leu Leu Leu Ser Ile Asn
1 5 10 15
Ile Leu Phe Ile Ser Met Val Ser Ser Ser Ser His Tyr Asp Pro Gln
20 25 30
Pro Gln Pro Ser His Val Thr Ala Leu Ile Thr Arg Pro Ser Cys Pro
35 40 45
Asp Leu Ser Ile Cys Leu Asn Ile Leu Gly Gly Ser Leu Gly Thr Val
50 55 60
Asp Asp Cys Cys Ala Leu Ile Gly Gly Leu Gly Asp Ile Glu Ala Ile
65 70 75 80
Val Cys Leu Cys Ile Gln Leu Arg Ala Leu Gly Ile Leu Asn Leu Asn
85 90 95
Arg Asn Leu Gln Leu Ile Leu Asn Ala Cys Gly Arg Ser Tyr Pro Ser
100 105 110
Asn Ala Thr Cys Pro Arg Thr
115
<210> 30
<211> 42
<212> PRT
<213>Manually
<220>
<223> Gly m 1 Ping AAB34755.1 42aa
<220>
<221> misc_feature
<222> (8)..(8)
<223> Xaa can be any naturally occurring amino acid
<220>
<221> misc_feature
<222> (14)..(14)
<223> Xaa can be any naturally occurring amino acid
<220>
<221> misc_feature
<222> (28)..(29)
<223> Xaa can be any naturally occurring amino acid
<220>
<221> misc_feature
<222> (36)..(36)
<223> Xaa can be any naturally occurring amino acid
<220>
<221> misc_feature
<222> (38)..(39)
<223> Xaa can be any naturally occurring amino acid
<400> 30
Ala Leu Ile Thr Arg Pro Ser Xaa Pro Asp Leu Ser Ile Xaa Leu Asn
1 5 10 15
Ile Leu Gly Gly Ser Leu Gly Thr Val Asp Asp Xaa Xaa Ala Leu Ile
20 25 30
Gly Gly Leu Xaa Asp Xaa Xaa Ala Ile Val
35 40
<210> 31
<211> 134
<212> PRT
<213>Manually
<220>
<223> Gly m 1 Ping ABA54897.1 134aa
<400> 31
Met Gly Ser Lys Val Val Ala Ser Val Ala Leu Leu Leu Ser Ile Asn
1 5 10 15
Ile Leu Phe Ile Ser Met Val Ser Ser Ser Ser His Tyr Asp Pro Pro
20 25 30
Pro Pro Pro Cys Tyr Val Pro Ala Pro Leu Thr Pro Pro Pro Ser Leu
35 40 45
Ser Pro Pro Pro Ser Leu Ser Pro Pro Pro Pro Ser Gly Pro Ser Cys
50 55 60
Pro Asp Leu Ser Val Cys Leu Asn Ile Leu Asp Gly Ser Pro Ala Asp
65 70 75 80
Asp Cys Cys Ala Leu Ile Ala Asp Leu Val Asp Leu Glu Ala Ser Val
85 90 95
Cys Leu Cys Ile Gln Leu Arg Val Leu Gly Ile Val Asn Leu Asp Leu
100 105 110
Asn Leu Gln Leu Ile Leu Asn Ala Cys Gly Pro Ser Tyr Pro Ser Asn
115 120 125
Ala Thr Cys Pro Arg Thr
130
<210> 32
<211> 118
<212> PRT
<213>Manually
<220>
<223> Gly m 1 Eric ABA54899 118aa
<400> 32
Gly Ser Lys Val Val Ala Ser Val Ala Leu Leu Leu Ser Ile Asn Ile
1 5 10 15
Leu Phe Ile Ser Met Val Ser Ser Ser Ser His Tyr Asp Pro Gln Pro
20 25 30
Gln Pro Ser His Val Thr Ala Leu Ile Thr Arg Pro Ser Cys Pro Asp
35 40 45
Leu Ser Ile Cys Leu Asn Ile Leu Gly Gly Ser Leu Gly Thr Val Asp
50 55 60
Asp Cys Cys Ala Leu Ile Gly Gly Leu Gly Asp Ile Glu Ala Ile Val
65 70 75 80
Cys Leu Cys Ile Gln Leu Arg Ala Leu Gly Ile Leu Asn Leu Asn Arg
85 90 95
Asn Leu Gln Leu Ile Leu Asn Ser Cys Gly Arg Ser Tyr Pro Ser Asn
100 105 110
Ala Thr Cys Pro Arg Thr
115
<210> 33
<211> 119
<212> PRT
<213>Manually
<220>
<223> Gly m 1 Glyma15g13740.1 BLAST 120aa
<400> 33
Met Gly Ser Lys Val Val Ala Tyr Val Ala Leu Leu Leu Ser Ile Asn
1 5 10 15
Ile Leu Phe Ile Ser Met Val Ser Ser Ser Ser His Tyr Asp Pro Gln
20 25 30
Pro Gln Pro Ser Tyr Val Thr Ala Leu Ile Thr Arg Pro Ser Cys Pro
35 40 45
Asp Leu Ser Val Cys Leu Asn Ile Leu Gly Gly Tyr Leu Gly Thr Val
50 55 60
Asp Asp Cys Cys Ala Leu Ile Gly Gly Leu Gly Asp Ile Glu Ala Thr
65 70 75 80
Val Cys Leu Cys Ile Gln Leu Arg Ala Leu Gly Ile Leu Asn Leu Asn
85 90 95
Arg Asn Leu Gln Leu Ile Leu Asn Ala Cys Gly Pro Ser Tyr Pro Ser
100 105 110
Asn Ala Thr Cys Pro Arg Thr
115
<210> 34
<211> 129
<212> PRT
<213>Manually
<220>
<223> Gly m 1 Glyma15g13770.1 BLAST 130aa
<400> 34
Met Gly Ser Lys Val Val Ala Ser Val Ala Leu Leu Leu Ser Ile Asn
1 5 10 15
Ile Leu Phe Ile Ser Met Val Ser Ser Ser Ser His Tyr Asp Pro Pro
20 25 30
Pro Pro Pro Cys Tyr Val Pro Ala Pro Phe Thr Pro Pro Pro Pro Ser
35 40 45
Leu Ser Pro Pro Pro Pro Ser Gly Pro Ser Cys Pro Asp Leu Ser Val
50 55 60
Cys Leu Asn Ile Leu Asp Gly Ser Pro Ala Asp Asp Cys Cys Ala Leu
65 70 75 80
Ile Ala Asp Leu Val Asp Leu Glu Ala Ser Val Cys Leu Cys Ile Gln
85 90 95
Leu Arg Val Leu Gly Ile Val Asn Leu Asp Leu Asn Leu Gln Leu Ile
100 105 110
Leu Asn Ala Cys Gly Pro Ser Tyr Pro Ser Asn Ala Thr Cys Pro Arg
115 120 125
Thr
<210> 35
<211> 119
<212> PRT
<213>Manually
<220>
<223> Gly m 1 Glyma15g13750.1 BLAST 120aa
<400> 35
Met Gly Ser Lys Val Val Ala Ser Val Ala Leu Leu Leu Ser Ile Asn
1 5 10 15
Ile Leu Phe Ile Ser Met Val Ser Ser Ser Ser His Tyr Asp Pro Pro
20 25 30
Pro Gln Pro Ser Tyr Val Thr Ala Leu Ile Thr Arg Pro Ser Cys Pro
35 40 45
Asp Leu Ser Ile Cys Leu Asn Ile Leu Gly Gly Ser Leu Gly Thr Val
50 55 60
Asp Asp Cys Cys Ala Leu Ile Gly Gly Leu Gly Asp Ile Glu Ala Ile
65 70 75 80
Val Cys Leu Cys Ile Gln Leu Arg Ala Leu Gly Ile Leu Asn Leu Asn
85 90 95
Arg Asn Leu Gln Leu Ile Leu Asn Ser Cys Gly Arg Ser Tyr Pro Ser
100 105 110
Asn Ala Thr Cys Pro Arg Thr
115
<210> 36
<211> 9
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 1
<400> 36
Ala Leu Gly Ile Leu Asn Leu Asn Arg
1 5
<210> 37
<211> 11
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 1
<400> 37
Asn Leu Gln Leu Ile Leu Asn Ser Cys Gly Arg
1 5 10
<210> 38
<211> 131
<212> PRT
<213>Manually
<220>
<223>The consensus sequences of Gly m 3
<400> 38
Met Ser Trp Gln Ala Tyr Val Asp Asp His Leu Leu Cys Gly Ile Glu
1 5 10 15
Gly Asn His Leu Thr His Ala Ala Ile Ile Gly Gln Asp Gly Ser Val
20 25 30
Trp Ala Gln Ser Thr Asp Phe Pro Gln Phe Lys Pro Glu Glu Ile Thr
35 40 45
Ala Ile Met Asn Asp Phe Asn Glu Pro Gly Ser Leu Ala Pro Thr Gly
50 55 60
Leu Tyr Leu Gly Gly Thr Lys Tyr Met Val Ile Gln Gly Glu Pro Gly
65 70 75 80
Ala Val Ile Arg Gly Lys Lys Gly Pro Gly Gly Val Thr Val Lys Lys
85 90 95
Thr Gly Ala Ala Leu Ile Ile Gly Ile Tyr Asp Glu Pro Met Thr Pro
100 105 110
Gly Gln Cys Asn Met Val Val Glu Arg Leu Gly Asp Tyr Leu Ile Asp
115 120 125
Gln Gly Tyr
130
<210> 39
<211> 131
<212> PRT
<213>Manually
<220>
<223> Gly m 3 Ping ABU97472.1 131aa
<400> 39
Met Ser Trp Gln Ala Tyr Val Asp Asp His Leu Leu Cys Glu Ile Glu
1 5 10 15
Gly Asn His Leu Thr His Ala Ala Ile Ile Gly Gln Asp Gly Ser Val
20 25 30
Trp Ala Gln Ser Thr Asn Phe Pro Gln Phe Lys Pro Glu Glu Ile Thr
35 40 45
Ala Ile Asn Asn Asp Phe Asn Glu Pro Gly Ser Leu Ala Pro Thr Gly
50 55 60
Leu Tyr Ile Gly Gly Thr Lys Tyr Met Val Ile Gln Gly Glu Pro Gly
65 70 75 80
Ala Val Ile Arg Gly Lys Lys Gly Pro Gly Gly Val Thr Val Lys Lys
85 90 95
Thr Gly Ala Ala Leu Ile Ile Gly Ile Tyr Asp Glu Pro Met Thr Pro
100 105 110
Gly Gln Cys Asn Met Val Val Glu Arg Leu Gly Asp Tyr Leu Ile Asp
115 120 125
Gln Gly Leu
130
<210> 40
<211> 131
<212> PRT
<213>Manually
<220>
<223> Gly m 3 Ping O65809.1 131aa
<400> 40
Met Ser Trp Gln Ala Tyr Val Asp Asp His Leu Leu Cys Asp Ile Glu
1 5 10 15
Gly Asn His Leu Thr His Ala Ala Ile Ile Gly Gln Asp Gly Ser Val
20 25 30
Trp Ala Gln Ser Thr Asp Phe Pro Gln Phe Lys Pro Glu Glu Ile Thr
35 40 45
Ala Ile Met Asn Asp Phe Asn Glu Pro Gly Ser Leu Ala Pro Thr Gly
50 55 60
Leu Tyr Leu Gly Gly Thr Lys Tyr Met Val Ile Gln Gly Glu Pro Gly
65 70 75 80
Ala Val Ile Arg Gly Lys Lys Gly Pro Gly Gly Val Thr Val Lys Lys
85 90 95
Thr Gly Ala Ala Leu Ile Ile Gly Ile Tyr Asp Glu Pro Met Thr Pro
100 105 110
Gly Gln Cys Asn Met Val Val Glu Arg Pro Gly Asp Tyr Leu Ile Asp
115 120 125
Gln Gly Tyr
130
<210> 41
<211> 8
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 3
<400> 41
Gly Pro Gly Gly Val Thr Val Lys
1 5
<210> 42
<211> 158
<212> PRT
<213>Manually
<220>
<223>The consensus sequences of Gly m 4
<400> 42
Met Gly Val Phe Thr Phe Glu Asp Glu Thr Thr Ser Pro Val Ala Pro
1 5 10 15
Ala Thr Leu Tyr Lys Ala Leu Val Thr Asp Ala Asp Asn Val Ile Pro
20 25 30
Lys Ala Val Asp Ala Phe Lys Ser Val Glu Asn Val Glu Gly Asn Gly
35 40 45
Gly Pro Gly Thr Ile Lys Lys Ile Thr Phe Val Glu Asp Gly Glu Thr
50 55 60
Lys Phe Val Leu His Lys Ile Glu Ala Ile Asp Glu Ala Asn Leu Gly
65 70 75 80
Tyr Ser Tyr Ser Val Val Gly Gly Ala Gly Leu Pro Asp Thr Val Glu
85 90 95
Lys Ile Thr Phe Glu Ala Lys Leu Ala Ala Gly Ala Asn Gly Gly Ser
100 105 110
Ala Gly Lys Leu Thr Val Lys Tyr Gln Thr Lys Gly Asp Ala Gln Pro
115 120 125
Asn Gln Asp Glu Leu Lys Ser Gly Lys Ala Lys Ala Asp Ala Leu Phe
130 135 140
Lys Ala Val Glu Ala Tyr Leu Leu Ala Asn Pro Asp Tyr Asn
145 150 155
<210> 43
<211> 165
<212> PRT
<213>Manually
<220>
<223> Gly m 4 Glyma07g37240.1 BLAST 165aa
<400> 43
Met Gly Val Phe Thr Phe Glu Asp Glu Ile Asn Ser Pro Val Ala Pro
1 5 10 15
Ala Thr Leu Tyr Lys Ala Leu Val Thr Asp Ala Asp Asn Val Ile Pro
20 25 30
Lys Ala Leu Asp Ser Phe Lys Ser Val Glu Asn Val Glu Gly Asn Gly
35 40 45
Gly Pro Gly Thr Ile Lys Lys Ile Thr Phe Leu Glu Ala Asp Val Asn
50 55 60
Glu Trp Ile Asp Gly Glu Thr Lys Phe Val Leu His Lys Ile Glu Ser
65 70 75 80
Ile Asp Glu Ala Asn Leu Gly Tyr Ser Tyr Ser Val Val Gly Gly Ala
85 90 95
Ala Leu Pro Asp Thr Ala Glu Lys Ile Thr Phe Asp Ser Lys Leu Val
100 105 110
Ala Gly Pro Asn Gly Gly Ser Ala Gly Lys Leu Thr Val Lys Tyr Glu
115 120 125
Thr Lys Gly Asp Ala Glu Pro Asn Gln Asp Glu Leu Lys Thr Gly Lys
130 135 140
Ala Lys Ala Asp Ala Leu Phe Lys Ala Ile Glu Ala Tyr Leu Leu Ala
145 150 155 160
His Pro Asp Tyr Asn
165
<210> 44
<211> 158
<212> PRT
<213>Manually
<220>
<223> Gly m 4 Glyma17g03365.1 BLAST 159aa
<400> 44
Met Gly Ile Phe Thr Phe Glu Asp Glu Ile Thr Ser Pro Val Ala Pro
1 5 10 15
Ala Thr Leu Tyr Lys Ala Leu Val Thr Asp Ala Asp Asn Ile Ile Pro
20 25 30
Lys Ala Leu Asp Ser Phe Lys Ser Val Glu Asn Val Glu Gly Asn Gly
35 40 45
Gly Pro Gly Thr Ile Lys Lys Ile Thr Phe Val Glu Asp Gly Glu Thr
50 55 60
Lys Phe Val Leu His Lys Ile Glu Ala Val Asp Glu Ala Asn Leu Gly
65 70 75 80
Tyr Ser Tyr Ser Val Val Gly Gly Ala Ala Leu Pro Asp Thr Ala Glu
85 90 95
Lys Ile Thr Phe His Ser Lys Leu Ala Ala Gly Pro Asn Gly Gly Ser
100 105 110
Ala Gly Lys Leu Thr Val Glu Tyr Gln Thr Lys Gly Asp Ala Gln Pro
115 120 125
Asn Gln Asp Gln Leu Lys Thr Gly Lys Ala Lys Ala Asp Ala Leu Phe
130 135 140
Lys Ala Ile Glu Ala Tyr Leu Leu Ala Asn Pro Asp Tyr Asn
145 150 155
<210> 45
<211> 146
<212> PRT
<213>Manually
<220>
<223> Gly m 4 Glyma07g37240.3 BLAST 147aa
<400> 45
Met Gly Val Phe Thr Phe Glu Asp Glu Ile Asn Ser Pro Val Ala Pro
1 5 10 15
Ala Thr Leu Tyr Lys Ala Leu Asp Ser Phe Lys Ser Val Glu Asn Val
20 25 30
Glu Gly Asn Gly Gly Pro Gly Thr Ile Lys Lys Ile Thr Phe Leu Glu
35 40 45
Asp Gly Glu Thr Lys Phe Val Leu His Lys Ile Glu Ser Ile Asp Glu
50 55 60
Ala Asn Leu Gly Tyr Ser Tyr Ser Val Val Gly Gly Ala Ala Leu Pro
65 70 75 80
Asp Thr Ala Glu Lys Ile Thr Phe Asp Ser Lys Leu Val Ala Gly Pro
85 90 95
Asn Gly Gly Ser Ala Gly Lys Leu Thr Val Lys Tyr Glu Thr Lys Gly
100 105 110
Asp Ala Glu Pro Asn Gln Asp Glu Leu Lys Thr Gly Lys Ala Lys Ala
115 120 125
Asp Ala Leu Phe Lys Ala Ile Glu Ala Tyr Leu Leu Ala His Pro Asp
130 135 140
Tyr Asn
145
<210> 46
<211> 158
<212> PRT
<213>Manually
<220>
<223> Gly m 4 Glyma07g37270.2 BLAST 159aa
<400> 46
Met Gly Val Phe Thr Phe Glu Asp Glu Ile Asn Ser Pro Val Ala Pro
1 5 10 15
Ala Thr Leu Tyr Lys Ala Leu Val Thr Asp Ala Asp Asn Val Ile Pro
20 25 30
Lys Ala Leu Asp Ser Phe Lys Ser Val Glu Asn Val Glu Gly Asn Gly
35 40 45
Gly Pro Gly Thr Ile Lys Lys Ile Thr Phe Leu Glu Asp Gly Glu Thr
50 55 60
Lys Phe Val Leu His Lys Ile Glu Ala Ile Asp Glu Ala Asn Leu Gly
65 70 75 80
Tyr Ser Tyr Ser Val Val Gly Gly Asp Gly Leu Pro Asp Thr Val Glu
85 90 95
Lys Ile Thr Phe Glu Cys Lys Leu Ala Ala Gly Ala Asn Gly Gly Ser
100 105 110
Ala Gly Lys Leu Thr Val Lys Tyr Gln Thr Lys Gly Asp Ala Gln Pro
115 120 125
Asn Gln Asp Asp Leu Lys Ile Gly Lys Ala Lys Ser Asp Ala Leu Phe
130 135 140
Lys Ala Val Glu Ala Tyr Leu Leu Ala His Pro Asp Tyr Asn
145 150 155
<210> 47
<211> 158
<212> PRT
