Table 2.

Computational alanine-scanning results for adenine/rMrgA (energies in kcal/mol).

	I.E.(WT)a	ΔI.E.(Ala)a
Asn88	−17.787	17.161	41%
Asn146	−12.819	12.275	29%
Met92	−4.741	2.844	7%
Phe83	−1.545	1.433	3%
His225	−1.505	1.349	3%
Leu174	−0.665	0.432	1%
Tyr95	−0.422	0.344	0.8%
Ile96	−0.450	0.333	0.8%
Phe178	−0.298	0.265	0.6%
Cys150	−0.494	0.207	0.5%
Thr170	−0.273	0.168	0.4%
Met91	−0.321	0.161	0.4%
Arg147	−0.360	0.091	0.2%
Pro85	−0.393	0.086	0.2%
Leu177	−0.102	0.066	0.2%

^aThe intermolecular interaction energy (IE) for the wild type (WT, no mutation) is shown for all residues within 5 Å of the ligand. After mutating the residue to Ala and minimizing, we recalculated the IE of the ligand to this Ala, IE(Ala).

^bThe percentage change in binding of the mutant relative to the calculated total binding of WT is shown in the last column.