{"resolution": "", "ligand_mw": "", "secondary_structure": "YEVHHQKLVFFAEDVGSNKGAIIGLM#CCCCCSSCCSSSTTTTSCSSSSSSCC", "inchi": "", "method": "SOLUTION NMR", "ec_number": "", "uniprot_ac": "P05067", "remarks": "The Alzheimer's peptide a beta adopts a collapsed coil structure in water", "description": "In contrast to studies in other solvents, in water ABeta is collapsed into a compact series of loops, strands, and turns and has no Alpha-helical or Beta-sheet structure. Conformational stabilization is primarily attributed to van der Waals and electrostatic forces. A large conspicuous uninterrupted hydrophobic patch covers approximately 25% of the surface. The compact coil structure appears meta-stable, and because fibrillization leads to formation of intermolecular Beta-sheet secondary structure, a global conformational rearrangement is highly likely.", "type": "Peptide", "ligand_smiles": "", "chain_id": "", "species": "Homo sapiens", "keyword": "A-BETA AMYLOID", "ligstr": "", "pmid": "10940221", "mutation_s_field": "No", "author": "Zhang, S., Iwata, K., Lachenmann, M.J., Peng, J.W., Li, S., Stimson, E.R., Lu, Y., Felix, A.M., Maggio, J.E., Lee, J.P.", "pdb_id": "1HZ3", "amyloid_non_amyloid": "Amyloid", "inchi_key": "", "ligand_name": "", "ligand_formula": "", "ligand_id": "", "r_value_free": "", "protein_name": "Amyloid-beta A4 protein", "gene_names": "APP, A4, AD1", "global_stoichiometry": "Monomer - A", "alternative_name": "ABPP, APPI, Alzheimer disease amyloid protein, Amyloid precursor protein, Amyloid-beta precursor protein, Cerebral vascular amyloid peptide, PreA4, Protease nexin-II", "peptide_protein_sequence": "chain-ID A: YEVHHQKLVFFAEDVGSNKGAIIGLM", "pdb_classification": "SUGAR BINDING PROTEIN", "reference": "J Struct Biol. 2000 Jun;130(2-3):130-41", "length": "26", "entry": "S-0032"}