<213>Manually
<220>
<223> Gly m 4 Glyma07g37270.1 BLAST 159aa
<400> 47
Met Gly Val Phe Thr Phe Glu Asp Glu Thr Thr Ser Pro Val Ala Pro
1 5 10 15
Ala Thr Leu Tyr Lys Ala Leu Val Thr Asp Ala Asp Asn Val Ile Pro
20 25 30
Lys Ala Val Asp Ala Phe Arg Ser Val Glu Asn Val Glu Gly Asn Gly
35 40 45
Gly Pro Gly Thr Ile Lys Lys Ile Thr Phe Leu Glu Asp Gly Glu Thr
50 55 60
Lys Phe Val Leu His Lys Ile Glu Ala Ile Asp Glu Ala Asn Leu Gly
65 70 75 80
Tyr Ser Tyr Ser Val Val Gly Gly Asp Gly Leu Pro Asp Thr Val Glu
85 90 95
Lys Ile Thr Phe Glu Cys Lys Leu Ala Ala Gly Ala Asn Gly Gly Ser
100 105 110
Ala Gly Lys Leu Thr Val Lys Tyr Gln Thr Lys Gly Asp Ala Gln Pro
115 120 125
Asn Gln Asp Asp Leu Lys Ile Gly Lys Ala Lys Ser Asp Ala Leu Phe
130 135 140
Lys Ala Val Glu Ala Tyr Leu Leu Ala His Pro Asp Tyr Asn
145 150 155
<210> 48
<211> 158
<212> PRT
<213>Manually
<220>
<223> Gly m 4 Glyma17g03360.1 BLAST 159aa
<400> 48
Met Gly Val Phe Thr Phe Glu Asp Glu Thr Thr Ser Pro Val Ala Pro
1 5 10 15
Ala Thr Leu Tyr Lys Ala Leu Val Thr Asp Ala Asp Asn Val Ile Pro
20 25 30
Lys Ala Val Asp Ala Phe Arg Ser Val Glu Asn Leu Glu Gly Asn Gly
35 40 45
Gly Pro Gly Thr Ile Lys Lys Ile Thr Phe Val Glu Asp Gly Glu Ser
50 55 60
Lys Phe Val Leu His Lys Ile Glu Ser Val Asp Glu Ala Asn Leu Gly
65 70 75 80
Tyr Ser Tyr Ser Val Val Gly Gly Val Gly Leu Pro Asp Thr Val Glu
85 90 95
Lys Ile Thr Phe Glu Cys Lys Leu Ala Ala Gly Ala Asn Gly Gly Ser
100 105 110
Ala Gly Lys Leu Thr Val Lys Tyr Gln Thr Lys Gly Asp Ala Gln Pro
115 120 125
Asn Pro Asp Asp Leu Lys Ile Gly Lys Val Lys Ser Asp Ala Leu Phe
130 135 140
Lys Ala Val Glu Ala Tyr Leu Leu Ala Asn Pro His Tyr Asn
145 150 155
<210> 49
<211> 158
<212> PRT
<213>Manually
<220>
<223> Gly m 4 Glyma17g03350.1 BLAST 159aa
<400> 49
Met Gly Ile Phe Thr Phe Glu Asp Glu Thr Thr Ser Pro Val Ala Pro
1 5 10 15
Ala Thr Leu Tyr Lys Ala Leu Val Thr Asp Ala Asp Asn Val Ile Pro
20 25 30
Lys Ala Val Glu Ala Phe Arg Ser Val Glu Asn Leu Glu Gly Asn Gly
35 40 45
Gly Pro Gly Thr Ile Lys Lys Ile Thr Phe Val Glu Asp Gly Glu Ser
50 55 60
Lys Phe Val Leu His Lys Ile Glu Ser Val Asp Glu Ala Asn Leu Gly
65 70 75 80
Tyr Ser Tyr Ser Val Val Gly Gly Val Gly Leu Pro Asp Thr Val Glu
85 90 95
Lys Ile Thr Phe Glu Cys Lys Leu Ala Ala Gly Ala Asn Gly Gly Ser
100 105 110
Ala Gly Lys Leu Thr Val Lys Tyr Gln Thr Lys Gly Asp Ala Gln Pro
115 120 125
Asn Pro Asp Asp Leu Lys Ile Gly Lys Val Lys Ser Asp Ala Leu Phe
130 135 140
Lys Ala Val Glu Ala Tyr Leu Leu Ala Asn Pro His Tyr Asn
145 150 155
<210> 50
<211> 158
<212> PRT
<213>Manually
<220>
<223> Gly m 4 Glyma09g04510.1 BLAST 159aa
<400> 50
Met Gly Val Phe Thr Phe Glu Asp Glu Thr Thr Ser Thr Val Ala Pro
1 5 10 15
Ala Arg Leu Tyr Lys Ala Leu Val Lys Asp Ala Asp Asn Leu Val Pro
20 25 30
Lys Ala Val Glu Ala Ile Lys Ser Val Glu Ile Val Glu Gly Asn Gly
35 40 45
Gly Pro Gly Thr Ile Lys Lys Leu Thr Phe Val Glu Asp Gly Gln Thr
50 55 60
Lys Tyr Val Leu His Lys Val Glu Ala Ile Asp Glu Ala Asn Trp Gly
65 70 75 80
Tyr Asn Tyr Ser Val Val Gly Gly Val Gly Leu Pro Asp Thr Val Glu
85 90 95
Lys Ile Ser Phe Glu Ala Lys Leu Val Ala Asp Pro Asn Gly Gly Ser
100 105 110
Ile Ala Lys Ile Thr Val Lys Tyr Gln Thr Lys Gly Asp Ala Asn Pro
115 120 125
Ser Glu Glu Glu Leu Lys Ser Gly Lys Ala Lys Gly Asp Ala Leu Phe
130 135 140
Lys Ala Leu Glu Gly Tyr Val Leu Ala Asn Pro Asp Tyr Asn
145 150 155
<210> 51
<211> 158
<212> PRT
<213>Manually
<220>
<223> Gly m 4 Glyma15g15590.1 BLAST 159aa
<400> 51
Met Gly Val Phe Thr Phe Glu Asp Glu Thr Thr Ser Thr Val Ala Pro
1 5 10 15
Ala Arg Leu Tyr Lys Ala Leu Val Lys Asp Ala Asp Asn Leu Val Pro
20 25 30
Lys Ala Val Glu Ala Ile Lys Ser Val Glu Ile Val Glu Gly Asn Gly
35 40 45
Gly Pro Gly Thr Ile Lys Lys Leu Thr Phe Val Glu Asp Gly Gln Thr
50 55 60
Lys Tyr Val Leu His Lys Val Glu Ala Ile Asp Glu Ala Asn Trp Gly
65 70 75 80
Tyr Asn Tyr Ser Val Val Gly Gly Val Gly Leu Pro Asp Thr Val Glu
85 90 95
Lys Ile Ser Phe Glu Ala Lys Leu Val Glu Gly Ala Ser Gly Gly Ser
100 105 110
Ile Ala Lys Ile Thr Val Lys Tyr Gln Thr Lys Gly Asp Val Asn Pro
115 120 125
Ser Glu Glu Glu Leu Lys Ser Gly Lys Ala Lys Gly Asp Ala Leu Phe
130 135 140
Lys Ala Leu Glu Gly Tyr Val Leu Ala Asn Pro Asp Tyr Asn
145 150 155
<210> 52
<211> 21
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 4
<400> 52
Met Gly Val Phe Thr Phe Glu Asp Glu Ile Asn Ser Pro Val Ala Pro
1 5 10 15
Ala Thr Leu Tyr Lys
20
<210> 53
<211> 6
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 4
<400> 53
Ala Leu Asp Ser Phe Lys
1 5
<210> 54
<211> 15
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 4
<400> 54
Ser Val Glu Asn Val Glu Gly Asn Gly Gly Pro Gly Thr Ile Lys
1 5 10 15
<210> 55
<211> 10
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 4
<400> 55
Ile Thr Phe Leu Glu Asp Gly Glu Thr Lys
1 5 10
<210> 56
<211> 5
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 4
<400> 56
Phe Val Leu His Lys
1 5
<210> 57
<211> 13
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 4
<400> 57
Ala Ile Glu Ala Tyr Leu Leu Ala His Pro Asp Tyr Asn
1 5 10
<210> 58
<211> 19
<212> PRT
<213>Artificial sequence
<220>
<223>Artificial sequence
<400> 58
Tyr Glu Gly Asn Trp Gly Pro Leu Val Asn Pro Glu Ser Gln Gln Gly
1 5 10 15
Ser Pro Arg
<210> 59
<211> 22
<212> PRT
<213>Artificial sequence
<220>
<223>Artificial sequence
<400> 59
Gly Ala Leu Gln Cys Lys Pro Gly Cys Pro Glu Thr Phe Glu Glu Pro
1 5 10 15
Gln Glu Gln Ser Asn Arg
20
<210> 60
<211> 8
<212> PRT
<213>Artificial sequence
<220>
<223>Artificial sequence
<400> 60
Leu Gln Ser Pro Asp Asp Glu Arg
1 5
<210> 61
<211> 621
<212> PRT
<213>Manually
<220>
<223>The consensus sequences of Gly m 5
<400> 61
Met Met Arg Ala Arg Phe Pro Leu Leu Leu Leu Gly Val Val Phe Leu
1 5 10 15
Ala Ser Val Ser Val Ser Phe Gly Ile Ala Tyr Trp Glu Lys Gln Asn
20 25 30
Pro Ser His Asn Lys Cys Leu Gln Ser Cys Asn Ser Glu Lys Asp Ser
35 40 45
Tyr Arg Asn Gln Ala Cys His Ala Arg Cys Asn Leu Leu Lys Val Glu
50 55 60
Glu Glu Glu Glu Cys Glu Glu Gly Gln Ile Pro Arg Pro Arg Pro Gln
65 70 75 80
His Pro Glu Arg Glu Arg Gln Gln His Gly Glu Lys Glu Glu Asp Glu
85 90 95
Gly Glu Gln Pro Arg Pro Phe Pro Phe Pro Arg Pro Arg Gln Pro His
100 105 110
Gln Glu Glu Glu His Glu Gln Lys Glu Glu His Glu Trp His Arg Lys
115 120 125
Glu Glu Lys His Gly Gly Lys Gly Ser Glu Glu Glu Gln Asp Glu Arg
130 135 140
Glu His Pro Arg Pro His Gln Pro His Gln Lys Glu Glu Glu Lys His
145 150 155 160
Glu Trp Gln His Lys Gln Glu Lys His Gln Gly Lys Glu Ser Glu Glu
165 170 175
Glu Glu Glu Asp Gln Asp Glu Asp Glu Glu Gln Asp Lys Glu Ser Gln
180 185 190
Glu Ser Glu Gly Ser Glu Ser Gln Arg Glu Pro Arg Arg His Lys Asn
195 200 205
Lys Asn Pro Phe His Phe Asn Ser Lys Arg Phe Gln Thr Leu Phe Lys
210 215 220
Asn Gln Tyr Gly His Val Arg Val Leu Gln Arg Phe Asn Lys Arg Ser
225 230 235 240
Gln Gln Leu Gln Asn Leu Arg Asp Tyr Arg Ile Leu Glu Phe Asn Ser
245 250 255
Lys Pro Asn Thr Leu Leu Leu Pro His His Ala Asp Ala Asp Tyr Leu
260 265 270
Ile Val Ile Leu Asn Gly Thr Ala Ile Leu Thr Leu Val Asn Asn Asp
275 280 285
Asp Arg Asp Ser Tyr Asn Leu Gln Ser Gly Asp Ala Leu Arg Val Pro
290 295 300
Ala Gly Thr Thr Tyr Tyr Val Val Asn Pro Asp Asn Asp Glu Asn Leu
305 310 315 320
Arg Met Ile Thr Leu Ala Ile Pro Val Asn Lys Pro Gly Arg Phe Glu
325 330 335
Ser Phe Phe Leu Ser Ser Thr Gln Ala Gln Gln Ser Tyr Leu Gln Gly
340 345 350
Phe Ser Lys Asn Ile Leu Glu Ala Ser Tyr Asp Thr Lys Phe Glu Glu
355 360 365
Ile Asn Lys Val Leu Phe Gly Arg Glu Glu Gly Gln Gln Gln Gly Glu
370 375 380
Glu Arg Leu Gln Glu Ser Val Ile Val Glu Ile Ser Lys Lys Gln Ile
385 390 395 400
Arg Glu Leu Ser Lys Arg Ala Lys Ser Ser Ser Arg Lys Thr Ile Ser
405 410 415
Ser Glu Asp Lys Pro Phe Asn Leu Arg Ser Arg Asp Pro Ile Tyr Ser
420 425 430
Asn Lys Leu Gly Lys Leu Phe Glu Ile Thr Pro Glu Lys Asn Pro Gln
435 440 445
Leu Arg Asp Leu Asp Val Phe Leu Ser Val Val Asp Met Asn Glu Gly
450 455 460
Ala Leu Leu Leu Pro His Phe Asn Ser Lys Ala Ile Val Val Leu Val
465 470 475 480
Ile Asn Glu Gly Asp Ala Asn Ile Glu Leu Val Gly Ile Lys Glu Gln
485 490 495
Gln Gln Arg Gln Gln Gln Glu Glu Gln Pro Leu Glu Val Arg Lys Tyr
500 505 510
Arg Ala Glu Leu Ser Glu Gln Asp Ile Phe Val Ile Pro Ala Gly Tyr
515 520 525
Pro Val Val Val Asn Ala Thr Ser Asn Leu Asn Phe Phe Ala Phe Gly
530 535 540
Ile Asn Ala Glu Asn Asn Gln Arg Asn Phe Leu Ala Gly Ser Lys Asp
545 550 555 560
Asn Val Ile Ser Gln Ile Pro Ser Gln Val Gln Glu Leu Ala Phe Pro
565 570 575
Gly Ser Ala Lys Asp Ile Glu Asn Leu Ile Lys Ser Gln Ser Glu Ser
580 585 590
Tyr Phe Val Asp Ala Gln Pro Gln Gln Lys Glu Glu Gly Asn Lys Gly
595 600 605
Arg Lys Gly Pro Leu Ser Ser Ile Leu Arg Ala Phe Tyr
610 615 620
<210> 62
<211> 600
<212> PRT
<213>Manually
<220>
<223> Gly m 5 ABH09130 BLAST 600aa
<400> 62
Met Phe Gly Ile Val Tyr Trp Glu Lys Gln Asn Pro Ser His Asn Lys
1 5 10 15
Cys Leu Arg Ser Cys Asn Ser Glu Lys Asp Ser Tyr Arg Asn Gln Ala
20 25 30
Cys His Ala Arg Cys Asn Leu Leu Lys Val Glu Glu Glu Glu Glu Cys
35 40 45
Glu Glu Gly Gln Ile Pro Arg Pro Arg Pro Gln His Pro Glu Arg Glu
50 55 60
Arg Gln Gln His Gly Glu Lys Glu Glu Asp Glu Gly Glu Gln Pro Arg
65 70 75 80
Pro Phe Pro Phe Pro Arg Pro Arg Gln Pro His Gln Glu Glu Glu His
85 90 95
Glu Gln Lys Glu Glu His Glu Trp His Arg Lys Glu Glu Lys His Gly
100 105 110
Gly Lys Gly Ser Glu Glu Glu Gln Asp Glu Arg Glu His Pro Arg Pro
115 120 125
His Gln Pro His Gln Lys Glu Glu Glu Lys His Glu Trp Gln His Lys
130 135 140
Gln Glu Lys His Gln Gly Lys Glu Ser Glu Glu Glu Glu Glu Asp Gln
145 150 155 160
Asp Glu Asp Glu Gly Gln Asp Lys Glu Ser Gln Glu Ser Glu Gly Ser
165 170 175
Glu Ser Gln Arg Glu Pro Arg Arg His Lys Asn Lys Asn Pro Phe His
180 185 190
Phe Asn Ser Lys Arg Phe Gln Thr Leu Phe Lys Asn Gln Tyr Gly His
195 200 205
Val Arg Val Leu Gln Arg Phe Asn Lys Arg Ser Gln Gln Leu Gln Asn
210 215 220
Leu Arg Asp Tyr Arg Ile Leu Glu Phe Asn Ser Lys Pro Asn Thr Leu
225 230 235 240
Leu Ser Pro Asn His Ala Asp Ala Asp Tyr Leu Ile Val Ile Leu Asn
245 250 255
Gly Thr Ala Ile Leu Thr Leu Val Asn Asn Asp Asp Arg Asp Ser Tyr
260 265 270
Asn Leu Gln Ser Gly Asp Ala Leu Arg Val Pro Ala Gly Thr Thr Tyr
275 280 285
Tyr Val Val Asn Pro Asp Asn Asp Glu Asn Leu Arg Met Ile Thr Leu
290 295 300
Ala Ile Pro Val Asn Lys Pro Gly Arg Phe Glu Ser Phe Phe Leu Ser
305 310 315 320
Ser Thr Gln Ala Gln Gln Ser Tyr Leu Gln Gly Phe Ser Lys Asn Ile
325 330 335
Leu Glu Ala Ser Tyr Asp Thr Lys Phe Glu Glu Ile Asn Lys Val Leu
340 345 350
Phe Gly Arg Glu Glu Gly Gln Gln Gln Gly Glu Glu Arg Leu Gln Glu
355 360 365
Ser Val Ile Val Glu Ile Ser Lys Lys Gln Ile Arg Glu Leu Ser Lys
370 375 380
His Ala Lys Pro Ser Ser Arg Lys Thr Ile Ser Ser Glu Asp Lys Pro
385 390 395 400
Phe Asn Leu Arg Ser Arg Asp Pro Ile Tyr Ser Asn Lys Leu Gly Lys
405 410 415
Leu Phe Glu Ile Thr Pro Glu Lys Asn Pro Gln Leu Arg Asp Leu Asp
420 425 430
Val Phe Leu Ser Val Val Asp Met Asn Glu Gly Ala Leu Phe Leu Pro
435 440 445
His Phe Asn Ser Lys Ala Ile Val Val Leu Val Ile Asn Glu Gly Glu
450 455 460
Ala Asn Ile Glu Leu Val Gly Ile Lys Glu Gln Gln Gln Arg Gln Gln
465 470 475 480
Gln Glu Glu Gln Pro Leu Glu Val Arg Lys Tyr Arg Ala Glu Leu Ser
485 490 495
Glu Gln Asp Ile Phe Val Ile Pro Ala Gly Tyr Pro Val Val Val Asn
500 505 510
Ala Thr Ser Asp Leu Asn Phe Phe Ala Phe Gly Ile Asn Ala Glu Asn
515 520 525
Asn Gln Arg Asn Phe Leu Ala Gly Ser Lys Asp Asn Val Ile Ser Gln
530 535 540
Ile Pro Ser Gln Val Gln Glu Leu Ala Phe Pro Gly Ser Ala Lys Asp
545 550 555 560
Ile Glu Asn Leu Ile Lys Ser Gln Ser Glu Ser Tyr Phe Val Asp Ala
565 570 575
Gln Pro Gln Gln Lys Glu Glu Gly Asn Lys Gly Arg Lys Gly Pro Leu
580 585 590
Ser Ser Ile Leu Arg Ala Phe Tyr
595 600
<210> 63
<211> 559
<212> PRT
<213>Manually
<220>
<223> Gly m 5 BAA74452 BLAST 559aa
<400> 63
Val Glu Glu Glu Glu Glu Cys Glu Glu Gly Gln Ile Pro Arg Pro Arg
1 5 10 15
Pro Gln His Pro Glu Arg Glu Arg Gln Gln His Gly Glu Lys Glu Glu
20 25 30
Asp Glu Gly Glu Gln Pro Arg Pro Phe Pro Phe Pro Arg Pro Arg Gln
35 40 45
Pro His Gln Glu Glu Glu His Glu Gln Lys Glu Glu His Glu Trp His
50 55 60
Arg Lys Glu Glu Lys His Gly Gly Lys Gly Ser Glu Glu Glu Gln Asp
65 70 75 80
Glu Arg Glu His Pro Arg Pro His Gln Pro His Gln Lys Glu Glu Glu
85 90 95
Lys His Glu Trp Gln His Lys Gln Glu Lys His Gln Gly Lys Glu Ser
100 105 110
Glu Glu Glu Glu Glu Asp Gln Asp Glu Asp Glu Glu Gln Asp Lys Glu
115 120 125
Ser Gln Glu Ser Glu Gly Ser Glu Ser Gln Arg Glu Pro Arg Arg His
130 135 140
Lys Asn Lys Asn Pro Phe His Phe Asn Ser Lys Arg Phe Gln Thr Leu
145 150 155 160
Phe Lys Asn Gln Tyr Gly His Val Arg Val Leu Gln Arg Phe Asn Lys
165 170 175
Arg Ser Gln Gln Leu Gln Asn Leu Arg Asp Tyr Arg Ile Leu Glu Phe
180 185 190
Asn Ser Lys Pro Asn Thr Leu Leu Leu Pro His His Ala Asp Ala Asp
195 200 205
Tyr Leu Ile Val Ile Leu Asn Gly Thr Ala Ile Leu Thr Leu Val Asn
210 215 220
Asn Asp Asp Arg Asp Ser Tyr Asn Leu Gln Ser Gly Asp Ala Leu Arg
225 230 235 240
Val Pro Ala Gly Thr Thr Tyr Tyr Val Val Asn Pro Asp Asn Asp Glu
245 250 255
Asn Leu Arg Met Ile Thr Leu Ala Ile Pro Val Asn Lys Pro Gly Arg
260 265 270
Phe Glu Ser Phe Phe Leu Ser Ser Thr Gln Ala Gln Gln Ser Tyr Leu
275 280 285
Gln Gly Phe Ser Lys Asn Ile Leu Glu Ala Ser Tyr Asp Thr Lys Phe
290 295 300
Glu Glu Ile Asn Lys Val Leu Phe Gly Arg Glu Glu Gly Gln Gln Gln
305 310 315 320
Gly Glu Glu Arg Leu Gln Glu Ser Val Ile Val Glu Ile Ser Lys Lys
325 330 335
Gln Ile Arg Glu Leu Ser Lys His Ala Lys Ser Ser Ser Arg Lys Thr
340 345 350
Ile Ser Ser Glu Asp Lys Pro Phe Asn Leu Arg Ser Arg Asp Pro Ile
355 360 365
Tyr Ser Asn Lys Leu Gly Lys Leu Phe Glu Ile Thr Pro Glu Lys Asn
370 375 380
Pro Gln Leu Arg Asp Leu Asp Val Phe Leu Ser Val Val Asp Met Asn
385 390 395 400
Glu Gly Ala Leu Phe Leu Pro His Phe Asn Ser Lys Ala Ile Val Val
405 410 415
Leu Val Ile Asn Glu Gly Glu Ala Asn Ile Glu Leu Val Gly Ile Lys
420 425 430
Glu Gln Gln Gln Arg Gln Gln Gln Glu Glu Gln Pro Leu Glu Val Arg
435 440 445
Lys Tyr Arg Ala Glu Leu Ser Glu Gln Asp Ile Phe Val Ile Pro Ala
450 455 460
Gly Tyr Pro Val Val Val Asn Ala Thr Ser Asp Leu Asn Phe Phe Ala
465 470 475 480
Phe Gly Ile Asn Ala Glu Asn Asn Gln Arg Asn Phe Leu Ala Gly Ser
485 490 495
Lys Asp Asn Val Ile Ser Gln Ile Pro Ser Gln Val Gln Glu Leu Ala
500 505 510
Phe Pro Gly Ser Ala Lys Asp Ile Glu Asn Leu Ile Lys Ser Gln Ser
515 520 525
Glu Ser Tyr Phe Val Asp Ala Gln Pro Gln Gln Lys Glu Glu Gly Asn
530 535 540
Lys Gly Arg Lys Gly Pro Leu Ser Ser Ile Leu Arg Ala Phe Tyr
545 550 555
<210> 64
<211> 621
<212> PRT
<213>Manually
<220>
<223> Gly m 5 BAC78524 BLAST 621aa
<400> 64
Met Met Arg Ala Arg Phe Pro Leu Leu Leu Leu Gly Val Val Phe Leu
1 5 10 15
Ala Ser Val Ser Val Ser Phe Gly Ile Ala Tyr Trp Glu Lys Gln Asn
20 25 30
Pro Ser His Asn Lys Cys Leu Arg Ser Cys Asn Ser Glu Lys Asp Ser
35 40 45
Tyr Arg Asn Gln Ala Cys His Ala Arg Cys Asn Leu Leu Lys Val Glu
50 55 60
Glu Glu Glu Glu Cys Glu Glu Gly Gln Ile Pro Arg Pro Arg Pro Gln
65 70 75 80
His Pro Glu Arg Glu Arg Gln Gln His Gly Glu Lys Glu Glu Asp Glu
85 90 95
Gly Glu Gln Pro Arg Pro Phe Pro Phe Pro Arg Pro Arg Gln Pro Arg
100 105 110
Gln Glu Glu Glu His Glu Gln Lys Glu Glu His Glu Trp His Arg Lys
115 120 125
Glu Glu Lys His Gly Gly Lys Gly Ser Glu Glu Glu Gln Asp Glu Arg
130 135 140
Glu His Pro Arg Pro His Gln Pro His Gln Lys Glu Glu Glu Lys His
145 150 155 160
Glu Trp Gln His Lys Gln Glu Lys His Gln Gly Lys Glu Ser Glu Glu
165 170 175
Glu Glu Glu Asp Gln Asp Glu Asp Glu Glu Gln Asp Lys Glu Ser Gln
180 185 190
Glu Ser Glu Gly Ser Glu Ser Gln Arg Glu Pro Arg Arg His Lys Asn
195 200 205
Lys Asn Pro Phe His Phe Asn Ser Lys Arg Phe Gln Thr Leu Phe Lys
210 215 220
Asn Gln Tyr Gly His Val Arg Val Leu Gln Arg Phe Asn Lys Arg Ser
225 230 235 240
Gln Gln Leu Gln Asn Leu Arg Asp Tyr Arg Ile Leu Glu Phe Asn Ser
245 250 255
Lys Pro Asn Thr Leu Leu Leu Pro His His Ala Asp Ala Asp Tyr Leu
260 265 270
Ile Val Ile Leu Asn Gly Thr Ala Ile Leu Thr Leu Val Asn Asn Asp
275 280 285
Asp Arg Asp Ser Tyr Asn Leu Gln Ser Gly Asp Ala Leu Arg Val Pro
290 295 300
Ala Gly Thr Thr Tyr Tyr Val Val Asn Pro Asp Asn Asp Glu Asn Leu
305 310 315 320
Arg Met Ile Thr Leu Ala Ile Pro Val Asn Lys Pro Gly Arg Phe Glu
325 330 335
Ser Phe Phe Leu Ser Ser Thr Gln Ala Gln Gln Ser Tyr Leu Gln Gly
340 345 350
Phe Ser Lys Asn Ile Leu Glu Ala Ser Tyr Asp Thr Lys Phe Glu Glu
355 360 365
Ile Asn Lys Val Leu Phe Gly Arg Glu Glu Gly Gln Gln Gln Gly Glu
370 375 380
Glu Arg Leu Gln Glu Ser Val Ile Val Glu Ile Ser Lys Lys Gln Ile
385 390 395 400
Arg Glu Leu Ser Lys His Ala Lys Ser Ser Ser Arg Lys Thr Ile Ser
405 410 415
Ser Glu Asp Lys Pro Phe Asn Leu Arg Ser Arg Asp Pro Ile Tyr Ser
420 425 430
Asn Lys Leu Gly Lys Leu Phe Glu Ile Thr Pro Glu Lys Asn Pro Gln
435 440 445
Leu Arg Asp Leu Asp Val Phe Leu Ser Val Val Asp Met Asn Glu Gly
450 455 460
Ala Leu Phe Leu Pro His Phe Asn Ser Lys Ala Ile Val Val Leu Val
465 470 475 480
Ile Asn Glu Gly Glu Ala Asn Ile Glu Leu Val Gly Ile Lys Glu Gln
485 490 495
Gln Gln Arg Gln Gln Gln Glu Glu Gln Pro Leu Glu Val Arg Lys Tyr
500 505 510
Arg Ala Glu Leu Ser Glu Gln Asp Ile Phe Val Ile Pro Ala Gly Tyr
515 520 525
Pro Val Val Val Asn Ala Thr Ser Asp Leu Asn Phe Phe Ala Phe Gly
530 535 540
Ile Asn Ala Glu Asn Asn Gln Arg Asn Phe Leu Ala Gly Ser Lys Asp
545 550 555 560
Asn Val Ile Ser Gln Ile Pro Ser Gln Val Gln Glu Leu Ala Phe Pro
565 570 575
Gly Ser Ala Lys Asp Ile Glu Asn Leu Ile Lys Ser Gln Ser Glu Ser
580 585 590
Tyr Phe Val Asp Ala Gln Pro Gln Gln Lys Glu Glu Gly Asn Lys Gly
595 600 605
Arg Lys Gly Pro Leu Ser Ser Ile Leu Arg Ala Phe Tyr
610 615 620
<210> 65
<211> 439
<212> PRT
<213>Manually
<220>
<223> Gly m 5 Glyma20g28460.1 BLAST 440aa
<400> 65
Met Met Arg Val Arg Phe Pro Leu Leu Val Leu Leu Gly Thr Val Phe
1 5 10 15
Leu Ala Ser Val Cys Val Ser Leu Lys Val Arg Glu Asp Glu Asn Asn
20 25 30
Pro Phe Tyr Leu Arg Ser Ser Asn Ser Phe Gln Thr Leu Phe Glu Asn
35 40 45
Gln Asn Gly Arg Ile Arg Leu Leu Gln Arg Phe Asn Lys Arg Ser Pro
50 55 60
Gln Leu Glu Asn Leu Arg Asp Tyr Arg Ile Val Gln Phe Gln Ser Lys
65 70 75 80
Pro Asn Thr Ile Leu Leu Pro His His Ala Asp Ala Asp Phe Leu Leu
85 90 95
Phe Val Leu Ser Gly Arg Ala Ile Leu Thr Leu Val Asn Asn Asp Asp
100 105 110
Arg Asp Ser Tyr Asn Leu His Pro Gly Asp Ala Gln Arg Ile Pro Ala
115 120 125
Gly Thr Thr Tyr Tyr Leu Val Asn Pro His Asp His Gln Asn Leu Lys
130 135 140
Ile Ile Lys Leu Ala Ile Pro Val Asn Lys Pro Gly Arg Tyr Asp Asp
145 150 155 160
Phe Phe Leu Ser Ser Thr Gln Ala Gln Gln Ser Tyr Leu Gln Gly Phe
165 170 175
Ser His Asn Ile Leu Glu Thr Ser Phe His Ser Glu Phe Glu Glu Ile
180 185 190
Asn Arg Val Leu Phe Gly Glu Glu Glu Glu Gln Arg Gln Gln Glu Gly
195 200 205
Val Ile Val Glu Leu Ser Lys Glu Gln Ile Arg Gln Leu Ser Arg Arg
210 215 220
Ala Lys Ser Ser Ser Arg Lys Thr Ile Ser Ser Glu Asp Glu Pro Phe
225 230 235 240
Asn Leu Arg Ser Arg Asn Pro Ile Tyr Ser Asn Asn Phe Gly Lys Phe
245 250 255
Phe Glu Ile Thr Pro Glu Lys Asn Pro Gln Leu Arg Asp Leu Asp Ile
260 265 270
Phe Leu Ser Ser Val Asp Ile Asn Glu Gly Ala Leu Leu Leu Pro His
275 280 285
Phe Asn Ser Lys Ala Ile Val Ile Leu Val Ile Asn Glu Gly Asp Ala
290 295 300
Asn Ile Glu Leu Val Gly Ile Lys Glu Gln Gln Gln Lys Gln Lys Gln
305 310 315 320
Glu Glu Glu Pro Leu Glu Val Gln Arg Tyr Arg Ala Glu Leu Ser Glu
325 330 335
Asp Asp Val Phe Val Ile Pro Ala Ala Tyr Pro Phe Val Val Asn Ala
340 345 350
Thr Ser Asn Leu Asn Phe Leu Ala Phe Gly Ile Asn Ala Glu Asn Asn
355 360 365
Gln Arg Asn Phe Leu Ala Gly Glu Lys Asp Asn Val Val Arg Gln Ile
370 375 380
Glu Arg Gln Val Gln Glu Leu Ala Phe Pro Gly Ser Ala Gln Asp Val
385 390 395 400
Glu Arg Leu Leu Lys Lys Gln Arg Glu Ser Tyr Phe Val Asp Ala Gln
405 410 415
Pro Gln Gln Lys Glu Glu Gly Ser Lys Gly Arg Lys Gly Pro Phe Pro
420 425 430
Ser Ile Leu Gly Ala Leu Tyr
435
<210> 66
<211> 439
<212> PRT
<213>Manually
<220>
<223> Gly m 5 Ping AAB23463 439aa
<400> 66
Met Met Arg Val Arg Phe Pro Leu Leu Val Leu Leu Gly Thr Val Phe
1 5 10 15
Leu Ala Ser Val Cys Val Ser Leu Lys Val Arg Glu Asp Glu Asn Asn
20 25 30
Pro Phe Tyr Phe Arg Ser Ser Asn Ser Phe Gln Thr Leu Phe Glu Asn
35 40 45
Gln Asn Val Arg Ile Arg Leu Leu Gln Arg Phe Asn Lys Arg Ser Pro
50 55 60
Gln Leu Glu Asn Leu Arg Asp Tyr Arg Ile Val Gln Phe Gln Ser Lys
65 70 75 80
Pro Asn Thr Ile Leu Leu Pro His His Ala Asp Ala Asp Phe Leu Leu
85 90 95
Phe Val Leu Ser Gly Arg Ala Ile Leu Thr Leu Val Asn Asn Asp Asp
100 105 110
Arg Asp Ser Tyr Asn Leu His Pro Gly Asp Ala Gln Arg Ile Pro Ala
115 120 125
Gly Thr Thr Tyr Tyr Leu Val Asn Pro His Asp His Gln Asn Leu Lys
130 135 140
Ile Ile Lys Leu Ala Ile Pro Val Asn Lys Pro Gly Arg Tyr Asp Asp
145 150 155 160
Phe Phe Leu Ser Ser Thr Gln Ala Gln Gln Ser Tyr Leu Gln Gly Phe
165 170 175
Ser His Asn Ile Leu Glu Thr Ser Phe His Ser Glu Phe Glu Glu Ile
180 185 190
Asn Arg Val Leu Phe Gly Glu Glu Glu Glu Gln Arg Gln Gln Glu Gly
195 200 205
Val Ile Val Glu Leu Ser Lys Glu Gln Ile Arg Gln Leu Ser Arg Arg
210 215 220
Ala Lys Ser Ser Ser Arg Lys Thr Ile Ser Ser Glu Asp Glu Pro Phe
225 230 235 240
Asn Leu Arg Ser Arg Asn Pro Ile Tyr Ser Asn Asn Phe Gly Lys Phe
245 250 255
Phe Glu Ile Thr Pro Glu Lys Asn Pro Gln Leu Arg Asp Leu Asp Ile
260 265 270
Phe Leu Ser Ser Val Asp Ile Asn Glu Gly Ala Leu Leu Leu Pro His
275 280 285
Phe Asn Ser Lys Ala Ile Val Ile Leu Val Ile Asn Glu Gly Asp Ala
290 295 300
Asn Ile Glu Leu Val Gly Ile Lys Glu Gln Gln Gln Lys Gln Lys Gln
305 310 315 320
Glu Glu Glu Pro Leu Glu Val Gln Arg Tyr Arg Ala Glu Leu Ser Glu
325 330 335
Asp Asp Val Phe Val Ile Pro Ala Ala Tyr Pro Phe Val Val Asn Ala
340 345 350
Thr Ser Asn Leu Asn Phe Leu Ala Phe Gly Ile Asn Ala Glu Asn Asn
355 360 365
Gln Arg Asn Phe Leu Ala Gly Glu Lys Asp Asn Val Val Arg Gln Ile
370 375 380
Glu Arg Gln Val Gln Glu Leu Ala Phe Pro Gly Ser Ala Gln Asp Val
385 390 395 400
Glu Arg Leu Leu Lys Lys Gln Arg Glu Ser Tyr Phe Val Asp Ala Gln
405 410 415
Pro Gln Gln Lys Glu Glu Gly Ser Lys Gly Arg Lys Gly Pro Phe Pro
420 425 430
Ser Ile Leu Gly Ala Leu Tyr
435
<210> 67
<211> 605
<212> PRT
<213>Manually
<220>
<223> Gly m 5 Glyma20g28650.1 BLAST 606aa
<400> 67
Met Met Arg Ala Arg Phe Pro Leu Leu Leu Leu Gly Leu Val Phe Leu
1 5 10 15
Ala Ser Val Ser Val Ser Phe Gly Ile Ala Tyr Trp Glu Lys Glu Asn
20 25 30
Pro Lys His Asn Lys Cys Leu Gln Ser Cys Asn Ser Glu Arg Asp Ser
35 40 45
Tyr Arg Asn Gln Ala Cys His Ala Arg Cys Asn Leu Leu Lys Val Glu
50 55 60
Lys Glu Glu Cys Glu Glu Gly Glu Ile Pro Arg Pro Arg Pro Arg Pro
65 70 75 80
Gln His Pro Glu Arg Glu Pro Gln Gln Pro Gly Glu Lys Glu Glu Asp
85 90 95
Glu Asp Glu Gln Pro Arg Pro Ile Pro Phe Pro Arg Pro Gln Pro Arg
100 105 110
Gln Glu Glu Glu His Glu Gln Arg Glu Glu Gln Glu Trp Pro Arg Lys
115 120 125
Glu Glu Lys Arg Gly Glu Lys Gly Ser Glu Glu Glu Asp Glu Asp Glu
130 135 140
Asp Glu Glu Gln Asp Glu Arg Gln Phe Pro Phe Pro Arg Pro Pro His
145 150 155 160
Gln Lys Glu Glu Arg Lys Gln Glu Glu Asp Glu Asp Glu Glu Gln Gln
165 170 175
