DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Structure (London, England : 1993) 2012 imex curation Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. Only protein-protein interactions ecolx Escherichia coli saxs x ray scattering saxs predetermined predetermined participant predetermined Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. DIP original experiment: DIP-250415X Structure (London, England : 1993) 2012 IMEx Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Structure (London, England : 1993) 2012 imex curation Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. DIP original experiment: DIP-250418X Structure (London, England : 1993) 2012 IMEx Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Structure (London, England : 1993) 2012 imex curation Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink weight by comassie molecular weight estimation by coomasie staining weight by comassie Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. DIP original experiment: DIP-250411X Structure (London, England : 1993) 2012 IMEx Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Structure (London, England : 1993) 2012 imex curation Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. DIP original experiment: DIP-250406X Structure (London, England : 1993) 2012 IMEx Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Structure (London, England : 1993) 2012 imex curation Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. Only protein-protein interactions ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. DIP original experiment: DIP-250416X Structure (London, England : 1993) 2012 IMEx Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Structure (London, England : 1993) 2012 imex curation Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. DIP original experiment: DIP-250409X Structure (London, England : 1993) 2012 IMEx Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Structure (London, England : 1993) 2012 imex curation Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. DIP original experiment: DIP-250419X Structure (London, England : 1993) 2012 IMEx Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Structure (London, England : 1993) 2012 imex curation Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink weight by comassie molecular weight estimation by coomasie staining weight by comassie Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. DIP original experiment: DIP-250412X Structure (London, England : 1993) 2012 IMEx Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Structure (London, England : 1993) 2012 imex curation Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. DIP original experiment: DIP-250408X Structure (London, England : 1993) 2012 IMEx Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Structure (London, England : 1993) 2012 imex curation Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink weight by comassie molecular weight estimation by coomasie staining weight by comassie Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. DIP original experiment: DIP-250414X Structure (London, England : 1993) 2012 IMEx Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Structure (London, England : 1993) 2012 imex curation Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. DIP original experiment: DIP-250417X Structure (London, England : 1993) 2012 IMEx Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Structure (London, England : 1993) 2012 imex curation Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. Only protein-protein interactions ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. DIP original experiment: DIP-250410X Structure (London, England : 1993) 2012 IMEx Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Structure (London, England : 1993) 2012 imex curation Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink weight by comassie molecular weight estimation by coomasie staining weight by comassie Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. DIP original experiment: DIP-250413X Structure (London, England : 1993) 2012 IMEx Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. Structure (London, England : 1993) 2012 imex curation Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G., Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z. DIP original experiment: DIP-250407X Structure (London, England : 1993) 2012 IMEx Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism. p2c16_arath Protein phosphatase 2C 16 HAB1 P2C-HA Protein phosphatase 2C HAB1 AtP2C-HA Protein HYPERSENSITIVE TO ABA 1 F28P22.4 At1g72770 