We recently introduced an alternative approach to equilibrating water in simulations, where translational MC moves allow water to jump between the protein interior and the bulk, while the number of waters in the simulation remains constant, and furthermore showed that this approach can improve both the precision and the accuracy of calculations of protein-ligand relative binding free energies. This MC/MD approach avoids the need of a GCMC/MD method to determine what chemical potential to use for each set of simulation conditions, and it also avoids any bookkeeping and software issues that might result from the time-varying number of water molecules. Although we took several algorithmic measures to speed the MC/MD method, integration of the MC steps with MD nonetheless markedly slowed the simulations in our initial implementation. We have also collaboratively explored the use of nonequilibrium candidate MC (NCMC) moves to increase the acceptance rate of the large translational MC water moves in this approach, but efficiency remains a concern.