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/ deaconescu-2012-6 Nucleotide excision repair (NER) machinery recruitment by the transcription-repair coupling factor involves unmasking of a conserved intramolecular interface. in vitro In vitro protease assay protease assay weight by comassie molecular weight estimation by coomasie staining weight by comassie Deaconescu A.M., Sevostyanova A., Artsimovitch I., Grigorieff N. niko@brandeis.edu,deaconescua@janelia.hhmi.org Proc. Natl. Acad. Sci. U.S.A. (0027-8424) 2012 Only protein-protein interactions imex curation mfd_ecoli Transcription-repair-coupling factor mfd b1114 JW1100 protein protein ecoli Escherichia coli (strain K12) MPEQYRYTLPVKAGEQRLLGELTGAACATLVAEIAERHAGPVVLIAPDMQNALRLHDEISQFTDQMVMNLADWETLPYDSFSPHQDIISSRLSTLYQLPTMQRGVLIVPVNTLMQRVCPHSFLHGHALVMKKGQRLSRDALRTQLDSAGYRHVDQVMEHGEYATRGALLDLFPMGSELPYRLDFFDDEIDSLRVFDVDSQRTLEEVEAINLLPAHEFPTDKAAIELFRSQWRDTFEVKRDPEHIYQQVSKGTLPAGIEYWQPLFFSEPLPPLFSYFPANTLLVNTGDLETSAERFQADTLARFENRGVDPMRPLLPPQSLWLRVDELFSELKNWPRVQLKTEHLPTKAANANLGFQKLPDLAVQAQQKAPLDALRKFLETFDGPVVFSVESEGRREALGELLARIKIAPQRIMRLDEASDRGRYLMIGAAEHGFVDTVRNLALICESDLLGERVARRRQDSRRTINPDTLIRNLAELHIGQPVVHLEHGVGRYAGMTTLEAGGITGEYLMLTYANDAKLYVPVSSLHLISRYAGGAEENAPLHKLGGDAWSRARQKAAEKVRDVAAELLDIYAQRAAKEGFAFKHDREQYQLFCDSFPFETTPDQAQAINAVLSDMCQPLAMDRLVCGDVGFGKTEVAMRAAFLAVDNHKQVAVLVPTTLLAQQHYDNFRDRFANWPVRIEMISRFRSAKEQTQILAEVAEGKIDILIGTHKLLQSDVKFKDLGLLIVDEEHRFGVRHKERIKAMRANVDILTLTATPIPRTLNMAMSGMRDLSIIATPPARRLAVKTFVREYDSMVVREAILREILRGGQVYYLYNDVENIQKAAERLAELVPEARIAIGHGQMRERELERVMNDFHHQRFNVLVCTTIIETGIDIPTANTIIIERADHFGLAQLHQLRGRVGRSHHQAYAWLLTPHPKAMTTDAQKRLEAIASLEDLGAGFALATHDLEIRGAGELLGEEQSGSMETIGFSLYMELLENAVDALKAGREPSLEDLTSQQTEVELRMPSLLPDDFIPDVNTRLSFYKRIASAKTENELEEIKVELIDRFGLLPDPARTLLDIARLRQQAQKLGIRKLEGNEKGGVIEFAEKNHVNPAWLIGLLQKQPQHYRLDGPTRLKFIQDLSERKTRIEWVRQFMRELEENAIA a5pjb8_bovin CTRB1 LOC618826 protein protein bovin Bos taurus (Bovine) Bovine MALLWVVLGFFLFGSSFGCGVPAIDPVLSGLSRIVNGEDAVPGSWPWQVSLQTSSGFHFCGGSLISEDWVVTAAHCGVRKGHLVVAGVSDQGSEEEAGQVLRVAEVFEHPQWDLRAVRNDVALLKLAAPARLSAAVAPVCLPSADTSFPTGSLCTVTGWGKTRYNAFDTPDKLQQATLPILSNADCREFWGSKITDVMICAGASGISSCMGDSGGPLVCQKDGAWTLAGIVSWGSSRCSPFLPGVYARVTKFIPWILEVLEAN subc_bacli Subtilisin Carlsberg subC apr protein protein bacli Bacillus licheniformis MMRKKSFWLGMLTAFMLVFTMAFSDSASAAQPAKNVEKDYIVGFKSGVKTASVKKDIIKESGGKVDKQFRIINAAKAKLDKEALKEVKNDPDVAYVEEDHVAHALAQTVPYGIPLIKADKVQAQGFKGANVKVAVLDTGIQASHPDLNVVGGASFVAGEAYNTDGNGHGTHVAGTVAALDNTTGVLGVAPSVSLYAVKVLNSSGSGSYSGIVSGIEWATTNGMDVINMSLGGASGSTAMKQAVDNAYAKGVVVVAAAGNSGSSGNTNTIGYPAKYDSVIAVGAVDSNSNRASFSSVGAELEVMAPGAGVYSTYPTNTYATLNGTSMASPHVAGAAALILSKHPNLSASQVRNRLSSTATYLGSSFYYGKGLINVEAAAQ Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides mint mfd-subtilisin 1467666 n/a 1467673 enzyme enzyme neutral component neutral component bacli Bacillus