DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. Structure (London, England : 1993) 2013 imex curation Hall Z., Hernández H., Marsh JA., Teichmann SA., Robinson CV. Only protein-protein interactions rabit Oryctolagus cuniculus (Rabbit) Rabbit ion mobility mass spec ion mobility mass spectrometry of complexes ion mobility mass spec predetermined predetermined participant predetermined Hall Z., Hernández H., Marsh JA., Teichmann SA., Robinson CV. DIP original experiment: DIP-254619X Structure (London, England : 1993) 2013 IMEx The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. Structure (London, England : 1993) 2013 imex curation Hall Z., Hernández H., Marsh JA., Teichmann SA., Robinson CV. Only protein-protein interactions ecolx Escherichia coli ion mobility mass spec ion mobility mass spectrometry of complexes ion mobility mass spec predetermined predetermined participant predetermined Hall Z., Hernández H., Marsh JA., Teichmann SA., Robinson CV. DIP original experiment: DIP-254620X Structure (London, England : 1993) 2013 IMEx The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. Structure (London, England : 1993) 2013 imex curation Hall Z., Hernández H., Marsh JA., Teichmann SA., Robinson CV. Only protein-protein interactions ecolx Escherichia coli ion mobility mass spec ion mobility mass spectrometry of complexes ion mobility mass spec predetermined predetermined participant predetermined Hall Z., Hernández H., Marsh JA., Teichmann SA., Robinson CV. DIP original experiment: DIP-254625X Structure (London, England : 1993) 2013 IMEx The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. Structure (London, England : 1993) 2013 imex curation Hall Z., Hernández H., Marsh JA., Teichmann SA., Robinson CV. Only protein-protein interactions human Homo sapiens Human ion mobility mass spec ion mobility mass spectrometry of complexes ion mobility mass spec predetermined predetermined participant predetermined Hall Z., Hernández H., Marsh JA., Teichmann SA., Robinson CV. DIP original experiment: DIP-254615X Structure (London, England : 1993) 2013 IMEx The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. Structure (London, England : 1993) 2013 imex curation Hall Z., Hernández H., Marsh JA., Teichmann SA., Robinson CV. Only protein-protein interactions ecolx Escherichia coli ion mobility mass spec ion mobility mass spectrometry of complexes ion mobility mass spec predetermined predetermined participant predetermined Hall Z., Hernández H., Marsh JA., Teichmann SA., Robinson CV. DIP original experiment: DIP-254624X Structure (London, England : 1993) 2013 IMEx The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. Structure (London, England : 1993) 2013 imex curation Hall Z., Hernández H., Marsh JA., Teichmann SA., Robinson CV. Only protein-protein interactions ecolx Escherichia coli ion mobility mass spec ion mobility mass spectrometry of complexes ion mobility mass spec predetermined predetermined participant predetermined Hall Z., Hernández H., Marsh JA., Teichmann SA., Robinson CV. DIP original experiment: DIP-254623X Structure (London, England : 1993) 2013 IMEx The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. Structure (London, England : 1993) 2013 imex curation Hall Z., Hernández H., Marsh JA., Teichmann SA., Robinson CV. Only protein-protein interactions metca Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath) ion mobility mass spec ion mobility mass spectrometry of complexes ion mobility mass spec predetermined predetermined participant predetermined Hall Z., Hernández H., Marsh JA., Teichmann SA., Robinson CV. DIP original experiment: DIP-254626X Structure (London, England : 1993) 2013 IMEx The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. Structure (London, England : 1993) 2013 imex curation Hall Z., Hernández H., Marsh JA., Teichmann SA., Robinson CV. Only protein-protein interactions ecolx Escherichia coli ion mobility mass spec ion mobility mass spectrometry of complexes ion mobility mass spec predetermined predetermined participant predetermined Hall Z., Hernández H., Marsh JA., Teichmann SA., Robinson CV. DIP original experiment: DIP-254622X Structure (London, England : 1993) 2013 IMEx The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. Structure (London, England : 1993) 2013 imex curation Hall Z., Hernández H., Marsh JA., Teichmann SA., Robinson CV. Only protein-protein interactions ecolx Escherichia coli ion mobility mass spec ion mobility mass spectrometry of complexes ion mobility mass spec predetermined predetermined participant predetermined Hall Z., Hernández H., Marsh JA., Teichmann SA., Robinson CV. DIP original experiment: DIP-254618X Structure (London, England : 1993) 2013 IMEx The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. Structure (London, England : 1993) 2013 imex curation Hall Z., Hernández H., Marsh JA., Teichmann SA., Robinson CV. Only protein-protein interactions human Homo sapiens Human ion mobility mass spec ion mobility mass spectrometry of complexes ion mobility mass spec predetermined predetermined participant predetermined Hall Z., Hernández H., Marsh JA., Teichmann SA., Robinson CV. DIP original experiment: DIP-254616X Structure (London, England : 1993) 2013 IMEx The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. Structure (London, England : 1993) 2013 imex curation Hall Z., Hernández H., Marsh JA., Teichmann SA., Robinson CV. Only protein-protein interactions bovin Bos taurus (Bovine) Bovine ion mobility mass spec ion mobility mass spectrometry of complexes ion mobility mass spec predetermined predetermined participant predetermined Hall Z., Hernández H., Marsh JA., Teichmann SA., Robinson CV. DIP original experiment: DIP-254621X Structure (London, England : 1993) 2013 IMEx The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. Structure (London, England : 1993) 2013 imex curation Hall Z., Hernández H., Marsh JA., Teichmann SA., Robinson CV. Only protein-protein interactions chick Gallus gallus (Chicken) Chicken ion mobility mass spec ion mobility mass spectrometry of complexes ion mobility mass spec predetermined predetermined participant predetermined Hall Z., Hernández