{"global_stoichiometry": "Homo 8-mer - A8 ", "ligstr": "", "uniprot_ac": "", "inchi": "", "reference": "J Biol Chem. 2018 Dec 21;293(51):19659-19671.", "author": "Brumshtein, B., Esswein, S.R., Sawaya, M.R., Rosenberg, G., Ly, A.T., Landau, M., Eisenberg, D.S.", "type": "Fibril", "ligand_id": "", "species": "Homo sapiens", "method": "X-RAY DIFFRACTION", "keyword": "ASLTVS segment from Light-Chain Variable Domain,  Lambda Mcg", "gene_names": "", "chain_id": "", "ligand_mw": "", "inchi_key": "", "secondary_structure": "ASLTVS#CCEEEC&ASLTVS#CCEEEC", "amyloid_non_amyloid": "Amyloid", "length": "6", "remarks": "ASLTVS segment from Human Immunoglobulin Light-Chain Variable Domain, Residues 73-78, assembled as an amyloid fibril", "protein_name": "Immunoglobulin Light-Chain Variable Domain", "peptide_protein_sequence": "chain-ID A: ASLTVS; chain-ID B: ASLTVS", "ligand_name": "", "ligand_smiles": "", "pdb_id": "6DJ0", "ec_number": "", "pdb_classification": "PROTEIN FIBRIL", "mutation_s_field": "No", "ligand_formula": "", "r_value_free": "0.218", "alternative_name": "", "description": "They identified segments within the variable domains of Ig light chains that drive the assembly of amyloid fibrils in AL. There are at least two such segments and that each one can drive amyloid fibril assembly independently of the other. Peptides derived from these segments form steric zippers featuring a typical dry interface with high-surface complementarity and occupy the same spatial location of the Greek-key immunoglobulin fold in both Lambda and Kappa variable domains.", "resolution": "1.3", "pmid": "30355736", "entry": "S-0534"}