{"resolution": "", "ligand_mw": "", "secondary_structure": "DAEFRHDSGYEVHHQKLVFFAENVGSNKGAIIGLMVGGVV#CCCCCCCCCCCCCCCEEEEEECCSSCSSSCEEEEESSCCC&DAEFRHDSGYEVHHQKLVFFAENVGSNKGAIIGLMVGGVV#CCCCCCCCCCCCCCCCEEEEEECCSCCSCEEEEEEECCCC&DAEFRHDSGYEVHHQKLVFFAENVGSNKGAIIGLMVGGVV#CCCCCCCCCCCCCCCEEEEEEECSSCCSCEEEEEEESCCC&DAEFRHDSGYEVHHQKLVFFAENVGSNKGAIIGLMVGGVV#CCCCCCCCCCCCCCCEEEEEEECSSCCSCEEEEEECCCCC&DAEFRHDSGYEVHHQKLVFFAENVGSNKGAIIGLMVGGVV#CCCCCCCCCCCCCCCEEEEEEECSSCCSCCEEEEEECCCC&DAEFRHDSGYEVHHQKLVFFAENVGSNKGAIIGLMVGGVV#CCCCCCCCCCCCCCCEEEEEEECSSCCCSCEEEEESSCCC&DAEFRHDSGYEVHHQKLVFFAENVGSNKGAIIGLMVGGVV#CCCCCCCCCCCCCCCCEEEEEECCSCCSCCEEEEEESSCC&DAEFRHDSGYEVHHQKLVFFAENVGSNKGAIIGLMVGGVV#CCCCCCCCCCCCCCCEEEEEECCCSSSCCEEEEEESCCCC", "inchi": "", "method": "SOLID-STATE NMR", "ec_number": "", "uniprot_ac": "P05067", "remarks": "Antiparallel beta-sheet architecture in Iowa-mutant beta-amyloid fibrils", "description": "\"They have reported a protocol for producing structurally pure antiparallel D23N-ABeta(1-40) fibril samples. It reveals how both parallel and antiparallel cross-Beta structures can be constructed from similar peptide monomer conformations and stabilized by similar sets of interactions, primarily hydrophobic in nature. antiparallel D23N-ABeta(1-40) fibrils are thermodynamically metastable with respect to conversion to parallel structures, propagate less efficiently than parallel fibrils in seeded fibril growth, and therefore must nucleate more efficiently than parallel fibrils in order to be observable. Experiments in neuronal cell cultures indicate that both antiparallel and parallel D23N-ABeta(1-40) fibrils are cytotoxic. Thus, our antiparallel D23N-ABeta(1-40) fibril model represents a specific \"\"toxic intermediate\"\" in the aggregation process of a disease-associated ABeta mutant.\"", "type": "Fibril", "ligand_smiles": "", "chain_id": "", "species": "Homo sapiens", "keyword": "P3(40)", "ligstr": "", "pmid": "22403062", "mutation_s_field": "D23N ", "author": "Qiang, W., Yau, W.M., Luo, Y., Mattson, M.P., Tycko, R.", "pdb_id": "2LNQ", "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": "Homo 8-mer - A8 ", "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: DAEFRHDSGYEVHHQKLVFFAENVGSNKGAIIGLMVGGVV; chain-ID B: DAEFRHDSGYEVHHQKLVFFAENVGSNKGAIIGLMVGGVV; chain-ID C: DAEFRHDSGYEVHHQKLVFFAENVGSNKGAIIGLMVGGVV; chain-ID D: DAEFRHDSGYEVHHQKLVFFAENVGSNKGAIIGLMVGGVV; chain-ID E: DAEFRHDSGYEVHHQKLVFFAENVGSNKGAIIGLMVGGVV; chain-ID F: DAEFRHDSGYEVHHQKLVFFAENVGSNKGAIIGLMVGGVV; chain-ID G: DAEFRHDSGYEVHHQKLVFFAENVGSNKGAIIGLMVGGVV; chain-ID H: DAEFRHDSGYEVHHQKLVFFAENVGSNKGAIIGLMVGGVV", "pdb_classification": "PROTEIN FIBRIL", "reference": "Proc Natl Acad Sci U S A. 2012 Mar 20;109(12):4443-8.", "length": "40", "entry": "S-0127"}