H., Marsh JA., Teichmann SA., Robinson CV. DIP original experiment: DIP-254617X Structure (London, England : 1993) 2013 IMEx The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. kpym_rabit Pyruvate kinase PKM PKM PKM2 Pyruvate kinase muscle isozyme protein protein rabit Oryctolagus cuniculus (Rabbit) Rabbit MSKSHSEAGSAFIQTQQLHAAMADTFLEHMCRLDIDSAPITARNTGIICTIGPASRSVETLKEMIKSGMNVARMNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIRTGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVDVGSKVYVDDGLISLQVKQKGPDFLVTEVENGGFLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMVFASFIRKAADVHEVRKILGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMIIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIMLSGETAKGDYPLEAVRMQHLIAREAEAAMFHRKLFEELARSSSHSTDLMEAMAMGSVEASYKCLAAALIVLTESGRSAHQVARYRPRAPIIAVTRNHQTARQAHLYRGIFPVVCKDPVQEAWAEDVDLRVNLAMNVGKARGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP DIP protein P11974 original sequence version: 133 mint Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP AC0AFB579FC505E6 bgal_ecoli Beta-galactosidase lacZ b0344 JW0335 Lactase protein protein ecoli Escherichia coli (strain K12) MTMITDSLAVVLQRRDWENPGVTQLNRLAAHPPFASWRNSEEARTDRPSQQLRSLNGEWRFAWFPAPEAVPESWLECDLPEADTVVVPSNWQMHGYDAPIYTNVTYPITVNPPFVPTENPTGCYSLTFNVDESWLQEGQTRIIFDGVNSAFHLWCNGRWVGYGQDSRLPSEFDLSAFLRAGENRLAVMVLRWSDGSYLEDQDMWRMSGIFRDVSLLHKPTTQISDFHVATRFNDDFSRAVLEAEVQMCGELRDYLRVTVSLWQGETQVASGTAPFGGEIIDERGGYADRVTLRLNVENPKLWSAEIPNLYRAVVELHTADGTLIEAEACDVGFREVRIENGLLLLNGKPLLIRGVNRHEHHPLHGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTLCDRYGLYVVDEANIETHGMVPMNRLTDDPRWLPAMSERVTRMVQRDRNHPSVIIWSLGNESGHGANHDALYRWIKSVDPSRPVQYEGGGADTTATDIICPMYARVDEDQPFPAVPKWSIKKWLSLPGETRPLILCEYAHAMGNSLGGFAKYWQAFRQYPRLQGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDRQFCMNGLVFADRTPHPALTEAKHQQQFFQFRLSGQTIEVTSEYLFRHSDNELLHWMVALDGKPLASGEVPLDVAPQGKQLIELPELPQPESAGQLWLTVRVVQPNATAWSEAGHISAWQQWRLAENLSVTLPAASHAIPHLTTSEMDFCIELGNKRWQFNRQSGFLSQMWIGDKKQLLTPLRDQFTRAPLDNDIGVSEATRIDPNAWVERWKAAGHYQAEAALLQCTADTLADAVLITTAHAWQHQGKTLFISRKTYRIDGSGQMAITVDVEVASDTPHPARIGLNCQLAQVAERVNWLGLGPQENYPDRLTAACFDRWDLPLSDMYTPYVFPSENGLRCGTRELNYGPHQWRGDFQFNISRYSQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSPSVSAEFQLSAGRYHYQLVWCQK DIP protein P00722 original sequence version: 148 DIP protein P00722 original sequence version: 154 DIP protein P00722 original sequence version: 167 9D295EF4CEF90B08 tthy_human Transthyretin Prealbumin TBPA ATTR TTR PALB protein protein human Homo sapiens Human MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE DIP protein P02766 original sequence version: 114 DIP protein P02766 original sequence version: 163 DIP protein P02766 original sequence version: 174 3A6AEBCBBA56BC44 adh1_yeast Alcohol dehydrogenase 1 ADH1 ADC1 YOL086C O0947 Alcohol dehydrogenase I YADH-1 protein protein yeast Saccharomyces cerevisiae Baker's yeast MSIPETQKGVIFYESHGKLEYKDIPVPKPKANELLINVKYSGVCHTDLHAWHGDWPLPVKLPLVGGHEGAGVVVGMGENVKGWKIGDYAGIKWLNGSCMACEYCELGNESNCPHADLSGYTHDGSFQQYATADAVQAAHIPQGTDLAQVAPILCAGITVYKALKSANLMAGHWVAISGAAGGLGSLAVQYAKAMGYRVLGIDGGEGKEELFRSIGGEVFIDFTKEKDIVGAVLKATDGGAHGVINVSVSEAAIEASTRYVRANGTTVLVGMPAGAKCCSDVFNQVVKSISIVGSYVGNRADTREALDFFARGLVKSPIKVVGLSTLPEIYEKMEKGQIVGRYVVDTSK