{"resolution": "1.69", "ligand_mw": "59.04%%78.13%%62.07%%186.21%%78.13%%62.07%%69.08%%186.21", "secondary_structure": "CPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNP#CCEEEEEEETTTTEECTTCEEEEEEECTTSCEEEEEEEECCTTSEECCSCCTTTCCSEEEEEEECHHHHHHHTTCCCSBSCEEEEEEECSCSSCEEEEEEEEETTEEEEEEEEECC&CPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNP#CCEEEEEEETTTTEECTTCEEEEEEECTTSCEEEEEEEECCTTSEECCSCCTTTCCSEEEEEEEECHHHHHHTTCCCSCCEEEEEEEESTTSCCEEEEEEEECSSEEEEEEEEECC", "inchi": "InChI=1S/C2H4O2/c1-2(3)4/h1H3,(H,3,4)/p-1%%InChI=1S/C2H6OS/c1-4(2)3/h1-2H3%%InChI=1S/C2H6O2/c3-1-2-4/h3-4H,1-2H2%%InChI=1S/Re%%InChI=1S/C2H6OS/c1-4(2)3/h1-2H3%%InChI=1S/C2H6O2/c3-1-2-4/h3-4H,1-2H2%%InChI=1S/C3H4N2/c1-2-5-3-4-1/h1-3H,(H,4,5)/p+1%%InChI=1S/Re", "method": "X-RAY DIFFRACTION", "ec_number": "", "uniprot_ac": "P02766", "remarks": "Human TTR altered by a rhenium tris-carbonyl Pyta-C8 derivative", "description": "Soaking TTR crystals in a solution containing rhenium tris-carbonyl derivatives yields a TTR conformer never observed before. Only one of the two monomers of the crystallographic dimer is significantly altered, and the inner part of the T4 binding cavity is expanded at one end and shrunk at the other. The result redefines the mechanism of allosteric communication between the two sites, suggesting that negative cooperativity is a function of dimer asymmetry, which can be induced through internal or external binding.", "type": "Inhibitor complex", "ligand_smiles": "CC(=O)[O-]%%CS(=O)C%%C(CO)O%%[Re]%%CS(=O)C%%C(CO)O%%c1c[nH+]c[nH]1%%[Re]", "chain_id": "A%%A%%A%%A%%B%%B%%B%%B", "species": "Homo sapiens", "keyword": "Transthyretin", "ligstr": "ACT:A:C2 H3 O2 -1:59.04:ACETATE ION:CC(=O)[O-]:InChI=1S/C2H4O2/c1-2(3)4/h1H3,(H,3,4)/p-1:QTBSBXVTEAMEQO-UHFFFAOYSA-M;DMS:A:C2 H6 O S:78.13:DIMETHYL SULFOXIDE:CS(=O)C:InChI=1S/C2H6OS/c1-4(2)3/h1-2H3:IAZDPXIOMUYVGZ-UHFFFAOYSA-N;EDO:A:C2 H6 O2:62.07:1,2-ETHANEDIOL:C(CO)O:InChI=1S/C2H6O2/c3-1-2-4/h3-4H,1-2H2:LYCAIKOWRPUZTN-UHFFFAOYSA-N;RE:A:Re:186.21:RHENIUM:[Re]:InChI=1S/Re:WUAPFZMCVAUBPE-UHFFFAOYSA-N;DMS:B:C2 H6 O S:78.13:DIMETHYL SULFOXIDE:CS(=O)C:InChI=1S/C2H6OS/c1-4(2)3/h1-2H3:IAZDPXIOMUYVGZ-UHFFFAOYSA-N;EDO:B:C2 H6 O2:62.07:1,2-ETHANEDIOL:C(CO)O:InChI=1S/C2H6O2/c3-1-2-4/h3-4H,1-2H2:LYCAIKOWRPUZTN-UHFFFAOYSA-N;IMD:B:C3 H5 N2 1:69.08:IMIDAZOLE:c1c[nH+]c[nH]1:InChI=1S/C3H4N2/c1-2-5-3-4-1/h1-3H,(H,4,5)/p+1:RAXXELZNTBOGNW-UHFFFAOYSA-O;RE:B:Re:186.21:RHENIUM:[Re]:InChI=1S/Re:WUAPFZMCVAUBPE-UHFFFAOYSA-N", "pmid": "27402536", "mutation_s_field": "No", "author": "Ciccone, L., Policar, C., Stura, E.A., Shepard, W.", "pdb_id": "5K1J", "amyloid_non_amyloid": "Non-amyloid", "inchi_key": "QTBSBXVTEAMEQO-UHFFFAOYSA-M%%IAZDPXIOMUYVGZ-UHFFFAOYSA-N%%LYCAIKOWRPUZTN-UHFFFAOYSA-N%%WUAPFZMCVAUBPE-UHFFFAOYSA-N%%IAZDPXIOMUYVGZ-UHFFFAOYSA-N%%LYCAIKOWRPUZTN-UHFFFAOYSA-N%%RAXXELZNTBOGNW-UHFFFAOYSA-O%%WUAPFZMCVAUBPE-UHFFFAOYSA-N", "ligand_name": "ACETATE ION%%DIMETHYL SULFOXIDE%%1,2-ETHANEDIOL%%RHENIUM%%DIMETHYL SULFOXIDE%%1,2-ETHANEDIOL%%IMIDAZOLE%%RHENIUM", "ligand_formula": "C2 H3 O2 -1%%C2 H6 O S%%C2 H6 O2%%Re%%C2 H6 O S%%C2 H6 O2%%C3 H5 N2 1%%Re", "ligand_id": "ACT%%DMS%%EDO%%RE%%DMS%%EDO%%IMD%%RE", "r_value_free": "0.222", "protein_name": "Transthyretin", "gene_names": "TTR, PALB", "global_stoichiometry": "Homo 4-mer - A4 ", "alternative_name": "ATTR, Prealbumin, TBPA", "peptide_protein_sequence": "chain-ID A: CPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNP; chain-ID B: CPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNP", "pdb_classification": "TRANSPORT PROTEIN", "reference": "J Struct Biol. 2016 Sep;195(3):353-364.", "length": "116", "entry": "S-0431"}