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 mihai-2013-1 Mechanism of Rab1b deactivation by the Legionella pneumophila GAP LepB. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Mihai Gazdag E., Streller A., Haneburger I., Hilbi H., Vetter I.R., Goody R.S., Itzen A. aymelt.itzen@tum.de EMBO Rep. (1469-221X) 2013 Only protein-protein interactions imex curation q5zsm7_legph lepB lpg2490 protein protein legph Legionella pneumophila subsp. pneumophila MLIYQGKEIVRFKEKTGGKNKSDVDGFYKDNDGGKFFIKKPGDPRELFTELFAGLLLKEFMKRGLIDESYFPSLICADVIQFEDKSYGLIQPLVSFDELHKVIGTSSGDGKDRNTLKETLFGPGYYAGITKQNKYFGLSMALMFSLLLGAHSVHSGNIVVLNGEEKEKSKQFGRIDWGDAFRYFAHPNNNDNLLYAYENRGWFNYKSLTKDYFLNYKKINGLFPAMAEKARQLQSKLNPELLVKIVTSALKNIPADLIDEKTKIQLAAYMCMDSFKEATFGTEGNCKDFAIAMATLLENRLGKIAVLKDMSPLSNPEELYQSILELKPLTLLMTSSTSFSETINQWADILKTTDMEKFSFDSNPINLLELVKQFNLYVDELAITCEANNVWAKERIDSTPNLFALYDNSGGEAIHGHAFVPYYKESIVLRRLFTVDPNTFNLSRFAAFEGPCQLYCKEHKDSAWVKIQTLLTLGNGIINTLKIIKQAQAFGIDEAVTENLKALKEQFIAFQLAEADIKESLKAPSFAEPLPNKESEFFYPIDEKALAKMNGYQLATICLEELNSPKPSPLIERILSNKKFWKRINSAFESGVFKGRTDDPAGKIAKIREWHQLLQISGKKTAGQIDELQKIVISLQSKIKRQTIEFEELEATLIQIKEKYQLLEKMAEQSEHEKSSAQSIIRSLNLELSQLKLQLQEQEKLQFQLKELKEKIHEQTTLSKRLGEELQTQKKTNTHQEETIQRITKEKSLADSSLESLRKELHELAKKERSLHKTLEEKQLQVQQLEEQLAEKEKENLALKKADKQSQHEKSLDKSAIESLTSELNQLKLELQKQETLQLQLKSLRKQIQEQTLVVEGLKEELQKQKKSNTHQEETIERITKEKSLADSALESLRKEMYELTRKNEENQLKLTKQVHSLSEQLEEKQLQIREFEKQLQEKEKRVEQSEKGKASAKRTVASLREQVSNLKLQLQQLGEVIQEKEKGSSLISQQSKQIIALQEIIEDQKRQLEELKIKIQELVSANQELGKQNQSLSKENLHNKNTVEDLKKKLNELNVQLEQLHQSSNEKEQTIRKLREELIKKDSSLKQNEEMQLAQKHLQEEIDRLQKEIKQQQLNTNQLESIIAQSKEAEKRYQQALQQKKGIYFARMERVSPIYLQIQQIEQKAKELEERRETEASTAAKTLATKLRLEIKNYLDNNESDEKSALNSFKINAKRHIENSKETLNQHREEWKYLLANVTLGVFLLGIGYLAAILINKATTGNYTFFSQTNSGKKLDALEKAISSTHSETLVYG rab1b_human Ras-related protein Rab-1B RAB1B protein protein human Homo sapiens Human MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTITSSYYRGAHGIIVVYDVTDQESYANVKQWLQEIDRYASENVNKLLVGNKSDLTTKKVVDNTTAKEFADSLGIPFLETSAKNATNVEQAFMTMAAEIKKRMGPGAASGGERPNLKIDSTPVKPAGGGCC lepb 1386776 n/a LepB 1386777 unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) Stoichiometry: 3.0 direct interaction direct interaction false false false table 1 fig 1 Rworking = 0.2 Rfree = 0.24 2.8A lepb-rab1b 1386776 n/a LepB 1386777 unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) n/a Rab1b 1386778 unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) 1386786 1386784 direct interaction direct interaction false false false table 1 fig 2 fig 4 2.7A R-Value: 0.219 R-Free: 0.249