IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ http://www.ebi.ac.uk/ abdurachim-2006-1 Detection of protein-protein interactions in the alkanesulfonate monooxygenase system from Escherichia coli. in vitro In vitro pull down pull down predetermined predetermined participant predetermined Abdurachim K., Ellis H.R. ellishr@auburn.edu J. Bacteriol. (0021-9193) 2006 Only protein-protein interactions imex curation abdurachim-2006-2 Detection of protein-protein interactions in the alkanesulfonate monooxygenase system from Escherichia coli. in vitro In vitro cd circular dichroism CD CD cd predetermined predetermined participant predetermined Abdurachim K., Ellis H.R. ellishr@auburn.edu J. Bacteriol. (0021-9193) 2006 Only protein-protein interactions imex curation abdurachim-2006-3 Detection of protein-protein interactions in the alkanesulfonate monooxygenase system from Escherichia coli. in vitro In vitro crosslink cross-linking study crosslink predetermined predetermined participant predetermined Abdurachim K., Ellis H.R. Crosslinking agent is ProFound Label Transfer Sulfo-SBED {sulfosuccinimidyl[2,6-(biotinamido)-2-(p-azidobenzamido)-hexanoamido]-ethyl-1,3′-dithiopropionate} Protein:Protein Interaction Agent (Pierce, Rockford, IL). ellishr@auburn.edu J. Bacteriol. (0021-9193) 2006 Only protein-protein interactions imex curation abdurachim-2006-4 Detection of protein-protein interactions in the alkanesulfonate monooxygenase system from Escherichia coli. in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Abdurachim K., Ellis H.R. FMN was first bound to SsuE before it was titrated with SsuD. ellishr@auburn.edu J. Bacteriol. (0021-9193) 2006 Only protein-protein interactions imex curation ssud_ecoli Alkanesulfonate monooxygenase Sulfate starvation-induced protein 6 ycbN FMNH2-dependent aliphatic sulfonate monooxygenase ssuD b0935 JW0918 protein protein ecoli Escherichia coli (strain K12) MSLNMFWFLPTHGDGHYLGTEEGSRPVDHGYLQQIAQAADRLGYTGVLIPTGRSCEDAWLVAASMIPVTQRLKFLVALRPSVTSPTVAARQAATLDRLSNGRALFNLVTGSDPQELAGDGVFLDHSERYEASAEFTQVWRRLLQRETVDFNGKHIHVRGAKLLFPAIQQPYPPLYFGGSSDVAQELAAEQVDLYLTWGEPPELVKEKIEQVRAKAAAHGRKIRFGIRLHVIVRETNDEAWQAAERLISHLDDETIAKAQAAFARTDSVGQQRMAALHNGKRDNLEISPNLWAGVGLVRGGAGTALVGDGPTVAARINEYAALGIDSFVLSGYPHLEEAYRVGELLFPLLDVAIPEIPQPQPLNPQGEAVANDFIPRKVAQS ssue_ecoli FMN reductase (NADPH) ycbP Sulfate starvation-induced protein 4 ssuE b0937 JW0920 FMN reductase protein protein ecoli Escherichia coli (strain K12) MRVITLAGSPRFPSRSSSLLEYAREKLNGLDVEVYHWNLQNFAPEDLLYARFDSPALKTFTEQLQQADGLIVATPVYKAAYSGALKTLLDLLPERALQGKVVLPLATGGTVAHLLAVDYALKPVLSALKAQEILHGVFADDSQVIDYHHRPQFTPNLQTRLDTALETFWQALHRRDVQVPDLLSLRGNAHA fmn FMN 1-deoxy-1-(7,8-dimethyl-2,4-dioxo-3,4-dihydrobenzo[g]pteridin-10(2H)-yl)-5-O-phosphono-D-ribitol Flavin mononucleotide FLAVIN MONONUCLEOTIDE FMN riboflavin 5'-(dihydrogen phosphate) riboflavin 5'-monophosphate riboflavin 5'-phosphate riboflavin monophosphate Riboflavin-5-phosphate riboflavine dihydrogen phosphate 1-deoxy-1-(7,8-dimethyl-2,4-dioxo-3,4-dihydrobenzo[g]pteridin-10(2H)-yl)-5-O-phosphono-D-ribitol small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) FVTCRASFADXXNN-SCRDCRAPSA-N ssud-ssue-1 1444426 n/a 1444430 unspecified role unspecified role bait bait c-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range false ecoli Escherichia coli (strain K12) n/a 1444431 unspecified role unspecified role prey prey ecoli Escherichia coli (strain K12) direct interaction direct interaction false false false Fig. 2 ssud-ssue-2 1444427 n/a 1444432 unspecified role unspecified role neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) n/a 1444431 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) direct interaction direct interaction false false false Fig. 4 The SsuD-His construct was not added as a participant because the spectrum did not change significantly when SsuD-His was added to the reaction. ssud-ssue-3 1444428 n/a 1444430 unspecified role unspecified role neutral component neutral component c-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range false ecoli Escherichia coli (strain K12) Stoichiometry: 1.0 n/a 1444431 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) Stoichiometry: 1.0 direct interaction direct interaction false false false Fig. 5b ssud-ssue-4 1444429 n/a 1444430 unspecified role unspecified role neutral component neutral component c-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range false ecoli Escherichia coli (strain K12) n/a 1444431 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) n/a 1444432 unspecified role unspecified role neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) direct interaction direct interaction false false false 1444429 Fig.s 6, 7