{"global_stoichiometry": "Monomer - A ", "ligstr": "", "uniprot_ac": "Q05876", "inchi": "", "reference": "Science. 2012 Apr 20;336(6079):362-6.", "author": "Neudecker, P., Robustelli, P., Cavalli, A., Walsh, P., Lundstrom, P., Zarrine-Afsar, A., Sharpe, S., Vendruscolo, M., Kay, L.E.", "type": "Protein", "ligand_id": "", "species": "Gallus gallus", "method": "SOLUTION NMR", "keyword": "Tyrosine-protein kinase Fyn", "gene_names": "FYN", "chain_id": "", "ligand_mw": "", "inchi_key": "", "secondary_structure": "GAMVQISTLFEALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEVRSLTTGETGYIPSPYLAPVDR#CCCCCCCCEEECSSCBCCSSSSBCCBCTTCEEEEEECTTSSEEEEEESSSCCEEEEEGGGTCCCCC", "amyloid_non_amyloid": "Amyloid", "length": "66", "remarks": "Folding Intermediate of the Fyn SH3 A39V/N53P/V55L from NMR Relaxation Dispersion Experiments", "protein_name": "Tyrosine-protein kinase Fyn", "peptide_protein_sequence": "chain-ID A: GAMVQISTLFEALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEVRSLTTGETGYIPSPYLAPVDR", "ligand_name": "", "ligand_smiles": "", "pdb_id": "2L2P", "ec_number": "2.7.10.2", "pdb_classification": "TRANSFERASE", "mutation_s_field": "A39V/N53P/V55L", "ligand_formula": "", "r_value_free": "", "alternative_name": "Proto-oncogene c-Fyn, p59-Fyn", "description": "The structure of a low-populated, on-pathway folding intermediate of the A39V/N53P/V55L (A, Ala; V, Val; N, Asn; P, Pro; L, Leu) Fyn SH3 domain. The carboxyl terminus remains disordered in this intermediate, thereby exposing the aggregation-prone amino-terminal Beta strand. Accordingly, mutants lacking the carboxyl terminus and thus mimicking the intermediate fail to safeguard the folding route and spontaneously form fibrillar aggregates. The structure provides a detailed characterization of the non-native interactions stabilizing an aggregation-prone intermediate under native conditions and insight into how such an intermediate can derail folding and initiate fibrillation.", "resolution": "", "pmid": "22517863", "entry": "S-0117"}