{"entry": "S-0001", "ligand_formula": "", "peptide_protein_sequence": "chain-ID A: DAEFRHDSGYEVHHQKLVFFAEDVGSNK", "remarks": "SOLUTION STRUCTURE OF RESIDUES 1-28 OF THE AMYLOID BETA-PEPTIDE", "pmid": "7516706", "chain_id": "", "mutation_s_field": "No", "ligstr": "", "r_value_free": "", "uniprot_ac": "P05067", "resolution": "", "pdb_id": "1AMB", "protein_name": "Amyloid-beta A4 protein", "gene_names": "APP, A4, AD1", "species": "Homo sapiens", "method": "SOLUTION NMR", "author": "Talafous, J., Marcinowski, K.J., Klopman, G., Zagorski, M.G.", "type": "Peptide", "ligand_mw": "", "secondary_structure": "DAEFRHDSGYEVHHQKLVFFAEDVGSNK#CHHHHHHHHHHHHHHHHHHHHHHHHHTC", "description": "Solution structure of residues 1-28 of the amyloid Beta-peptide was determined using nuclear magnetic resonance spectroscopy. In membrane-like media, the peptide folds to form a predominately Alpha-helical structure with a bend centered at residue 12. An Alpha-helix-->Beta-sheet conversion may occur during the early stages of amyloid formation in Alzheimer's disease.", "ec_number": "", "global_stoichiometry": "Monomer - A ", "ligand_name": "", "ligand_id": "", "pdb_classification": "PROTEINASE INHIBITOR(TRYPSIN)", "length": "28", "keyword": "AMYLOID BETA-PEPTIDE", "amyloid_non_amyloid": "Amyloid", "inchi": "", "reference": "Biochemistry. 1994 Jun 28;33(25):7788-96", "alternative_name": "ABPP, APPI, Alzheimer disease amyloid protein, Amyloid precursor protein, Amyloid-beta precursor protein, Cerebral vascular amyloid peptide, PreA4, Protease nexin-II", "ligand_smiles": "", "inchi_key": ""}