In silico screening of mutational effects on enzyme-proteic inhibitor affinity: a docking-based approach

BMC Structural Biology

Table 4 β-Trypsin – BPTI interaction: thermodynamic data and ZD scores for X-ray determined and in silico modeled BPTI-Lys 15 mutants

Mutation^a	ΔG° (kcal/mol)^b	N_sol^xr,c	Best Rank^xr	ZD_best	ZD-s^xr	ZD_sc^xr	ZD_el^xr	ZD_des^xr	ZD-s^xr2,d	N_sol^xr2	Best Rank^xr2	ZD-s^mod,e	N_sol^mod	Best Rank^mod
GLY	-5.73	63	9	51.7	43.2	34.8	-0.9	9.3	42.3	62	13	42.5	62	1
THR	-7.50	80	1	54.3	45.0	35.8	-1.2	10.4	44.4	79	1	45.5	70	1
ASP	-6.54	76	1	54.9	44.7	37.6	-2.2	9.3	44.8	71	1	44.2	78	1
MET	-10.36	79	1	56.8	47.1	36.7	-1.1	11.5	46.1	78	1	45.4	74	1
GLU	-8.59	73	1	58.7	47.7	38.8	-1.2	10.1	47.3	74	1	44.8	76	1
GLN	-8.73	89	1	55.5	44.8	36.4	-0.8	9.2	45.1	84	1	43.9	74	1
HIS	-9.27	88	1	62.5	48.7	38.6	0.2	9.9	49.4	87	1	47.0	77	1
PHE	-11.04	85	1	67.1	51.8	40.1	-0.1	11.8	51.6	85	1	49.0	71	1

^aResidue in which BPTI-Lys 15 was mutated. The PDB entries corresponding to these variants are 3BTG, 3BTT, 3BTD, 3BTM, 3BTE, 3BTQ, 3BTH and 3BTF [28]
^bStandard free energy of association as obtained from the relationship ΔG° = RT ln K_D. Experimental data from Ref [10]
^cHere, and in the following columns, xr refers to the results of docking runs from the experimentally resolved X-ray structures
^dHere, and in the following columns, xr2 refers to the results of docking runs from the experimentally resolved X-ray structures in the absence of interface water molecules
^eHere, and in the following columns, mod refers to the results of docking runs from the in silico modelled structures of the same complexes

ISSN: 1472-6807