{"global_stoichiometry": "", "ligstr": "", "uniprot_ac": "P02767", "inchi": "", "reference": "Proc Natl Acad Sci U S A. 2004 Jan 20;101(3):711-6. Epub  2004 Jan 8", "author": "Jaroniec, C.P., MacPhee, C.E., Bajaj, V.S., McMahon, M.T., Dobson, C.M., Griffin, R.G.", "type": "FIbril", "ligand_id": "", "species": "Rattus norvegicus", "method": "SOLID-STATE NMR", "keyword": "Transthyretin", "gene_names": "", "chain_id": "", "ligand_mw": "", "inchi_key": "", "secondary_structure": "YTIAALLSPYS#CCCCCCCCCCC", "amyloid_non_amyloid": "Amyloid", "length": "11", "remarks": "STRUCTURE OF TRANSTHYRETIN IN AMYLOID FIBRILS DETERMINED BY SOLID-STATE MAGIC ANGLE SPINNING NMR", "protein_name": "Transthyretin", "peptide_protein_sequence": "chain-ID A: YTIAALLSPYS", "ligand_name": "", "ligand_smiles": "", "pdb_id": "1RVS", "ec_number": "", "pdb_classification": "DE NOVO PROTEIN", "mutation_s_field": "No", "ligand_formula": "", "r_value_free": "", "alternative_name": "", "description": "High-resolution structure of a peptide fragment of the amyloidogenic protein transthyretin, TTR(105-115), in its fibrillar form, determined by magic angle spinning NMR spectroscopy. The structure resolves the backbone fold but also the precise conformation of the side chains. Nearly complete (13)C and (15)N resonance assignments for TTR(105-115) formed the basis for the extraction of a set of distance and dihedral angle restraints.", "resolution": "", "pmid": "14715898", "entry": "S-0060"}