{"global_stoichiometry": "Monomer - A", "ligstr": "", "uniprot_ac": "P02766", "inchi": "", "reference": "J Biol Chem. 2009 Sep 18;284(38):25832-41.", "author": "Cendron, L., Trovato, A., Seno, F., Folli, C., Alfieri, B., Zanotti, G., Berni, R.", "type": "Protein", "ligand_id": "", "species": "Homo sapiens", "method": "X-RAY DIFFRACTION", "keyword": "Transthyretin", "gene_names": "TTR, PALB", "chain_id": "", "ligand_mw": "", "inchi_key": "", "secondary_structure": "GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGHTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE#CCCCCCCCCCCEEEEEEETTTTEECCSCEEEEEEECTTSSEEEEEEEECCTTSEECCSSCTTTCCSEEEEEEECHHHHHHTTTCCCSEEEEEEEEEESTTSCCEEEEEEEEETTEEEEEEEEECCCC&GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGHTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE#CCCCCCCCCCCEEEEEEETTTTEECTTCEEEEEEEETTTEEEEEEEEECCTTSEECCCSCTTTCCSEEEEEEECHHHHHHHTTCCCSEEEEEEEEEECCSSSCEEEEEEEEETTEEEEEEEEECCCC", "amyloid_non_amyloid": "Amyloid", "length": "127", "remarks": "CRYSTAL STRUCTURE OF TRANSTHYRETIN VARIANT L58H at neutral pH", "protein_name": "Transthyretin", "peptide_protein_sequence": "chain-ID A: GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGHTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE; chain-ID B: GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGHTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE", "ligand_name": "", "ligand_smiles": "", "pdb_id": "3DJR", "ec_number": "", "pdb_classification": "TRANSPORT PROTEIN", "mutation_s_field": "L58H ", "ligand_formula": "", "r_value_free": "0.228", "alternative_name": "ATTR, Prealbumin, TBPA", "description": "Human transthyretin (TTR) is an amyloidogenic protein whose mild amyloidogenicity is enhanced by many point mutations affecting considerably the amyloid disease phenotype. To ascertain whether the high amyloidogenic potential of TTR variants may be explained on the basis of the conformational change hypothesis, an aim of this work was to determine structural alterations for five amyloidogenic TTR variants crystallized under native and/or destabilizing (moderately acidic pH) conditions.", "resolution": "2.02", "pmid": "19602727", "entry": "S-0214"}