{"method": "SOLUTION NMR", "mutation_s_field": "No", "ec_number": "", "description": "ABeta(1-40) can adopt a compact, partially folded structure. In this structure (PDB ID: 2LFM), the central hydrophobic region of the peptide forms a 3(10) helix from H13 to D23 and the N- and C-termini collapse against the helix due to the clustering of hydrophobic residues. Helical intermediates have been predicted to be crucial on-pathway intermediates in amyloid fibrillogenesis, and the structure presented here presents a new target for investigation of early events in ABeta(1-40) fibrillogenesis.", "ligstr": "", "pmid": "21726530", "remarks": "A partially folded structure of amyloid-beta(1 40) in an aqueous environment", "amyloid_non_amyloid": "Amyloid", "type": "Peptide", "inchi": "", "resolution": "", "species": "Homo sapiens", "secondary_structure": "DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV#CCCSCCSCCCSCGGGGGGHHHHTTSCCSCCTTCSSCTTTC", "chain_id": "", "gene_names": "APP, A4, AD1", "r_value_free": "", "pdb_id": "2LFM", "reference": "Biochem Biophys Res Commun. 2011 Jul 29;411(2):312-6.", "keyword": "Beta-amyloid protein 40", "protein_name": "Amyloid-beta A4 protein", "ligand_formula": "", "peptide_protein_sequence": "chain-ID A: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV", "entry": "S-0120", "length": "40", "uniprot_ac": "P05067", "author": "Vivekanandan, S., Brender, J.R., Lee, S.Y., Ramamoorthy, A.", "ligand_smiles": "", "ligand_mw": "", "alternative_name": "ABPP, APPI, Alzheimer disease amyloid protein, Amyloid precursor protein, Amyloid-beta precursor protein, Cerebral vascular amyloid peptide, PreA4, Protease nexin-II", "ligand_name": "", "pdb_classification": "PROTEIN FIBRIL", "global_stoichiometry": "Monomer - A ", "inchi_key": "", "ligand_id": ""}