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Electrostatic interactions contribute to KRAS4b-FMe/CaM binding. (A) Steady-state binding of GDP-bound KRAS4b-FMe to avi-CaM at 50, 150, and 500 mM NaCl is shown. (B) Data were fit using a one-site model and yielded Kd values of 0.1, 0.4, and 6 μM, respectively.
