DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Protein conformation ensembles monitored by HDX reveal a structural rationale for abscisic acid signaling protein affinities and activities. Protein conformation ensembles monitored by HDX reveal a structural rationale for abscisic acid signaling protein affinities and activities. Structure (London, England : 1993) 2013 imex curation West GM., Pascal BD., Ng LM., Soon FF., Melcher K., Xu HE., Chalmers MJ., Griffin PR. Only protein-protein interactions in vitro In vitro h1-h2 ms mass spectrometry study of hydrogen/deuterium exchange h1-h2 ms predetermined predetermined participant predetermined West GM., Pascal BD., Ng LM., Soon FF., Melcher K., Xu HE., Chalmers MJ., Griffin PR. DIP original experiment: DIP-251913X Structure (London, England : 1993) 2013 IMEx Protein conformation ensembles monitored by HDX reveal a structural rationale for abscisic acid signaling protein affinities and activities. Protein conformation ensembles monitored by HDX reveal a structural rationale for abscisic acid signaling protein affinities and activities. Protein conformation ensembles monitored by HDX reveal a structural rationale for abscisic acid signaling protein affinities and activities. Structure (London, England : 1993) 2013 imex curation West GM., Pascal BD., Ng LM., Soon FF., Melcher K., Xu HE., Chalmers MJ., Griffin PR. Only protein-protein interactions in vitro In vitro h1-h2 ms mass spectrometry study of hydrogen/deuterium exchange h1-h2 ms predetermined predetermined participant predetermined West GM., Pascal BD., Ng LM., Soon FF., Melcher K., Xu HE., Chalmers MJ., Griffin PR. DIP original experiment: DIP-251914X Structure (London, England : 1993) 2013 IMEx Protein conformation ensembles monitored by HDX reveal a structural rationale for abscisic acid signaling protein affinities and activities. Protein conformation ensembles monitored by HDX reveal a structural rationale for abscisic acid signaling protein affinities and activities. Protein conformation ensembles monitored by HDX reveal a structural rationale for abscisic acid signaling protein affinities and activities. Structure (London, England : 1993) 2013 imex curation West GM., Pascal BD., Ng LM., Soon FF., Melcher K., Xu HE., Chalmers MJ., Griffin PR. Only protein-protein interactions in vitro In vitro h1-h2 ms mass spectrometry study of hydrogen/deuterium exchange h1-h2 ms predetermined predetermined participant predetermined West GM., Pascal BD., Ng LM., Soon FF., Melcher K., Xu HE., Chalmers MJ., Griffin PR. DIP original experiment: DIP-251915X Structure (London, England : 1993) 2013 IMEx Protein conformation ensembles monitored by HDX reveal a structural rationale for abscisic acid signaling protein affinities and activities. srk2e_arath Serine/threonine-protein kinase SRK2E SNRK2.6 Serine/threonine-protein kinase OST1 Protein OPEN STOMATA 1 SNF1-related kinase 2.6 F17I5.140 SRK2E OST1 At4g33950 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MDRPAVSGPMDLPIMHDSDRYELVKDIGSGNFGVARLMRDKQSNELVAVKYIERGEKIDENVKREIINHRSLRHPNIVRFKEVILTPTHLAIVMEYASGGELFERICNAGRFSEDEARFFFQQLISGVSYCHAMQVCHRDLKLENTLLDGSPAPRLKICDFGYSKSSVLHSQPKSTVGTPAYIAPEVLLKKEYDGKVADVWSCGVTLYVMLVGAYPFEDPEEPKNFRKTIHRILNVQYAIPDYVHISPECRHLISRIFVADPAKRISIPEIRNHEWFLKNLPADLMNDNTMTTQFDESDQPGQSIEEIMQIIAEATVPPAGTQNLNHYLTGSLDIDDDMEEDLESDLDDLDIDSSGEIVYAM DIP protein Q940H6 original sequence version: 63 DIP protein Q940H6-1 original sequence version: 62 DIP protein Q940H6-1 original sequence version: 66 DIP protein Q940H6 original sequence version: 76 DIP protein Q940H6-1 original sequence version: 67 DIP protein Q940H6 original sequence version: 89 DIP protein Q940H6 original sequence version: 91 FFBCCA1474839B88 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 srk2i_arath Serine/threonine-protein kinase SRK2I SRK2I 41K OSKL2 SNRK2.3 Protein ATHPROKIN B OST1-kinase-like 2 SNF1-related kinase 2.3 MUD21.14 At5g66880 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MDRAPVTTGPLDMPIMHDSDRYDFVKDIGSGNFGVARLMRDKLTKELVAVKYIERGDKIDENVQREIINHRSLRHPNIVRFKEVILTPTHLAIIMEYASGGELYERICNAGRFSEDEARFFFQQLLSGVSYCHSMQICHRDLKLENTLLDGSPAPRLKICDFGYSKSSVLHSQPKSTVGTPAYIAPEVLLRQEYDGKIADVWSCGVTLYVMLVGAYPFEDPEEPRDYRKTIQRILSVKYSIPDDIRISPECCHLISRIFVADPATRISIPEIKTHSWFLKNLPADLMNESNTGSQFQEPEQPMQSLDTIMQIISEATIPAVRNRCLDDFMTDNLDLDDDMDDFDSESEIDIDSSGEIVYAL DIP protein Q39193 original sequence version: 71 DIP protein Q39193 original sequence version: 69 DIP protein Q39193 original sequence version: 73 DIP protein Q39193 original sequence version: 93 01200388CD0124B9 hab1-pyl2-6 1 6 unspecified role unspecified role unspecified role unspecified role Region 14-188 Region 14-188 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 5 unspecified role unspecified role unspecified role unspecified role Region 172-511 Region 172-511 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction hab1-srk2e-3 3 4 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 5 unspecified role unspecified role unspecified role unspecified role Region 172-511 Region 172-511 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction hab1-srk2i-1 2 7 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 5 unspecified role unspecified role unspecified role unspecified role Region 172-511 Region 172-511 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction