Table 1.

Rapid kinetics of imatinib binding to wild-type and mutant forms of Abl

	Binding	Conformational change
WT	kon = 1.0 ± 0.1 μM−1⋅s−1	kfwd = 1.5 ± 0.1 s−1
	koff = 25 ± 4 s−1	krev = (17 ± 5) × 10−4 s−1
F317L	kon = 1.1 ± 0.1 μM−1⋅s−1	kfwd = 1.3 ± 0.1 s−1
	koff = 25 ± 3 s−1	krev = (25 ± 3) × 10−4 s−1
G250E	kon = 1.3 ± 0.1 μM−1⋅s−1	kfwd = 0.5 ± 0.1 s−1
	koff = 25 ± 4 s−1	krev = (23 ± 3) × 10−4 s−1
Y253F	kon = 1.2 ± 0.1 μM−1⋅s−1	kfwd = 0.9 ± 0.1 s−1
	koff = 25 ± 3 s−1	krev = (22 ± 3) × 10−4 s−1

Results from fitting of rapid kinetics from stopped-flow experiments (Fig. 2 and SI Appendix, Figs. S2–S5). Rate constants for the binding step of wild type (WT) and mutants are shown in the second column: physical binding (k_on) and dissociation of imatinib (k_off). Rate constants for slow conformational change after imatinib binding are shown in the last column (forward, k_fwd; and reverse, k_rev).