Fig. 2
Cross-comparison of the experimentally measured effects that mutations in Abl kinase have on ligand binding, performed by different labs. ΔΔG was computed from publicly available ΔpIC50 or ΔpKd measurements and these values of ΔΔG were then plotted and the RMSE between them reported. a ΔpIC50 measurements (X-axis) from ref. 79 compared with ΔpIC50 measurements (Y-axis) from ref. 81. b ΔpIC50 measurements (X-axis) from ref. 79 compared with ΔpIC50 measurements (Y-axis) from ref. 80. c ΔpIC50 measurements (X-axis) from ref. 81 compared with ΔpIC50 measurements (Y-axis) from ref. 80. d ΔpIC50 measurements (X-axis) from ref. 79 compared with ΔpKd measurements (Y-axis) from ref. 82 using non-phosphorylated Abl kinase. Scatter plot error bars in (a–c) are ±standard error (SE) taken from the combined 97 inter-lab ΔΔGs derived from the ΔpIC50 measurements, which was \(0.32_{0.28}^{0.36}\); the RMSE was \(0.45_{0.39}^{0.51}\) kcal mol−1. Scatter plot error bars in (d) are the ±standard error (SE) of ΔΔGs derived from ΔpIC50 and ΔpKd from a set of 27 mutations, which is \(0.58_{0.42}^{0.74}\) kcal mol−1; the RMSE was \(0.81_{0.59}^{1.04}\) kcal mol−1
