Table 3.

Comparison of experimental K_D values (nM) of the LP1 peptide and mutant ligands with the energies (kcal/mol) calculated both from the combinatorial mutation calculations and from the MD simulations^a.

	KD(exp’t)	ΔB.E.(calcComb)b	ΔB.E.(calcMD)c	ΔEint(calc)d
WT	18.5	0.00	0.00	0.00
L11Q	24.5	−5.63	−13.49	−22.66
Y9F	49.5	−0.18	−11.00	−12.88
W5F	12000	8.81	5.66	10.78
W5K	No binding	−4.62	6.30	8.02
R15Q	37.7	12.92	−8.63	0.91

^aRelative to WT, for the 2 ns-equilibrated complex structures after mutation

^bCalculated binding energy from combinatorial mutation calculation (from Table 2)

^cCalculated binding energy after MD; delphi solvation energy is included; B.E. (WT) = −68.25 kcal/mol

^dIntermolecular interaction energies, calculated for the residues within 5 Å of the ligand; E_int (WT) = −61.62 kcal/mol