{"global_stoichiometry": "Homo 4-mer - A4 ", "ligstr": "", "uniprot_ac": "P61769", "inchi": "", "reference": "Nat Struct Mol Biol. 2006 Mar;13(3):202-8. Epub  2006 Feb 19", "author": "Eakin, C.M., Berman, A.J., Miranker, A.D.", "type": "Protein", "ligand_id": "", "species": "Homo sapiens", "method": "X-RAY DIFFRACTION", "keyword": "Beta-2-microglobulin", "gene_names": "B2M, CDABP0092, HDCMA22P", "chain_id": "", "ligand_mw": "", "inchi_key": "", "secondary_structure": "MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHASDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM#CCCCCCEEEEEESSCCCTTSCEEEEEEEEEECCTTCEEEEEETTEECSSCEEEEEEETTTTEEEEEEEEEECCCSSCCEEEEEECTTCSSCEEEECCCCC&MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHASDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM#CCCCCCEEEEEESSCCCTTSCEEEEEEEEEESCCSCEEEEEETTEECSSCEEEEEEETTTTEEEEEEEEEECCCSSCCEEEEEECTTCSSCEEEECCCCC", "amyloid_non_amyloid": "Amyloid", "length": "100", "remarks": "A Native to Amyloidogenic Transition Regulated by a Backbone Trigger", "protein_name": "Beta-2-microglobulin", "peptide_protein_sequence": "chain-ID A: MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHASDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM; chain-ID B: MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHASDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM", "ligand_name": "", "ligand_smiles": "", "pdb_id": "2F8O", "ec_number": "", "pdb_classification": "IMMUNE SYSTEM", "mutation_s_field": "P32A", "ligand_formula": "", "r_value_free": "0.22699999", "alternative_name": "", "description": "Access of Beta2m to amyloidogenic conformations is catalyzed by selective binding of divalent cations. The chemical basis of this process was determined to be backbone isomerization of a conserved proline. On the basis of this finding, a Beta2m variant was designed that closely adopts intermediate state (conformational changes that initiate fiber formation by Beta-2-microglobulin). The variant has kinetic, thermodynamic and catalytic properties consistent with its being a fibrillogenic intermediate of wild-type Beta2m. Furthermore, it is stable and folded, enabling us to unambiguously determine the initiating conformational changes for amyloid assembly at atomic resolution.", "resolution": "1.7", "pmid": "16491088", "entry": "S-0098"}