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 Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper. Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper. J. Mol. Biol. (0022-2836) 1998 Lavigne P., Crump MP., Gagné SM., Hodges RS., Kay CM., Sykes BD. Virus - Publications including interactions involving viral proteins no in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Lavigne P., Crump MP., Gagné SM., Hodges RS., Kay CM., Sykes BD. Virus - Publications including interactions involving viral proteins no J. Mol. Biol. (0022-2836) 1998 max_human Protein max MAX BHLHD4 Class D basic helix-loop-helix protein 4 Myc-associated factor X protein protein human Homo sapiens Human MSDNDDIEVESDEEQPRFQSAADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEAS DIP protein P61244 original sequence version: 132 DIP protein P61244 original sequence version: 128 DIP protein P61244 original sequence version: 150 DIP protein P61244 original sequence version: 120 EB10F3137727A56F myc_human Myc proto-oncogene protein BHLHE39 Transcription factor p64 MYC Proto-oncogene c-Myc Class E basic helix-loop-helix protein 39 protein protein human Homo sapiens Human MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENVKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNSCA DIP protein P01106 original sequence version: 195 DIP protein P01106 original sequence version: 196 DIP protein P01106 original sequence version: 148 DIP protein P01106-1 original sequence version: 161 DIP protein P01106 original sequence version: 182 DIP protein P01106 original sequence version: 197 DIP protein P01106-1 original sequence version: 208 DIP protein P01106 original sequence version: 121 DIP protein P01106-1 original sequence version: 144 DIP protein P01106 original sequence version: 144 ED5C028029A4C5D1 max-myc-1 1 2 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 3 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 direct interaction direct interaction In the xray complex 1a93, P01106 is chain A and P25912 is chain B Resolution homomint mint