{"global_stoichiometry": "Homo 2-mer - A2 ", "ligstr": "15P:A:C69 H140 O35:1529.83:POLYETHYLENE GLYCOL (N=34):COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO:InChI=1S/C69H140O35/c1-71-4-5-73-8-9-75-12-13-77-16-17-79-20-21-81-24-25-83-28-29-85-32-33-87-36-37-89-40-41-91-44-45-93-48-49-95-52-53-97-56-57-99-60-61-101-64-65-103-68-69-104-67-66-102-63-62-100-59-58-98-55-54-96-51-50-94-47-46-92-43-42-90-39-38-88-35-34-86-31-30-84-27-26-82-23-22-80-19-18-78-15-14-76-11-10-74-7-6-72-3-2-70/h70H,2-69H2,1H3:VUYXVWGKCKTUMF-UHFFFAOYSA-N;SO4:B:O4 S -2:96.06:SULFATE ION:[O-]S(=O)(=O)[O-]:InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2:QAOWNCQODCNURD-UHFFFAOYSA-L", "uniprot_ac": "P01709", "inchi": "InChI=1S/C69H140O35/c1-71-4-5-73-8-9-75-12-13-77-16-17-79-20-21-81-24-25-83-28-29-85-32-33-87-36-37-89-40-41-91-44-45-93-48-49-95-52-53-97-56-57-99-60-61-101-64-65-103-68-69-104-67-66-102-63-62-100-59-58-98-55-54-96-51-50-94-47-46-92-43-42-90-39-38-88-35-34-86-31-30-84-27-26-82-23-22-80-19-18-78-15-14-76-11-10-74-7-6-72-3-2-70/h70H,2-69H2,1H3%%InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2", "reference": "J Biol Chem. 2014 Oct 3;289(40):27513-25.", "author": "Brumshtein, B., Esswein, S.R., Landau, M., Ryan, C.M., Whitelegge, J.P., Phillips, M.L., Cascio, D., Sawaya, M.R., Eisenberg, D.S.", "type": "Protein", "ligand_id": "15P%%SO4", "species": "Homo sapiens", "method": "X-RAY DIFFRACTION", "keyword": "IG LAMBDA CHAIN V-II REGION MGC", "gene_names": "IGLV2-8", "chain_id": "A%%B", "ligand_mw": "1529.83%%96.06", "inchi_key": "VUYXVWGKCKTUMF-UHFFFAOYSA-N%%QAOWNCQODCNURD-UHFFFAOYSA-L", "secondary_structure": "GQSALTQPPSASGSLGQSVTISCTGTSSDVGGYNYVSWYQQHAGKAPKVIIYEVNKRPSGVPDRFSGSKSGNTASLTVSGLQAEDEADYYCSSYEGSDNFVFGTGTKVTVL#CCCCBBCCSEEEECTTSCEEEEEECCTTTTTTCSCEEEEEECTTSCCEEEEBTTTBCCTTCCTTEEEEEETTEEEEEECSCCGGGCEEEEEEEECSTTCEEEBCCEEEEEC&GQSALTQPPSASGSLGQSVTISCTGTSSDVGGYNYVSWYQQHAGKAPKVIIYEVNKRPSGVPDRFSGSKSGNTASLTVSGLQAEDEADYYCSSYEGSDNFVFGTGTKVTVL#CCCCBBCCSEEEECTTSCEEEEEECCTTTTTTCSCEEEEEECTTSCCEEEEBTTTBCCTTCCTTEEEEEETTEEEEEECSCCGGGCEEEEEEEECSTTCEEEBCCEEEEEC", "amyloid_non_amyloid": "Amyloid", "length": "111", "remarks": "MCG - a dimer of lambda variable domains", "protein_name": "Immunoglobulin lambda variable 2-8", "peptide_protein_sequence": "chain-ID A: GQSALTQPPSASGSLGQSVTISCTGTSSDVGGYNYVSWYQQHAGKAPKVIIYEVNKRPSGVPDRFSGSKSGNTASLTVSGLQAEDEADYYCSSYEGSDNFVFGTGTKVTVL; chain-ID B: GQSALTQPPSASGSLGQSVTISCTGTSSDVGGYNYVSWYQQHAGKAPKVIIYEVNKRPSGVPDRFSGSKSGNTASLTVSGLQAEDEADYYCSSYEGSDNFVFGTGTKVTVL", "ligand_name": "POLYETHYLENE GLYCOL (N=34)%%SULFATE ION", "ligand_smiles": "COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO%%[O-]S(=O)(=O)[O-]", "pdb_id": "4UNU", "ec_number": "", "pdb_classification": "IMMUNE SYSTEM", "mutation_s_field": "No", "ligand_formula": "C69 H140 O35%%O4 S -2", "r_value_free": "0.13", "alternative_name": "Ig lambda chain V-II region BO, Ig lambda chain V-II region MGC", "description": "They identify the monomeric form of the Mcg immunoglobulin light chain variable domain as the quaternary unit required for amyloid fiber assembly. Dimers of Mcg variable domains remain stable and soluble, yet become prone to assemble into amyloid fibers upon disassociation into monomers. ", "resolution": "0.95", "pmid": "25138218", "entry": "S-0403"}