Arg Glu Ser Glu Glu Ser Glu Asp Ser Glu Leu Arg Arg His Lys Asn
180 185 190
Lys Asn Pro Phe Leu Phe Gly Ser Asn Arg Phe Glu Thr Leu Phe Lys
195 200 205
Asn Gln Tyr Gly Arg Ile Arg Val Leu Gln Arg Phe Asn Gln Arg Ser
210 215 220
Pro Gln Leu Gln Asn Leu Arg Asp Tyr Arg Ile Leu Glu Phe Asn Ser
225 230 235 240
Lys Pro Asn Thr Leu Leu Leu Pro Asn His Ala Asp Ala Asp Tyr Leu
245 250 255
Ile Val Ile Leu Asn Gly Thr Ala Ile Leu Ser Leu Val Asn Asn Asp
260 265 270
Asp Arg Asp Ser Tyr Arg Leu Gln Ser Gly Asp Ala Leu Arg Val Pro
275 280 285
Ser Gly Thr Thr Tyr Tyr Val Val Asn Pro Asp Asn Asn Glu Asn Leu
290 295 300
Arg Leu Ile Thr Leu Ala Ile Pro Val Asn Lys Pro Gly Arg Phe Glu
305 310 315 320
Ser Phe Phe Leu Ser Ser Thr Glu Ala Gln Gln Ser Tyr Leu Gln Gly
325 330 335
Phe Ser Arg Asn Ile Leu Glu Ala Ser Tyr Asp Thr Lys Phe Glu Glu
340 345 350
Ile Asn Lys Val Leu Phe Ser Arg Glu Glu Gly Gln Gln Gln Gly Glu
355 360 365
Gln Arg Leu Gln Glu Ser Val Ile Val Glu Ile Ser Lys Glu Gln Ile
370 375 380
Arg Ala Leu Ser Lys Arg Ala Lys Ser Ser Ser Arg Lys Thr Ile Ser
385 390 395 400
Ser Glu Asp Lys Pro Phe Asn Leu Arg Ser Arg Asp Pro Ile Tyr Ser
405 410 415
Asn Lys Leu Gly Lys Phe Phe Glu Ile Thr Pro Glu Lys Asn Pro Gln
420 425 430
Leu Arg Asp Leu Asp Ile Phe Leu Ser Ile Val Asp Met Asn Glu Gly
435 440 445
Ala Leu Leu Leu Pro His Phe Asn Ser Lys Ala Ile Val Ile Leu Val
450 455 460
Ile Asn Glu Gly Asp Ala Asn Ile Glu Leu Val Gly Leu Lys Glu Gln
465 470 475 480
Gln Gln Glu Gln Gln Gln Glu Glu Gln Pro Leu Glu Val Arg Lys Tyr
485 490 495
Arg Ala Glu Leu Ser Glu Gln Asp Ile Phe Val Ile Pro Ala Gly Tyr
500 505 510
Pro Val Val Val Asn Ala Thr Ser Asn Leu Asn Phe Phe Ala Ile Gly
515 520 525
Ile Asn Ala Glu Asn Asn Gln Arg Asn Phe Leu Ala Gly Ser Gln Asp
530 535 540
Asn Val Ile Ser Gln Ile Pro Ser Gln Val Gln Glu Leu Ala Phe Pro
545 550 555 560
Gly Ser Ala Gln Ala Val Glu Lys Leu Leu Lys Asn Gln Arg Glu Ser
565 570 575
Tyr Phe Val Asp Ala Gln Pro Lys Lys Lys Glu Glu Gly Asn Lys Gly
580 585 590
Arg Lys Gly Pro Leu Ser Ser Ile Leu Arg Ala Phe Tyr
595 600 605
<210> 68
<211> 605
<212> PRT
<213>Manually
<220>
<223> Gly m 5 Glyma20g28660.1 BLAST 606aa
<400> 68
Met Met Arg Ala Arg Phe Pro Leu Leu Leu Leu Gly Leu Val Phe Leu
1 5 10 15
Ala Ser Val Ser Val Ser Phe Gly Ile Ala Tyr Trp Glu Lys Glu Asn
20 25 30
Pro Lys His Asn Lys Cys Leu Gln Ser Cys Asn Ser Glu Arg Asp Ser
35 40 45
Tyr Arg Asn Gln Ala Cys His Ala Arg Cys Asn Leu Leu Lys Val Glu
50 55 60
Lys Glu Glu Cys Glu Glu Gly Glu Ile Pro Arg Pro Arg Pro Arg Pro
65 70 75 80
Gln His Pro Glu Arg Glu Pro Gln Gln Pro Gly Glu Lys Glu Glu Asp
85 90 95
Glu Asp Glu Gln Pro Arg Pro Ile Pro Phe Pro Arg Pro Gln Pro Arg
100 105 110
Gln Glu Glu Glu His Glu Gln Arg Glu Glu Gln Glu Trp Pro Arg Lys
115 120 125
Glu Glu Lys Arg Gly Glu Lys Gly Ser Glu Glu Glu Asp Glu Asp Glu
130 135 140
Asp Glu Glu Gln Asp Glu Arg Gln Phe Pro Phe Pro Arg Pro Pro His
145 150 155 160
Gln Lys Glu Glu Arg Lys Gln Glu Glu Asp Glu Asp Glu Glu Gln Gln
165 170 175
Arg Glu Ser Glu Glu Ser Glu Asp Ser Glu Leu Arg Arg His Lys Asn
180 185 190
Lys Asn Pro Phe Leu Phe Gly Ser Asn Arg Phe Glu Thr Leu Phe Lys
195 200 205
Asn Gln Tyr Gly Arg Ile Arg Val Leu Gln Arg Phe Asn Gln Arg Ser
210 215 220
Pro Gln Leu Gln Asn Leu Arg Asp Tyr Arg Ile Leu Glu Phe Asn Ser
225 230 235 240
Lys Pro Asn Thr Leu Leu Leu Pro Asn His Ala Asp Ala Asp Tyr Leu
245 250 255
Ile Val Ile Leu Asn Gly Thr Ala Ile Leu Ser Leu Val Asn Asn Asp
260 265 270
Asp Arg Asp Ser Tyr Arg Leu Gln Ser Gly Asp Ala Leu Arg Val Pro
275 280 285
Ser Gly Thr Thr Tyr Tyr Val Val Asn Pro Asp Asn Asn Glu Asn Leu
290 295 300
Arg Leu Ile Thr Leu Ala Ile Pro Val Asn Lys Pro Gly Arg Phe Glu
305 310 315 320
Ser Phe Phe Leu Ser Ser Thr Glu Ala Gln Gln Ser Tyr Leu Gln Gly
325 330 335
Phe Ser Arg Asn Ile Leu Glu Ala Ser Tyr Asp Thr Lys Phe Glu Glu
340 345 350
Ile Asn Lys Val Leu Phe Ser Arg Glu Glu Gly Gln Gln Gln Gly Glu
355 360 365
Gln Arg Leu Gln Glu Ser Val Ile Val Glu Ile Ser Lys Glu Gln Ile
370 375 380
Arg Ala Leu Ser Lys Arg Ala Lys Ser Ser Ser Arg Lys Thr Ile Ser
385 390 395 400
Ser Glu Asp Lys Pro Phe Asn Leu Arg Ser Arg Asp Pro Ile Tyr Ser
405 410 415
Asn Lys Leu Gly Lys Phe Phe Glu Ile Thr Pro Glu Lys Asn Pro Gln
420 425 430
Leu Arg Asp Leu Asp Ile Phe Leu Ser Ile Val Asp Met Asn Glu Gly
435 440 445
Ala Leu Leu Leu Pro His Phe Asn Ser Lys Ala Ile Val Ile Leu Val
450 455 460
Ile Asn Glu Gly Asp Ala Asn Ile Glu Leu Val Gly Leu Lys Glu Gln
465 470 475 480
Gln Gln Glu Gln Gln Gln Glu Glu Gln Pro Leu Glu Val Arg Lys Tyr
485 490 495
Arg Ala Glu Leu Ser Glu Gln Asp Ile Phe Val Ile Pro Ala Gly Tyr
500 505 510
Pro Val Val Val Asn Ala Thr Ser Asn Leu Asn Phe Phe Ala Ile Gly
515 520 525
Ile Asn Ala Glu Asn Asn Gln Arg Asn Phe Leu Ala Gly Ser Gln Asp
530 535 540
Asn Val Ile Ser Gln Ile Pro Ser Gln Val Gln Glu Leu Ala Phe Pro
545 550 555 560
Gly Ser Ala Gln Ala Val Glu Lys Leu Leu Lys Asn Gln Arg Glu Ser
565 570 575
Tyr Phe Val Asp Ala Gln Pro Lys Lys Lys Glu Glu Gly Asn Lys Gly
580 585 590
Arg Lys Gly Pro Leu Ser Ser Ile Leu Arg Ala Phe Tyr
595 600 605
<210> 69
<211> 542
<212> PRT
<213>Manually
<220>
<223> Gly m 5 Glyma20g28650.2 BLAST 543aa
<400> 69
Met Met Arg Ala Arg Phe Pro Leu Leu Leu Leu Gly Leu Val Phe Leu
1 5 10 15
Ala Ser Val Ser Val Ser Phe Gly Ile Ala Tyr Trp Glu Lys Glu Asn
20 25 30
Pro Lys His Asn Lys Cys Leu Gln Ser Cys Asn Ser Glu Arg Asp Ser
35 40 45
Tyr Arg Asn Gln Ala Cys His Ala Arg Cys Asn Leu Leu Lys Val Glu
50 55 60
Lys Glu Glu Cys Glu Glu Gly Glu Ile Pro Arg Pro Arg Pro Arg Pro
65 70 75 80
Gln His Pro Glu Arg Glu Pro Gln Gln Pro Gly Glu Lys Glu Glu Asp
85 90 95
Glu Asp Glu Gln Pro Arg Pro Ile Pro Phe Pro Arg Pro Gln Pro Arg
100 105 110
Gln Glu Glu Glu His Glu Gln Arg Glu Glu Gln Glu Trp Pro Arg Lys
115 120 125
Glu Glu Lys Arg Gly Glu Lys Gly Ser Glu Glu Glu Asp Glu Asp Glu
130 135 140
Asp Glu Glu Gln Asp Glu Arg Gln Phe Pro Phe Pro Arg Pro Pro His
145 150 155 160
Gln Lys Glu Glu Arg Lys Gln Glu Glu Asp Glu Asp Glu Glu Gln Gln
165 170 175
Arg Glu Ser Glu Glu Ser Glu Asp Ser Glu Leu Arg Arg His Lys Asn
180 185 190
Lys Asn Pro Phe Leu Phe Gly Ser Asn Arg Phe Glu Thr Leu Phe Lys
195 200 205
Asn Gln Tyr Gly Arg Ile Arg Val Leu Gln Arg Phe Asn Gln Arg Ser
210 215 220
Pro Gln Leu Gln Asn Leu Arg Asp Tyr Arg Ile Leu Glu Phe Asn Ser
225 230 235 240
Lys Pro Asn Thr Leu Leu Leu Pro Asn His Ala Asp Ala Asp Tyr Leu
245 250 255
Ile Val Ile Leu Asn Gly Thr Ala Ile Leu Ser Leu Val Asn Asn Asp
260 265 270
Asp Arg Asp Ser Tyr Arg Leu Gln Ser Gly Asp Ala Leu Arg Val Pro
275 280 285
Ser Gly Thr Thr Tyr Tyr Val Val Asn Pro Asp Asn Asn Glu Asn Leu
290 295 300
Arg Leu Ile Thr Leu Ala Ile Pro Val Asn Lys Pro Gly Arg Phe Glu
305 310 315 320
Ser Phe Phe Leu Ser Ser Thr Glu Ala Gln Gln Ser Tyr Leu Gln Gly
325 330 335
Phe Ser Arg Asn Ile Leu Glu Ala Ser Tyr Asp Thr Lys Phe Glu Glu
340 345 350
Ile Asn Lys Val Leu Phe Ser Arg Glu Glu Gly Gln Gln Gln Gly Glu
355 360 365
Gln Arg Leu Gln Glu Ser Val Ile Val Glu Ile Ser Lys Glu Gln Ile
370 375 380
Arg Ala Leu Ser Lys Arg Ala Lys Ser Ser Ser Arg Lys Thr Ile Ser
385 390 395 400
Ser Glu Asp Lys Pro Phe Asn Leu Arg Ser Arg Asp Pro Ile Tyr Ser
405 410 415
Asn Lys Leu Gly Lys Phe Phe Glu Ile Thr Pro Glu Lys Asn Pro Gln
420 425 430
Leu Arg Asp Leu Asp Ile Phe Leu Ser Ile Val Asp Met Asn Glu Gly
435 440 445
Ala Leu Leu Leu Pro His Phe Asn Ser Lys Ala Ile Val Ile Leu Val
450 455 460
Ile Asn Glu Gly Asp Ala Asn Ile Glu Leu Val Gly Leu Lys Glu Gln
465 470 475 480
Gln Gln Glu Gln Gln Gln Glu Glu Gln Pro Leu Glu Val Arg Lys Tyr
485 490 495
Arg Ala Glu Leu Ser Glu Gln Asp Ile Phe Val Ile Pro Ala Gly Tyr
500 505 510
Pro Val Val Val Asn Ala Thr Ser Asn Leu Asn Phe Phe Ala Ile Gly
515 520 525
Ile Asn Ala Glu Asn Asn Gln Arg Asn Phe Leu Ala Gly Ile
530 535 540
<210> 70
<211> 218
<212> PRT
<213>Manually
<220>
<223> Gly m 5 Ping AAA33947 218aa
<400> 70
Ser Lys Arg Ala Lys Ser Ser Ser Arg Lys Thr Ile Ser Ser Glu Asp
1 5 10 15
Lys Pro Phe Asn Leu Gly Ser Arg Asp Pro Ile Tyr Ser Lys Lys Leu
20 25 30
Gly Lys Phe Phe Glu Ile Thr Pro Glu Lys Asn Pro Gln Leu Arg Asp
35 40 45
Leu Asp Ile Phe Leu Ser Ile Val Asp Met Asn Glu Gly Ala Leu Leu
50 55 60
Leu Pro His Phe Asn Ser Lys Ala Ile Val Ile Leu Val Ile Asn Glu
65 70 75 80
Gly Asp Ala Asn Ile Glu Leu Val Gly Leu Lys Glu Gln Gln Gln Glu
85 90 95
Gln Gln Gln Glu Glu Gln Pro Leu Glu Val Arg Lys Tyr Arg Ala Glu
100 105 110
Leu Ser Glu Gln Asp Ile Phe Val Ile Pro Ala Gly Tyr Pro Val Val
115 120 125
Val Asn Ala Thr Ser Asn Leu Asn Phe Phe Ala Ile Gly Ile Asn Ala
130 135 140
Glu Asn Asn Gln Arg Asn Phe Leu Ala Gly Ser Gln Asp Asn Val Ile
145 150 155 160
Ser Gln Ile Pro Ser Gln Val Gln Glu Leu Ala Phe Pro Gly Ser Ala
165 170 175
Gln Ala Val Glu Lys Leu Leu Lys Asn Gln Arg Glu Ser Tyr Phe Val
180 185 190
Asp Ala Gln Pro Asn Glu Lys Glu Glu Gly Asn Lys Gly Arg Lys Gly
195 200 205
Pro Leu Ser Ser Ile Leu Arg Ala Phe Tyr
210 215
<210> 71
<211> 621
<212> PRT
<213>Manually
<220>
<223> Gly m 5 NP_001237316 BLAST 621aa
<400> 71
Met Met Arg Ala Arg Phe Pro Leu Leu Leu Leu Gly Val Val Phe Leu
1 5 10 15
Ala Ser Val Ser Val Ser Phe Gly Ile Ala Tyr Trp Glu Lys Gln Asn
20 25 30
Pro Ser His Asn Lys Cys Leu Arg Ser Cys Asn Ser Glu Lys Asp Ser
35 40 45
Tyr Arg Asn Gln Ala Cys His Ala Arg Cys Asn Leu Leu Lys Val Glu
50 55 60
Glu Glu Glu Glu Cys Glu Glu Gly Gln Ile Pro Arg Pro Arg Pro Gln
65 70 75 80
His Pro Glu Arg Glu Arg Gln Gln His Gly Glu Lys Glu Glu Asp Glu
85 90 95
Gly Glu Gln Pro Arg Pro Phe Pro Phe Pro Arg Pro Arg Gln Pro Arg
100 105 110
Gln Glu Gly Glu His Glu Gln Lys Glu Glu His Glu Trp His Arg Lys
115 120 125
Glu Glu Lys His Gly Gly Lys Gly Ser Glu Glu Glu Gln Asp Gly Arg
130 135 140
Glu His Pro Arg Pro His Gln Pro His Gln Lys Glu Glu Glu Lys His
145 150 155 160
Glu Trp Gln His Lys Gln Glu Lys His Gln Gly Lys Glu Ser Glu Glu
165 170 175
Glu Glu Glu Asp Gln Asp Glu Asp Glu Glu Gln Asp Lys Glu Ser Gln
180 185 190
Glu Ser Glu Gly Ser Glu Ser Gln Arg Glu Pro Arg Arg His Lys Asn
195 200 205
Lys Asn Pro Phe His Phe Asn Ser Lys Arg Phe Gln Thr Leu Phe Lys
210 215 220
Asn Gln Tyr Gly His Val Arg Val Leu Gln Arg Phe Asn Lys Arg Ser
225 230 235 240
Gln Gln Leu Gln Asn Leu Arg Asp Tyr Arg Ile Leu Glu Phe Asn Ser
245 250 255
Lys Pro Asn Thr Leu Leu Leu Pro His His Ala Asp Ala Asp Tyr Leu
260 265 270
Ile Val Ile Leu Asn Gly Thr Ala Ile Leu Thr Leu Val Asn Asn Asp
275 280 285
Asp Arg Asp Ser Tyr Asn Leu Gln Ser Gly Asp Ala Leu Arg Val Pro
290 295 300
Ala Gly Thr Thr Tyr Tyr Val Val Asn Pro Asp Asn Asp Glu Asn Leu
305 310 315 320
Arg Met Ile Thr Leu Ala Ile Pro Val Asn Lys Pro Gly Arg Phe Glu
325 330 335
Ser Phe Phe Leu Ser Ser Thr Gln Ala Gln Gln Ser Tyr Leu Gln Gly
340 345 350
Phe Ser Lys Asn Ile Leu Glu Ala Ser Tyr Asp Thr Lys Phe Glu Glu
355 360 365
Ile Asn Lys Val Leu Phe Gly Arg Glu Glu Gly Gln Gln Gln Gly Glu
370 375 380
Glu Arg Leu Gln Glu Ser Val Ile Val Glu Ile Ser Lys Lys Gln Ile
385 390 395 400
Arg Glu Leu Ser Lys Arg Ala Lys Ser Ser Ser Arg Lys Thr Ile Ser
405 410 415
Ser Glu Asp Lys Pro Phe Asn Leu Arg Ser Arg Asp Pro Ile Tyr Ser
420 425 430
Asn Lys Leu Gly Lys Leu Phe Glu Ile Thr Pro Glu Lys Asn Pro Gln
435 440 445
Leu Arg Asp Leu Asp Val Phe Leu Ser Val Val Asp Met Asn Glu Gly
450 455 460
Ala Leu Phe Leu Pro His Phe Asn Ser Lys Ala Ile Val Val Leu Val
465 470 475 480
Ile Asn Glu Gly Glu Ala Asn Ile Glu Leu Val Gly Ile Lys Glu Gln
485 490 495
