title: Backbone and side chain 1H, 15N and 13C assignments of the KSR1 CA1 domain.
abstract: The backbone and side chain resonance assignments of the murine KSR1 CA1 domain have been determined based on triple-resonance experiments using uniformly [(13)C, (15)N]-labeled protein. This assignment is the first step towards the determination of the three-dimensional structure of the unique KSR1 CA1 domain.
authors.affiliation: Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, RI 02903, USA.
authors.forename: Dorothy
authors.initials: D
authors.lastname: Koveal
authors.forename: Anderson S
authors.initials: AS
authors.lastname: Pinheiro
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Peti
authors.forename: Rebecca
authors.initials: R
authors.lastname: Page
mesh_terms: D000818:Animals; D002247:Carbon Isotopes; D006859:Hydrogen; D051379:Mice; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D011494:Protein Kinases / Q000737:chemistry*; D017434:Protein Structure, Tertiary
chemical_list: D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D006859:Hydrogen; D011494:Protein Kinases; C097199:KSR-1 protein kinase