{"global_stoichiometry": "Homo 8-mer - A8", "ligstr": "", "uniprot_ac": "", "inchi": "", "reference": "Nat Commun. 2019 Mar 20;10(1):1103.", "author": "Radamaker, L., Lin, Y.H., Annamalai, K., Huhn, S., Hegenbart, U., Schonland, S.O., Fritz, G., Schmidt, M., Fandrich, M.", "type": "Fibril", "ligand_id": "", "species": "Homo sapiens", "method": "ELECTRON MICROSCOPY", "keyword": "lambda 1 light chain fragment,  residues 3-118", "gene_names": "", "chain_id": "", "ligand_mw": "", "inchi_key": "", "secondary_structure": "VLTQPPSASGTPGQRVTISCSGRSSNIGRNLVKWYQQFPGTAPKLLIYSNDQRPSGVPDRFSGSKSGTSASLAVSGLQSEDEADYYCAAWDATLNAWVFGGGTKLTVLSQPKAAPS#CCCCCCCCCCCCCCEEECCCCCEEESCSSCBCCCCCCSCEECCCEEESCCCCCCCCCCSEECCSBCCCCCCCCCBSSCCEECCCCCSCCSSEECCCCCCCCCCCCCCCCCCCCCCC&VLTQPPSASGTPGQRVTISCSGRSSNIGRNLVKWYQQFPGTAPKLLIYSNDQRPSGVPDRFSGSKSGTSASLAVSGLQSEDEADYYCAAWDATLNAWVFGGGTKLTVLSQPKAAPS#CCCCCCCCCCCCCCEEECCCCCEEESCSSCBCCCCCCSCEECCCEEESCCCCCCCCCCSEECCSBCCCCCCCCCBSSCCEECCCCCSCCSSEECCCCCCCCCCCCCCCCCCCCCCC&VLTQPPSASGTPGQRVTISCSGRSSNIGRNLVKWYQQFPGTAPKLLIYSNDQRPSGVPDRFSGSKSGTSASLAVSGLQSEDEADYYCAAWDATLNAWVFGGGTKLTVLSQPKAAPS#CCCCCCCCCCCCCCEEECCCCCEEESCSSCBCCCCCCSCEECCCEEESCCCCCCCCCCSEECCSBCCCCCCCCCBSSCCEECCCCCSCCSSEECCCCCCCCCCCCCCCCCCCCCCC&VLTQPPSASGTPGQRVTISCSGRSSNIGRNLVKWYQQFPGTAPKLLIYSNDQRPSGVPDRFSGSKSGTSASLAVSGLQSEDEADYYCAAWDATLNAWVFGGGTKLTVLSQPKAAPS#CCCCCCCCCCCCCCEEECCCCCEEESCSSCBCCCCCCSCEECCCEEESCCCCCCCCCCSEECCSBCCCCCCCCCBSSCCEECCCCCSCCSSEECCCCCCCCCCCCCCCCCCCCCCC&VLTQPPSASGTPGQRVTISCSGRSSNIGRNLVKWYQQFPGTAPKLLIYSNDQRPSGVPDRFSGSKSGTSASLAVSGLQSEDEADYYCAAWDATLNAWVFGGGTKLTVLSQPKAAPS#CCCCCCCCCCCCCCEEECCCCCEEESCSSCBCCCCCCSCEECCCEEESCCCCCCCCCCSEECCSBCCCCCCCCCBSSCCEECCCCCSCCSSEECCCCCCCCCCCCCCCCCCCCCCC&VLTQPPSASGTPGQRVTISCSGRSSNIGRNLVKWYQQFPGTAPKLLIYSNDQRPSGVPDRFSGSKSGTSASLAVSGLQSEDEADYYCAAWDATLNAWVFGGGTKLTVLSQPKAAPS#CCCCCCCCCCCCCCEEECCCCCEEESCSSCBCCCCCCSCEECCCEEESCCCCCCCCCCSEECCSBCCCCCCCCCBSSCCEECCCCCSCCSSEECCCCCCCCCCCCCCCCCCCCCCC&VLTQPPSASGTPGQRVTISCSGRSSNIGRNLVKWYQQFPGTAPKLLIYSNDQRPSGVPDRFSGSKSGTSASLAVSGLQSEDEADYYCAAWDATLNAWVFGGGTKLTVLSQPKAAPS#CCCCCCCCCCCCCCEEECCCCCEEESCSSCEEECCCCSCEECCCEEESCCCCCCCCCCSEECCSBCCCCCCCCCBSSCCEECCCCCSCCSSEECCCCCCCCCCCCCCCCCCCCCCC&VLTQPPSASGTPGQRVTISCSGRSSNIGRNLVKWYQQFPGTAPKLLIYSNDQRPSGVPDRFSGSKSGTSASLAVSGLQSEDEADYYCAAWDATLNAWVFGGGTKLTVLSQPKAAPS#CCCCCCCCCCCCCCEEECCCCCEEESCSSCEEECCCCSCEECCCEEESCCCCCCCCCCSEECCSBCCCCCCCCCBSSCCCBCCCCCSCCSSEECCCCCCCCCCCCCCCCCCCCCCC", "amyloid_non_amyloid": "Amyloid", "length": "116", "remarks": "AL