{"global_stoichiometry": "Homo 20-mer - A20 ", "ligstr": "", "uniprot_ac": "", "inchi": "", "reference": "Protein Sci. 2018 Jul;27(7):1295-1303.", "author": "Saelices, L., Sievers, S.A., Sawaya, M.R., Eisenberg, D.S.", "type": "Fibril", "ligand_id": "", "species": "Homo sapiens", "method": "X-RAY DIFFRACTION", "keyword": "THR-ILE-ALA-ALA-LEU-LEU-SER", "gene_names": "", "chain_id": "", "ligand_mw": "", "inchi_key": "", "secondary_structure": "TIAALLS#CEEEEEC&TIAALLS#CEEEEEC", "amyloid_non_amyloid": "Amyloid", "length": "7", "remarks": "AMYLOID FORMING PEPTIDE TIAALLS FROM TRANSTHYRETIN", "protein_name": "Transthyretin", "peptide_protein_sequence": "chain-ID A: TIAALLS; chain-ID B: TIAALLS", "ligand_name": "", "ligand_smiles": "", "pdb_id": "6C4O", "ec_number": "", "pdb_classification": "PROTEIN FIBRIL", "mutation_s_field": "No", "ligand_formula": "", "r_value_free": "0.228", "alternative_name": "", "description": "They study amyloidogenic segments of transthyretin (TTR). TTR is a transporter of thyroxine and retinol in the blood and cerebrospinal fluid. When mutated and/or as a result of aging, TTR aggregates into amyloid fibrils that accumulate in organs such as the heart. The segments from the C-terminal region of TTR form in-register steric-zippers with highly-interdigitated, wet interfaces, whereas the Beta-strand B from the N-terminal region of TTR forms an out-of-register assembly, previously associated with oligomeric formation.", "resolution": "1.79", "pmid": "29626847", "entry": "S-0513"}