Gln Gln Arg Gln Gln Gln Glu Glu Gln Pro Leu Glu Val Arg Lys Tyr
500 505 510
Arg Ala Glu Leu Ser Glu Gln Asp Ile Phe Val Ile Pro Ala Gly Tyr
515 520 525
Pro Val Val Val Asn Ala Thr Ser Asp Leu Asn Phe Phe Ala Phe Gly
530 535 540
Ile Asn Ala Glu Asn Asn Gln Arg Asn Phe Leu Ala Gly Ser Lys Asp
545 550 555 560
Asn Val Ile Ser Gln Ile Pro Ser Gln Val Gln Glu Leu Ala Phe Leu
565 570 575
Gly Ser Ala Lys Asp Ile Glu Asn Leu Ile Lys Ser Gln Ser Glu Ser
580 585 590
Tyr Phe Val Asp Ala Gln Pro Gln Gln Lys Glu Glu Gly Asn Lys Gly
595 600 605
Arg Lys Gly Pro Leu Ser Ser Ile Leu Arg Ala Phe Tyr
610 615 620
<210> 72
<211> 621
<212> PRT
<213>Manually
<220>
<223> Gly m 5 BAE02726 BLAST 621aa
<400> 72
Met Met Arg Ala Arg Phe Pro Leu Leu Leu Leu Gly Val Val Phe Leu
1 5 10 15
Ala Ser Val Ser Val Ser Phe Gly Ile Ala Tyr Trp Glu Lys Gln Asn
20 25 30
Pro Ser His Asn Lys Cys Leu Arg Ser Cys Asn Ser Glu Lys Asp Ser
35 40 45
Tyr Arg Asn Gln Ala Cys His Ala Arg Cys Asn Leu Leu Lys Val Glu
50 55 60
Glu Glu Glu Glu Cys Glu Glu Gly Gln Ile Pro Arg Pro Arg Pro Gln
65 70 75 80
His Pro Glu Arg Glu Arg Gln Gln His Gly Glu Lys Glu Glu Asp Glu
85 90 95
Gly Glu Gln Pro Arg Pro Phe Pro Phe Pro Arg Pro Arg Gln Pro His
100 105 110
Gln Glu Glu Glu His Glu Gln Lys Glu Glu His Glu Trp His Arg Lys
115 120 125
Glu Glu Lys His Gly Gly Lys Gly Ser Glu Glu Glu Gln Asp Glu Arg
130 135 140
Glu His Pro Arg Pro His Gln Pro His Gln Lys Glu Glu Glu Lys His
145 150 155 160
Glu Trp Gln His Lys Gln Glu Lys His Gln Gly Lys Glu Ser Glu Glu
165 170 175
Glu Glu Glu Asp Gln Asp Glu Asp Glu Glu Gln Asp Lys Glu Ser Gln
180 185 190
Glu Ser Glu Gly Ser Glu Ser Gln Arg Glu Pro Arg Arg His Lys Asn
195 200 205
Lys Asn Pro Phe His Phe Asn Ser Lys Arg Phe Gln Thr Leu Phe Lys
210 215 220
Asn Gln Tyr Gly His Val Arg Val Leu Gln Arg Phe Asn Lys Arg Ser
225 230 235 240
Gln Gln Leu Gln Asn Leu Arg Asp Tyr Arg Ile Leu Glu Phe Asn Ser
245 250 255
Lys Pro Asn Thr Leu Leu Leu Pro His His Ala Asp Ala Asp Tyr Leu
260 265 270
Ile Val Ile Leu Asn Gly Thr Ala Ile Leu Thr Leu Val Asn Asn Asp
275 280 285
Asp Arg Asp Ser Tyr Asn Leu Gln Ser Gly Asp Ala Leu Arg Val Pro
290 295 300
Ala Gly Thr Thr Tyr Tyr Val Val Asn Pro Asp Asn Asp Glu Asn Leu
305 310 315 320
Arg Met Ile Thr Leu Ala Ile Pro Val Asn Lys Pro Gly Arg Phe Glu
325 330 335
Ser Phe Phe Leu Ser Ser Thr Gln Ala Gln Gln Ser Tyr Leu Gln Gly
340 345 350
Phe Ser Lys Asn Ile Leu Glu Ala Ser Tyr Asp Thr Lys Phe Glu Glu
355 360 365
Ile Asn Lys Val Leu Phe Gly Arg Glu Glu Gly Gln Gln Gln Gly Glu
370 375 380
Glu Arg Leu Gln Glu Ser Val Ile Val Glu Ile Ser Lys Lys Gln Ile
385 390 395 400
Arg Glu Leu Ser Lys His Ala Lys Ser Ser Ser Arg Lys Thr Ile Ser
405 410 415
Ser Glu Asp Lys Pro Phe Asn Leu Arg Ser Arg Asp Pro Ile Tyr Ser
420 425 430
Asn Lys Leu Gly Lys Leu Phe Glu Ile Thr Pro Glu Lys Asn Pro Gln
435 440 445
Leu Arg Asp Leu Asp Val Phe Leu Ser Val Val Asp Met Asn Glu Gly
450 455 460
Ala Leu Phe Leu Pro His Phe Asn Ser Lys Ala Ile Val Val Leu Val
465 470 475 480
Ile Asn Glu Gly Glu Ala Asn Ile Glu Leu Val Gly Ile Lys Glu Gln
485 490 495
Gln Gln Arg Gln Gln Gln Glu Glu Gln Pro Leu Glu Val Arg Lys Tyr
500 505 510
Arg Ala Glu Leu Ser Glu Gln Asp Ile Phe Val Ile Pro Ala Gly Tyr
515 520 525
Pro Val Val Val Asn Ala Thr Ser Asp Leu Asn Phe Phe Ala Phe Gly
530 535 540
Ile Asn Ala Glu Asn Asn Gln Arg Asn Phe Leu Ala Gly Ser Lys Asp
545 550 555 560
Asn Val Ile Ser Gln Ile Pro Ser Gln Val Gln Glu Leu Ala Phe Pro
565 570 575
Gly Ser Ala Lys Asp Ile Glu Asn Leu Ile Lys Ser Gln Ser Glu Ser
580 585 590
Tyr Phe Val Asp Ala Gln Pro Gln Gln Lys Glu Glu Gly Asn Lys Gly
595 600 605
Arg Lys Gly Pro Leu Ser Ser Ile Leu Arg Ala Phe Tyr
610 615 620
<210> 73
<211> 639
<212> PRT
<213>Manually
<220>
<223> Gly m 5 Ping AAB01374 639aa
<400> 73
Met Met Arg Ala Arg Phe Pro Leu Leu Leu Leu Gly Val Val Phe Leu
1 5 10 15
Ala Ser Val Ser Val Ser Phe Gly Ile Ala Tyr Trp Glu Lys Gln Asn
20 25 30
Pro Ser His Asn Lys Cys Leu Arg Ser Cys Asn Ser Glu Lys Asp Ser
35 40 45
Tyr Arg Asn Gln Ala Cys His Ala Arg Cys Asn Leu Leu Lys Val Glu
50 55 60
Glu Glu Glu Glu Cys Glu Glu Gly Gln Ile Pro Arg Pro Arg Pro Gln
65 70 75 80
His Pro Glu Arg Glu Arg Gln Gln His Gly Glu Lys Glu Glu Asp Glu
85 90 95
Gly Glu Gln Pro Arg Pro Phe Pro Phe Pro Arg Pro Arg Gln Pro His
100 105 110
Gln Glu Glu Glu His Glu Gln Lys Glu Glu His Glu Trp His Arg Lys
115 120 125
Glu Glu Lys His Gly Gly Lys Gly Ser Glu Glu Glu Gln Asp Glu Arg
130 135 140
Glu His Pro Arg Pro His Gln Pro His Gln Lys Glu Glu Glu Lys His
145 150 155 160
Glu Trp Gln His Lys Gln Glu Lys His Gln Gly Lys Glu Ser Glu Glu
165 170 175
Glu Glu Glu Asp Gln Asp Glu Asp Glu Glu Gln Asp Lys Glu Ser Gln
180 185 190
Glu Ser Glu Gly Ser Glu Ser Gln Arg Glu Pro Arg Arg His Lys Asn
195 200 205
Lys Asn Pro Phe His Phe Asn Ser Lys Arg Phe Gln Thr Leu Phe Lys
210 215 220
Asn Gln Tyr Gly His Val Arg Val Leu Gln Arg Phe Asn Lys Arg Ser
225 230 235 240
Gln Gln Leu Gln Asn Leu Arg Asp Tyr Arg Ile Leu Glu Phe Asn Ser
245 250 255
Lys Pro Asn Thr Leu Leu Leu Pro His His Ala Asp Ala Asp Tyr Leu
260 265 270
Ile Val Ile Leu Asn Gly Thr Ala Ile Leu Thr Leu Val Asn Asn Asp
275 280 285
Asp Arg Asp Ser Tyr Asn Leu Gln Ser Gly Asp Ala Leu Arg Val Pro
290 295 300
Ala Gly Thr Thr Phe Tyr Val Val Asn Pro Asp Asn Asp Glu Asn Leu
305 310 315 320
Arg Met Ile Ala Gly Thr Thr Phe Tyr Val Val Asn Pro Asp Asn Asp
325 330 335
Glu Asn Leu Arg Met Ile Thr Leu Ala Ile Pro Val Asn Lys Pro Gly
340 345 350
Arg Phe Glu Ser Phe Phe Leu Ser Ser Thr Gln Ala Gln Gln Ser Tyr
355 360 365
Leu Gln Gly Phe Ser Lys Asn Ile Leu Glu Ala Ser Tyr Asp Thr Lys
370 375 380
Phe Glu Glu Ile Asn Lys Val Leu Phe Gly Arg Glu Glu Gly Gln Gln
385 390 395 400
Gln Gly Glu Glu Arg Leu Gln Glu Ser Val Ile Val Glu Ile Ser Lys
405 410 415
Lys Gln Ile Arg Glu Leu Ser Lys His Ala Lys Ser Ser Ser Arg Lys
420 425 430
Thr Ile Ser Ser Glu Asp Lys Pro Phe Asn Leu Gly Ser Arg Asp Pro
435 440 445
Ile Tyr Ser Asn Lys Leu Gly Lys Leu Phe Glu Ile Thr Gln Arg Asn
450 455 460
Pro Gln Leu Arg Asp Leu Asp Val Phe Leu Ser Val Val Asp Met Asn
465 470 475 480
Glu Gly Ala Leu Phe Leu Pro His Phe Asn Ser Lys Ala Ile Val Val
485 490 495
Leu Val Ile Asn Glu Gly Glu Ala Asn Ile Glu Leu Val Gly Ile Lys
500 505 510
Glu Gln Gln Gln Arg Gln Gln Gln Glu Glu Gln Pro Leu Glu Val Arg
515 520 525
Lys Tyr Arg Ala Glu Leu Ser Glu Gln Asp Ile Phe Val Ile Pro Ala
530 535 540
Gly Tyr Pro Val Met Val Asn Ala Thr Ser Asp Leu Asn Phe Phe Ala
545 550 555 560
Phe Gly Ile Asn Ala Glu Asn Asn Gln Arg Asn Phe Leu Ala Gly Ser
565 570 575
Lys Asp Asn Val Ile Ser Gln Ile Pro Ser Gln Val Gln Glu Leu Ala
580 585 590
Phe Pro Arg Ser Ala Lys Asp Ile Glu Asn Leu Ile Lys Ser Gln Ser
595 600 605
Glu Ser Tyr Phe Val Asp Ala Gln Pro Gln Gln Lys Glu Glu Gly Asn
610 615 620
Lys Gly Arg Lys Gly Pro Leu Ser Ser Ile Leu Arg Ala Phe Tyr
625 630 635
<210> 74
<211> 621
<212> PRT
<213>Manually
<220>
<223> Gly m 5 Glyma10g39150.1 BLAST 622aa
<400> 74
Met Met Arg Ala Arg Phe Pro Leu Leu Leu Leu Gly Val Val Phe Leu
1 5 10 15
Ala Ser Val Ser Val Ser Phe Gly Ile Ala Tyr Trp Glu Lys Gln Asn
20 25 30
Pro Ser His Asn Lys Cys Leu Arg Ser Cys Asn Ser Glu Lys Asp Ser
35 40 45
Tyr Arg Asn Gln Ala Cys His Ala Arg Cys Asn Leu Leu Lys Val Glu
50 55 60
Glu Glu Glu Glu Cys Glu Glu Gly Gln Ile Pro Arg Pro Arg Pro Gln
65 70 75 80
His Pro Glu Arg Glu Arg Gln Gln His Gly Glu Lys Glu Glu Asp Glu
85 90 95
Gly Glu Gln Pro Arg Pro Phe Pro Phe Pro Arg Pro Arg Gln Pro His
100 105 110
Gln Glu Glu Glu His Glu Gln Lys Glu Glu His Glu Trp His Arg Lys
115 120 125
Glu Glu Lys His Gly Gly Lys Gly Ser Glu Glu Glu Gln Asp Glu Arg
130 135 140
Glu His Pro Arg Pro His Gln Pro His Gln Lys Glu Glu Glu Lys His
145 150 155 160
Glu Trp Gln His Lys Gln Glu Lys His Gln Gly Lys Glu Ser Glu Glu
165 170 175
Glu Glu Glu Asp Gln Asp Glu Asp Glu Glu Gln Asp Lys Glu Ser Gln
180 185 190
Glu Ser Glu Gly Ser Glu Ser Gln Arg Glu Pro Arg Arg His Lys Asn
195 200 205
Lys Asn Pro Phe His Phe Asn Ser Lys Arg Phe Gln Thr Leu Phe Lys
210 215 220
Asn Gln Tyr Gly His Val Arg Val Leu Gln Arg Phe Asn Lys Arg Ser
225 230 235 240
Gln Gln Leu Gln Asn Leu Arg Asp Tyr Arg Ile Leu Glu Phe Asn Ser
245 250 255
Lys Pro Asn Thr Leu Leu Leu Pro His His Ala Asp Ala Asp Tyr Leu
260 265 270
Ile Val Ile Leu Asn Gly Thr Ala Ile Leu Thr Leu Val Asn Asn Asp
275 280 285
Asp Arg Asp Ser Tyr Asn Leu Gln Ser Gly Asp Ala Leu Arg Val Pro
290 295 300
Ala Gly Thr Thr Tyr Tyr Val Val Asn Pro Asp Asn Asp Glu Asn Leu
305 310 315 320
Arg Met Ile Thr Leu Ala Ile Pro Val Asn Lys Pro Gly Arg Phe Glu
325 330 335
Ser Phe Phe Leu Ser Ser Thr Gln Ala Gln Gln Ser Tyr Leu Gln Gly
340 345 350
Phe Ser Lys Asn Ile Leu Glu Ala Ser Tyr Asp Thr Lys Phe Glu Glu
355 360 365
Ile Asn Lys Val Leu Phe Gly Arg Glu Glu Gly Gln Gln Gln Gly Glu
370 375 380
Glu Arg Leu Gln Glu Ser Val Ile Val Glu Ile Ser Lys Lys Gln Ile
385 390 395 400
Arg Glu Leu Ser Lys His Ala Lys Ser Ser Ser Arg Lys Thr Ile Ser
405 410 415
Ser Glu Asp Lys Pro Phe Asn Leu Arg Ser Arg Asp Pro Ile Tyr Ser
420 425 430
Asn Lys Leu Gly Lys Leu Phe Glu Ile Thr Pro Glu Lys Asn Pro Gln
435 440 445
Leu Arg Asp Leu Asp Val Phe Leu Ser Val Val Asp Met Asn Glu Gly
450 455 460
Ala Leu Phe Leu Pro His Phe Asn Ser Lys Ala Ile Val Val Leu Val
465 470 475 480
Ile Asn Glu Gly Glu Ala Asn Ile Glu Leu Val Gly Ile Lys Glu Gln
485 490 495
Gln Gln Arg Gln Gln Gln Glu Glu Gln Pro Leu Glu Val Arg Lys Tyr
500 505 510
Arg Ala Glu Leu Ser Glu Gln Asp Ile Phe Val Ile Pro Ala Gly Tyr
515 520 525
Pro Val Val Val Asn Ala Thr Ser Asp Leu Asn Phe Phe Ala Phe Gly
530 535 540
Ile Asn Ala Glu Asn Asn Gln Arg Asn Phe Leu Ala Gly Ser Lys Asp
545 550 555 560
Asn Val Ile Ser Gln Ile Pro Ser Gln Val Gln Glu Leu Ala Phe Pro
565 570 575
Gly Ser Ala Lys Asp Ile Glu Asn Leu Ile Lys Ser Gln Ser Glu Ser
580 585 590
Tyr Phe Val Asp Ala Gln Pro Gln Gln Lys Glu Glu Gly Asn Lys Gly
595 600 605
Arg Lys Gly Pro Leu Ser Ser Ile Leu Arg Ala Phe Tyr
610 615 620
<210> 75
<211> 5
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 5
<400> 75
Cys Asn Leu Leu Lys
1 5
<210> 76
<211> 19
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 5
<400> 76
Glu Glu Asp Glu Asp Glu Gln Pro Arg Pro Ile Pro Phe Pro Arg Pro
1 5 10 15
Gln Pro Arg
<210> 77
<211> 7
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 5
<400> 77
Glu Glu Gln Glu Trp Pro Arg
1 5
<210> 78
<211> 11
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 5
<400> 78
Gln Phe Pro Phe Pro Arg Pro Pro His Gln Lys
1 5 10
<210> 79
<211> 11
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 5
<400> 79
Glu Ser Glu Glu Ser Glu Asp Ser Glu Leu Arg
1 5 10
<210> 80
<211> 9
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 5
<400> 80
Asn Pro Phe Leu Phe Gly Ser Asn Arg
1 5
<210> 81
<211> 6
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 5
<400> 81
Phe Glu Thr Leu Phe Lys
1 5
<210> 82
<211> 8
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 5
<400> 82
Ser Pro Gln Leu Gln Asn Leu Arg
1 5
<210> 83
<211> 8
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 5
<400> 83
Leu Gln Ser Gly Asp Ala Leu Arg
1 5
<210> 84
<211> 19
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 5
<400> 84
Val Pro Ser Gly Thr Thr Tyr Tyr Val Val Asn Pro Asp Asn Asn Glu
1 5 10 15
Asn Leu Arg
<210> 85
<211> 21
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 5
<400> 85
Phe Glu Ser Phe Phe Leu Ser Ser Thr Glu Ala Gln Gln Ser Tyr Leu
1 5 10 15
Gln Gly Phe Ser Arg