F14AE24B5D8D12A5 F14AE24B5D8D12A5 memb_metca Methane monooxygenase component A beta chain mmoY Methane hydroxylase MCA1195 protein protein metca Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath) MSMLGERRRGLTDPEMAAVILKALPEAPLDGNNKMGYFVTPRWKRLTEYEALTVYAQPNADWIAGGLDWGDWTQKFHGGRPSWGNETTELRTVDWFKHRDPLRRWHAPYVKDKAEEWRYTDRFLQGYSADGQIRAMNPTWRDEFINRYWGAFLFNEYGLFNAHSQGAREALSDVTRVSLAFWGFDKIDIAQMIQLERGFLAKIVPGFDESTAVPKAEWTNGEVYKSARLAVEGLWQEVFDWNESAFSVHAVYDALFGQFVRREFFQRLAPRFGDNLTPFFINQAQTYFQIAKQGVQDLYYNCLGDDPEFSDYNRTVMRNWTGKWLEPTIAALRDFMGLFAKLPAGTTDKEEITASLYRVVDDWIEDYASRIDFKADRDQIVKAVLAGLK DIP protein P18798 original sequence version: 100 DIP protein P18798 original sequence version: 103 DIP protein P18798 original sequence version: 97 1737FEA30EEA9875 dhe3_bovin Glutamate dehydrogenase 1, mitochondrial GLUD1 GLUD protein protein bovin Bos taurus (Bovine) Bovine MYRYLGEALLLSRAGPAALGSASADSAALLGWARGQPAAAPQPGLVPPARRHYSEAAADREDDPNFFKMVEGFFDRGASIVEDKLVEDLKTRETEEQKRNRVRSILRIIKPCNHVLSLSFPIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFGGAKAGVKINPKNYTDNELEKITRRFTMELAKKGFIGPGVDVPAPDMSTGEREMSWIADTYASTIGHYDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEASYMSILGMTPGFGDKTFVVQGFGNVGLHSMRYLHRFGAKCITVGESDGSIWNPDGIDPKELEDFKLQHGTILGFPKAKIYEGSILEVDCDILIPAASEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLERNIMVIPDLYLNAGGVTVSYFEWLNNLNHVSYGRLTFKYERDSNYHLLMSVQESLERKFGKHGGTIPIVPTAEFQDRISGASEKDIVHSGLAYTMERSARQIMRTAMKYNLGLDLRTAAYVNAIEKVFRVYNEAGVTFT DIP protein P00366 original sequence version: 115 194D74A33F2310E7 o87802_psest touE protein protein psest Pseudomonas stutzeri Pseudomonas perfectomarina MSEQQPEALKPLKTWSHLAGNRRRPSEYEVVSTNLHYFTDNPERPWELDSNLPMQTWYKKYCFDSPLKHDDWNAFRDPDQLVYRTYNLLQDGQESYVQGLFDQLNDRGHDQMLTREWVETLARFYTPARYLFHALQMGSVYIHQIAPASTITNCATYETADHLRWLTHTAYRTRELANCYPDVGFGKRERDVWENDPAWQGFRELIEKALIAWDWGEAFTAINLVTKPAVEEALLQQLGSLAQSEGDTLLGLLAQAQKRDAERHRRWSSALVKMALEKEGNREVLQKWVAKWEPLADKAIEAYCSALPDGENAIVEAKSASRYVRQMMGL DIP protein O87802 original sequence version: 65 DIP protein O87802 original sequence version: 56 09F9A3180112D88B o87798_psest touA protein protein psest Pseudomonas stutzeri Pseudomonas perfectomarina MSMLKREDWYDLTRTTNWTPKYVTENELFPEEMSGARGISMEAWEKYDEPYKITYPEYVSIQREKDSGAYSIKAALERDGFVDRADPGWVSTMQLHFGAIALEEYAASTAEARMARFAKAPGNRNMATFGMMDENRHGQIQLYFPYANVKRSRKWDWAHKAIHTNEWAAIAARSFFDDMMMTRDSVAVSIMLTFAFETGFTNMQFLGLAADAAEAGDHTFASLISSIQTDESRHAQQGGPSLKILVENGKKDEAQQMVDVAIWRSWKLFSVLTGPIMDYYTPLESRNQSFKEFMLEWIVAQFERQLLDLGLDKPWYWDQFMQDLDETHHGMHLGVWYWRPTVWWDPAAGVSPEEREWLEEKYPGWNDTWGQCWDVITDNLVNGKPELTVPETLPTICNMCNLPIAHTPGNKWNVKDYQLEYEGRLYHFGSEADRWCFQIDPERYKNHTNLVDRFLKGEIQPADLAGALMYMSLEPGVMGDDAHDYEWVKAYQKKTNAA DIP protein O87798 original sequence version: 65 DIP protein O87798 original sequence version: 56 E49B0C06D5BB43D8 memg_metca Methane monooxygenase component A gamma chain mmoZ Methane hydroxylase MCA1198 protein protein