{"reference": "Proc Natl Acad Sci U S A. 2014 Jan 7;111(1):197-201.", "alternative_name": "", "entry": "S-0346", "gene_names": "", "remarks": "DSVISLS segment 101-107 from Human Superoxide Dismutase", "secondary_structure": "DSVISLS#CCCCCCC", "chain_id": "A", "inchi": "InChI=1S/Zn/q+2", "amyloid_non_amyloid": "Amyloid", "pmid": "24344300", "ligand_smiles": "[Zn+2]", "keyword": "DSVISLS segment from Superoxide dismutase [Cu-Zn]", "peptide_protein_sequence": "chain-ID A: DSVISLS", "uniprot_ac": "P00441", "protein_name": "Superoxide dismutase [Cu-Zn]", "r_value_free": "0.228", "mutation_s_field": "No", "ligand_mw": "65.41", "pdb_id": "4NIN", "inchi_key": "PTFCDOFLOPIGGS-UHFFFAOYSA-N", "ec_number": "", "pdb_classification": "PROTEIN FIBRIL", "type": "Fibril", "author": "Ivanova, M.I., Sievers, S.A., Guenther, E.L., Johnson, L.M., Winkler, D.D., Galaleldeen, A., Sawaya, M.R., Hart, P.J., Eisenberg, D.S.", "species": "Homo sapiens", "ligand_id": "ZN", "method": "X-RAY DIFFRACTION", "ligand_name": "ZINC ION", "global_stoichiometry": "Homo 10-mer - A10 ", "resolution": "1.4", "ligand_formula": "Zn 2", "length": "7", "ligstr": "ZN:A:Zn 2:65.41:ZINC ION:[Zn+2]:InChI=1S/Zn/q+2:PTFCDOFLOPIGGS-UHFFFAOYSA-N", "description": "The atomic structures of two fibril-forming segments from the C terminus, (101)DSVISLS(107) and (147)GVIGIAQ(153), reveal tightly packed Beta-sheets with steric zipper interfaces characteristic of the amyloid state. Based on these structures, we conclude that both C-terminal segments are likely to form aggregates if available for interaction. Proline substitutions in (101)DSVISLS(107) and (147)GVIGIAQ(153) impaired nucleation and fibril growth of full-length protein, confirming that these segments participate in aggregate formation."}