{"global_stoichiometry": "Monomer - A", "ligstr": "", "uniprot_ac": "P61769", "inchi": "", "reference": "Biochem Biophys Res Commun. 2008 Dec 5;377(1):146-50.", "author": "Ricagno, S., Colombo, M., de Rosa, M., Sangiovanni, E., Giorgetti, S., Raimondi, S., Bellotti, V., Bolognesi, M.", "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": "MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDCSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM#CCCBCCEEEEEEECCGGGTTCCEEEEEEEEEBSSCCEEEEEETTEECSCCCEEEEEECTTCCEEEEEEEECCCCTTCCEEEEEECTTCSSCEEEECCTTC", "amyloid_non_amyloid": "Amyloid", "length": "100", "remarks": "Beta 2 microglobulin mutant W60C; reduces aggregation capability", "protein_name": "Beta-2-microglobulin", "peptide_protein_sequence": "chain-ID A: MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDCSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM", "ligand_name": "", "ligand_smiles": "", "pdb_id": "3DHJ", "ec_number": "", "pdb_classification": "IMMUNE SYSTEM", "mutation_s_field": "W60C", "ligand_formula": "", "r_value_free": "0.212", "alternative_name": "", "description": "The stability to thermal denaturation and propensity to fibrillar aggregation have been analysed and  their crystal structures were determined for Beta2-microglobulin. The experimental evidences gathered on mutant reinforce the hypothesis that conformational strain in the DE loop can affect Beta2m stability and amyloid aggregation properties.", "resolution": "2.0", "pmid": "18835253", "entry": "S-0211"}