metca Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath) MAKLGIHSNDTRDAWVNKIAQLNTLEKAAEMLKQFRMDHTTPFRNSYELDNDYLWIEAKLEEKVAVLKARAFNEVDFRHKTAFGEDAKSVLDGTVAKMNAAKDKWEAEKIHIGFRQAYKPPIMPVNYFLDGERQLGTRLMELRNLNYYDTPLEELRKQRGVRVVHLQSPH DIP protein P11987 original sequence version: 96 DIP protein P11987 original sequence version: 99 DIP protein P11987 original sequence version: 93 6030AF38130BA497 samp_human Serum amyloid P-component APCS PTX2 9.5S alpha-1-glycoprotein protein protein human Homo sapiens Human MNKPLLWISVLTSLLEAFAHTDLSGKVFVFPRESVTDHVNLITPLEKPLQNFTLCFRAYSDLSRAYSLFSYNTQGRDNELLVYKERVGEYSLYIGRHKVTSKVIEKFPAPVHICVSWESSSGIAEFWINGTPLVKKGLRQGYFVEAQPKIVLGQEQDSYGGKFDRSQSFVGEIGDLYMWDSVLPPENILSAYQGTPLPANILDWQALNYEIRGYVIIKPLVWV DIP protein P02743 original sequence version: 159 DIP protein P02743 original sequence version: 163 6C88A515FE88B393 q8rtl4_9burk nbzAc protein protein comsp Comamonas sp. JS765 MSYQNLVSEAGLTQKLLIHGDKELFQHELKTIFARNWLFLTHDSLIPSPGDYVKAKMGVDEVIVSRQNDGSVRAFLNVCRHRGKTLVHAEAGNAKGFVCGYHGWGYGSNGELQSVPFEKELYGDAIKKKCLGLKEVPRIESFHGFIYGCFDAEAPPLIDYLGDAAWYLEPTFKYSGGLELVGPPGKVVVKANWKSFAENFVGDGYHVGWTHAAALRAGQSVFSSIAGNAKLPPEGAGLQMTSKYGSGMGVFWGYYSGNFSADMIPDLMAFGAAKQEKLAKEIGDVRARIYRSFLNGTIFPNNSFLTGSAAFRVWNPIDENTTEVWTYAFVEKDMPEDLKRRVADAVQRSIGPAGFWESDDNENMETMSQNGKKYQSSNIDQIASLGFGKDVYGDECYPGVVGKSAIGETSYRGFYRAYQAHISSSNWAEFENASRNWHIEHTKTTDR DIP protein Q8RTL4 original sequence version: 58 DIP protein Q8RTL4 original sequence version: 53 4CA961F99A37DF3A o87799_psest touB protein protein psest Pseudomonas stutzeri Pseudomonas perfectomarina MATFPIMSNFERDFVIQLVPVDTEDTMDQVAEKCAYHSINRRVHPQPEKILRVRRHEDGTLFPRGMIVSDAGLRPTETLDIIFMDN DIP protein O87799 original sequence version: 44 DIP protein O87799 original sequence version: 38 669356DF62EE5FAE q8rtl3_9burk nbzAd protein protein comsp Comamonas sp. JS765 MMINTQEDKLVSAHDAEEFHRFFVGHDSDLQQEVTTLLTREAHLLDIQAYKAWLEHFVAPEIKYQVISRELRSTSERRYQLNDAVNLYNENYQQLKVRVEHQMDPQNWANNPKIRFTRFVTNVTAAKDKSAPEILHVRSNLILHRARRENQVDVFYATREDKWKRIEGGGIKLVERFVDYPERIPQTHNLLVFL DIP protein Q8RTL3 original sequence version: 42 DIP protein Q8RTL3 original sequence version: 37 DA5F55AEFA1C4D94 trpa_salty Tryptophan synthase alpha chain trpA STM1727 protein protein salty Salmonella typhimurium MERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLADGPTIQNANLRAFAAGVTPAQCFEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADDDLLRQVASYGRGYTYLLSRSGVTGAENRGALPLHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKIIEKNLASPKQMLAELRSFVSAMKAASRA DIP protein P00929 original sequence version: 136 DIP protein P00929 original sequence version: 128 F409BF1A931581B5 trpb_salty Tryptophan synthase beta chain trpB STM1726 protein protein salty Salmonella typhimurium MTTLLNPYFGEFGGMYVPQILMPALNQLEEAFVSAQKDPEFQAQFADLLKNYAGRPTALTKCQNITAGTRTTLYLKREDLLHGGAHKTNQVLGQALLAKRMGKSEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRLMGAEVIPVHSGSATLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIVREFQRMIGEETKAQILDKEGRLPDAVIACVGGGSNAIGMFADFINDTSVGLIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTADGQIEESYSISAGLDFPSVGPQHAYLNSIGRADYVSITDDEALEAFKTLCRHEGIIPALESSHALAHALKMMREQPEKEQLLVVNLSGRGDKDIFTVHDILKARGEI DIP protein P0A2K1 original sequence version: 72 