DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding. Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding. Nature structural & molecular biology 2010 imex curation Schulz EC., Dickmanns A., Urlaub H., Schmitt A., Mühlenhoff M., Stummeyer K., Schwarzer D., Gerardy-Schahn R., Ficner 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 Schulz EC., Dickmanns A., Urlaub H., Schmitt A., Mühlenhoff M., Stummeyer K., Schwarzer D., Gerardy-Schahn R., Ficner R. DIP original experiment: DIP-133994X Nature structural & molecular biology 2010 IMEx Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding. Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding. Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding. Nature structural & molecular biology 2010 imex curation Schulz EC., Dickmanns A., Urlaub H., Schmitt A., Mühlenhoff M., Stummeyer K., Schwarzer D., Gerardy-Schahn R., Ficner R. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Schulz EC., Dickmanns A., Urlaub H., Schmitt A., Mühlenhoff M., Stummeyer K., Schwarzer D., Gerardy-Schahn R., Ficner R. DIP original experiment: DIP-133992X Nature structural & molecular biology 2010 IMEx Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding. Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding. Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding. Nature structural & molecular biology 2010 imex curation Schulz EC., Dickmanns A., Urlaub H., Schmitt A., Mühlenhoff M., Stummeyer K., Schwarzer D., Gerardy-Schahn R., Ficner 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 Schulz EC., Dickmanns A., Urlaub H., Schmitt A., Mühlenhoff M., Stummeyer K., Schwarzer D., Gerardy-Schahn R., Ficner R. DIP original experiment: DIP-133993X Nature structural & molecular biology 2010 IMEx Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding. Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding. Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding. Nature structural & molecular biology 2010 imex curation Schulz EC., Dickmanns A., Urlaub H., Schmitt A., Mühlenhoff M., Stummeyer K., Schwarzer D., Gerardy-Schahn R., Ficner R. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Schulz EC., Dickmanns A., Urlaub H., Schmitt A., Mühlenhoff M., Stummeyer K., Schwarzer D., Gerardy-Schahn R., Ficner R. DIP original experiment: DIP-133995X Nature structural & molecular biology 2010 IMEx Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding. fiber_bpk1f Tail spike protein Endo-N-acetylneuraminidase Endo-alpha-sialidase EndoNF G102 protein protein bpk1f Enterobacteria phage K1F Bacteriophage K1F MSTITQFPSGNTQYRIEFDYLARTFVVVTLVNSSNPTLNRVLEVGRDYRFLNPTMIEMLVDQSGFDIVRIHRQTGTDLVVDFRNGSVLTASDLTTAELQAIHIAEEGRDQTVDLAKEYADAAGSSAGNAKDSEDEARRIAESIRAAGLIGYMTRRSFEKGYNVTTWSEVLLWEEDGDYYRWDGTLPKNVPAGSTPETSGGIGLGAWVSVGDAALRSQISNPEGAILYPELHRARWLDEKDARGWGAKGDGVTDDTAALTSALNDTPVGQKINGNGKTYKVTSLPDISRFINTRFVYERIPGQPLYYASEEFVQGELFKITDTPYYNAWPQDKAFVYENVIYAPYMGSDRHGVSRLHVSWVKSGDDGQTWSTPEWLTDLHPDYPTVNYHCMSMGVCRNRLFAMIETRTLAKNALTNCALWDRPMSRSLHLTGGITKAANQRYATIHVPDHGLFVGDFVNFSNSAVTGVSGDMTVATVIDKDNFTVLTPNQQTSDLNNAGKNWHMGTSFHKSPWRKTDLGLIPSVTEVHSFATIDNNGFAMGYHQGDVAPREVGLFYFPDAFNSPSNYVRRQIPSEYEPDASEPCIKYYDGVLYLITRGTRGDRLGSSLHRSRDIGQTWESLRFPHNVHHTTLPFAKVGDDLIMFGSERAENEWEAGAPDDRYKASYPRTFYARLNVNNWNADDIEWVNITDQIYQGGIVNSGVGVGSVVVKDNYIYYMFGGEDHFNPWTYGDNSAKDPFKSDGHPSDLYCYKMKIGPDNRVSRDFRYGAVPNRAVPVFFDTNGVRTVPAPMEFTGDLGLGHVTIRASTSSNIRSEVLMEGEYGFIGKSIPTDNPAGQRIIFCGGEGTSSTTGAQITLYGANNTDSRRIVYNGDEHLFQSADVKPYNDNVTALGGPSNRFTTAYLGSNPIVTSNGERKTEPVVFDDAFLDAWGDVHYIMYQWLDAVQLKGNDARIHFGVIAQQIRDVFIAHGLMDENSTNCRYAVLCYDKYPRMTDTVFSHNEIVEHTDEEGNVTTTEEPVYTEVVIHEEGEEWGVRPDGIFFAEAAYQRRKLERIEARLSALEQK This sequence has been withdrawn from Uniprot. 82FAB75EDC68DAB6 q9fzw3_bpga1 gene 12 protein protein bpga1 Bacillus phage GA-1 Bacteriophage GA-1 MHRPPFNKLRTIDNLSAYKYHIDYLPTAMDESLTLLQKVNMLIYNVNQTNAITNDLAERWNEIIEWLNTEAISKEVEKILEKWLSDGTLADIITDAVLGDIEKIKLALAEFEQLKKDFDKLRYDVDSITQTSGNAIYQKLIMRPFFGTETEQIFSGAENAPQGMAYVEFKGKKYIFILSRVEGTTWTKAERHRITQFELTEDGSLTQPLTFTKPLELGHQGLSAMVDNDKIWLFAGYGYGDFENNGKGYTKIEWKGSNTDECDIYRYRLLGAHGSNERYNEYNHATPTISTDGRFIVLAVATTFEANTRYMLIFDRKQVERAENPMSVPALNIFQIYAAPYVGSHIVQDVACDGNYVYIYTSDVAPLGVKIITIMSMQGFVVGYYKVDGGLALYDSLTGDPRYGDAVQMEAEGLTIMGSDLLLLSTDVWQKDGQYTKRDKLVYKVYRGCATCEGEPINQGIQPLTSPASVHIRGTVHDVSFPYGDGFTVSQWDEQNNEIYPSLSYNGQSIFRIYDTRPDSNNELPMTLRNNKAPSGGWVEIRSGSTLEDGAGINMYNVTNSALGGRMRLYVTDPVTLESVYFQIYQNGAIVPSTDNLQNMGQXSNRMRNIYAGTGAINTSDERHKTDIAPISDKVLDAWEKVKFYQYKFKDAVDEKGEEARYHFGVIAQQIVKVFEDEGLSAFDYGLVGYDEWEATEDEYDSEGNLVEKGREAGNIYSIRPTECQWLEMACMRRKLERLS DIP protein Q9FZW3 original sequence version: 24 gene 12-1 4 6 unspecified role unspecified role unspecified role unspecified role C-terminal domain Region 622-740 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction endonf-1 2 5 unspecified role unspecified role unspecified role unspecified role Region 785-1064 Region 785-1064 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction endonf-2 3 5 unspecified role unspecified role unspecified role unspecified role Region 785-1064 Region 785-1064 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction gene 12-2 1 6 unspecified role unspecified role unspecified role unspecified role C-terminal domain Region 622-740 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction