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. Author manuscript; available in PMC: 2013 Apr 10.

Published in final edited form as: J Mol Biol. 2006 Sep 1;364(3):352–363. doi: 10.1016/j.jmb.2006.08.077

a)¹⁵N-HSQC spectrum of the F495A/K296R kinase alone (blue) and in the presence of 5-fold excess RBD (1-178) (red). Affected residues (red labels) are assigned based on the corresponding peaks in the K296R KD spectrum (black trace). Major differences between the K296R and the K296R/F495A spectra are observed in the vicinity of F495 (labeled in black letters); b) Mapping of the residues indicated in (a) on the kinase structure. Chemical shift changes upon addition of RBD are indicated in red (δδ > 0.03ppm) and orange (0.03ppm > δδ > 0.01ppm). Differences in the spectra of K296R and K296R/F495A labeled in (a) are colored green. The mutated F495 is shown in blue.

a)¹⁵N-HSQC spectrum of the F495A/K296R kinase alone (blue) and in the presence of 5-fold excess RBD (1-178) (red). Affected residues (red labels) are assigned based on the corresponding peaks in the K296R KD spectrum (black trace). Major differences between the K296R and the K296R/F495A spectra are observed in the vicinity of F495 (labeled in black letters); b) Mapping of the residues indicated in (a) on the kinase structure. Chemical shift changes upon addition of RBD are indicated in red (δδ > 0.03ppm) and orange (0.03ppm > δδ > 0.01ppm). Differences in the spectra of K296R and K296R/F495A labeled in (a) are colored green. The mutated F495 is shown in blue.