The initial coordinates for the WT CM complex were taken from the crystal structure of Bacillus subtilis chorismate mutase enzyme bound with Bartlett's inhibitor (a transition state analogue inhibitor) from the protein data bank (PDB code: 2CHT) . The imported structure contains several missing hydrogen atoms which were added by Leap module of Amber 20. Three different variants of the Bacillus subtilis chorismate mutase enzyme, i.e., R90A, R90G and R90K/C88S variants were produced by mutating Arg90 residues using pdb4amber module of Amber 20. The parameters for the TSA inhibitor and substrate chorismate were generated by using antechamber module of Amber20 for GAFF2 parameters for a QM optimized geometry at HF/6-31G(d,p) level of theory. Thereafter, all complexes were solvated in a truncated octahedron box of TIP3P water molecules with 12 Å cutoff from the protein boundary . An appropriate number of Na+ ions were added to neutralize the total charge of the system. Since crystal structure of the CM was with TSA, we used the same active site conformation to dock chorismate substrate using Autodock Vina implemented in UCSF Chimera .