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MEEMTPAVAMTLSLAANTMCESSPVEITQLKNVTDAADLLSDSENQSFCNGGTECTMEDVSELEEVGEQDLLKTLSDTRSGSSNVFDEDDVLSVVEDNSAVISEGLLVVDAGSELSLSNTAMEIDNGRVLATAIIVGESSIEQVPTAEVLIAGVNQDTNTSEVVIRLPDENSNHLVKGRSVYELDCIPLWGTVSIQGNRSEMEDAFAVSPHFLKLPIKMLMGDHEGMSPSLTHLTGHFFGVYDGHGGHKVADYCRDRLHFALAEEIERIKDELCKRNTGEGRQVQWDKVFTSCFLTVDGEIEGKIGRAVVGSSDKVLEAVASETVGSTAVVALVCSSHIVVSNCGDSRAVLFRGKEAMPLSVDHKPDREDEYARIENAGGKVIQWQGARVFGVLAMSRSIGDRYLKPYVIPEPEVTFMPRSREDECLILASDGLWDVMNNQEVCEIARRRILMWHKKNGAPPLAERGKGIDPACQAAADYLSMLALQKGSKDNISIIVIDLKAQRKFKTRT DIP protein Q9CAJ0 original sequence version: 64 DIP protein Q9CAJ0-1 original sequence version: 62 DIP protein Q9CAJ0-1 original sequence version: 77 DIP protein Q9CAJ0 original sequence version: 62 DIP protein Q9CAJ0 original sequence version: 65 DIP protein Q9CAJ0-1 original sequence version: 66 DIP protein Q9CAJ0 original sequence version: 81 DIP protein Q9CAJ0-1 original sequence version: 86 DIP protein Q9CAJ0-1 original sequence version: 108 DIP protein Q9CAJ0 original sequence version: 112 DIP protein Q9CAJ0-1 original sequence version: 81 B001BAF0DD8333E1 pyl2_arath Abscisic acid receptor PYL2 PYL2 RCAR14 PYR1-like protein 2 Regulatory components of ABA receptor 14 T19L18.15 At2g26040 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MSSSPAVKGLTDEEQKTLEPVIKTYHQFEPDPTTCTSLITQRIHAPASVVWPLIRRFDNPERYKHFVKRCRLISGDGDVGSVREVTVISGLPASTSTERLEFVDDDHRVLSFRVVGGEHRLKNYKSVTSVNEFLNQDSGKVYTVVLESYTVDIPEGNTEEDTKMFVDTVVKLNLQKLGVAATSAPMHDDE DIP protein O80992 original sequence version: 50 DIP protein O80992 original sequence version: 47 DIP protein O80992 original sequence version: 51 DIP protein O80992 original sequence version: 69 DIP protein O80992 original sequence version: 65 CBB16E64BE2B8164 pyl3_arath Abscisic acid receptor PYL3 PYL3 RCAR13 PYR1-like protein 3 Regulatory components of ABA receptor 13 F3N23.20 At1g73000 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MNLAPIHDPSSSSTTTTSSSTPYGLTKDEFSTLDSIIRTHHTFPRSPNTCTSLIAHRVDAPAHAIWRFVRDFANPNKYKHFIKSCTIRVNGNGIKEIKVGTIREVSVVSGLPASTSVEILEVLDEEKRILSFRVLGGEHRLNNYRSVTSVNEFVVLEKDKKKRVYSVVLESYIVDIPQGNTEEDTRMFVDTVVKSNLQNLAVISTASPT DIP protein Q9SSM7 original sequence version: 37 DIP protein Q9SSM7 original sequence version: 43 DIP protein Q9SSM7 original sequence version: 59 4A25A6E47D469890 pyl3-1 4 17 unspecified role unspecified role unspecified role unspecified role Region 25-209 Region 25-209 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction pyl3-2 8 17 unspecified role unspecified role unspecified role unspecified role Q9SSM7:p.[Asn180Cys;Thr209Cys] N180C/T209C mutation mutation certain certain sequence position certain certain certain sequence position certain T C certain certain sequence position certain certain certain sequence position certain N C This feature has been corrected as a result of our quality control procedures. The original label was 'N180C/T209C'. Wed May 02 18:04:30 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asn180cys,thr209cys' Tue Jun 30 16:50:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Asn180Cys;Thr209Cys]' ecolx Escherichia coli direct interaction direct interaction pyl3-hab1-1 2 15 unspecified role unspecified role prey prey Region 169-511 Region 169-511 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 17 unspecified role unspecified role bait bait Q9SSM7:p.[Phe81Ala;Val202Ala;Ile203Ala] F81A/V202A/I203A mutation increasing strength mutation increasing interaction strength mutation increasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain F A certain certain sequence position certain certain certain sequence position certain I A certain certain sequence position certain certain certain sequence position certain V A This feature has been corrected as a result of our quality control procedures. The original label was 'F81A/V202A/I203A'. Wed May 02 18:31:16 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe81ala,val202ala,ile203ala' Tue Jun 30 18:11:35 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Phe81Ala;Val202Ala;Ile203Ala]' Q9SSM7:p.Ser195Leu S195L mutation increasing strength mutation increasing interaction strength mutation increasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain S L This feature has been corrected as a result of our quality control procedures. The original label was 'S195L'. Wed May 02 16:13:38 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser195leu' Tue Jun 30 16:17:32 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser195Leu' yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast direct interaction direct interaction hab1-pyl3-3 14 15 unspecified role unspecified role unspecified role unspecified role Region 169-511 Region 169-511 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction pyl3-pyl3-1 13 17 unspecified role unspecified role unspecified role unspecified role