20
<210> 86
<211> 6
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 5
<400> 86
Phe Glu Glu Ile Asn Lys
1 5
<210> 87
<211> 5
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 5
<400> 87
Val Leu Phe Ser Arg
1 5
<210> 88
<211> 12
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 5
<400> 88
Thr Ile Ser Ser Glu Asp Lys Pro Phe Asn Leu Arg
1 5 10
<210> 89
<211> 7
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 5
<400> 89
Asp Pro Ile Tyr Ser Asn Lys
1 5
<210> 90
<211> 8
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 5
<400> 90
Phe Phe Glu Ile Thr Pro Glu Lys
1 5
<210> 91
<211> 20
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 5
<400> 91
Ala Ile Val Ile Leu Val Ile Asn Glu Gly Asp Ala Asn Ile Glu Leu
1 5 10 15
Val Gly Leu Lys
20
<210> 92
<211> 16
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 5
<400> 92
Glu Gln Gln Gln Glu Gln Gln Gln Glu Glu Gln Pro Leu Glu Val Arg
1 5 10 15
<210> 93
<211> 32
<212> PRT
<213>Artificial sequence
<220>
<223>Artificial sequence
<400> 93
Asn Phe Leu Ala Gly Ser Gln Asp Asn Val Ile Ser Gln Ile Pro Ser
1 5 10 15
Gln Val Gln Glu Leu Ala Phe Pro Gly Ser Ala Gln Ala Val Glu Lys
20 25 30
<210> 94
<211> 10
<212> PRT
<213>Manually
<220>
<223>The feature peptides of Gly m 5
<400> 94
Glu Ser Tyr Phe Val Asp Ala Gln Pro Lys
1 5 10
<210> 95
<211> 495
<212> PRT
<213>Manually
<220>
<223> Gly m 6 G1 Ping CAA26723.1 495aa
<400> 95
Met Ala Lys Leu Val Phe Ser Leu Cys Phe Leu Leu Phe Ser Gly Cys
1 5 10 15
Cys Phe Ala Phe Ser Ser Arg Glu Gln Pro Gln Gln Asn Glu Cys Gln
20 25 30
Ile Gln Lys Leu Asn Ala Leu Lys Pro Gly Asn Arg Ile Glu Ser Glu
35 40 45
Gly Gly Leu Ile Glu Thr Trp Asn Pro Asn Asn Lys Pro Phe Gln Cys
50 55 60
Ala Gly Val Ala Leu Ser Arg Cys Thr Leu Asn Arg Asn Ala Leu Arg
65 70 75 80
Arg Pro Ser Tyr Thr Asn Gly Pro Gln Glu Ile Tyr Ile Gln Gln Gly
85 90 95
Lys Gly Ile Phe Gly Met Ile Tyr Pro Gly Cys Ser Ser Thr Phe Glu
100 105 110
Glu Pro Gln Gln Pro Gln Gln Arg Gly Gln Ser Ser Arg Pro Gln Asp
115 120 125
Arg His Gln Lys Ile Tyr Asn Ser Arg Glu Gly Asp Leu Ile Ala Val
130 135 140
Pro Thr Gly Val Ala Trp Trp Met Tyr Asn Asn Glu Asp Thr Pro Val
145 150 155 160
Val Ala Val Ser Ile Ile Asp Thr Asn Ser Leu Glu Asn Gln Leu Asp
165 170 175
Gln Met Pro Arg Arg Phe Tyr Leu Ala Gly Asn Gln Glu Gln Glu Phe
180 185 190
Leu Lys Tyr Gln Gln Glu Gln Gly Gly His Gln Ser Gln Lys Gly Lys
195 200 205
His Gln Gln Glu Glu Glu Asn Glu Gly Gly Ser Ile Leu Ser Gly Phe
210 215 220
Thr Leu Glu Phe Leu Glu His Ala Phe Ser Val Asp Lys Gln Ile Ala
225 230 235 240
Lys Asn Leu Gln Gly Glu Asn Glu Gly Glu Asp Lys Gly Ala Ile Val
245 250 255
Thr Val Lys Gly Gly Leu Ser Val Ile Lys Pro Pro Thr Asp Glu Gln
260 265 270
Gln Gln Arg Pro Gln Glu Glu Glu Glu Glu Glu Glu Asp Glu Lys Pro
275 280 285
Gln Cys Lys Gly Lys Asp Lys His Cys Gln Arg Pro Arg Gly Ser Gln
290 295 300
Ser Lys Ser Arg Arg Asn Gly Ile Asp Glu Thr Ile Cys Thr Met Arg
305 310 315 320
Leu Arg His Asn Ile Gly Gln Thr Ser Ser Pro Asp Ile Tyr Asn Pro
325 330 335
Gln Ala Gly Ser Val Thr Thr Ala Thr Ser Leu Asp Phe Pro Ala Leu
340 345 350
Ser Trp Leu Arg Leu Ser Ala Gly Phe Gly Ser Leu Arg Lys Asn Ala
355 360 365
Met Phe Val Pro His Tyr Asn Leu Asn Ala Asn Ser Ile Ile Tyr Ala
370 375 380
Leu Asn Gly Arg Ala Leu Ile Gln Val Val Asn Cys Asn Gly Glu Arg
385 390 395 400
Val Phe Asp Gly Glu Leu Gln Glu Gly Arg Val Leu Ile Val Pro Gln
405 410 415
Asn Phe Val Val Ala Ala Arg Ser Gln Ser Asp Asn Phe Glu Tyr Val
420 425 430
Ser Phe Lys Thr Asn Asp Thr Pro Met Ile Gly Thr Leu Ala Gly Ala
435 440 445
Asn Ser Leu Leu Asn Ala Leu Pro Glu Glu Val Ile Gln His Thr Phe
450 455 460
Asn Leu Lys Ser Gln Gln Ala Arg Gln Ile Lys Asn Asn Asn Pro Phe
465 470 475 480
Lys Phe Leu Val Pro Pro Gln Glu Ser Gln Lys Arg Ala Val Ala
485 490 495
<210> 96
<211> 20
<212> PRT
<213>Manually
<220>
<223>The G1 feature peptides of Gly m 6
<400> 96
Leu Val Phe Ser Leu Cys Phe Leu Leu Phe Ser Gly Cys Cys Phe Ala
1 5 10 15
Phe Ser Ser Arg
20
<210> 97
<211> 12
<212> PRT
<213>Manually
<220>
<223>The G1 feature peptides of Gly m 6
<400> 97
Glu Gln Pro Gln Gln Asn Glu Cys Gln Ile Gln Lys
1 5 10
<210> 98
<211> 17
<212> PRT
<213>Manually
<220>
<223>The G1 feature peptides of Gly m 6
<400> 98
Arg Pro Ser Tyr Thr Asn Gly Pro Gln Glu Ile Tyr Ile Gln Gln Gly
1 5 10 15
Lys
<210> 99
<211> 29
<212> PRT
<213>Manually
<220>
<223>The G1 feature peptides of Gly m 6
<400> 99
His Gln Gln Glu Glu Glu Asn Glu Gly Gly Ser Ile Leu Ser Gly Phe
1 5 10 15
Thr Leu Glu Phe Leu Glu His Ala Phe Ser Val Asp Lys
20 25
<210> 100
<211> 6
<212> PRT
<213>Manually
<220>
<223>The G1 feature peptides of Gly m 6
<400> 100
His Cys Gln Arg Pro Arg
1 5
<210> 101
<211> 34
<212> PRT
<213>Manually
<220>
<223>The G1 feature peptides of Gly m 6
<400> 101
His Asn Ile Gly Gln Thr Ser Ser Pro Asp Ile Tyr Asn Pro Gln Ala
1 5 10 15
Gly Ser Val Thr Thr Ala Thr Ser Leu Asp Phe Pro Ala Leu Ser Trp
20 25 30
Leu Arg
<210> 102
<211> 12
<212> PRT
<213>Manually
<220>
<223>The G1 feature peptides of Gly m 6
<400> 102
Ala Leu Ile Gln Val Val Asn Cys Asn Gly Glu Arg
1 5 10
<210> 103
<211> 10
<212> PRT
<213>Manually
<220>
<223>The G1 feature peptides of Gly m 6
<400> 103
Val Phe Asp Gly Glu Leu Gln Glu Gly Arg
1 5 10
<210> 104
<211> 32
<212> PRT
<213>Manually
<220>
<223>The G1 feature peptides of Gly m 6
<400> 104
Thr Asn Asp Thr Pro Met Ile Gly Thr Leu Ala Gly Ala Asn Ser Leu
1 5 10 15
Leu Asn Ala Leu Pro Glu Glu Val Ile Gln His Thr Phe Asn Leu Lys
20 25 30
<210> 105
<211> 6
<212> PRT
<213>Manually
<220>
<223>The G1 feature peptides of Gly m 6
<400> 105
Asn Asn Asn Pro Phe Lys
1 5
<210> 106
<211> 10
<212> PRT
<213>Manually
<220>
<223>The G1 feature peptides of Gly m 6
<400> 106
Phe Leu Val Pro Pro Gln Glu Ser Gln Lys
1 5 10
<210> 107
<211> 485
<212> PRT
<213>Manually
<220>
<223> Gly m 6 G2 Ping CAA26575.1 485aa
<400> 107
Met Ala Lys Leu Val Leu Ser Leu Cys Phe Leu Leu Phe Ser Gly Cys
1 5 10 15
Phe Ala Leu Arg Glu Gln Ala Gln Gln Asn Glu Cys Gln Ile Gln Lys
20 25 30
Leu Asn Ala Leu Lys Pro Gly Asn Arg Ile Glu Ser Glu Gly Gly Phe
35 40 45
Ile Glu Thr Trp Asn Pro Asn Asn Lys Pro Phe Gln Cys Ala Gly Val
50 55 60
Ala Leu Ser Arg Cys Thr Leu Asn Arg Asn Ala Leu Arg Arg Pro Ser
65 70 75 80
Tyr Thr Asn Gly Pro Gln Glu Ile Tyr Ile Gln Gln Gly Asn Gly Ile
85 90 95
Phe Gly Met Ile Phe Pro Gly Cys Pro Ser Thr Tyr Gln Glu Pro Gln
100 105 110
Glu Ser Gln Gln Arg Gly Arg Ser Gln Arg Pro Gln Asp Arg His Gln
115 120 125
Lys Val His Arg Phe Arg Glu Gly Asp Leu Ile Ala Val Pro Thr Gly
130 135 140
Val Ala Trp Trp Met Tyr Asn Asn Glu Asp Thr Pro Val Val Ala Val
145 150 155 160
Ser Ile Ile Asp Thr Asn Ser Leu Glu Asn Gln Leu Asp Gln Met Pro
165 170 175
Arg Arg Phe Tyr Leu Ala Gly Asn Gln Glu Gln Glu Phe Leu Lys Tyr
180 185 190
Gln Gln Gln Gln Gln Gly Gly Ser Gln Ser Gln Lys Gly Lys Gln Gln
195 200 205
Glu Glu Glu Asn Glu Gly Ser Asn Ile Leu Ser Gly Phe Ala Pro Glu
210 215 220
Phe Leu Lys Glu Ala Phe Gly Val Asn Met Gln Ile Val Arg Asn Leu
225 230 235 240
Gln Gly Glu Asn Glu Glu Glu Asp Ser Gly Ala Ile Val Thr Val Lys
245 250 255
Gly Gly Leu Arg Val Thr Ala Pro Ala Met Arg Lys Pro Gln Gln Glu
260 265 270
Glu Asp Asp Asp Asp Glu Glu Glu Gln Pro Gln Cys Val Glu Thr Asp
275 280 285
Lys Gly Cys Gln Arg Gln Ser Lys Arg Ser Arg Asn Gly Ile Asp Glu
290 295 300
Thr Ile Cys Thr Met Arg Leu Arg Gln Asn Ile Gly Gln Asn Ser Ser
305 310 315 320
Pro Asp Ile Tyr Asn Pro Gln Ala Gly Ser Ile Thr Thr Ala Thr Ser
325 330 335
Leu Asp Phe Pro Ala Leu Trp Leu Leu Lys Leu Ser Ala Gln Tyr Gly
340 345 350
Ser Leu Arg Lys Asn Ala Met Phe Val Pro His Tyr Thr Leu Asn Ala
355 360 365
Asn Ser Ile Ile Tyr Ala Leu Asn Gly Arg Ala Leu Val Gln Val Val
370 375 380
Asn Cys Asn Gly Glu Arg Val Phe Asp Gly Glu Leu Gln Glu Gly Gly
385 390 395 400
Val Leu Ile Val Pro Gln Asn Phe Ala Val Ala Ala Lys Ser Gln Ser
405 410 415
Asp Asn Phe Glu Tyr Val Ser Phe Lys Thr Asn Asp Arg Pro Ser Ile
420 425 430
Gly Asn Leu Ala Gly Ala Asn Ser Leu Leu Asn Ala Leu Pro Glu Glu
435 440 445
Val Ile Gln His Thr Phe Asn Leu Lys Ser Gln Gln Ala Arg Gln Val
450 455 460
Lys Asn Asn Asn Pro Phe Ser Phe Leu Val Pro Pro Gln Glu Ser Gln
465 470 475 480
Arg Arg Ala Val Ala
485
<210> 108
<211> 17
<212> PRT
<213>Manually
<220>
<223>The G2 feature peptides of Gly m 6
<400> 108
Leu Val Leu Ser Leu Cys Phe Leu Leu Phe Ser Gly Cys Phe Ala Leu
1 5 10 15
Arg
<210> 109
<211> 12
<212> PRT
<213>Manually
<220>
<223>The G2 feature peptides of Gly m 6
<400> 109
Glu Gln Ala Gln Gln Asn Glu Cys Gln Ile Gln Lys
1 5 10
<210> 110
<211> 40
<212> PRT
<213>Manually
<220>
<223>The G2 feature peptides of Gly m 6
<400> 110
Arg Pro Ser Tyr Thr Asn Gly Pro Gln Glu Ile Tyr Ile Gln Gln Gly
1 5 10 15
Asn Gly Ile Phe Gly Met Ile Phe Pro Gly Cys Pro Ser Thr Tyr Gln
20 25 30
Glu Pro Gln Glu Ser Gln Gln Arg
35 40
<210> 111
<211> 7
<212> PRT
<213>Manually
<220>
<223>The G2 feature peptides of Gly m 6
<400> 111
Ser Gln Arg Pro Gln Asp Arg
1 5
<210> 112
<211> 21
<212> PRT
<213>Manually
<220>
<223>The G2 feature peptides of Gly m 6
<400> 112
Gln Gln Glu Glu Glu Asn Glu Gly Ser Asn Ile Leu Ser Gly Phe Ala
1 5 10 15
Pro Glu Phe Leu Lys
20
<210> 113
<211> 11
<212> PRT
<213>Manually
<220>
<223>The G2 feature peptides of Gly m 6
<400> 113
Glu Ala Phe Gly Val Asn Met Gln Ile Val Arg
1 5 10
<210> 114
<211> 22
<212> PRT
<213>Manually
<220>
<223>The G2 feature peptides of Gly m 6
<400> 114
Lys Pro Gln Gln Glu Glu Asp Asp Asp Asp Glu Glu Glu Gln Pro Gln
1 5 10 15
Cys Val Glu Thr Asp Lys
20
<210> 115
<211> 9
<212> PRT
<213>Manually
<220>
<223>The G2 feature peptides of Gly m 6
<400> 115
Leu Ser Ala Gln Tyr Gly Ser Leu Arg
1 5
<210> 116
<211> 22
<212> PRT
<213>Manually
<220>
<223>The G2 feature peptides of Gly m 6
<400> 116
Asn Ala Met Phe Val Pro His Tyr Thr Leu Asn Ala Asn Ser Ile Ile
1 5 10 15
Tyr Ala Leu Asn Gly Arg
20
<210> 117
<211> 12
<212> PRT
<213>Manually
<220>
<223>The G2 feature peptides of Gly m 6
<400> 117
Ala Leu Val Gln Val Val Asn Cys Asn Gly Glu Arg
1 5 10
<210> 118
<211> 23
<212> PRT
<213>Manually
<220>
<223>The G2 feature peptides of Gly m 6
<400> 118
Val Phe Asp Gly Glu Leu Gln Glu Gly Gly Val Leu Ile Val Pro Gln
1 5 10 15
Asn Phe Ala Val Ala Ala Lys
20
<210> 119
<211> 32
<212> PRT
<213>Manually
<220>
<223>The G2 feature peptides of Gly m 6
<400> 119
Thr Asn Asp Arg Pro Ser Ile Gly Asn Leu Ala Gly Ala Asn Ser Leu
1 5 10 15
Leu Asn Ala Leu Pro Glu Glu Val Ile Gln His Thr Phe Asn Leu Lys
20 25 30
<210> 120
<211> 16
<212> PRT
<213>Manually
<220>
<223>The G2 feature peptides of Gly m 6
<400> 120
Asn Asn Asn Pro Phe Ser Phe Leu Val Pro Pro Gln Glu Ser Gln Arg
1 5 10 15
<210> 121
<211> 20
<212> PRT
<213>Manually
<220>
<223>The G3 feature peptides of Gly m 6
<400> 121
Leu Val Leu Ser Leu Cys Phe Leu Leu Phe Ser Gly Cys Cys Phe Ala
1 5 10 15
Phe Ser Phe Arg
20
<210> 122
<211> 12
<212> PRT
<213>Manually
<220>
<223>The G3 feature peptides of Gly m 6
<400> 122
Glu Gln Pro Gln Gln Asn Glu Cys Gln Ile Gln Arg
1 5 10
<210> 123
<211> 28
<212> PRT
<213>Manually
<220>
<223>The G3 feature peptides of Gly m 6
<400> 123
Gln Gln Glu Glu Glu Asn Glu Gly Gly Ser Ile Leu Ser Gly Phe Ala
1 5 10 15
Pro Glu Phe Leu Glu His Ala Phe Val Val Asp Arg
20 25
<210> 124
<211> 10
<212> PRT
<213>Manually
<220>
<223>The G3 feature peptides of Gly m 6
<400> 124
Leu Gln Gly Glu Asn Glu Glu Glu Glu Lys
1 5 10
<210> 125
<211> 28
<212> PRT
<213>Manually
<220>
