{"global_stoichiometry": "Monomer - A", "ligstr": "ACT:A:C2 H3 O2 -1:59.04:ACETATE ION:CC(=O)[O-]:InChI=1S/C2H4O2/c1-2(3)4/h1H3,(H,3,4)/p-1:QTBSBXVTEAMEQO-UHFFFAOYSA-M;GOL:A:C3 H8 O3:92.09:GLYCEROL:C(C(CO)O)O:InChI=1S/C3H8O3/c4-1-3(6)2-5/h3-6H,1-2H2:PEDCQBHIVMGVHV-UHFFFAOYSA-N;PEG:A:C4 H10 O3:106.12:DI(HYDROXYETHYL)ETHER:C(COCCO)O:InChI=1S/C4H10O3/c5-1-3-7-4-2-6/h5-6H,1-4H2:MTHSVFCYNBDYFN-UHFFFAOYSA-N", "uniprot_ac": "P61769", "inchi": "InChI=1S/C2H4O2/c1-2(3)4/h1H3,(H,3,4)/p-1%%InChI=1S/C3H8O3/c4-1-3(6)2-5/h3-6H,1-2H2%%InChI=1S/C4H10O3/c5-1-3-7-4-2-6/h5-6H,1-4H2", "reference": "Sci Rep. 2016 May 6;6:25559.", "author": "Camilloni, C., Sala, B.M., Sormanni, P., Porcari, R., Corazza, A., De Rosa, M., Zanini, S., Barbiroli, A., Esposito, G., Bolognesi, M., Bellotti, V., Vendruscolo, M., Ricagno, S.", "type": "Protein", "ligand_id": "ACT%%GOL%%PEG", "species": "Homo sapiens", "method": "X-RAY DIFFRACTION", "keyword": "Beta-2-microglobulin", "gene_names": "B2M, CDABP0092, HDCMA22P", "chain_id": "A%%A%%A", "ligand_mw": "59.04%%92.09%%106.12", "inchi_key": "QTBSBXVTEAMEQO-UHFFFAOYSA-M%%PEDCQBHIVMGVHV-UHFFFAOYSA-N%%MTHSVFCYNBDYFN-UHFFFAOYSA-N", "secondary_structure": "MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDGSFYLLYYTEFTPTEKDEYACRVVHVTLSQPKIVKWDRDM#CCCBCCEEEEEEECCTTCTTCCEEEEEEEEEBSSCCEEEEEETTEECCCCCEEEEEECTTSCEEEEEEEECCCCTTCCEEEEEECTTCSSCEEEECCTTC", "amyloid_non_amyloid": "Amyloid", "length": "100", "remarks": "Human beta-2 microglobulin double mutant W60G-N83V", "protein_name": "Beta-2-microglobulin", "peptide_protein_sequence": "chain-ID A: MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDGSFYLLYYTEFTPTEKDEYACRVVHVTLSQPKIVKWDRDM", "ligand_name": "ACETATE ION%%GLYCEROL%%DI(HYDROXYETHYL)ETHER", "ligand_smiles": "CC(=O)[O-]%%C(C(CO)O)O%%C(COCCO)O", "pdb_id": "5CKA", "ec_number": "", "pdb_classification": "IMMUNE SYSTEM", "mutation_s_field": "W60G/N83V", "ligand_formula": "C2 H3 O2 -1%%C3 H8 O3%%C4 H10 O3", "r_value_free": "0.226", "alternative_name": "", "description": "They compare the native state dynamics of Beta-2 microglobulin (Beta2m), whose aggregation is associated with dialysis-related amyloidosis, and its aggregation-resistant mutant W60G. Their results indicate that W60G low aggregation propensity can be explained, beyond its higher stability, by an increased average protection of the aggregation-prone residues at its surface. To validate these findings, They designed Beta2m variants that alter the aggregation-prone exposed surface of wild-type and W60G Beta2m modifying their aggregation propensity. the W60G Beta 2m variant (W60G-Y63W and W60G-N83V) are expected to weakly (the former) or largely (the latter) increase the W60G aggregation propensity.", "resolution": "1.7", "pmid": "27150430", "entry": "S-0420"}