{"global_stoichiometry": "Homo 12-mer - A12 ", "ligstr": "", "uniprot_ac": "P04156", "inchi": "", "reference": "J Biol Chem. 2010 Sep 24;285(39):29671-5.", "author": "Apostol, M.I., Sawaya, M.R., Cascio, D., Eisenberg, D.", "type": "Fibril", "ligand_id": "", "species": "Homo sapiens", "method": "X-RAY DIFFRACTION", "keyword": "Major prion protein", "gene_names": "", "chain_id": "", "ligand_mw": "", "inchi_key": "", "secondary_structure": "GYMLGS#CEEEEC&GYMLGS#CEEEEC", "amyloid_non_amyloid": "Amyloid", "length": "6", "remarks": "GYMLGS segment 127-132 from human prion with M129", "protein_name": "Major prion protein", "peptide_protein_sequence": "chain-ID A: GYMLGS; chain-ID B: GYMLGS", "ligand_name": "", "ligand_smiles": "", "pdb_id": "3NHC", "ec_number": "", "pdb_classification": "PROTEIN FIBRIL", "mutation_s_field": "M129", "ligand_formula": "", "r_value_free": "0.253", "alternative_name": "", "description": "\"They determined crystal structures of prion segments having either Met or Val at residue 129. These 6-residue segments of PrP centered on residue 129 are \"\"steric zippers,\"\" pairs of interacting Beta-sheets. Both structures of these \"\"homozygous steric zippers\"\" reveal direct intermolecular interactions between Met or Val in one sheet and the identical residue in the mating sheet.\"", "resolution": "1.57", "pmid": "20685658", "entry": "S-0274"}