title: Chemical shift assignments for Rv0577, a putative glyoxylase associated with virulence from Mycobacterium tuberculosis.
abstract: Approximately one-third of mankind has been exposed to Mycobacterium tuberculosis, the etiological agent responsible for tuberculosis (TB). As part of an effort to develop a new generation of anti-TB agents, the chemical shifts for the 261-residue, virulence-associated protein Rv0577 from M. tuberculosis has been extensively assigned.
authors.affiliation: Biological Sciences Division and Seattle Structural Genomics Center for Infectious Disease, Pacific Northwest National Laboratory, Richland, WA 99352, USA. garry.buchko@pnl.gov
authors.forename: Garry W
authors.initials: GW
authors.lastname: Buchko
authors.forename: Heungbok
authors.initials: H
authors.lastname: Kim
authors.forename: Peter J
authors.initials: PJ
authors.lastname: Myler
authors.forename: Thomas C
authors.initials: TC
authors.lastname: Terwilliger
authors.forename: Chang-Yub
authors.initials: CY
authors.lastname: Kim
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D008024:Ligands; D008969:Molecular Sequence Data; D009169:Mycobacterium tuberculosis / Q000201:enzymology* / Q000472:pathogenicity*; D019906:Nuclear Magnetic Resonance, Biomolecular
chemical_list: D001426:Bacterial Proteins; C480221:Cfp32 protein, Mycobacterium tuberculosis; D008024:Ligands