title: Backbone chemical shift assignments of the LexA catalytic domain in its active conformation.
authors.forename: Mark
authors.initials: M
authors.lastname: Okon
authors.forename: Richard A
authors.initials: RA
authors.lastname: Pfuetzner
authors.forename: Mariha
authors.initials: M
authors.lastname: Vuckovic
authors.forename: John W
authors.initials: JW
authors.lastname: Little
authors.forename: Natalie C J
authors.initials: NC
authors.lastname: Strynadka
authors.forename: Lawrence P
authors.initials: LP
authors.lastname: McIntosh
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D002247:Carbon Isotopes; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D019281:Dimerization; D004926:Escherichia coli / Q000378:metabolism; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy; D008968:Molecular Conformation; D009154:Mutation; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011938:Rec A Recombinases / Q000737:chemistry; D012697:Serine Endopeptidases / Q000737:chemistry*; D000099160:LexA Repressor Protein
chemical_list: D001426:Bacterial Proteins; D002247:Carbon Isotopes; D006859:Hydrogen; D009587:Nitrogen Isotopes; D011938:Rec A Recombinases; D012697:Serine Endopeptidases; D000099160:LexA Repressor Protein