{"amyloid_non_amyloid": "Amyloid", "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.", "ligand_formula": "C3 H8 O3", "chain_id": "B", "global_stoichiometry": "Homo 20-mer - A20 ", "gene_names": "", "mutation_s_field": "No", "uniprot_ac": "", "species": "Homo sapiens", "ligand_name": "GLYCEROL", "pdb_id": "6C88", "ligand_id": "GOL", "reference": "Protein Sci. 2018 Jul;27(7):1295-1303.", "resolution": "1.85", "inchi": "InChI=1S/C3H8O3/c4-1-3(6)2-5/h3-6H,1-2H2", "method": "X-RAY DIFFRACTION", "ligand_smiles": "C(C(CO)O)O", "keyword": "VAL-ALA-VAL-HIS-VAL-PHE", "remarks": "STRUCTURE OF THE AMYLOID FORMING PEPTIDE VAVHVF FROM TRANSTHYRETIN", "length": "6", "peptide_protein_sequence": "chain-ID A: VAVHVF; chain-ID B: VAVHVF", "protein_name": "Transthyretin", "entry": "S-0520", "inchi_key": "PEDCQBHIVMGVHV-UHFFFAOYSA-N", "author": "Saelices, L., Sievers, S.A., Sawaya, M.R., Eisenberg, D.S.", "ligstr": "GOL:B:C3 H8 O3:92.09:GLYCEROL:C(C(CO)O)O:InChI=1S/C3H8O3/c4-1-3(6)2-5/h3-6H,1-2H2:PEDCQBHIVMGVHV-UHFFFAOYSA-N", "secondary_structure": "VAVHVF#CCEEEC&VAVHVF#CCEEEC", "pdb_classification": "PROTEIN FIBRIL", "ligand_mw": "92.09", "r_value_free": "0.17800000", "alternative_name": "", "type": "Fibril", "pmid": "29626847", "ec_number": ""}