{"resolution": "", "ligand_mw": "", "secondary_structure": "DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV#CCCCCCCCCCCCCCCCEEEEEEEEEGGGEEEEEEEESSCC&GSSHHHHHHLQVDNKFNKEMASAGGEIVYLPNLNPDQLCAFIHSLHDDPSQSANLLAEAKKLNDAQAPKVD#CCCCCCCCCCCCCCCCCCCCCCCCCEEEECTTSCHHHHHHHHHHHHHCSTTHHHHHHHHHHHHHHCCCCCC&GSSHHHHHHLQVDNKFNKEMASAGGEIVYLPNLNPDQLCAFIHSLHDDPSQSANLLAEAKKLNDAQAPKVD#CCCCCCCCCCCCCCCCCCCCCCCCCCEEEESSSCHHHHHHHHHHHHHCHHHHHHHHHHHHHHHHHCCCCCC", "inchi": "", "method": "SOLUTION NMR", "ec_number": "", "uniprot_ac": "", "remarks": "Structure of Alzheimer Ab peptide in complex with an engineered binding protein; Stabilization of a beta-hairpin in monomeric Alzheimer's amyloid-beta peptide inhibits amyloid formation.", "description": "The solution structure of ABeta(1-40) in complex with the phage-display selected affibody protein Z(ABeta3), a binding protein of nanomolar affinity. Bound ABeta(1-40) features a Beta-hairpin comprising residues 17-36, providing the first high-resolution structure of ABeta in Beta conformation. The positions of the secondary structure elements strongly resemble those observed for fibrillar ABeta. Z(ABeta3) stabilizes the Beta-sheet by extending it intermolecularly and by burying both of the mostly nonpolar faces of the ABeta hairpin within a large hydrophobic tunnel-like cavity. Consequently, Z(ABeta3) acts as a stoichiometric inhibitor of ABeta fibrillation.", "type": "Inhibitor complex", "ligand_smiles": "", "chain_id": "", "species": "", "keyword": "", "ligstr": "", "pmid": "18375754", "mutation_s_field": "No", "author": "Hoyer, W., Gronwall, C., Jonsson, A., Stahl, S., Hard, T.", "pdb_id": "2OTK", "amyloid_non_amyloid": "Non-amyloid", "inchi_key": "", "ligand_name": "", "ligand_formula": "", "ligand_id": "", "r_value_free": "", "protein_name": "Amyloid-beta ", "gene_names": "APP, A4, AD1", "global_stoichiometry": "Hetero 3-mer - A2B ", "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 C: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV; chain-ID E: GSSHHHHHHLQVDNKFNKEMASAGGEIVYLPNLNPDQLCAFIHSLHDDPSQSANLLAEAKKLNDAQAPKVD; chain-ID F: GSSHHHHHHLQVDNKFNKEMASAGGEIVYLPNLNPDQLCAFIHSLHDDPSQSANLLAEAKKLNDAQAPKVD", "pdb_classification": "DE NOVO PROTEIN", "reference": "Proc Natl Acad Sci U S A. 2008 Apr 1;105(13):5099-104.", "length": "40 ,  71 ,  71", "entry": "S-0168"}