DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Solution structure of the A4 domain of factor XI sheds light on the mechanism of zymogen activation. Solution structure of the A4 domain of factor XI sheds light on the mechanism of zymogen activation. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Samuel D., Cheng H., Riley PW., Canutescu AA., Nagaswami C., Weisel JW., Bu Z., Walsh PN., Roder H. Only protein-protein interactions human Homo sapiens Human saxs x ray scattering saxs predetermined predetermined participant predetermined Samuel D., Cheng H., Riley PW., Canutescu AA., Nagaswami C., Weisel JW., Bu Z., Walsh PN., Roder H. DIP original experiment: DIP-261804X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Solution structure of the A4 domain of factor XI sheds light on the mechanism of zymogen activation. Solution structure of the A4 domain of factor XI sheds light on the mechanism of zymogen activation. Solution structure of the A4 domain of factor XI sheds light on the mechanism of zymogen activation. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Samuel D., Cheng H., Riley PW., Canutescu AA., Nagaswami C., Weisel JW., Bu Z., Walsh PN., Roder H. Only protein-protein interactions human Homo sapiens Human tem transmission electron microscopy tem predetermined predetermined participant predetermined Samuel D., Cheng H., Riley PW., Canutescu AA., Nagaswami C., Weisel JW., Bu Z., Walsh PN., Roder H. DIP original experiment: DIP-261803X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Solution structure of the A4 domain of factor XI sheds light on the mechanism of zymogen activation. Solution structure of the A4 domain of factor XI sheds light on the mechanism of zymogen activation. Solution structure of the A4 domain of factor XI sheds light on the mechanism of zymogen activation. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Samuel D., Cheng H., Riley PW., Canutescu AA., Nagaswami C., Weisel JW., Bu Z., Walsh PN., Roder H. Only protein-protein interactions ecolx Escherichia coli nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Samuel D., Cheng H., Riley PW., Canutescu AA., Nagaswami C., Weisel JW., Bu Z., Walsh PN., Roder H. DIP original experiment: DIP-261802X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Solution structure of the A4 domain of factor XI sheds light on the mechanism of zymogen activation. Solution structure of the A4 domain of factor XI sheds light on the mechanism of zymogen activation. Solution structure of the A4 domain of factor XI sheds light on the mechanism of zymogen activation. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Samuel D., Cheng H., Riley PW., Canutescu AA., Nagaswami C., Weisel JW., Bu Z., Walsh PN., Roder H. Only protein-protein interactions human Homo sapiens Human dls dynamic light scattering dls predetermined predetermined participant predetermined Samuel D., Cheng H., Riley PW., Canutescu AA., Nagaswami C., Weisel JW., Bu Z., Walsh PN., Roder H. DIP original experiment: DIP-261805X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Solution structure of the A4 domain of factor XI sheds light on the mechanism of zymogen activation. p03951-1 Coagulation factor XI F11 Plasma thromboplastin antecedent protein protein human Homo sapiens Human MIFLYQVVHFILFTSVSGECVTQLLKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFTFTAESPSEDPTRWFTCVLKDSVTETLPRVNRTAAISGYSFKQCSHQISACNKDIYVDLDMKGINYNSSVAKSAQECQERCTDDVHCHFFTYATRQFPSLEHRNICLLKHTQTGTPTRITKLDKVVSGFSLKSCALSNLACIRDIFPNTVFADSNIDSVMAPDAFVCGRICTHHPGCLFFTFFSQEWPKESQRNLCLLKTSESGLPSTRIKKSKALSGFSLQSCRHSIPVFCHSSFYHDTDFLGEELDIVAAKSHEACQKLCTNAVRCQFFTYTPAQASCNEGKGKCYLKLSSNGSPTKILHGRGGISGYTLRLCKMDNECTTKIKPRIVGGTASVRGEWPWQVTLHTTSPTQRHLCGGSIIGNQWILTAAHCFYGVESPKILRVYSGILNQSEIKEDTSFFGVQEIIIHDQYKMAESGYDIALLKLETTVNYTDSQRPICLPSKGDRNVIYTDCWVTGWGYRKLRDKIQNTLQKAKIPLVTNEECQKRYRGHKITHKMICAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWILEKTQAV DIP protein P03951-1 original sequence version: 96 DIP protein P03951-1 original sequence version: 179 DIP protein P03951 original sequence version: 179 f11-2 3 5 unspecified role unspecified role unspecified role unspecified role Region 290-379 Region 290-379 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction f11-3 2 5 unspecified role unspecified role unspecified role unspecified role human Homo sapiens Human direct interaction direct interaction f11-4 1 5 unspecified role unspecified role unspecified role unspecified role human Homo sapiens Human direct interaction direct interaction f11-5 4 5 unspecified role unspecified role unspecified role unspecified role human Homo sapiens Human direct interaction direct interaction