. 2014 Jan 9;9(1):e84808. doi: 10.1371/journal.pone.0084808

Table 1. Equilibrium dissociation constants (K_D) for binding of NNIs to Δ21 and fold-shifts in K_D for association to Δ55 and Δ21-Δ8 determined by SPR.

		K_D (nM)^a	Fold shift from Δ21^b
Site	Inhibitor	Δ21	Δ55	Δ21-Δ8
Thumb site I	B	11.7	1.0	1.6
Thumb site II	GS-9669	1.6	5.5	1.7
Thumb site II	Lomibuvir	3.3	9.0	2.0
Thumb site II	Filibuvir	38.2	9.3	2.4
Palm site I	A-837093	0.04	433	n/a^c
Palm site II	HCV-796	174.0	n/a^c	n/a^c

^a Sensorgrams for the binding of NNIs to Δ21, Δ55 and Δ21-Δ8 along with a table of equilibrium and kinetic parameters of interaction are shown in Figure S2 and Table S1 in File S1, respectively.

^b Fold shift in K_D for association of NNIs to Δ55 and Δ21-Δ8 was calculated relative to the K_D determined for binding towards Δ21.

^c Where K_D values could not be obtained either due to complex binding kinetics (Palm Site II inhibitor binding to Δ55 and Δ21-Δ8) or super-stoichiometric binding (Palm Site I inhibitor binding to Δ21-Δ8), numerical values have been replaced by n/a (not applicable).

Table 1. Equilibrium dissociation constants (KD) for binding of NNIs to Δ21 and fold-shifts in KD for association to Δ55 and Δ21-Δ8 determined by SPR.

Table 1. Equilibrium dissociation constants (K_D) for binding of NNIs to Δ21 and fold-shifts in K_D for association to Δ55 and Δ21-Δ8 determined by SPR.