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. Author manuscript; available in PMC: 2012 Jul 25.
Published in final edited form as: J Chem Inf Model. 2011 Jul 11;51(7):1648–1655. doi: 10.1021/ci200126v

Table 1.

Comparison between MF-FEB Calculations and Experimental Binding Energies a

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
a

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.