Table 1.

Average per-residue energy^[a] contributions for key^[b] residues in the protein and the ligand.

Residue	CDR[c]	H bond[d]	vdW[e]	electrostatic	Polar desolvation	Nonpolar desolvation	Total
Protein
Trp33	H1	Y	−4.2	−2.4	1.6	−0.5	−5.5
Tyr98	H3	Y	−4.6	−3.8	4.1	−0.8	−5.0
Asp91	L3	Y	0.6	−16.7	13.5	−0.1	−2.5
His35	H1	Y	−0.1	−3.4	1.2	0.0	−2.4
Asn97	H3	Y	−2.8	−2.6	4.2	−0.3	−1.5
Ser50	H2	Y	−0.1	−2.1	0.8	0.0	−1.5
Tyr96	L3	Y	−1.0	−0.8	1.0	−0.1	−0.9
Asn58	H2	Y	−0.6	−0.7	0.7	−0.1	−0.6
Phe95	H3	N	−3.7	−0.2	0.5	−0.4	−3.8
Val99	H3	N	−1.9	−0.3	0.7	−0.1	−1.5
Tyr50	L2	N	−1.9	0.4	0.3	−0.2	−1.5
Pro100	H3	N	−1.2	0.4	−0.3	0.0	−1.2
Pro94	L3	N	−1.0	−0.2	0.3	−0.1	−1.1
Tyr49	L2	N	−0.9	−0.2	0.2	0.0	−0.9
Tyr32	L1	N	−1.1	0.2	0.4	−0.1	−0.6
Tyr52	H2	N	−0.5	−0.3	0.4	−0.1	−0.5
Gly96	H3	N	−0.8	−0.6	0.9	0.0	−0.5
subtotal			−25.8	−33.3	30.5	−2.9	−31.5
Ligand
A	–	Y	−10.7	−29.7	27.5	−1.9	−14.9
B	–	N	−5.4	−11.0	11.9	−0.5	−5.1
E	–	Y	−7.4	−1.8	5.5	−1.4	−5.1
D	–	N	−2.8	−1.2	3.3	−0.6	−1.3
C	–	Y	−3.6	−0.6	3.4	−0.3	−1.0
F	–	N	−0.6	7.4	−6.5	−0.1	0.1
subtotal			−30.6	−36.9	45.1	−4.8	−27.2

^[a]In kcalmol⁻¹.

^[b]Residues that contribute greater than 0.5 kcalmol⁻¹ to the total binding energy.

^[c]Complementarity determining regions.

^[d]Intermolecular hydrogen bonds observed, based on a distance cut-off of 3.5 Å.

^[e]vdW: van der Waals.