{"resolution": "", "ligand_mw": "", "secondary_structure": "DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV#CCCCCCCCCCCCCCCEEEEEECCTTSCCCCEEEEEECSCC&DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV#CCCCCCCCCCEEEEEEEEEEECCCSCCSCCEEEEEECSCC&DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV#CCCCCCCCCCEEEEEEEEEEECCCSCCSCCEEEEEECSCC&DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV#CCCCCCCCCCEECCCCEEEEEECCSCCSSCEEEEEECCCC&DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV#CCCCCCCCCCCCCCCCEEEEEECTTCCSCCEEEEEECSCC&DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV#CCCCCCCCCCCCCCCCEEEEESCCCCSTTCEEEEEESSCC&DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV#CCCCCCCCCEEEEEEEEEEEECSCSSCCCEEEEEEEESCC&DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV#CCCCCCCCCEEEEEEEEEEEEECCSSCCCEEEEEEEESCC&DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV#CCCCCCCCCCCEEEEEEEEEEECCSCCSSCEEEEEECSCC&DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV#CCCCCCCCCCEEEEEEEEEEECCCSCCSCCEEEEEECCCC&DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV#CCCCCCCCCCEEEEEEEEEEECCTTCTTCCEEEEEECSCC&DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV#CCCCCCCCCCCCEEEEEEEEECSCCSSSCSEEEEEECSCC&DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV#CCCCCCCCCCCBCCCEEEEEECSCSSCCCEEEEEEECSCC&DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV#CCCCCCCCCCCBCCCEEEEEECCCSSCCCEEEEEEECSCC&DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV#CCCCCCCCCCCCEECCEEEEECCCSSCCCEEEEEEECSCC&DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV#CCCCCCCCCCCCEECEEEEEECCCSCCSSEEEEEEECCCC&DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV#CCCCCCCCCCCCCCCEEEEEECCCSCCTTEEEEEECCSCC&DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV#CCCCCCCCCCCCCCCCEEEEESSTTCCTTCEEEEECCSCC", "inchi": "", "method": "SOLID-STATE NMR", "ec_number": "", "uniprot_ac": "P05067", "remarks": "Structural Model for a 40-residue Beta-Amyloid Fibril with Three-Fold Symmetry, Negative Stagger", "description": "They have described a full structural model for amyloid fibrils formed by the 40-residue Beta-amyloid peptide associated with Alzheimer's disease (ABeta(1-40)), based on numerous constraints from solid state NMR and electron microscopy. This model applies specifically to fibrils with a periodically twisted morphology, with twist period equal to 120 +/- 20 nm (defined as the distance between apparent minima in fibril width in negatively stained transmission electron microscope images).", "type": "Fibril", "ligand_smiles": "", "chain_id": "", "species": "Homo sapiens", "keyword": "Beta-amyloid protein 40", "ligstr": "", "pmid": "19015532", "mutation_s_field": "No", "author": "Paravastu, A.K., Leapman, R.D., Yau, W.M., Tycko, R.", "pdb_id": "2LMQ", "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 18-mer - A18", "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: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV; chain-ID B: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV; chain-ID C: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV; chain-ID D: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV; chain-ID E: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV; chain-ID F: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV; chain-ID G: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV; chain-ID H: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV; chain-ID I: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV; chain-ID J: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV; chain-ID K: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV; chain-ID L: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV; chain-ID M: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV; chain-ID N: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV; chain-ID O: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV; chain-ID P: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV; chain-ID Q: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV; chain-ID R: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV", "pdb_classification": "PROTEIN FIBRIL", "reference": "Proc Natl Acad Sci U S A. 2008 Nov 25;105(47):18349-54.", "length": "40", "entry": "S-0126"}