{"global_stoichiometry": "Homo 2-mer - A2", "ligstr": "", "uniprot_ac": "Q15828", "inchi": "", "reference": "J Biol Chem. 2018 Aug 24;293(34):13151-13165.", "author": "Dall, E., Hollerweger, J.C., Dahms, S.O., Cui, H., Haussermann, K., Brandstetter, H.", "type": "Protein", "ligand_id": "", "species": "Homo sapiens", "method": "X-RAY DIFFRACTION", "keyword": "Cystatin-M", "gene_names": "CST6", "chain_id": "", "ligand_mw": "", "inchi_key": "", "secondary_structure": "MDRPQERMVGELRDLSPDDPQVQKAAQAAVASYNMGSNSIYYFRDTHIIKAQSQLVAGIKYFLTMEMGSTDCRKTRVTGDHVDLTTCPLAAGAQQEKLRCDFEVLVVPWQNSSQLLKHNCVQMLEHHHHHH#CCCCCCCCCCCCEEECTTCHHHHHHHHHHHHHHHHHCCCSEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEECCCCCCCCCCGGGSCBCCGGGCCEEEEEEEEEECSSSSCEEEEEEEEEECCCCCCCCC&MDRPQERMVGELRDLSPDDPQVQKAAQAAVASYNMGSNSIYYFRDTHIIKAQSQLVAGIKYFLTMEMGSTDCRKTRVTGDHVDLTTCPLAAGAQQEKLRCDFEVLVVPWQNSSQLLKHNCVQMLEHHHHHH#CCCCCCCCCCCCEECCTTCHHHHHHHHHHHHHHHHHCSCSEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEECCCCCCCCCCGGGSCBCCGGGSCEEEEEEEEEECSSCSCCEEEEEEEEECCCCCCCCC", "amyloid_non_amyloid": "Amyloid", "length": "131", "remarks": "Xray structure of domain-swapped cystatin E dimer", "protein_name": "Cystatin-M", "peptide_protein_sequence": "chain-ID A: MDRPQERMVGELRDLSPDDPQVQKAAQAAVASYNMGSNSIYYFRDTHIIKAQSQLVAGIKYFLTMEMGSTDCRKTRVTGDHVDLTTCPLAAGAQQEKLRCDFEVLVVPWQNSSQLLKHNCVQMLEHHHHHH; chain-ID B: MDRPQERMVGELRDLSPDDPQVQKAAQAAVASYNMGSNSIYYFRDTHIIKAQSQLVAGIKYFLTMEMGSTDCRKTRVTGDHVDLTTCPLAAGAQQEKLRCDFEVLVVPWQNSSQLLKHNCVQMLEHHHHHH", "ligand_name": "", "ligand_smiles": "", "pdb_id": "6FK0", "ec_number": "", "pdb_classification": "hydrolase inhibitor", "mutation_s_field": "No", "ligand_formula": "", "r_value_free": "0.273", "alternative_name": "Cystatin-6, Cystatin-E", "description": "Conformational destabilization of cystatin E leads to the formation of a domain-swapped dimer with increased conformational stability. This dimer was active as a legumain inhibitor by forming a trimeric complex. By contrast, the binding sites toward papain-like proteases were buried within the cystatin E dimer. They also showed that the dimers could further convert to amyloid fibrils. Cystatin E amyloid fibrils contained functional protein, which inhibited both legumain and papain-like enzymes. Fibril formation was further regulated by glycosylation.", "resolution": "2.9", "pmid": "29967063", "entry": "S-0543"}