{"resolution": "1.1", "ligand_mw": "", "secondary_structure": "KFFEAAAKKFFE#CCCCCCCCCCCC", "inchi": "", "method": "X-RAY DIFFRACTION", "ec_number": "", "uniprot_ac": "", "remarks": "SYNTHETIC PEPTIDE", "description": "A detailed structure for amyloid. The structure reveals that the polypeptides form fibrous crystals composed of antiparallel Beta-sheets in a cross-Beta arrangement, characteristic of all amyloid fibers, and allows us to determine the side-chain packing within an amyloid fiber. The antiparallel Beta-sheets are zipped together by means of pi-bonding between adjacent phenylalanine rings and salt-bridges between charge pairs (glutamic acid-lysine), thus controlling and stabilizing the structure. These interactions are likely to be important in the formation and stability of other amyloid fibrils.", "type": "FIbril", "ligand_smiles": "", "chain_id": "", "species": "synthetic construct", "keyword": "SYNTHETIC PEPTIDE", "ligstr": "", "pmid": "15630094", "mutation_s_field": "No", "author": "Sumner Makin, O., Atkins, E., Sikorski, P., Johansson, J., Serpell, L.C.", "pdb_id": "2BFI", "amyloid_non_amyloid": "Amyloid", "inchi_key": "", "ligand_name": "", "ligand_formula": "", "ligand_id": "", "r_value_free": "", "protein_name": "Synthetic", "gene_names": "", "global_stoichiometry": "", "alternative_name": "", "peptide_protein_sequence": "chain-ID A: KFFEAAAKKFFE", "pdb_classification": "AMYLOID", "reference": "Proc Natl Acad Sci U S A. 2005 Jan 11;102(2):315-20. Epub  2005 Jan 3", "length": "12", "entry": "S-0090"}