{"remarks": "SOLUTION NMR STRUCTURE OF AMYLOID BETA[E16]", "ligand_id": "", "secondary_structure": "DAEFRHDSGYEVHHQELVFFAEDVGSNK#CCSSSSSSSCCTTTTHHHHHHHHHSSCC", "mutation_s_field": "K16E", "keyword": "AMYLOID BETA-PEPTIDE", "ligstr": "", "alternative_name": "ABPP, APPI, Alzheimer disease amyloid protein, Amyloid precursor protein, Amyloid-beta precursor protein, Cerebral vascular amyloid peptide, PreA4, Protease nexin-II", "species": "Homo sapiens", "r_value_free": "", "pdb_id": "1BJB", "pmid": "10940222", "peptide_protein_sequence": "chain-ID A: DAEFRHDSGYEVHHQELVFFAEDVGSNK", "resolution": "", "ec_number": "", "uniprot_ac": "P05067", "protein_name": "Amyloid-beta A4 protein", "global_stoichiometry": "Monomer - A ", "ligand_smiles": "", "author": "Poulsen, S.-A., Watson, A.A., Craik, D.J.", "description": "The structural effects of these mutations of a positively charged residue to anionic 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 K16E mutation, which might be expected to stabilize the macrodipole of the helix, slightly increased the helix length.", "ligand_mw": "", "entry": "S-0007", "ligand_name": "", "pdb_classification": "GLYCOPROTEIN", "amyloid_non_amyloid": "Amyloid", "chain_id": "", "inchi_key": "", "gene_names": "APP, A4, AD1", "method": "SOLUTION NMR", "length": "28", "inchi": "", "type": "Peptide", "reference": "J Struct Biol. 2000 Jun;130(2-3):142-52", "ligand_formula": ""}