<223>The G3 feature peptides of Gly m 6
<400> 125
Gly Gly Leu Ser Val Ile Ser Pro Pro Thr Glu Glu Gln Gln Gln Arg
1 5 10 15
Pro Glu Glu Glu Glu Lys Pro Asp Cys Asp Glu Lys
20 25
<210> 126
<211> 7
<212> PRT
<213>Manually
<220>
<223>The G3 feature peptides of Gly m 6
<400> 126
His Cys Gln Ser Gln Ser Arg
1 5
<210> 127
<211> 9
<212> PRT
<213>Manually
<220>
<223>The G3 feature peptides of Gly m 6
<400> 127
Leu Ser Ala Gln Phe Gly Ser Leu Arg
1 5
<210> 128
<211> 23
<212> PRT
<213>Manually
<220>
<223>The G3 feature peptides of Gly m 6
<400> 128
Val Phe Asp Gly Glu Leu Gln Glu Gly Gln Val Leu Ile Val Pro Gln
1 5 10 15
Asn Phe Ala Val Ala Ala Arg
20
<210> 129
<211> 32
<212> PRT
<213>Manually
<220>
<223>The G3 feature peptides of Gly m 6
<400> 129
Thr Asn Asp Arg Pro Ser Ile Gly Asn Leu Ala Gly Ala Asn Ser Leu
1 5 10 15
Leu Asn Ala Leu Pro Glu Glu Val Ile Gln Gln Thr Phe Asn Leu Arg
20 25 30
<210> 130
<211> 299
<212> PRT
<213>Manually
<220>
<223>The G4 consensus sequences of Gly m 6
<400> 130
Met Gly Lys Pro Phe Thr Leu Ser Leu Ser Ser Leu Cys Leu Leu Leu
1 5 10 15
Leu Ser Ser Ala Cys Phe Ala Ile Ser Ser Ser Lys Leu Asn Glu Cys
20 25 30
Gln Leu Asn Asn Leu Asn Ala Leu Glu Pro Asp His Arg Val Glu Ser
35 40 45
Glu Gly Gly Leu Ile Gln Thr Trp Asn Ser Gln His Pro Glu Leu Lys
50 55 60
Cys Ala Gly Val Thr Val Ser Lys Leu Thr Leu Asn Arg Asn Gly Leu
65 70 75 80
His Leu Pro Ser Tyr Ser Pro Tyr Pro Arg Met Ile Ile Ile Ala Gln
85 90 95
Gly Lys Gly Ala Leu Gly Val Ala Ile Pro Gly Cys Pro Glu Thr Phe
100 105 110
Glu Glu Pro Gln Glu Gln Ser Asn Arg Arg Gly Ser Arg Ser Gln Lys
115 120 125
Gln Gln Leu Gln Asp Ser His Gln Lys Ile Arg His Phe Asn Glu Gly
130 135 140
Asp Val Leu Val Ile Pro Pro Gly Val Pro Tyr Trp Thr Tyr Asn Thr
145 150 155 160
Gly Asp Glu Pro Val Val Ala Ile Ser Leu Leu Asp Thr Ser Asn Phe
165 170 175
Asn Asn Gln Leu Asp Gln Thr Pro Arg Val Phe Tyr Leu Ala Gly Asn
180 185 190
Pro Asp Ile Glu Tyr Pro Glu Thr Met Gln Gln Gln Gln Gln Gln Lys
195 200 205
Ser His Gly Gly Arg Lys Gln Gly Gln His Gln Gln Glu Glu Glu Glu
210 215 220
Glu Gly Gly Ser Val Leu Ser Gly Phe Ser Lys His Phe Leu Ala Gln
225 230 235 240
Ser Phe Asn Thr Asn Glu Asp Ile Ala Glu Lys Leu Gln Ser Pro Asp
245 250 255
Asp Glu Arg Lys Gln Ile Val Thr Val Glu Gly Gly Leu Ser Val Ile
260 265 270
Ser Pro Lys Trp Gln Glu Gln Gln Asp Glu Asp Glu Asp Glu Asp Glu
275 280 285
Asp Asp Glu Asp Glu Gln Ile Pro Ser His Pro
290 295
<210> 131
<211> 563
<212> PRT
<213>Manually
<220>
<223> Gly m 6 G4 Ping CAA60533.1 563aa
<400> 131
Met Gly Lys Pro Phe Thr Leu Ser Leu Ser Ser Leu Cys Leu Leu Leu
1 5 10 15
Leu Ser Ser Ala Cys Phe Ala Ile Ser Ser Ser Lys Leu Asn Glu Cys
20 25 30
Gln Leu Asn Asn Leu Asn Ala Leu Glu Pro Asp His Arg Val Glu Ser
35 40 45
Glu Gly Gly Leu Ile Gln Thr Trp Asn Ser Gln His Pro Glu Leu Lys
50 55 60
Cys Ala Gly Val Thr Val Ser Lys Leu Thr Leu Asn Arg Asn Gly Leu
65 70 75 80
His Leu Pro Ser Tyr Ser Pro Tyr Pro Arg Met Ile Ile Ile Ala Gln
85 90 95
Gly Lys Gly Ala Leu Gly Val Ala Ile Pro Gly Cys Pro Glu Thr Phe
100 105 110
Glu Glu Pro Gln Glu Gln Ser Asn Arg Arg Gly Ser Arg Ser Gln Lys
115 120 125
Gln Gln Leu Gln Asp Ser His Gln Lys Ile Arg His Phe Asn Glu Gly
130 135 140
Asp Val Leu Val Ile Pro Pro Gly Val Pro Tyr Trp Thr Tyr Asn Thr
145 150 155 160
Gly Asp Glu Pro Val Val Ala Ile Ser Leu Leu Asp Thr Ser Asn Phe
165 170 175
Asn Asn Gln Leu Asp Gln Thr Pro Arg Val Phe Tyr Leu Ala Gly Asn
180 185 190
Pro Asp Ile Glu Tyr Pro Glu Thr Met Gln Gln Gln Gln Gln Gln Lys
195 200 205
Ser His Gly Gly Arg Lys Gln Gly Gln His Gln Gln Glu Glu Glu Glu
210 215 220
Glu Gly Gly Ser Val Leu Ser Gly Phe Ser Lys His Phe Leu Ala Gln
225 230 235 240
Ser Phe Asn Thr Asn Glu Asp Ile Ala Glu Lys Leu Gln Ser Pro Asp
245 250 255
Asp Glu Arg Lys Gln Ile Val Thr Val Glu Gly Gly Leu Ser Val Ile
260 265 270
Ser Pro Lys Trp Gln Glu Gln Gln Asp Glu Asp Glu Asp Glu Asp Glu
275 280 285
Asp Asp Glu Asp Glu Gln Ile Pro Ser His Pro Pro Arg Arg Pro Ser
290 295 300
His Gly Lys Arg Glu Gln Asp Glu Asp Glu Asp Glu Asp Glu Asp Lys
305 310 315 320
Pro Arg Pro Ser Arg Pro Ser His Gly Lys Arg Glu Gln Asp Gln Asp
325 330 335
Gln Asp Glu Asp Glu Asp Glu Asp Glu Asp Gln Pro Arg Lys Ser Arg
340 345 350
Glu Trp Arg Ser Lys Lys Thr Gln Pro Arg Arg Pro Arg Gln Glu Glu
355 360 365
Pro Arg Glu Arg Gly Cys Glu Thr Arg Asn Gly Val Glu Glu Asn Ile
370 375 380
Cys Thr Leu Lys Leu His Glu Asn Ile Ala Arg Pro Ser Arg Ala Asp
385 390 395 400
Phe Tyr Asn Pro Lys Ala Gly Arg Ile Ser Thr Leu Asn Ser Leu Thr
405 410 415
Leu Pro Ala Leu Arg Gln Phe Gln Leu Ser Ala Gln Tyr Val Val Leu
420 425 430
Tyr Lys Asn Gly Ile Tyr Ser Pro His Trp Asn Leu Asn Ala Asn Ser
435 440 445
Val Ile Tyr Val Thr Arg Gly Gln Gly Lys Val Arg Val Val Asn Cys
450 455 460
Gln Gly Asn Ala Val Phe Asp Gly Glu Leu Arg Arg Gly Gln Leu Leu
465 470 475 480
Val Val Pro Gln Asn Phe Val Val Ala Glu Gln Ala Gly Glu Gln Gly
485 490 495
Phe Glu Tyr Ile Val Phe Lys Thr His His Asn Ala Val Thr Ser Tyr
500 505 510
Leu Lys Asp Val Phe Arg Ala Ile Pro Ser Glu Val Leu Ala His Ser
515 520 525
Tyr Asn Leu Arg Gln Ser Gln Val Ser Glu Leu Lys Tyr Glu Gly Asn
530 535 540
Trp Gly Pro Leu Val Asn Pro Glu Ser Gln Gln Gly Ser Pro Arg Val
545 550 555 560
Lys Val Ala
<210> 132
<211> 563
<212> PRT
<213>Manually
<220>
<223> Gly m 6 G4 UniProt Q9SB11 G4 563aa
<400> 132
Met Gly Lys Pro Phe Thr Leu Ser Leu Ser Ser Leu Cys Leu Leu Leu
1 5 10 15
Leu Ser Ser Ala Cys Phe Ala Ile Ser Ser Ser Lys Leu Asn Glu Cys
20 25 30
Gln Leu Asn Asn Leu Asn Ala Leu Glu Pro Asp His Arg Val Glu Ser
35 40 45
Glu Gly Gly Leu Ile Gln Thr Trp Asn Ser Gln His Pro Glu Leu Lys
50 55 60
Cys Ala Gly Val Thr Val Ser Lys Leu Thr Leu Asn Arg Asn Gly Leu
65 70 75 80
His Leu Pro Ser Tyr Ser Pro Tyr Pro Arg Met Ile Ile Ile Ala Gln
85 90 95
Gly Lys Gly Ala Leu Gly Val Ala Ile Pro Gly Cys Pro Glu Thr Phe
100 105 110
Glu Glu Pro Gln Glu Gln Ser Asn Arg Arg Gly Ser Arg Ser Gln Lys
115 120 125
Gln Gln Leu Gln Asp Ser His Gln Lys Ile Arg His Phe Asn Glu Gly
130 135 140
Asp Val Leu Val Ile Pro Pro Gly Val Pro Tyr Trp Thr Tyr Asn Thr
145 150 155 160
Gly Asp Glu Pro Val Val Ala Ile Ser Leu Leu Asp Thr Ser Asn Phe
165 170 175
Asn Asn Gln Leu Asp Gln Thr Pro Arg Val Phe Tyr Leu Ala Gly Asn
180 185 190
Pro Asp Ile Glu Tyr Pro Glu Thr Met Gln Gln Gln Gln Gln Gln Lys
195 200 205
Ser His Gly Gly Arg Lys Gln Gly Gln His Gln Gln Glu Glu Glu Glu
210 215 220
Glu Gly Gly Ser Val Leu Ser Gly Phe Ser Lys His Phe Leu Ala Gln
225 230 235 240
Ser Phe Asn Thr Asn Glu Asp Ile Ala Glu Lys Leu Gln Ser Pro Asp
245 250 255
Asp Glu Arg Lys Gln Ile Val Thr Val Glu Gly Gly Leu Ser Val Ile
260 265 270
Ser Pro Lys Trp Gln Glu Gln Gln Asp Glu Asp Glu Asp Glu Asp Glu
275 280 285
Asp Asp Glu Asp Glu Gln Ile Pro Ser His Pro Pro Arg Arg Pro Ser
290 295 300
His Gly Lys Arg Glu Gln Asp Glu Asp Glu Asp Glu Asp Glu Asp Lys
305 310 315 320
Pro Arg Pro Ser Arg Pro Ser Gln Gly Lys Arg Glu Gln Asp Gln Asp
325 330 335
Gln Asp Glu Asp Glu Asp Glu Asp Glu Asp Gln Pro Arg Lys Ser Arg
340 345 350
Glu Trp Arg Ser Lys Lys Thr Gln Pro Arg Arg Pro Arg Gln Glu Glu
355 360 365
Pro Arg Glu Arg Gly Cys Glu Thr Arg Asn Gly Val Glu Glu Asn Ile
370 375 380
Cys Thr Leu Lys Leu His Glu Asn Ile Ala Arg Pro Ser Arg Ala Asp
385 390 395 400
Phe Tyr Asn Pro Lys Ala Gly Arg Ile Ser Thr Leu Asn Ser Leu Thr
405 410 415
Leu Pro Ala Leu Arg Gln Phe Gln Leu Ser Ala Gln Tyr Val Val Leu
420 425 430
Tyr Lys Asn Gly Ile Tyr Ser Pro His Trp Asn Leu Asn Ala Asn Ser
435 440 445
Val Ile Tyr Val Thr Arg Gly Gln Gly Lys Val Arg Val Val Asn Cys
450 455 460
Gln Gly Asn Ala Val Phe Asp Gly Glu Leu Arg Arg Gly Gln Leu Leu
465 470 475 480
Val Val Pro Gln Asn Phe Val Val Ala Glu Gln Ala Gly Glu Gln Gly
485 490 495
Phe Glu Tyr Ile Val Phe Lys Thr His His Asn Ala Val Thr Ser Tyr
500 505 510
Leu Lys Asp Val Phe Arg Ala Ile Pro Ser Glu Val Leu Ala His Ser
515 520 525
Tyr Asn Leu Arg Gln Ser Gln Val Ser Glu Leu Lys Tyr Glu Gly Asn
530 535 540
Trp Gly Pro Leu Val Asn Pro Glu Ser Gln Gln Gly Ser Pro Arg Val
545 550 555 560
Lys Val Ala
<210> 133
<211> 517
<212> PRT
<213>Manually
<220>
<223> Gly m 6 G4 Ping CAA55977.1 517aa
<400> 133
Met Gly Lys Pro Phe Phe Thr Leu Ser Leu Ser Ser Leu Cys Leu Leu
1 5 10 15
Leu Leu Ser Ser Ala Cys Phe Ala Ile Thr Ser Ser Lys Phe Asn Glu
20 25 30
Cys Gln Leu Asn Asn Leu Asn Ala Leu Glu Pro Asp His Arg Val Glu
35 40 45
Ser Glu Gly Gly Leu Ile Glu Thr Trp Asn Ser Gln His Pro Glu Leu
50 55 60
Gln Cys Ala Gly Val Thr Val Ser Lys Arg Thr Leu Asn Arg Asn Gly
65 70 75 80
Leu His Leu Pro Ser Tyr Ser Pro Tyr Pro Gln Met Ile Ile Val Val
85 90 95
Gln Gly Lys Gly Ala Ile Gly Phe Ala Phe Pro Gly Cys Pro Glu Thr
100 105 110
Phe Glu Lys Pro Gln Gln Gln Ser Ser Arg Arg Gly Ser Arg Ser Gln
115 120 125
Gln Gln Leu Gln Asp Ser His Gln Lys Ile Arg His Phe Asn Glu Gly
130 135 140
Asp Val Leu Val Ile Pro Pro Gly Val Pro Tyr Trp Thr Tyr Asn Thr
145 150 155 160
Gly Asp Glu Pro Val Val Ala Ile Ser Leu Leu Asp Thr Ser Asn Phe
165 170 175
Asn Asn Gln Leu Asp Gln Asn Pro Arg Val Phe Tyr Leu Ala Gly Asn
180 185 190
Pro Asp Ile Glu His Pro Glu Thr Met Gln Gln Gln Gln Gln Gln Lys
195 200 205
Ser His Gly Gly Arg Lys Gln Gly Gln His Gln Gln Gln Glu Glu Glu
210 215 220
Gly Gly Ser Val Leu Ser Gly Phe Ser Lys His Phe Leu Ala Gln Ser
225 230 235 240
Phe Asn Thr Asn Glu Asp Thr Ala Glu Lys Leu Arg Ser Pro Asp Asp
245 250 255
Glu Arg Lys Gln Ile Val Thr Val Glu Gly Gly Leu Ser Val Ile Ser
260 265 270
Pro Lys Trp Gln Glu Gln Glu Asp Glu Asp Glu Asp Glu Asp Glu Glu
275 280 285
Tyr Glu Gln Thr Pro Ser Tyr Pro Pro Arg Arg Pro Ser His Gly Lys
290 295 300
His Glu Asp Asp Glu Asp Glu Asp Glu Glu Glu Asp Gln Pro Arg Pro
305 310 315 320
Asp His Pro Pro Gln Arg Pro Ser Arg Pro Glu Gln Gln Glu Pro Arg
325 330 335
Gly Arg Gly Cys Gln Thr Arg Asn Gly Val Glu Glu Asn Ile Cys Thr
340 345 350
Met Lys Leu His Glu Asn Ile Ala Arg Pro Ser Arg Ala Asp Phe Tyr
355 360 365
Asn Pro Lys Ala Gly Arg Ile Ser Thr Leu Asn Ser Leu Thr Leu Pro
370 375 380
Ala Leu Arg Gln Phe Gly Leu Ser Ala Gln Tyr Val Val Leu Tyr Arg
385 390 395 400
Asn Gly Ile Tyr Ser Pro His Trp Asn Leu Asn Ala Asn Ser Val Ile
405 410 415
Tyr Val Thr Arg Gly Lys Gly Arg Val Arg Val Val Asn Cys Gln Gly
420 425 430
Asn Ala Val Phe Asp Gly Glu Leu Arg Arg Gly Gln Leu Leu Val Val
435 440 445
Pro Gln Asn Phe Val Val Ala Glu Gln Gly Gly Glu Gln Gly Leu Glu
450 455 460
Tyr Val Val Phe Lys Thr His His Asn Ala Val Ser Ser Tyr Ile Lys
465 470 475 480
Asp Val Phe Arg Ala Ile Pro Ser Glu Val Leu Ser Asn Ser Tyr Asn
485 490 495
Leu Gly Gln Ser Gln Val Arg Gln Leu Lys Tyr Gln Gly Asn Ser Gly
500 505 510
Pro Leu Val Asn Pro
515
<210> 134
<211> 516
<212> PRT
<213>Manually
<220>
<223> Gly m 6 G4 Ping AAA33964.1 516aa
<400> 134
Met Gly Lys Pro Phe Phe Thr Leu Ser Leu Ser Ser Leu Cys Leu Leu
1 5 10 15
Leu Leu Ser Ser Ala Cys Phe Ala Ile Thr Ser Ser Lys Phe Asn Glu
20 25 30
Cys Gln Leu Asn Asn Leu Asn Ala Leu Glu Pro Asp His Arg Val Glu
35 40 45
Ser Glu Gly Gly Leu Ile Glu Thr Trp Asn Ser Gln His Pro Glu Leu
50 55 60
Gln Cys Ala Gly Val Thr Val Ser Lys Arg Thr Leu Asn Arg Asn Gly
65 70 75 80
Ser His Leu Pro Ser Tyr Leu Pro Tyr Pro Gln Met Ile Ile Val Val
85 90 95
Gln Gly Lys Gly Ala Ile Gly Phe Ala Phe Pro Gly Cys Pro Glu Thr
100 105 110
Phe Glu Lys Pro Gln Gln Gln Ser Ser Arg Arg Gly Ser Arg Ser Gln
115 120 125
Gln Gln Leu Gln Asp Ser His Gln Lys Ile Arg His Phe Asn Glu Gly
130 135 140
