{"global_stoichiometry": "Monomer - A ", "ligstr": "", "uniprot_ac": "P0AE95", "inchi": "", "reference": "Proc Natl Acad Sci U S A. 2016 Jun 28;113(26):7130-5.", "author": "Shu, Q., Krezel, A.M., Cusumano, Z.T., Pinkner, J.S., Klein, R., Hultgren, S.J., Frieden, C.", "type": "Protein", "ligand_id": "", "species": "Escherichia coli", "method": "SOLUTION NMR", "keyword": "Curli production assembly/transport component CsgE", "gene_names": "csgE, b1039, JW1022", "chain_id": "", "ligand_mw": "", "inchi_key": "", "secondary_structure": "AVEVEVPGLLTDHTVSSIGHDFYRAFSDKWESDYTGNLTINERPSARAGSWITITVNQDVIFQTFLFPLKRDFEKTVVAALIQTEEALNRRQINQALLSTGDLAHDEFHHHHHH#CCCCCCCCCCCEECCSTTHHHHHHHHHHHCCCSSCCCEEEEEEEETTTEEEEEEEETTEEEEEEEECSSSSCHHHHHHHHHHHHHHHHTTTTHHHHHHHSCCCCSCCCCCCCCC", "amyloid_non_amyloid": "Non-amyloid", "length": "114", "remarks": "Curli secretion specificity factor CsgE W48A/F79A mutant; CsgE (W48A/F79A) that appears to be similar to the wild-type (WT) protein in overall structure and function but does not form mixed oligomers at NMR concentrations similar to the WT", "protein_name": "Curli production assembly/transport component CsgE", "peptide_protein_sequence": "chain-ID A: AVEVEVPGLLTDHTVSSIGHDFYRAFSDKWESDYTGNLTINERPSARAGSWITITVNQDVIFQTFLFPLKRDFEKTVVAALIQTEEALNRRQINQALLSTGDLAHDEFHHHHHH", "ligand_name": "", "ligand_smiles": "", "pdb_id": "2NA4", "ec_number": "", "pdb_classification": "CHAPERONE", "mutation_s_field": "W48A/F79A", "ligand_formula": "", "r_value_free": "", "alternative_name": "", "description": "The solution NMR structure of a double mutant of CsgE (W48A/F79A) appears to be similar to the wild-type (WT) protein in overall structure and function but does not form mixed oligomers at NMR concentrations similar to the WT. The well-converged structure of this mutant has a core scaffold composed of a layer of two Alpha-helices and a layer of three-stranded antiparallel Beta-sheet with flexible N and C termini.", "resolution": "", "pmid": "27298344", "entry": "S-0149"}