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

BMC Structural Biology

Table 5 Decomposition of ZD-s in three components for the enzyme-proteic inhibitor complexes. Statistical analysis of the empirical correlations

		ZD_sc				ZD_el				ZD_des				ZD_sc+el				ZD_sc+des				ZD_el+des
	N^a	A^b	B^b	R^c	p(R)^d	A	B	R	p(R)	A	B	R	p(R)	A	B	R	p(R)	A	B	R	p(R)	A	B	R	p(R)
HRI-ANG	24	35.5	-0.5	0.82	< 0.0001	10.2	-0.3	0.73	< 0.0001	-2.0	-0.1	0.34	0.105	45.6	-0.9	0.93	< 0.0001	33.4	-0.6	0.73	< 0.0001	8.1	-0.4	0.90	< 0.0001
BN-BS_1^e	11	56.4	-1.8	0.91	0.0001	-6.4	-0.8	0.56	0.073	-20.3	2.2	0.62	0.042	30.2	-0.9	0.87	0.0005	41.1	-1.3	0.61	0.045	-1.1	-1.1	0.46	0.150
BN-BS_2^f	11	56.8	-1.8	0.89	0.0002	-9.0	-0.6	0.36	0.282	-19.4	1.7	0.53	0.092	35.5	-1.0	0.81	0.0023	26.3	-1.0	0.50	0.1139	-11	-0.3	0.1	0.7628
BPTI-βtTRYPS	8	31.9	0.9	0.67	0.071	-2.9	0.3	0.57	0.137	6.6	0.6	0.79	0.021	29.0	1.2	0.75	0.032	38.5	1.5	0.82	0.013	3.7	0.9	0.85	0.008

^aNumber of analyzed interactions, i.e. three docking runs for each variant.
^bCoefficients of the linear regression equation fitting the experimental data. In detail, the equation is in the form Y = A + BX, where Y is the experimental ΔG° expressed in kcal/mol, A (kcal/mol) is the intercept, B (kcal/mol) is the slope and X is the corresponding ZD-s component.
^cLinear correlation coefficient.
^dLinear correlation coefficient probability.
^eData referring to the protonated form of H102^Bn.
^fData referring to the neutral form of H102^Bn.

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