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 ortiz-2015-1 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Ortiz C., Kureisaite-Ciziene D., Schmitz F., McLaughlin SH., Vicente M., Löwe J. jyl@mrc-lmb.cam.ac.uk FEBS letters 2015 Only protein-protein interactions imex curation imex curation ortiz-2015-2 in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Ortiz C., Kureisaite-Ciziene D., Schmitz F., McLaughlin SH., Vicente M., Löwe J. jyl@mrc-lmb.cam.ac.uk FEBS letters 2015 Only protein-protein interactions imex curation imex curation ortiz-2015-3 in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Ortiz C., Kureisaite-Ciziene D., Schmitz F., McLaughlin SH., Vicente M., Löwe J. jyl@mrc-lmb.cam.ac.uk FEBS letters 2015 Only protein-protein interactions imex curation imex curation zapc_ecoli Cell division protein ZapC b0946 JW5125 zapC ycbW FtsZ-associated protein C Z-ring-associated protein C protein protein ecoli Escherichia coli (strain K12) MRIKPDDNWRWYYDEEHDRMMLDLANGMLFRSRFARKMLTPDAFSPAGFCVDDAALYFSFEEKCRDFNLSKEQKAELVLNALVAIRYLKPQMPKSWHFVSHGEMWVPMPGDAACVWLSDTHEQVNLLVVESGENAALCLLAQPCVVIAGRAMQLGDAIKIMNDRLKPQVNVDSFSLEQAV ftsz_ecoli Cell division protein FtsZ ftsZ sfiB sulB b0095 JW0093 protein protein ecoli Escherichia coli (strain K12) MFEPMELTNDAVIKVIGVGGGGGNAVEHMVRERIEGVEFFAVNTDAQALRKTAVGQTIQIGSGITKGLGAGANPEVGRNAADEDRDALRAALEGADMVFIAAGMGGGTGTGAAPVVAEVAKDLGILTVAVVTKPFNFEGKKRMAFAEQGITELSKHVDSLITIPNDKLLKVLGRGISLLDAFGAANDVLKGAVQGIAELITRPGLMNVDFADVRTVMSEMGYAMMGSGVASGEDRAEEAAEMAISSPLLEDIDLSGARGVLVNITAGFDLRLDEFETVGNTIRAFASDNATVVIGTSLDPDMNDELRVTVVATGIGMDKRPEITLVTNKQVQQPVMDRYQQHGMAPLTQEQKPVAKVVNDNAPQTAKEPDYLDIPAFLRKQAD zapc-1 1894445 n/a 1894448 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 false direct interaction direct interaction false false false t1 f2c Phasing, automated and manual model building, and refinement produced an atomic model of very good quality, resolving residues 1–168 of ZapC, with two molecules in the asymmetric unit, at 2.9 Å resolution (Table 1). zapc-3 1894446 N/A 1894449 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 false n/a 1894448 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 false direct interaction direct interaction false false false 1894446 f2b zapc-2 1894447 n/a 1894448 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 false direct interaction direct interaction false false false f2d In order to clarify the oligomeric state of the protein in solution, we performed analytical ultracentrifugation (Fig. 2D), finding that ZapC runs as three species. The two major species corresponded very well with theoretical values for ZapC monomers and dimers.