. Author manuscript; available in PMC: 2020 Dec 3.

Published in final edited form as: Structure. 2019 Oct 14;27(12):1820–1829.e4. doi: 10.1016/j.str.2019.09.011

Table 1.

Kinetic and equilibrium binding constants for the interaction of U^TRITCN with ^Cy5p97 and its mutants (technical replicates N ≥ 3 ± S.D.).

	K_D (nM)			k_on (×10⁶ M⁻¹s⁻¹)			k_off (s⁻¹)			K_i (nM)
	ATP	ADP	ATPYS	ATP	ADP	ATPYS	ATP	ADP	ATPYS	ATP
WT	302 ± 51	636 ± 96	177 ± 32	1.6 ± 0.3^*	n.d.	1.9 ± 0.3^*	0.48 ± 0.01	n.d.	0.33 ± 0.01	110 ± 20
R155H	6.3 ± 0.1^*	n.d.	n.d.	53 ± 1	n.d.	n.d.	0.332 ± 0.001	n.d.	n.d.	n.d.
A232E	4.6 ± 0.2^*	50 ± 11	4.6 ± 0.2^*	54 ± 1	3.3 ± 0.7^*	61 ± 1	0.25 ± 0.01	0.165 ± 0.003	0.28 ± 0.01	3.8 ± 0.6
T262A	3.5 ± 0.1^*	n.d.	n.d.	60 ± 1	n.d.	n.d.	0.210 ± 0.001	n.d.	n.d.	n.d.
Mixed 2	n.d.	n.d.	n.d.	n.d.	n.d.	n.d.	n.d.	n.d.	n.d.	17 ± 2

Indicates parameters calculated from other measurements using K_D = k_off/k_on. n.d. = not determined. See also Figure 5 and Figure S3.