DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ di-2012-5 in vitro In vitro ion exchange chrom ion exchange chromatography IEC IEC ion exchange chrom predetermined predetermined participant predetermined Di Yu X., Dubnovitsky A., Pudney AF., Macintyre S., Knight SD., Zavialov AV. DIP original experiment: DIP-251173X Structure (London, England : 1993) 2012 IMEx Allosteric mechanism controls traffic in the chaperone/usher pathway. Di Yu X., Dubnovitsky A., Pudney AF., Macintyre S., Knight SD., Zavialov AV. Only protein-protein interactions imex curation di-2012-6 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Di Yu X., Dubnovitsky A., Pudney AF., Macintyre S., Knight SD., Zavialov AV. DIP original experiment: DIP-251175X Structure (London, England : 1993) 2012 IMEx Allosteric mechanism controls traffic in the chaperone/usher pathway. Di Yu X., Dubnovitsky A., Pudney AF., Macintyre S., Knight SD., Zavialov AV. Only protein-protein interactions imex curation di-2012-7 in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Di Yu X., Dubnovitsky A., Pudney AF., Macintyre S., Knight SD., Zavialov AV. DIP original experiment: DIP-251174X Structure (London, England : 1993) 2012 IMEx Allosteric mechanism controls traffic in the chaperone/usher pathway. Di Yu X., Dubnovitsky A., Pudney AF., Macintyre S., Knight SD., Zavialov AV. Only protein-protein interactions imex curation di-2012-8 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Di Yu X., Dubnovitsky A., Pudney AF., Macintyre S., Knight SD., Zavialov AV. DIP original experiment: DIP-251176X Structure (London, England : 1993) 2012 IMEx Allosteric mechanism controls traffic in the chaperone/usher pathway. Di Yu X., Dubnovitsky A., Pudney AF., Macintyre S., Knight SD., Zavialov AV. Only protein-protein interactions imex curation caf1_yerpe F1 capsule antigen caf1 YPMT1.84 YP_pMT082 Y1100 protein protein yerpe Yersinia pestis MKKISSVIAIALFGTIATANAADLTASTTATATLVEPARITLTYKEGAPITIMDNGNIDTELLVGTLTLGGYKTGTTSTSVNFTDAAGDPMYLTFTSQDGNNHQFTTKVIGKDSRDFDISPKVNGENLVGDDVVLATGSQDFFVRSIGSKGGKLAAGKYTDAVTVTVSNQ caf1m_yerpe Chaperone protein caf1M caf1M YPMT1.82 YP_pMT084 Capsule protein fraction 1 Y1098 protein protein yerpe Yersinia pestis MILNRLSTLGIITFGMLSFAANSAQPDIKFASKEYGVTIGESRIIYPLDAAGVMVSVKNTQDYPVLIQSRIYDENKEKESEDPFVVTPPLFRLDAKQQNSLRIAQAGGVFPRDKESLKWLCVKGIPPKDEDIWVDDATNKQKFNPDKDVGVFVQFAINNCIKLLVRPNELKGTPIQFAENLSWKVDGGKLIAENPSPFYMNIGELTFGGKSIPSHYIPPKSTWAFDLPKGLAGARNVSWRIINDQGGLDRLYSKNVTL caf1a_yerpe F1 capsule-anchoring protein caf1A YPMT1.83 Y1099 YP_pMT083 protein protein yerpe Yersinia pestis MRYSKLFLCAGLTLATLPCWGRAYTFDSTMLDTNSGESIDVSLFNQGLQLPGNYFVNVFVNGRKVDSGNIDFRLEKHNGKELLWPCLSSLQLTKYGIDIDKYPDLIKSGTEQCVDLLAIPHSDVQFYFNQQKLSLIVPPQALLPRFDGIMPMQLWDDGIPALFMNYNTNMQTRKFREGGKSLDSYYAQLQPGLNIGAWRFRSSTSWWKQQGWQRSYIYAERGLNTIKSRLTLGETYSDSSIFDSIPIKGIKIASDESMVPYYQWNFAPVVRGIARTQARVEVLRDGYTVSNELVPSGPFELANLPLGGGSGELKVIIHESDGTKQVFTVPYDTPAVALRKGYFEYSMMGGEYRPANDLTQTSYVGALGMKYGLPRNLTLYGGLQGSQNYHAAALGIGAMLGDFGAISTDVTQADSQKNKQKKESGQRWRVRYNKYLQSGTSLNIASEEYATEGFNKLADTLNTYCKPNTRNDCRFDYAKPKNKVQFNLSQSIPGSGTLNFSGYRKNYWRDSRSTTSFSVGYNHFFRNGMSLTLNLSKTQNINKYGEKTSELLSNIWLSFPLSRWLGNNSINSNYQMTSDSHGNTTHEVGVYGEAFDRQLYWDVRERFNEKGRKYTSNALNLNYRGTYGEISGNYSYDQTQSQLGIGVNGNMVITQYGITAGQKTGDTIALVQAPDISGASVGYWPGMKTDFRGYTNYGYLTPYRENKVEINPVTLPNDAEITNNIVSVIPTKGAVVLAKFNARIGGRLFLHLKRSDNKPVPFGSIVTIEGQSSSSGIVGDNSGVYLTGLPKKSKILVKWGRDKNQSCSSNVVLPEKTDISGAYRLSTTCILNN caf1-caf1a-1 3244947 N/A 3244951 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3244952 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3244953 unspecified role unspecified role unspecified role unspecified role N-terminal domain Region 1-158 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli association association false false false caf1-caf1a-2 3244948 N/A 3244951 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3244952 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3244953 unspecified role unspecified role unspecified role unspecified role N-terminal domain Region 1-158 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false caf1-caf1a-3 3244949 N/A 3244951 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3244952 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3244953 unspecified role unspecified role unspecified role unspecified role N-terminal domain Region 1-158 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli physical association physical association false false false caf1-caf1m-1 3244950 N/A 3244951 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3244952 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false