Q9SSM7:p.Thr209Cys T209C mutation mutation certain certain sequence position certain certain certain sequence position certain T C This feature has been corrected as a result of our quality control procedures. The original label was 'T209C'. Wed May 02 18:52:36 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr209cys' Tue Jun 30 19:21:46 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr209Cys' ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Q9SSM7:p.Asn180Cys N180C mutation mutation certain certain sequence position certain certain certain sequence position certain N C This feature has been corrected as a result of our quality control procedures. The original label was 'N180C'. Wed May 02 19:44:09 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asn180cys' Tue Jun 30 19:00:05 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asn180Cys' ecolx Escherichia coli direct interaction direct interaction hab1-pyl3-4 9 15 unspecified role unspecified role unspecified role unspecified role Region 169-511 Region 169-511 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction hab1-pyl3-5 7 15 unspecified role unspecified role bait bait Region 169-511 Region 169-511 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain GST-tag GST-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 17 unspecified role unspecified role prey prey ecolx Escherichia coli direct interaction direct interaction pyl3-3 10 17 unspecified role unspecified role unspecified role unspecified role Q9SSM7:p.[Asn180Cys;Pro208Cys;Thr209Cys] N180C/P208C/T209C mutation mutation certain certain sequence position certain certain certain sequence position certain T C certain certain sequence position certain certain certain sequence position certain P C certain certain sequence position certain certain certain sequence position certain N C This feature has been corrected as a result of our quality control procedures. The original label was 'N180C/P208C/T209C'. Wed May 02 19:41:30 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asn180cys,pro208cys,thr209cys' Tue Jun 30 19:19:03 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Asn180Cys;Pro208Cys;Thr209Cys]' ecolx Escherichia coli direct interaction direct interaction pyl3-4 6 17 unspecified role unspecified role unspecified role unspecified role Q9SSM7:p.[Phe81Ala;Val202Ala;Ile203Ala] F81A/V202A/I203A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain F A certain certain sequence position certain certain certain sequence position certain I A certain certain sequence position certain certain certain sequence position certain V A This feature has been corrected as a result of our quality control procedures. The original label was 'F81A/V202A/I203A'. Wed May 02 16:31:49 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe81ala,val202ala,ile203ala' Tue Jun 30 18:54:06 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Phe81Ala;Val202Ala;Ile203Ala]' ecolx Escherichia coli direct interaction direct interaction pyl3-5 1 17 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction pyl3-6 12 17 unspecified role unspecified role unspecified role unspecified role Q9SSM7:p.[Phe81Ala;Val202Ala;Ile203Ala] F81A/V202A/I203A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain F A certain certain sequence position certain certain certain sequence position certain I A certain certain sequence position certain certain certain sequence position certain V A This feature has been corrected as a result of our quality control procedures. The original label was 'F81A/V202A/I203A'. Wed May 02 16:16:28 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe81ala,val202ala,ile203ala' Tue Jun 30 15:55:48 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Phe81Ala;Val202Ala;Ile203Ala]' ecolx Escherichia coli direct interaction direct interaction pyl2-3 5 16 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction pyl2-4 11 16 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction pyl3-7 3 17 unspecified role unspecified role unspecified role unspecified role Q9SSM7:p.[Phe81Ala;Val202Ala;Ile203Ala] F81A/V202A/I203A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain F A certain certain sequence position certain certain certain sequence position certain I A certain certain sequence position certain certain certain sequence position certain V A This feature has been corrected as a result of our quality control procedures. The original label was 'F81A/V202A/I203A'. Wed May 02 18:07:37 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe81ala,val202ala,ile203ala' Tue Jun 30 17:03:22 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Phe81Ala;Val202Ala;Ile203Ala]' ecolx Escherichia coli direct interaction direct interaction