{"resolution": "1.7", "ligand_mw": "", "secondary_structure": "MMHFGN#CEEECC&MMHFGN#CEEECC", "inchi": "", "method": "X-RAY DIFFRACTION", "ec_number": "", "uniprot_ac": "P04273", "remarks": "MMHFGN segment 138-143 from Syrian Hamster prion", "description": "Prion represents a unique class of pathogens devoid of nucleic acid. The deadly diseases transmitted by it between members of one species and, in certain instances, to members of other species present a public health concern. Here we present three X-ray atomic structures of the same segment from human, mouse, and hamster PrP, which is critical for forming amyloid and confers species specificity in PrP seeding experiments. The structures reveal that different sequences encode different steric zippers and suggest that the degree of dissimilarity of these zipper structures gives rise to transmission barriers in prion disease,", "type": "Fibril", "ligand_smiles": "", "chain_id": "", "species": "Mesocricetus auratus", "keyword": "Major prion protein", "ligstr": "", "pmid": "21323366", "mutation_s_field": "No", "author": "Apostol, M.I., Wiltzius, J.J., Sawaya, M.R., Cascio, D., Eisenberg, D.", "pdb_id": "3NVE", "amyloid_non_amyloid": "Amyloid", "inchi_key": "", "ligand_name": "", "ligand_formula": "", "ligand_id": "", "r_value_free": "0.26899999", "protein_name": "Major prion protein", "gene_names": "", "global_stoichiometry": "Homo 12-mer - A12 ", "alternative_name": "", "peptide_protein_sequence": "chain-ID A: MMHFGN; chain-ID B: MMHFGN", "pdb_classification": "PROTEIN FIBRIL", "reference": "Biochemistry. 2011 Apr 5;50(13):2456-63.", "length": "6", "entry": "S-0276"}