TABLE 2.

Association and dissociation rates for the IAS derivatives to the different enzyme-substrate complexes for wild-type RT and the Lys103Asn mutant^a

RT type and inhibitor	Rate for:
	RT			RT/TP			RT/TP/dNTP
	Ki (nM)	kon (s−1M−1)	koff (s−1)	Kibin (nM)	konbin (s−1M−1)	koffbin (s−1)	Kiter (nM)	konter (s−1M−1)	koffter (s−1)
Wild-type RT
RS1202	0.3	(11 ± 1) × 105	(4 ± 0.5) × 10−4	1.6	(3 ± 0.5) × 105	(5 ± 0.5) × 10−4	1.2	(2 ± 0.3) × 105	(3 ± 0.3) × 10−4
RS1588	0.3	(6 ± 0.5) × 105	(2 ± 0.3) × 10−4	2.7	(2 ± 0.5) × 105	(6 ± 0.5) × 10−4	n.d.	n.d.	n.d.
RS1866	2.2	(4 ± 0.6) × 105	(9 ± 1) × 10−4	2.3	(3 ± 0.2) × 105	(7 ± 1) × 10−4	n.d.	n.d.	n.d.
RS1980	0.3	(6 ± 0.5) × 105	(2 ± 0.3) × 10−4	0.4	(7 ± 0.5) × 105	(3 ± 0.3) × 10−4	3	(1 ± 0.3) × 105	(3 ± 0.3) × 10−4
EFV	30	(0.1 ± 0.02) × 105	(4 ± 1) × 10−4	.30	(0.1 ± 0.02) × 105	(4 ± 1) × 10−4	4	(0.4 ± 0.02) × 105	(1.6 ± 0.3) × 10−4
NVP	400	(0.04 ± 0.01) × 105	(16 ± 1) × 10−4	500	(0.03 ± 0.01) × 105	(15 ± 1) × 10−4	375	(0.04 ± 0.01) × 105	(15 ± 1) × 10−4
Lys103Asn mutant RT
RS1202	1.3	(1.9 ± 0.2) × 105	(2.5 ± 0.5) × 10−4	5	(5 ± 1) × 104	(2.5 ± 0.5) × 10−4	5	(5 ± 1) × 104	(2.5 ± 1) × 10−4
RS1588	0.3	(7.1 ± 0.5) × 104	(2 ± 0.2) × 10−5	3	(4.5 ± 0.5) × 104	(1.5 ± 0.2) × 10−4	n.d.	n.d.	n.d.
EFV	n.a.	n.a.	n.a.	n.a.	n.a.	n.a.	200	(0.6 ± 0.01) × 104	(1.2 ± 0.1) × 10−3
NVP	3,300	(0.03 ± 0.005) × 104	(1 ± 0.2) × 10−3	3,300	(0.03 ± 0.005) × 104	(1 ± 0.2) × 10−3	n.d.	n.d.	n.d.

^aEnzyme-substrate complexes and kinetic constants are as defined in Fig. 1. Numbers are the mean values of three independent experiments and (standard deviations). n.d., not determined; EFV, efavirenz; NVP, nevirapine; n.a., not applicable (the affinity of EFV for the RT_K103N and RT_K103N/TP complexes was too low to be measured).