{"method": "X-RAY DIFFRACTION", "mutation_s_field": "No", "ec_number": "", "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.", "ligstr": "TFA:A:C2 H F3 O2:114.02:trifluoroacetic acid:C(=O)(C(F)(F)F)O:InChI=1S/C2HF3O2/c3-2(4,5)1(6)7/h(H,6,7):DTQVDTLACAAQTR-UHFFFAOYSA-N", "pmid": "29626847", "remarks": "AMYLOID FORMING PEPTIDE IYKVEI FROM TRANSTHYRETIN", "amyloid_non_amyloid": "Amyloid", "type": "Fibril", "inchi": "InChI=1S/C2HF3O2/c3-2(4,5)1(6)7/h(H,6,7)", "resolution": "1.5", "species": "Homo sapiens", "secondary_structure": "IYKVEI#CEEEEC&IYKVEI#CEEEEC", "chain_id": "A", "gene_names": "", "r_value_free": "0.262", "pdb_id": "6C3F", "reference": "Protein Sci. 2018 Jul;27(7):1295-1303.", "keyword": "ILE-TYR-LYS-VAL-GLU-ILE", "protein_name": "Transthyretin", "ligand_formula": "C2 H F3 O2", "peptide_protein_sequence": "chain-ID A: IYKVEI; chain-ID B: IYKVEI", "entry": "S-0509", "length": "6", "uniprot_ac": "", "author": "Saelices, L., Sievers, S.A., Sawaya, M.R., Eisenberg, D.S.", "ligand_smiles": "C(=O)(C(F)(F)F)O", "ligand_mw": "114.02", "alternative_name": "", "ligand_name": "trifluoroacetic acid", "pdb_classification": "PROTEIN FIBRIL", "global_stoichiometry": "Homo 20-mer - A20 ", "inchi_key": "DTQVDTLACAAQTR-UHFFFAOYSA-N", "ligand_id": "TFA"}