DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB. Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Tanabe M., Nimigean CM., Iverson TM. Only protein-protein interactions ecolx Escherichia coli light scattering light scattering predetermined predetermined participant predetermined Tanabe M., Nimigean CM., Iverson TM. DIP original experiment: DIP-216397X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB. Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB. Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Tanabe M., Nimigean CM., Iverson TM. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Tanabe M., Nimigean CM., Iverson TM. DIP original experiment: DIP-216395X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB. Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB. Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Tanabe M., Nimigean CM., Iverson TM. 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 Tanabe M., Nimigean CM., Iverson TM. DIP original experiment: DIP-216398X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB. Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB. Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Tanabe M., Nimigean CM., Iverson TM. 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 Tanabe M., Nimigean CM., Iverson TM. DIP original experiment: DIP-216396X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB. tlr2_human Toll-like receptor 2 Toll/interleukin-1 receptor-like protein 4 TLR2 TIL4 protein protein human Homo sapiens Human MPHTLWMVWVLGVIISLSKEESSNQASLSCDRNGICKGSSGSLNSIPSGLTEAVKSLDLSNNRITYISNSDLQRCVNLQALVLTSNGINTIEEDSFSSLGSLEHLDLSYNYLSNLSSSWFKPLSSLTFLNLLGNPYKTLGETSLFSHLTKLQILRVGNMDTFTKIQRKDFAGLTFLEELEIDASDLQSYEPKSLKSIQNVSHLILHMKQHILLLEIFVDVTSSVECLELRDTDLDTFHFSELSTGETNSLIKKFTFRNVKITDESLFQVMKLLNQISGLLELEFDDCTLNGVGNFRASDNDRVIDPGKVETLTIRRLHIPRFYLFYDLSTLYSLTERVKRITVENSKVFLVPCLLSQHLKSLEYLDLSENLMVEEYLKNSACEDAWPSLQTLILRQNHLASLEKTGETLLTLKNLTNIDISKNSFHSMPETCQWPEKMKYLNLSSTRIHSVTGCIPKTLEILDVSNNNLNLFSLNLPQLKELYISRNKLMTLPDASLLPMLLVLKISRNAITTFSKEQLDSFHTLKTLEAGGNNFICSCEFLSFTQEQQALAKVLIDWPANYLCDSPSHVRGQQVQDVRLSVSECHRTALVSGMCCALFLLILLTGVLCHRFHGLWYMKMMWAWLQAKRKPRKAPSRNICYDAFVSYSERDAYWVENLMVQELENFNPPFKLCLHKRDFIPGKWIIDNIIDSIEKSHKTVFVLSENFVKSEWCKYELDFSHFRLFDENNDAAILILLEPIEKKAIPQRFCKLRKIMNTKTYLEWPMDEAQREGFWVNLRAAIKS DIP protein O60603 original sequence version: 92 DIP protein O60603 original sequence version: 114 7DBE6B24CF1FAF8B q9z3b6_neime porB protein protein neime Neisseria meningitidis EVSRVKNQGVKTKTATQIADFGSKIGFKGQEDLGNGMKAIWQLEQKASIAGTNSGWGNRQSFIGLKGGFGTVRVGNLNTVLKDSGDNVNAWESGSNTGDVLGLGTIGRVESREISVRYDSPVFAGFSGSVQYVPRDNANDKDKYTHKQSSRESYHAGLKYENAGFFGQYAGSFAKYADLKDNAERVAVGTTGAHPVKDYQVHRVVAGYDANDLYVSVAGQYEAAKNNDTNPATNGKKLEQTQVAATAAYRFGNVTPRVSYAHGFKAKVNGKKAARYQYDQVIVGADYDFSKRTSALVSVGWLKEGKGVNKTEKTASM DIP protein Q9Z3B6 original sequence version: 53 porb-1 3 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction porb-2 2 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction porb-tlr2-1 4 5 unspecified role unspecified role unspecified role unspecified role Ectodomain Region 19-588 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain picpa Pichia pastoris (Yeast) Yeast Pichia pastoris 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction porb-3 1 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction