Table 2.

Results of in silico site-directed mutagenesis docking simulations for AChE.^{a, b}

Mutation	Organophosphate Bindingc	Carbamate Bindingc	Predicted Mechanism	Same Side Chain Class	Molecular Weight Difference (g/mol)	Susceptibility Prediction
W117Y	No change	No change	None	Yes	23	Yes
W117A	No change	No change	None	No	115	Yes
G152A	No change	No change	None	Yes	14	Yes
G152S	Decrease	Decrease	Steric hindrance	No	30	No
A235S	No change	No change	None	No	16	Yes
F326C	No change	No change	None	No	44	No
F368A	Decrease	No change	Electrostatic	No	76	No
F368W	Decrease	No change	Electrostatic	Yes	39	Yes
F369L	Decrease	Decrease	Steric hindrance	No	34	No
F369S	Decrease	Decrease	Steric hindrance	No	60	No
F369W	Decrease	Decrease	Steric hindrance	Yes	39	Yes

^aRaw data results are presented (Supplementary Data File).

^bAmino acids represented by acronyms is listed (Table 1).

^cBinding -log of the 50 % inhibition concentration (pIC₅₀) of mutant model relative to binding pIC₅₀ of wild-type model.