amyloid fibril from a lambda 1 light chain", "protein_name": "Immunoglobulin  lambda 1 light chain", "peptide_protein_sequence": "chain-ID A: VLTQPPSASGTPGQRVTISCSGRSSNIGRNLVKWYQQFPGTAPKLLIYSNDQRPSGVPDRFSGSKSGTSASLAVSGLQSEDEADYYCAAWDATLNAWVFGGGTKLTVLSQPKAAPS; chain-ID B: VLTQPPSASGTPGQRVTISCSGRSSNIGRNLVKWYQQFPGTAPKLLIYSNDQRPSGVPDRFSGSKSGTSASLAVSGLQSEDEADYYCAAWDATLNAWVFGGGTKLTVLSQPKAAPS; chain-ID C: VLTQPPSASGTPGQRVTISCSGRSSNIGRNLVKWYQQFPGTAPKLLIYSNDQRPSGVPDRFSGSKSGTSASLAVSGLQSEDEADYYCAAWDATLNAWVFGGGTKLTVLSQPKAAPS; chain-ID D: VLTQPPSASGTPGQRVTISCSGRSSNIGRNLVKWYQQFPGTAPKLLIYSNDQRPSGVPDRFSGSKSGTSASLAVSGLQSEDEADYYCAAWDATLNAWVFGGGTKLTVLSQPKAAPS; chain-ID E: VLTQPPSASGTPGQRVTISCSGRSSNIGRNLVKWYQQFPGTAPKLLIYSNDQRPSGVPDRFSGSKSGTSASLAVSGLQSEDEADYYCAAWDATLNAWVFGGGTKLTVLSQPKAAPS; chain-ID F: VLTQPPSASGTPGQRVTISCSGRSSNIGRNLVKWYQQFPGTAPKLLIYSNDQRPSGVPDRFSGSKSGTSASLAVSGLQSEDEADYYCAAWDATLNAWVFGGGTKLTVLSQPKAAPS; chain-ID G: VLTQPPSASGTPGQRVTISCSGRSSNIGRNLVKWYQQFPGTAPKLLIYSNDQRPSGVPDRFSGSKSGTSASLAVSGLQSEDEADYYCAAWDATLNAWVFGGGTKLTVLSQPKAAPS; chain-ID H: VLTQPPSASGTPGQRVTISCSGRSSNIGRNLVKWYQQFPGTAPKLLIYSNDQRPSGVPDRFSGSKSGTSASLAVSGLQSEDEADYYCAAWDATLNAWVFGGGTKLTVLSQPKAAPS", "ligand_name": "", "ligand_smiles": "", "pdb_id": "6IC3", "ec_number": "", "pdb_classification": "PROTEIN FIBRIL", "mutation_s_field": "No", "ligand_formula": "", "r_value_free": "", "alternative_name": "", "description": "The structure of a Lambda1 AL amyloid fibril from an explanted human heart. The fibril core consists of a 91-residue segment presenting an all-beta fold with ten mutagenic changes compared to the germ line. The conformation differs substantially from natively folded light chains: a rotational switch around the intramolecular disulphide bond being the crucial structural rearrangement underlying fibril formation.", "resolution": "3.3", "pmid": "30894526", "entry": "S-0555"}