Table 1.
Ligands | Experimental | MF-FEB | |
---|---|---|---|
ΔGexp (kcal/mol) | rmsd* (Å) | ΔΔGbinding ( kcal/mol) | |
n-butylbenzene | −6.7 ± 0.02 | 0.9 | −7.8 ± 0.5 |
i-butylbenzene | −6.5 ± 0.06 | 0.9 | −9.5 ± 0.6 |
ethylbenzene | −5.8 ± 0.07 | 1.3 | −8.0 ± 0.2 |
benzofuran | −5.5 ± 0.03 | 0.3 | −6.5 ± 0.4 |
benzene | −5.2 ± 0.2 | 0.8 | −5.2 ± 1.0 |
indole | −4.9 ± 0.06 | 0.7 | −3.9 ± 0.2 |
p-xylene | −4.7 ± 0.06 | 0.6 | −5.5 ± 0.8 |
o-xylene | −4.6 ± 0.06 | 0.3 | −5.3 ± 0.2 |
Inhibitor-lysozyme co-crystal structures were used as the starting poses for the ΔΔGbinding calculations. MF-FEB calculations were performed in triplicate. Root-mean-square deviation (rmsd) reflects the displacement of heavy atom positions between the final equilibrated pose and the starting structure.