Asp Val Leu Val Ile Pro Leu Gly Val Pro Tyr Trp Thr Tyr Asn Thr
145 150 155 160
Gly Asp Glu Pro Val Val Ala Ile Ser Pro Leu Asp Thr Ser Asn Phe
165 170 175
Asn Asn Gln Leu Asp Gln Asn Pro Arg Val Phe Tyr Leu Ala Gly Asn
180 185 190
Pro Asp Ile Glu His Pro Glu Thr Met Gln Gln Gln Gln Gln Gln Lys
195 200 205
Ser His Gly Gly Arg Lys Gln Gly Gln His Arg Gln Gln Glu Glu Glu
210 215 220
Gly Gly Ser Val Leu Ser Gly Phe Ser Lys His Phe Leu Ala Gln Ser
225 230 235 240
Phe Asn Thr Asn Glu Asp Thr Ala Glu Lys Leu Arg Ser Pro Asp Asp
245 250 255
Glu Arg Lys Gln Ile Val Thr Val Glu Gly Gly Leu Ser Val Ile Ser
260 265 270
Pro Lys Trp Gln Glu Gln Glu Asp Glu Asp Glu Asp Glu Asp Glu Glu
275 280 285
Tyr Gly Arg Thr Pro Ser Tyr Pro Pro Arg Arg Pro Ser His Gly Lys
290 295 300
His Glu Asp Asp Glu Asp Glu Asp Glu Glu Glu Asp Gln Pro Arg Pro
305 310 315 320
Asp His Pro Pro Gln Arg Pro Ser Arg Pro Glu Gln Gln Glu Pro Arg
325 330 335
Gly Arg Gly Cys Gln Thr Arg Asn Gly Val Glu Glu Asn Ile Cys Thr
340 345 350
Met Lys Leu His Glu Asn Ile Ala Arg Pro Ser Arg Ala Asp Phe Tyr
355 360 365
Asn Pro Lys Ala Gly Arg Ile Ser Thr Leu Asn Ser Leu Thr Leu Pro
370 375 380
Ala Leu Arg Gln Phe Gly Leu Ser Ala Gln Tyr Val Val Leu Tyr Arg
385 390 395 400
Asn Gly Ile Tyr Ser Pro Asp Trp Asn Leu Asn Ala Asn Ser Val Thr
405 410 415
Met Thr Arg Gly Lys Gly Arg Val Arg Val Val Asn Cys Gln Gly Asn
420 425 430
Ala Val Phe Asp Gly Glu Leu Arg Arg Gly Gln Leu Leu Val Val Pro
435 440 445
Gln Asn Pro Ala Val Ala Glu Gln Gly Gly Glu Gln Gly Leu Glu Tyr
450 455 460
Val Val Phe Lys Thr His His Asn Ala Val Ser Ser Tyr Ile Lys Asp
465 470 475 480
Val Phe Arg Val Ile Pro Ser Glu Val Leu Ser Asn Ser Tyr Asn Leu
485 490 495
Gly Gln Ser Gln Val Arg Gln Leu Lys Tyr Gln Gly Asn Ser Gly Pro
500 505 510
Leu Val Asn Pro
515
<210> 135
<211> 17
<212> PRT
<213>Manually
<220>
<223>The G4 feature peptides of Gly m 6
<400> 135
Leu Asn Glu Cys Gln Leu Asn Asn Leu Asn Ala Leu Glu Pro Asp His
1 5 10 15
Arg
<210> 136
<211> 8
<212> PRT
<213>Manually
<220>
<223>The G4 feature peptides of Gly m 6
<400> 136
Cys Ala Gly Val Thr Val Ser Lys
1 5
<210> 137
<211> 5
<212> PRT
<213>Manually
<220>
<223>The G4 feature peptides of Gly m 6
<400> 137
Leu Thr Leu Asn Arg
1 5
<210> 138
<211> 8
<212> PRT
<213>Manually
<220>
<223>The G4 feature peptides of Gly m 6
<400> 138
Met Ile Ile Ile Ala Gln Gly Lys
1 5
<210> 139
<211> 23
<212> PRT
<213>Manually
<220>
<223>The G4 feature peptides of Gly m 6
<400> 139
Gly Ala Leu Gly Val Ala Ile Pro Gly Cys Pro Glu Thr Phe Glu Glu
1 5 10 15
Pro Gln Glu Gln Ser Asn Arg
20
<210> 140
<211> 9
<212> PRT
<213>Manually
<220>
<223>The G4 feature peptides of Gly m 6
<400> 140
Gln Gln Leu Gln Asp Ser His Gln Lys
1 5
<210> 141
<211> 23
<212> PRT
<213>Manually
<220>
<223>The G4 feature peptides of Gly m 6
<400> 141
Val Phe Tyr Leu Ala Gly Asn Pro Asp Ile Glu Tyr Pro Glu Thr Met
1 5 10 15
Gln Gln Gln Gln Gln Gln Lys
20
<210> 142
<211> 21
<212> PRT
<213>Manually
<220>
<223>The G4 feature peptides of Gly m 6
<400> 142
Gln Gly Gln His Gln Gln Glu Glu Glu Glu Glu Gly Gly Ser Val Leu
1 5 10 15
Ser Gly Phe Ser Lys
20
<210> 143
<211> 16
<212> PRT
<213>Manually
<220>
<223>The G4 feature peptides of Gly m 6
<400> 143
His Phe Leu Ala Gln Ser Phe Asn Thr Asn Glu Asp Ile Ala Glu Lys
1 5 10 15
<210> 144
<211> 15
<212> PRT
<213>Manually
<220>
<223>The G4 feature peptides of Gly m 6
<400> 144
Gln Ile Val Thr Val Glu Gly Gly Leu Ser Val Ile Ser Pro Lys
1 5 10 15
<210> 145
<211> 26
<212> PRT
<213>Manually
<220>
<223>The G4 feature peptides of Gly m 6
<400> 145
Trp Gln Glu Gln Gln Asp Glu Asp Glu Asp Glu Asp Glu Asp Asp Glu
1 5 10 15
Asp Glu Gln Ile Pro Ser His Pro Pro Arg
20 25
<210> 146
<211> 6
<212> PRT
<213>Manually
<220>
<223>The G4 feature peptides of Gly m 6
<400> 146
Arg Pro Ser His Gly Lys
1 5
<210> 147
<211> 22
<212> PRT
<213>Manually
<220>
<223>The G4 feature peptides of Gly m 6
<400> 147
Glu Gln Asp Glu Asp Glu Asp Glu Asp Glu Asp Lys Pro Arg Pro Ser
1 5 10 15
Arg Pro Ser Gln Gly Lys
20
<210> 148
<211> 5
<212> PRT
<213>Manually
<220>
<223>The G4 feature peptides of Gly m 6
<400> 148
Gln Glu Glu Pro Arg
1 5
<210> 149
<211> 11
<212> PRT
<213>Manually
<220>
<223>The G4 feature peptides of Gly m 6
<400> 149
Asn Gly Val Glu Glu Asn Ile Cys Thr Leu Lys
1 5 10
<210> 150
<211> 10
<212> PRT
<213>Manually
<220>
<223>The G4 feature peptides of Gly m 6
<400> 150
Leu His Glu Asn Ile Ala Arg Pro Ser Arg
1 5 10
<210> 151
<211> 13
<212> PRT
<213>Manually
<220>
<223>The G4 feature peptides of Gly m 6
<400> 151
Ile Ser Thr Leu Asn Ser Leu Thr Leu Pro Ala Leu Arg
1 5 10
<210> 152
<211> 13
<212> PRT
<213>Manually
<220>
<223>The G4 feature peptides of Gly m 6
<400> 152
Gln Phe Gln Leu Ser Ala Gln Tyr Val Val Leu Tyr Lys
1 5 10
<210> 153
<211> 20
<212> PRT
<213>Manually
<220>
<223>The G4 feature peptides of Gly m 6
<400> 153
Asn Gly Ile Tyr Ser Pro His Trp Asn Leu Asn Ala Asn Ser Val Ile
1 5 10 15
Tyr Val Thr Arg
20
<210> 154
<211> 4
<212> PRT
<213>Manually
<220>
<223>The G4 feature peptides of Gly m 6
<400> 154
Asp Val Phe Arg
1
<210> 155
<211> 14
<212> PRT
<213>Manually
<220>
<223>The G4 feature peptides of Gly m 6
<400> 155
Ala Ile Pro Ser Glu Val Leu Ala His Ser Tyr Asn Leu Arg
1 5 10
<210> 156
<211> 8
<212> PRT
<213>Manually
<220>
<223>The G4 feature peptides of Gly m 6
<400> 156
Gln Ser Gln Val Ser Glu Leu Lys
1 5

Claims (19)

1. it is a kind of to select the candidate feature peptide to be used for quantitative known allergen and potential allergen from the sample based on plant Method, including:
A () is based on the potential allergen of homological identification with least one known allergenic proteins sequence;
B () carries out the sequence alignment of at least one known allergen and the potential allergen of identification in step (a);
C () is based on the sequence alignment and selects consensus sequence or representative series;
D () is based on from the consensus sequence of selection in step (c) or the sequence alignment of representative series and computer digestion data Conservative region or domain, it is determined that multiple candidate feature peptide;With
E () is based on the measurement of the feature peptide, the described at least one known allergen in the quantitative sample based on plant With the amount of potential allergen.
2. the method for claim 1 wherein the quantification steps use column chromatography and mass spectrum.
3. the method for claim 1 wherein the quantification steps include being surveyed using high-resolution accurate mass mass spectrum (HRAM MS) Measure the multiple candidate feature peptide.
4. include being calculated from mass spectrum the corresponding peak height of the candidate feature peptide the method for claim 1 wherein the quantification steps Degree or peak area.
5. the method for claim 1 wherein the quantification steps include will be from mass spectrographic fragmentation mode high and low fragmentation mode Data be compared.
6. the method for claim 1 wherein at least one known allergen includes Gly m 1, Gly m 3, Gly m 4, Gly m 5 (beta-conglycinin), Gly m 6 (glycinin) G1, Gly m 6) G2, (the soybean ball eggs of Gly m 6 G3 in vain), Gly m 6 (glycinin) G4 or Gly m 6 (glycinin) precursor.
7. the method for claim 1 wherein the potential allergen includes at least one sequence being selected from the group:
A () is SEQ ID NO for Gly m 1:12 and 30-35;
B () is SEQ ID NO for Gly m 3:13 and 39-40;
C () is SEQ ID NO for Gly m 4:14 and 43-51;
D () is SEQ ID NO for Gly m 5:15 and 62-74;
E () is SEQ ID NO for the G1 of Gly m 6:16 and 95;
F () is SEQ ID NO for the G2 of Gly m 6:17 and 107;
G () is SEQ ID NO for the G3 of Gly m 6:18;
H () is SEQ ID NO for the G4 of Gly m 6:19 and 131-134;With
I () is SEQ ID NO for the precursors of Gly m 6:20.
8. the method for claim 1 wherein the candidate feature peptide includes at least one sequence being selected from the group:
A () is SEQ ID NO for Gly m 1:1,36 and 37;
B () is SEQ ID NO for Gly m 3:2 and 41;
C () is SEQ ID NO for Gly m 4:52-57;
D () is SEQ ID NO for Gly m 5:3 and 75-94;
E () is SEQ ID NO for the G1 of Gly m 6:96-106;
F () is SEQ ID NO for the G2 of Gly m 6:4 and 108-120;
G () is SEQ ID NO for the G3 of Gly m 6:5 and 121-129;
H () is SEQ ID NO for the G4 of Gly m 6:135-156 and 58;With
I () is SEQ ID NO for the precursors of Gly m 6:6,59 and 60.
9. the method for claim 1 wherein part of the sample based on plant comprising soya seeds or soya seeds.
10. a kind of for quantitative one or more target protein with known amino acid sequence in the sample based on plant System, the system includes:
A () is used to be extracted from the sample based on plant the high flux means of protein;
B () is used for the processing module of the protein extracted with least one protease digestion;
C () is used for the separation module of isolated peptides in a single step;
(d) selecting module, for being at least one known allergen and the multiple feature peptides of potential allergen selection;With
E () is used to measure the mass spectrum of multiple feature peptides.
The system of 11. claims 10, wherein the separation module includes column chromatography.
The system of 12. claims 11, wherein the column chromatography includes LCC.
The system of 13. claims 10, wherein the mass spectrum includes high-resolution accurate mass mass spectrum (HRAM MS).
The system of 14. claims 10, wherein the selecting module uses method according to claim 1.
The system of 15. claims 10, wherein at least one known allergen includes Gly m 1, Gly m 3, Gly m 4, Gly m 5 (beta-conglycinin), Gly m 6 (glycinin) G1, Gly m 6) G2, (the soybean ball eggs of Gly m 6 G3 in vain), Gly m 6 (glycinin) G4 or Gly m 6 (glycinin) precursor.
The system of 16. claims 10, wherein the potential allergen includes being selected from following at least one sequence:
The SEQ ID NO of (a) Gly m 1:12 and 30-35;
The SEQ ID NO of (b) Gly m 3:13 and 39-40;
The SEQ ID NO of (c) Gly m 4:14 and 43-51;
The SEQ ID NO of (d) Gly m 5:15 and 62-74;
The SEQ ID NO of the G1 of (e) Gly m 6:16 and 95;
The SEQ ID NO of the G2 of (f) Gly m 6:17 and 107;
The SEQ ID NO of the G3 of (g) Gly m 6:18;
The SEQ ID NO of the G4 of (h) Gly m 6:19 and 131-134;With
The SEQ ID NO of the precursors of (i) Gly m 6:20.
The system of 17. claims 10, wherein the feature peptide includes at least one sequence being selected from the group:
The SEQ ID NO of (a) Gly m 1:1,36 and 37;
The SEQ ID NO of (b) Gly m 3:2 and 41;
The SEQ ID NO of (c) Gly m 4:52-57;
The SEQ ID NO of (d) Gly m 5:3 and 75-94;
The SEQ ID NO of the G1 of (e) Gly m 6:96-106;
The SEQ ID NO of the G2 of (f) Gly m 6:4 and 108-120;
The SEQ ID NO of the G3 of (g) Gly m 6:5 and 121-129;
The SEQ ID NO of the G4 of (h) Gly m 6:135-156 and 58;With
The SEQ ID NO of the precursors of (i) Gly m 6:6,59 and 60.
The system of 18. claims 10, wherein the sample based on plant includes the part of soya seeds or soya seeds.
19. a kind of at least one allergens with known amino acid sequence quantitative in the sample based on plant and homologous potential The high throughput method of allergen, including the system that usage right requires 10.
CN201580054874.8A 2014-08-11 2015-08-11 For the quantitative method and system with detection of selectivity of allergen Pending CN106796242A (en)

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