DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Infinite kinetic stability against dissociation of supramolecular protein complexes through donor strand complementation. Infinite kinetic stability against dissociation of supramolecular protein complexes through donor strand complementation. Structure (London, England : 1993) 2008 imex curation Puorger C., Eidam O., Capitani G., Erilov D., Grütter MG., Glockshuber R. 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 Puorger C., Eidam O., Capitani G., Erilov D., Grütter MG., Glockshuber R. DIP original experiment: DIP-68418X Structure (London, England : 1993) 2008 IMEx Infinite kinetic stability against dissociation of supramolecular protein complexes through donor strand complementation. Infinite kinetic stability against dissociation of supramolecular protein complexes through donor strand complementation. Infinite kinetic stability against dissociation of supramolecular protein complexes through donor strand complementation. Structure (London, England : 1993) 2008 imex curation Puorger C., Eidam O., Capitani G., Erilov D., Grütter MG., Glockshuber R. Only protein-protein interactions in vitro In vitro cd circular dichroism CD CD cd predetermined predetermined participant predetermined Puorger C., Eidam O., Capitani G., Erilov D., Grütter MG., Glockshuber R. DIP original experiment: DIP-68416X Structure (London, England : 1993) 2008 IMEx Infinite kinetic stability against dissociation of supramolecular protein complexes through donor strand complementation. Infinite kinetic stability against dissociation of supramolecular protein complexes through donor strand complementation. Infinite kinetic stability against dissociation of supramolecular protein complexes through donor strand complementation. Structure (London, England : 1993) 2008 imex curation Puorger C., Eidam O., Capitani G., Erilov D., Grütter MG., Glockshuber R. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Puorger C., Eidam O., Capitani G., Erilov D., Grütter MG., Glockshuber R. DIP original experiment: DIP-68417X Structure (London, England : 1993) 2008 IMEx Infinite kinetic stability against dissociation of supramolecular protein complexes through donor strand complementation. Infinite kinetic stability against dissociation of supramolecular protein complexes through donor strand complementation. Infinite kinetic stability against dissociation of supramolecular protein complexes through donor strand complementation. Structure (London, England : 1993) 2008 imex curation Puorger C., Eidam O., Capitani G., Erilov D., Grütter MG., Glockshuber R. Only protein-protein interactions ecolx Escherichia coli cd circular dichroism CD CD cd predetermined predetermined participant predetermined Puorger C., Eidam O., Capitani G., Erilov D., Grütter MG., Glockshuber R. DIP original experiment: DIP-68419X Structure (London, England : 1993) 2008 IMEx Infinite kinetic stability against dissociation of supramolecular protein complexes through donor strand complementation. Infinite kinetic stability against dissociation of supramolecular protein complexes through donor strand complementation. Infinite kinetic stability against dissociation of supramolecular protein complexes through donor strand complementation. Structure (London, England : 1993) 2008 imex curation Puorger C., Eidam O., Capitani G., Erilov D., Grütter MG., Glockshuber R. 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 Puorger C., Eidam O., Capitani G., Erilov D., Grütter MG., Glockshuber R. DIP original experiment: DIP-68415X Structure (London, England : 1993) 2008 IMEx Infinite kinetic stability against dissociation of supramolecular protein complexes through donor strand complementation. Infinite kinetic stability against dissociation of supramolecular protein complexes through donor strand complementation. Infinite kinetic stability against dissociation of supramolecular protein complexes through donor strand complementation. Structure (London, England : 1993) 2008 imex curation Puorger C., Eidam O., Capitani G., Erilov D., Grütter MG., Glockshuber R. 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 Puorger C., Eidam O., Capitani G., Erilov D., Grütter MG., Glockshuber R. DIP original experiment: DIP-68414X Structure (London, England : 1993) 2008 IMEx Infinite kinetic stability against dissociation of supramolecular protein complexes through donor strand complementation. dsf Donor strand peptide of FimF peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) ADSTITIRGYVRDNR fima1_ecoli Type-1 fimbrial protein, A chain fimA Type-1A pilin pilA JW4277 b4314 protein protein ecoli Escherichia coli (strain K12) MKIKTLAIVVLSALSLSSTAALAAATTVNGGTVHFKGEVVNAACAVDAGSVDQTVQLGQVRTASLAQEGATSSAVGFNIQLNDCDTNVASKAAVAFLGTAIDAGHTNVLALQSSAAGSATNVGVQILDRTGAALTLDGATFSSETTLNNGTNTIPFQARYFATGAATPGAANADATFKVQYQ 35B2016BDD21A2C1 fimg_ecoli Protein FimG fimG b4319 JW4282 protein protein ecoli Escherichia coli (strain K12) MKWCKRGYVLAAILALASATIQAADVTITVNGKVVAKPCTVSTTNATVDLGDLYSFSLMSAGAASAWHDVALELTNCPVGTSRVTASFSGAADSTGYYKNQGTAQNIQLELQDDSGNTLNTGATKTVQVDDSSQSAHFPLQVRALTVNGGATQGTIQAVISITYTYS 8C3EF95FD442E22C 8C3EF95FD442E22C dsf-fimg-1 6 7 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 9 unspecified role unspecified role unspecified role unspecified role Region 36-167 Region 36-167 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction fima-1 4 8 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction dsf-fimg-2 3 7 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 9 unspecified role unspecified role unspecified role unspecified role Region 36-167 Region 36-167 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction dsf-fimg-3 5 7 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 9 unspecified role unspecified role unspecified role unspecified role Region 36-167 Region 36-167 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction fima-2 1 8 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction dsf-fimg-4 2 7 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 9 unspecified role unspecified role unspecified role unspecified role Region 36-167 Region 36-167 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction