IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ High resolution NMR solution structure of the leucine zipper domain of the c-Jun homodimer. High resolution NMR solution structure of the leucine zipper domain of the c-Jun homodimer. The Journal of biological chemistry 1996 imex curation Junius FK., O'Donoghue SI., Nilges M., Weiss AS., King GF. King@biochem.usyd.edu.au 04-05-20: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Junius FK., O'Donoghue SI., Nilges M., Weiss AS., King GF. King@biochem.usyd.edu.au Accepted 2020-MAR-16 AT 10:37 GMT AT 10:37 GMT by PPORRAS The Journal of biological chemistry 1996 Only protein-protein interactions imex curation imex curation jun_human Transcription factor AP-1 JUN Activator protein 1 Proto-oncogene c-Jun V-jun avian sarcoma virus 17 oncogene homolog p39 protein protein human Homo sapiens Human MTAKMETTFYDDALNASFLPSESGPYGYSNPKILKQSMTLNLADPVGSLKPHLRAKNSDLLTSPDVGLLKLASPELERLIIQSSNGHITTTPTPTQFLCPKNVTDEQEGFAEGFVRALAELHSQNTLPSVTSAAQPVNGAGMVAPAVASVAGGSGSGGFSASLHSEPPVYANLSNFNPGALSSGGGAPSYGAAGLAFPAQPQQQQQPPHHLPQQMPVQHPRLQALKEEPQTVPEMPGETPPLSPIDMESQERIKAERKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNHVNSGCQLMLTQQLQTF DIP protein P05412 original sequence version: 119 DIP protein P05412 original sequence version: 114 DIP protein P05412 original sequence version: 185 DIP protein P05412 original sequence version: 145 DIP protein P05412 original sequence version: 202 DIP protein P05412 original sequence version: 206 DIP protein P05412 original sequence version: 163 DIP protein P05412 original sequence version: 175 DIP protein P05412 original sequence version: 189 DIP protein P05412 original sequence version: 169 0695E23AC4D33561 jun-1 1 2 unspecified role unspecified role neutral component neutral component purified purified N-terminal AcCGG tag disulfide crosslinked residues disulfide crosslinked residues n-term range n-terminal range n-term range n-term range n-terminal range n-term range This is an N-terminal addition to covalently link the subunits of the homodimer through the cysteins for structure determination purposes (as described in Experimental procedures and Fig.1A). Leucine zipper domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 15N radiolabelled 15n label 15n label 15N N15 15N N15 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined P05412:p.His315Tyr mutation mutation certain certain sequence position certain certain certain sequence position certain H Y Tue Jun 30 19:57:11 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.His315Tyr' chemical synthesis Chemical synthesis (Chemical synthesis) 2 unspecified role unspecified role neutral component neutral component purified purified N-terminal AcCGG tag disulfide crosslinked residues disulfide crosslinked residues n-term range n-terminal range n-term range n-term range n-terminal range n-term range This is an N-terminal addition to covalently link the subunits of the homodimer through the cysteins for structure determination purposes (as described in Experimental procedures and Fig.1A). Leucine zipper domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 15N radiolabelled 15n label 15n label 15N N15 15N N15 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined P05412:p.His315Tyr mutation mutation certain certain sequence position certain certain certain sequence position certain H Y Tue Jun 30 18:07:31 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.His315Tyr' chemical synthesis Chemical synthesis (Chemical synthesis) 5 10 6 11 direct interaction direct interaction Fig. 2 The authors state in the "Experimental procedures" section that the monomers were covalently linked via a disulfide bond formed between the cysteine residues located in the N-terminal linker regions(shown in reverse type in Fig. 1A of the publication). This is captured in the cross linker annotation at the N-terminal region of the monomers.