title: Docking of components in a bacterial complex.
authors.affiliation: Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
authors.forename: T
authors.initials: T
authors.lastname: Ishikawa
authors.forename: M R
authors.initials: MR
authors.lastname: Maurizi
authors.forename: D
authors.initials: D
authors.lastname: Belnap
authors.forename: A C
authors.initials: AC
authors.lastname: Steven
mesh_terms: D049069:ATP-Dependent Proteases; D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000648:ultrastructure; D010450:Endopeptidases / Q000737:chemistry* / Q000648:ultrastructure; D004926:Escherichia coli / Q000201:enzymology*; D006360:Heat-Shock Proteins; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012697:Serine Endopeptidases
chemical_list: D006360:Heat-Shock Proteins; D010450:Endopeptidases; D049069:ATP-Dependent Proteases; D012697:Serine Endopeptidases; D000251:Adenosine Triphosphatases