licheniformis n/a 1467671 enzyme target enzyme target substrate substrate neutral component neutral component n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range false ecoli Escherichia coli (strain K12) protein cleavage protein cleavage false false false Fig. S3a mfd-chymotrypsin-1 1467666 n/a 1467671 enzyme target enzyme target substrate substrate neutral component neutral component n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range false ecoli Escherichia coli (strain K12) n/a 1467674 enzyme enzyme neutral component neutral component bovin Bos taurus (Bovine) Bovine protein cleavage protein cleavage false false false Fig. S3a MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it http://mint.bio.uniroma2.it/mint bode-1987-1 The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis. Structural analysis, subtilisin structure and interface geometry. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Bode W., Papamokos E., Musil D. Eur. J. Biochem. (0014-2956) 1987 derache-2012-1 Crystal structure of greglin, a novel non-classical Kazal inhibitor, in complex with subtilisin. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction experimental particp experimental participant identification experimental particp Derache C., Epinette C., Roussel A., Gabant G., Cadene M., Korkmaz B., Gauthier F., Kellenberger C. FEBS J. (1742-464X) 2012 spi_schgr Greglin protein protein desert locust Schistocerca gregaria Gryllus gregarius SEDDGSASPESQEMSYTELPCPSICPLIYAPVCVEDSNQDFYLFVNECEVRKCGCEAGFVYTFVPREMCKATTSLCPMQTKSS mint icic_hirme Eglin C protein protein medicinal leech Hirudo medicinalis TEFGSELKSFPEVVGKTVDQAREYFTLHYPQYDVYFLPEGSPVTLDLRYNRVRVFYNPGTNVVNHVPHVG mint Inhibits both elastase and cathepsin G subc_bacli Subtilisin Carlsberg subC apr protein protein bacli Bacillus licheniformis MMRKKSFWLGMLTAFMLVFTMAFSDSASAAQPAKNVEKDYIVGFKSGVKTASVKKDIIKESGGKVDKQFRIINAAKAKLDKEALKEVKNDPDVAYVEEDHVAHALAQTVPYGIPLIKADKVQAQGFKGANVKVAVLDTGIQASHPDLNVVGGASFVAGEAYNTDGNGHGTHVAGTVAALDNTTGVLGVAPSVSLYAVKVLNSSGSGSYSGIVSGIEWATTNGMDVINMSLGGASGSTAMKQAVDNAYAKGVVVVAAAGNSGSSGNTNTIGYPAKYDSVIAVGAVDSNSNRASFSSVGAELEVMAPGAGVYSTYPTNTYATLNGTSMASPHVAGAAALILSKHPNLSASQVRNRLSSTATYLGSSFYYGKGLINVEAAAQ Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides mint apr-icic-2 100910 icic_hirme 100911 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 subt_bacli 100912 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 direct interaction direct interaction false false false In the xray complex 1cse, P00780 is chain E and P01051 is chain I Resolution 1.200 mint apr-spi 1321426 spi_schgr Greglin 1321427 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified subt_bacli Subtilisin Carlsberg 100912 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction false false false mint t1 f1 sf6