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 anonymous-2014c-1 Expression from engineered Escherichia coli chromosome and crystallographic study of archaeal N,N′- diacetylchitobiose deacetylase in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined k-uegaki@aist.go.jp; nakamura-t@aist.go.jp 2014 imex curation Mine S., Niiyama M., Hashimoto W., Ikegami T., Koma D., Ohmoto T., Fukuda Y., Inoue T., Abe Y., Ueda T., Morita J., Uegaki K., Nakamura T. FEBS J. (1742-464X) Only protein-protein interactions o58092_pyrho AcnX domain-containing protein PH0354 protein protein pyrho Pyrococcus horikoshii MITLYLTKEEELALSGEYGPALQKAMEILVALGDLYGADRLIPIKSAQIAGVSYKNLGEAGLEFLRDLVEMGAKVSVYTTLNPPGIGNEDFMEKQEEIISLYREMGIEVTSTCTPYYGANLPKFGDHLAWSESSAVSFANSVLGARTNREGGPSSLAAAIVGKTPNYGLHLDENRKATHFVKVTFEPKNEVEYSLLGYRVGEIVENGIPYFSNLTPSLDELKALGASMAASGGVALYHVEKHTPEWRGAINDKVEKITIDSKEVEDVKERFNADWGEVDFILLGCPHASLKEVKNIAELLKMRGKPLRIPLYITISRSVKALADFLGYTEVIERYNGKLLQDVCLVVSPVKEWYSGVATNSGKAAFYFKSFGLNVKLESVEKIIMEAP mint q8u3r6_pyrfu AcnX domain-containing protein PF0390 protein protein pyrfu Pyrococcus furiosus MYLTKEEELALSGEYGPAIQKAMEILVALGDIYNADRLIPIKSAQIAGVSYKNIGDEGIEFLRDFVEAGAKVSVYTTLNPAGIGDEDFMEKQAEIIELYRKMGVEITSTCTPYYGPNLPKYGDHLAWSESSAVIFANSVLGARTNREGGPSSLAAAIVGKTPNYGLHLEENRKATHIIEVKDKLKSRTEYSLLGYKIGEIVENGVPYIRGIAPTTEDLKALGASMAASGGVGLYHVEGSTPEWRGAIVDKIEKIEIGRKDLEDVRQRFSVDWGDVDIILLGCPHASLREIKEIAELLRMRDKPLKIPLFITVSRGIKALADYLGYTEIIERYNGKLLPDVCLVVSPIKEWYSGVATDSGKAAFYLKSFGLKVLLDTTENIIMGAP o58092 1533432 n/a Ph-Dac 1533433 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 3.0 direct interaction direct interaction false false false f3 t1 In the crystal structure of Ph-Dac, the asymmetric unit contained three polypeptides correlated with a non-crystallographic three-fold axis. A symmetry operation generated an assembly of Ph-Dac with six molecules consisting of two trimers (Fig. 3A). o58092-1 1533432 n/a Pf-Dac 1533434 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction false false false t1 The asymmetric unit of the Pf-Dac crystal contained two polypeptides, which corresponded to chains A and D of Ph-Dac. The symmetry operation generated a hexameric assembly of two trimers, similar to that of Ph-Dac