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 Crystal structure of the bacteriophage P2 integrase catalytic domain. Crystal structure of the bacteriophage P2 integrase catalytic domain. FEBS letters 2015 imex curation Skaar K., Claesson M., Odegrip R., Högbom M., Haggård-Ljungquist E., Stenmark P. stenmark@dbb.su.se 19-Jan-2016: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Skaar K., Claesson M., Odegrip R., Högbom M., Haggård-Ljungquist E., Stenmark P. stenmark@dbb.su.se Accepted 2016-JAN-11 AT 13:12 GMT AT 13:12 GMT by MARTA FEBS letters 2015 Only protein-protein interactions imex curation imex curation vint_bpp2 Integrase int protein protein Bacteriophage P2 Enterobacteria phage P2 MAIKKLDDGRYEVDIRPTGRNGKRIRRKFDKKSEAVAFEKYTLYNHHNKEWLSKPTDKRRLSELTQIWWDLKGKHEEHGKSNLGKIEIFTKITNDPCAFQITKSLISQYCATRRSQGIKPSSINRDLTCISGMFTALIEAELFFGEHPIRGTKRLKEEKPETGYLTQEEIALLLAALDGDNKKIAILCLSTGARWGEAARLKAENIIHNRVTFVKTKTNKPRTVPISEAVAKMIADNKRGFLFPDADYPRFRRTMKAIKPDLPMGQATHALRHSFATHFMINGGSIITLQRILGHTRIEQTMVYAHFAPEYLQDAISLNPLRGGTEAESVHTVSTVE C6FC3F87FD6F79DD int-1 1 2 unspecified role unspecified role neutral component neutral component purified purified range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f2 t1 f3 The P2 Int45–337 construct used yielded crystals from which Xray diffraction data to 1.9 Å was collected (see Table 1). However, the collected data only revealed electron density corresponding to the C-terminal catalytic domain of P2 Int. The asymmetric unit contains, as judged by the electron density, the catalytic domain of P2 Int forming a dimer consisting of residues Thr162-Glu326 of one protomer (chain A), Gly163-Thr216 and Thr218-Val330 of the second protomer (chain B), see Fig. 2.