{"ligand_smiles": "", "ligand_id": "", "ligstr": "", "ligand_name": "", "global_stoichiometry": "Monomer - A ", "chain_id": "", "pmid": "9693002", "alternative_name": "ABPP, APPI, Alzheimer disease amyloid protein, Amyloid precursor protein, Amyloid-beta precursor protein, Cerebral vascular amyloid peptide, PreA4, Protease nexin-II", "pdb_classification": "GLYCOPROTEIN", "amyloid_non_amyloid": "Amyloid", "reference": "Biochemistry. 1998 Aug 4;37(31):11064-77", "length": "40", "inchi_key": "", "pdb_id": "1BA4", "inchi": "", "type": "Peptide", "gene_names": "APP, A4, AD1", "ligand_mw": "", "species": "Homo sapiens", "entry": "S-0005", "mutation_s_field": "No", "author": "Coles, M., Bicknell, W., Watson, A.A., Fairlie, D.P., Craik, D.J.", "secondary_structure": "DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV#CCSSTTCCCCCSSSHHHHHHHHHHHHHHHHHHHHHHCTTC", "ec_number": "", "method": "SOLUTION NMR", "r_value_free": "", "uniprot_ac": "P05067", "resolution": "", "description": "The solution structure of ABeta(1-40) determined using NMR spectroscopy at pH 5.1, in aqueous sodium dodecyl sulfate (SDS) micelles, which simulates to some extent a water-membrane medium, the peptide is unstructured between residues 1 and 14 which are mainly polar and likely solvated by water. However, the rest of the protein adopts an Alpha-helical conformation between residues 15 and 36 with a kink or hinge at 25-27. The pH-dependent unfolding to a random coil conformation precedes any tendency of this peptide to aggregate to a Beta-sheet as the pH increases.", "peptide_protein_sequence": "chain-ID A: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV", "protein_name": "Amyloid-beta A4 protein", "keyword": "AMYLOID BETA-PEPTIDE", "remarks": "THE SOLUTION STRUCTURE OF AMYLOID BETA-PEPTIDE (1-40) IN A WATER-MICELLE ENVIRONMENT", "ligand_formula": ""}