Multiple residues were found to bind to the membrane. To quantify the significance for individual residues in protein-membrane interactions, we used free energy perturbation (FEP) simulations to determine the relative affinity of multiple mutants to the membrane when compared to the wild type. Four aromatic residues in the binding region stood out for mutation to alanine or aspartate-W12, F15, W238, and F241. Alanine mutants were developed specifically to test the importance of individual amino acids in the binding, while aspartate mutants probe the impact of charge. Several double mutants were also tested, to investigate if combining mutants would result in a greater than additive increase in binding free energy. The full set of mutants tested is W12A, W12D, F15A, F15D, W238A, W238D, F241A, F241D, W12AW238A, W12DW238D, F15AF241A, F15DF241D, W238AF241A, and W238DF241D. A custom python script was used to create dual topology structures within VMD.