{"resolution": "1.85", "ligand_mw": "", "secondary_structure": "AEVVFT#CCCCCC&AEVVFT#CCCCCC", "inchi": "", "method": "X-RAY DIFFRACTION", "ec_number": "", "uniprot_ac": "", "remarks": "Structure of an Amyloid forming peptide AEVVFT from Human Transthyretin", "description": "They identify Beta-strands F and H as necessary for TTR aggregation. Based on the crystal structures of these segments, they designed two non-natural peptide inhibitors that block aggregation. This work provides the first characterization of peptide inhibitors for TTR aggregation, establishing a novel therapeutic strategy.", "type": "Fibril", "ligand_smiles": "", "chain_id": "", "species": "synthetic construct", "keyword": "Amyloid forming peptide AEVVFT", "ligstr": "", "pmid": "26459562", "mutation_s_field": "No", "author": "Saelices, L., Johnson, L.M., Liang, W.Y., Sawaya, M.R., Cascio, D., Ruchala, P., Whitelegge, J., Jiang, L., Riek, R., Eisenberg, D.S.", "pdb_id": "4XFN", "amyloid_non_amyloid": "Amyloid", "inchi_key": "", "ligand_name": "", "ligand_formula": "", "ligand_id": "", "r_value_free": "0.201", "protein_name": "Transthyretin", "gene_names": "", "global_stoichiometry": "Homo 8-mer - A8 ", "alternative_name": "", "peptide_protein_sequence": "chain-ID A: AEVVFT; chain-ID B: AEVVFT", "pdb_classification": "PROTEIN FIBRIL", "reference": "J Biol Chem. 2015 Nov 27;290(48):28932-43.", "length": "6", "entry": "S-0405"}