DIP protein P0A2K1 original sequence version: 62 73D210F5C6F2FEBD mema_metca Methane monooxygenase component A alpha chain mmoX Methane hydroxylase MCA1194 protein protein metca Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath) MALSTATKAATDALAANRAPTSVNAQEVHRWLQSFNWDFKNNRTKYATKYKMANETKEQFKLIAKEYARMEAVKDERQFGSLQDALTRLNAGVRVHPKWNETMKVVSNFLEVGEYNAIAATGMLWDSAQAAEQKNGYLAQVLDEIRHTHQCAYVNYYFAKNGQDPAGHNDARRTRTIGPLWKGMKRVFSDGFISGDAVECSLNLQLVGEACFTNPLIVAVTEWAAANGDEITPTVFLSIETDELRHMANGYQTVVSIANDPASAKYLNTDLNNAFWTQQKYFTPVLGMLFEYGSKFKVEPWVKTWNRWVYEDWGGIWIGRLGKYGVESPRSLKDAKQDAYWAHHDLYLLAYALWPTGFFRLALPDQEEMEWFEANYPGWYDHYGKIYEEWRARGCEDPSSGFIPLMWFIENNHPIYIDRVSQVPFCPSLAKGASTLRVHEYNGQMHTFSDQWGERMWLAEPERYECQNIFEQYEGRELSEVIAELHGLRSDGKTLIAQPHVRGDKLWTLDDIKRLNCVFKNPVKAFN DIP protein P22869 original sequence version: 100 DIP protein P22869 original sequence version: 103 DIP protein P22869 original sequence version: 97 953438FDF5208374 avid_chick Avidin AVD protein protein chick Gallus gallus (Chicken) Chicken MVHATSPLLLLLLLSLALVAPGLSARKCSLTGKWTNDLGSNMTIGAVNSRGEFTGTYITAVTATSNEIKESPLHGTQNTINKRTQPTFGFTVNWKFSESTTVFTGQCFIDRNGKEVLKTMWLLRSSVNDIGDDWKATRVGINIFTRLRTQKE DIP protein P02701 original sequence version: 121 pkm-1 1 13 unspecified role unspecified role unspecified role unspecified role rabit Oryctolagus cuniculus (Rabbit) Rabbit direct interaction direct interaction apcs-1 4 22 unspecified role unspecified role unspecified role unspecified role human Homo sapiens Human direct interaction direct interaction trpb-5 6 27 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction lacz-1 2 14 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction ttr-7 10 15 unspecified role unspecified role unspecified role unspecified role human Homo sapiens Human direct interaction direct interaction nbzac-nbzad-6 5 25 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 23 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction mmox-mmoy-2 7 21 unspecified role unspecified role unspecified role unspecified role metca Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath) 17 unspecified role unspecified role unspecified role unspecified role metca Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath) 28 unspecified role unspecified role unspecified role unspecified role metca Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath) physical association physical association glud1-2 11 18 unspecified role unspecified role unspecified role unspecified role bovin Bos taurus (Bovine) Bovine direct interaction direct interaction avd-1 12 29 unspecified role unspecified role unspecified role unspecified role chick Gallus gallus (Chicken) Chicken direct interaction direct interaction trpa-trpb-25 8 27 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 26 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction adh-2 9 16 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction toua-toub-8 3 19 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 24 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 20 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association