Table 3.

The amino acid residues’ contribution to binding free energies and interfaces for the complexes of inhibitors with trypsin. Amino acid residues making the greatest contribution to binding free energy are highlighted in light green.

	Reactive site					Weak contact site
BPTI (3OTJ)	Pro12	Cys13	Lys14	Ala15	Arg16	Cys37	Arg38	Lys45
ΔGbind, Kcal/Mol	−2.1	−4.8	−8.1	−3.3	−3.2	−1.8	−2	1.1
ΔSASA, Ǻ2	33	51.6	165.2	36	110.8	27.2	97.2	0
BPTI mutant (3BTT)	Pro12	Cys13	Thr14	Ala15	Arg16	Cys37	Arg38	Lys45
ΔGbind, Kcal/Mol	−2.1	−4,6	−4.4	−3.5	−3.5	−1.7	−1.6	0.3
ΔSASA, Ǻ2	37.9	55.5	101.4	36.5	118.3	28.6	94.6	0
SHPI-1 (3M7Q)	Arg12	Cys13	Lys14	Gly15	Tyr16	Cys37	Gly38	Glu45
ΔGbind, Kcal/Mol	−3.4	−2.9	−8.4	−2.2	−4.5	−1.4	−0.1	−0.5
ΔSASA, Ǻ2	143.8	52	163.6	19.9	88.7	30	0.9	0
InhVJ	Pro12	Cys13	Thr14	Ala15	Tyr16	Cys37	Glu38	Glu45
ΔGbind, Kcal/Mol	−2.1	−4.4	−4.7	−2.6	−5.9	−1.1	−0.2	−8.4
ΔSASA, Ǻ2	50.5	53	106.1	30.5	102.2	37.2	0	37.9