{"method": "X-RAY DIFFRACTION", "mutation_s_field": "No", "ec_number": "", "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.", "ligstr": "", "pmid": "24344300", "remarks": "GVTGIAQ segment 147-153 from Human Superoxide Dismutase with I149T mutation associated with a familial form of amyotrophic lateral sclerosis", "amyloid_non_amyloid": "Amyloid", "type": "Fibril", "inchi": "", "resolution": "1.3", "species": "Homo sapiens", "secondary_structure": "GVTGIAQ#CCCCCCC", "chain_id": "", "gene_names": "", "r_value_free": "0.233", "pdb_id": "4NIO", "reference": "Proc Natl Acad Sci U S A. 2014 Jan 7;111(1):197-201.", "keyword": "GVTGIAQ segment from Superoxide dismutase [Cu-Zn]", "protein_name": "Superoxide dismutase [Cu-Zn]", "ligand_formula": "", "peptide_protein_sequence": "chain-ID A: GVTGIAQ", "entry": "S-0347", "length": "7", "uniprot_ac": "P00441", "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.", "ligand_smiles": "", "ligand_mw": "", "alternative_name": "", "ligand_name": "", "pdb_classification": "PROTEIN FIBRIL", "global_stoichiometry": "Homo 10-mer - A10 ", "inchi_key": "", "ligand_id": ""}