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 structural and energetic basis for high selectivity in a high-affinity protein-protein interaction. The structural and energetic basis for high selectivity in a high-affinity protein-protein interaction. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Meenan NA., Sharma A., Fleishman SJ., Macdonald CJ., Morel B., Boetzel R., Moore GR., Baker D., Kleanthous C. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Meenan NA., Sharma A., Fleishman SJ., Macdonald CJ., Morel B., Boetzel R., Moore GR., Baker D., Kleanthous C. DIP original experiment: DIP-219797X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx The structural and energetic basis for high selectivity in a high-affinity protein-protein interaction. The structural and energetic basis for high selectivity in a high-affinity protein-protein interaction. The structural and energetic basis for high selectivity in a high-affinity protein-protein interaction. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Meenan NA., Sharma A., Fleishman SJ., Macdonald CJ., Morel B., Boetzel R., Moore GR., Baker D., Kleanthous C. 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 Meenan NA., Sharma A., Fleishman SJ., Macdonald CJ., Morel B., Boetzel R., Moore GR., Baker D., Kleanthous C. DIP original experiment: DIP-219798X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx The structural and energetic basis for high selectivity in a high-affinity protein-protein interaction. The structural and energetic basis for high selectivity in a high-affinity protein-protein interaction. The structural and energetic basis for high selectivity in a high-affinity protein-protein interaction. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Meenan NA., Sharma A., Fleishman SJ., Macdonald CJ., Morel B., Boetzel R., Moore GR., Baker D., Kleanthous C. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Meenan NA., Sharma A., Fleishman SJ., Macdonald CJ., Morel B., Boetzel R., Moore GR., Baker D., Kleanthous C. DIP original experiment: DIP-219796X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx The structural and energetic basis for high selectivity in a high-affinity protein-protein interaction. The structural and energetic basis for high selectivity in a high-affinity protein-protein interaction. The structural and energetic basis for high selectivity in a high-affinity protein-protein interaction. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Meenan NA., Sharma A., Fleishman SJ., Macdonald CJ., Morel B., Boetzel R., Moore GR., Baker D., Kleanthous C. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink predetermined predetermined participant predetermined Meenan NA., Sharma A., Fleishman SJ., Macdonald CJ., Morel B., Boetzel R., Moore GR., Baker D., Kleanthous C. DIP original experiment: DIP-219799X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx The structural and energetic basis for high selectivity in a high-affinity protein-protein interaction. cea9_ecolx Colicin-E9 col cei protein protein ecolx Escherichia coli MSGGDGRGHNTGAHSTSGNINGGPTGIGVSGGASDGSGWSSENNPWGGGSGSGIHWGGGSGRGNGGGNGNSGGGSGTGGNLSAVAAPVAFGFPALSTPGAGGLAVSISASELSAAIAGIIAKLKKVNLKFTPFGVVLSSLIPSEIAKDDPNMMSKIVTSLPADDITESPVSSLPLDKATVNVNVRVVDDVKDERQNISVVSGVPMSVPVVDAKPTERPGVFTASIPGAPVLNISVNDSTPAVQTLSPGVTNNTDKDVRPAGFTQGGNTRDAVIRFPKDSGHNAVYVSVSDVLSPDQVKQRQDEENRRQQEWDATHPVEAAERNYERARAELNQANEDVARNQERQAKAVQVYNSRKSELDAANKTLADAIAEIKQFNRFAHDPMAGGHRMWQMAGLKAQRAQTDVNNKQAAFDAAAKEKSDADAALSAAQERRKQKENKEKDAKDKLDKESKRNKPGKATGKGKPVGDKWLDDAGKDSGAPIPDRIADKLRDKEFKSFDDFRKAVWEEVSKDPELSKNLNPSNKSSVSKGYSPFTPKNQQVGGRKVYELHHDKPISQGGEVYDMDNIRVTTPKRHIDIHRGK DIP protein P09883 original sequence version: 99 DIP protein P09883 original sequence version: 76 DIP protein P09883 original sequence version: 81 DIP protein P09883 original sequence version: 84 DIP protein P09883 original sequence version: 86 47A71B57B45AFDD9 imm2_ecolx Colicin-E2 immunity protein imm ceiB ImmE2 Microcin-E2 immunity protein protein protein ecolx Escherichia coli MELKHSISDYTEAEFLEFVKKICRAEGATEEDDNKLVREFERLTEHPDGSDLIYYPRDDREDSPEGIVKEIKEWRAANGKSGFKQG DIP protein P04482 original sequence version: 52 col-imm-4 3 5 unspecified role unspecified role unspecified role unspecified role DNase domain Region 450-582 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction col-imm-5 4 5 unspecified role unspecified role unspecified role unspecified role DNase domain Region 450-582 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain P09883:p.Gly543Cys G543C mutation mutation certain certain sequence position certain certain certain sequence position certain G C This feature has been corrected as a result of our quality control procedures. The original label was 'G543C'. Wed May 02 16:21:39 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly543cys' Tue Jun 30 17:48:43 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly543Cys' ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role P04482:p.Glu31Cys E31C mutation mutation certain certain sequence position certain certain certain sequence position certain E C This feature has been corrected as a result of our quality control procedures. The original label was 'E31C'. Wed May 02 14:39:16 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu31cys' Tue Jun 30 19:38:55 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu31Cys' ecolx Escherichia coli direct interaction direct interaction col-imm-6 1 5 unspecified role unspecified role unspecified role unspecified role DNase domain Region 450-582 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction col-imm-7 2 5 unspecified role unspecified role unspecified role unspecified role DNase domain Region 450-582 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction