The estimated electrostatic contributions from both protein and solvent to the calculated activation free energies for the deprotonation of DHAP and GAP were reported in a previous computational study of wild-type and I170A, L230A, and I170A/L230A variants of TIM, where the changes in the total electrostatic interactions are the sum of many small changes in individual interactions, including the electrostatic contributions from N10, K12, H95, S96, and E129. These computational results are consistent with a small weakening in the electrostatic interactions for these enzyme variants.