Table 1.

Binding affinities of the lead compounds and the Nesbuvir (standard) in the molecular docking studies, along with the molecular interactions observed with the HCV NS5B Palm Site-II allosteric residues.

Compounds	Binding Affinities with NS5B PS-II (Kcal/mol)	Hydrogen Bonds with PS-II Residues	Hydrophobic Interactions with PS-II Residues	Other Interactions, e.g., Sulfur-X, Pi-Sulfur, and Halogen Interactions with PS-II Residues
BF-9	−16.09	CYS316, SER365, CYS366,SER368, TYR415	LEU204, LEU 314,VAL321, ILE363,SER365, CYS366, LEU384	CYS316, CYS366, ARG200, TYR555
BF-12	−15.75	CYS366, SER368, LEU384,PRO197, LEU384, TYR383, ARG200	VAL201,LEU314, VAL321, CYS316, PRO417, HIS467, CYS366, LEU384	HIS467, MET414,
BF-13	−15.82	CYS316, ARG200, SER368,	LEU204, LEU 314, VAL321, ILE363, SER365, CYS366, LEU384, TYR415 MET414, PRO197, TYR448	CYS366, ARG200
Nesbuvir	−15.42	CYS316, SER368, ASP319, ARG200, LEU314	CYS366, SER365, LEU384, PHE193, CYS316, LEU204, VAL321, SER365, TYR448	MET414, CYS316