{"global_stoichiometry": "", "ligstr": "", "uniprot_ac": "", "inchi": "", "reference": "Nature. 2007 May 24;447(7143):453-7. Epub  2007 Apr 29", "author": "Sawaya, M.R., Sambashivan, S., Nelson, R., Ivanova, M.I., Sievers, S.A., Apostol, M.I., Thompson, M.J., Balbirnie, M., Wiltzius, J.J., McFarlane, H.T., Madsen, A.O., Riekel, C., Eisenberg, D.", "type": "Fibril", "ligand_id": "", "species": "", "method": "X-RAY DIFFRACTION", "keyword": "NNQQ peptide derived from Yeast Prion Sup35", "gene_names": "", "chain_id": "", "ligand_mw": "", "inchi_key": "", "secondary_structure": "NNQQ#CCCC", "amyloid_non_amyloid": "Amyloid", "length": "4", "remarks": "Structure of NNQQ Peptide from Yeast Prion SUP35", "protein_name": "Yeast Prion SUP35", "peptide_protein_sequence": "chain-ID A: NNQQ", "ligand_name": "", "ligand_smiles": "", "pdb_id": "2OLX", "ec_number": "", "pdb_classification": "PROTEIN FIBRIL", "mutation_s_field": "No", "ligand_formula": "", "r_value_free": "0.235", "alternative_name": "", "description": "Amyloid fibrils formed from different proteins, each associated with a particular disease, contain a common cross-Beta spine. Structures of microcrystals all reveal steric zippers, but with variations that expand the range of atomic architectures for amyloid-like fibrils and offer an atomic-level hypothesis for the basis of prion strains.", "resolution": "1.42", "pmid": "17468747", "entry": "S-0159"}