{"uniprot_ac": "P05067", "ligand_formula": "", "pdb_classification": "SERINE PROTEASE INHIBITOR", "amyloid_non_amyloid": "Amyloid", "ligand_smiles": "", "protein_name": "Amyloid-beta A4 protein", "type": "Peptide", "inchi_key": "", "remarks": "Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease", "method": "SOLUTION NMR", "global_stoichiometry": "Monomer - A ", "inchi": "", "ligand_id": "", "entry": "S-0003", "keyword": "AMYLOID A4", "mutation_s_field": "No", "peptide_protein_sequence": "chain-ID A: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV", "reference": "Eur J Biochem. 1995 Oct 1;233(1):293-8", "description": "One of the principle peptide components of the amyloid plaque deposits of Alzheimer's disease in humans is the 40-amino-acid peptide Beta-amyloid A4-(1-40)-peptide. Synthetic human A4-(1-40)-peptide was soluble and non-aggregating for several days in 40% (by vol). The main secondary-structure elements found were two helices, Gln15-Asp23 and Ile31-Met35, whereas the rest of the peptide was in random-coil conformation. A similar secondary structure is suggested for the aggregation part of prions.", "ec_number": "", "gene_names": "APP, A4, AD1", "ligand_name": "", "chain_id": "", "pmid": "7588758", "author": "Sticht, H., Bayer, P., Willbold, D., Dames, S., Hilbich, C., Beyreuther, K., Frank, R.W., Rosch, P.", "r_value_free": "", "species": "Homo sapiens", "length": "40", "secondary_structure": "DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV#CCCSSCCSSCCSSHHHHHHHHHHHSSSCCSSHHHHTTTTC", "ligstr": "", "resolution": "", "ligand_mw": "", "pdb_id": "1AML", "alternative_name": "ABPP, APPI, Alzheimer disease amyloid protein, Amyloid precursor protein, Amyloid-beta precursor protein, Cerebral vascular amyloid peptide, PreA4, Protease nexin-II"}