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 The structure of Ca2+-loaded S100A2 at 1.3-A resolution. The structure of Ca2+-loaded S100A2 at 1.3-A resolution. FEBS J. (1742-464X) 2012 Koch M., Fritz G. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Koch M., Fritz G. FEBS J. (1742-464X) 2012 s10a2_human Protein S100-A2 S100 calcium-binding protein A2 CAN19 S100A2 S100L Protein S-100L protein protein human Homo sapiens Human MMCSSLEQALAVLVTTFHKYSCQEGDKFKLSKGEMKELLHKELPSFVGEKVDEEGLKKLMGSLDENSDQQVDFQEYAVFLALITVMCNDFFQGCPDRP 56D09548450142A9 s100a2-1 1 S100A2 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction mint f1 f2 f3 The final model of Ca2+-bound S100A2 consists of two protein chains (subunit A and B) each containing residues A2-A89 and B2-B91, four Ca2+ ions as well as 173 water molecules and two PEG 400 molecules. Using fully anisotropic displacement parameters in refinement resulted in a final Rcryst to 13.6% and Rfree to 16.8%, respectively Since S100A2-wt is prone to air oxidation [41, 74] a S100A2-C2S-C21S-C86S-C93S variant was used for crystallization experiments