We found that the switch peptide binds to the hydrophobic patch more strongly upon phosphorylation with similar ∆∆G values for the wild-type and G159D mutant. This result correctly reproduced the trend found by the WT NMR titration; comparing the difference in ∆∆G upon phosphorylation for the WT there is, perhaps fortuitously, a similarity in the magnitude between experiment and simulation, ∆∆G = -1.2 kcal/mol and -3.5 kcal/mol respectively .