{"global_stoichiometry": "Monomer - A ", "ligstr": "", "uniprot_ac": "P05067", "inchi": "", "reference": "J Struct Biol. 2000 Jun;130(2-3):142-52", "author": "Poulsen, S.-A., Watson, A.A., Craik, D.J.", "type": "Peptide", "ligand_id": "", "species": "Homo sapiens", "method": "SOLUTION NMR", "keyword": "AMYLOID BETA-PEPTIDE", "gene_names": "APP, A4, AD1", "chain_id": "", "ligand_mw": "", "inchi_key": "", "secondary_structure": "DAEFRHDSGYEVHHQFLVFFAEDVGSNK#CCTTTTCCCCCCCCTTHHHHHHHHSTTC", "amyloid_non_amyloid": "Amyloid", "length": "28", "remarks": "SOLUTION NMR STRUCTURE OF AMYLOID BETA[F16]", "protein_name": "Amyloid-beta A4 protein", "peptide_protein_sequence": "chain-ID A: DAEFRHDSGYEVHHQFLVFFAEDVGSNK", "ligand_name": "", "ligand_smiles": "", "pdb_id": "1BJC", "ec_number": "", "pdb_classification": "GLYCOPROTEIN", "mutation_s_field": "K16F", "ligand_formula": "", "r_value_free": "", "alternative_name": "ABPP, APPI, Alzheimer disease amyloid protein, Amyloid precursor protein, Amyloid-beta precursor protein, Cerebral vascular amyloid peptide, PreA4, Protease nexin-II", "description": "The structural effects of these mutations of a positively charged residue to hydrophobic residues at the Alpha-secretase cleavage site (Lys16-Leu17) were examined in the membrane-simulating solvent aqueous SDS micelles. Overall the three-dimensional structures were similar to that for the native ABeta(1-28) sequence in that they contained an unstructured N-terminus and a helical C-terminus. the K16F mutation shortened the helix to between residues 16 and 24.", "resolution": "", "pmid": "10940222", "entry": "S-0008"}