Backbone and side chain 1H, 15N and 13C assignments of the KSR1 CA1 domain.
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.
Koveal
Dorothy
D
Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, RI 02903, USA.
Pinheiro
Anderson S
AS
Peti
Wolfgang
W
Page
Rebecca
R
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
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D006859:Hydrogen; D011494:Protein Kinases; C097199:KSR-1 protein kinase