We tested the performance of our PET parameters when modeling protein binding events by simulating the binding of a hevein, a lectin with chitin-binding specificity from Hevea brasiliensis, to the PET crystal film described above. To do so, we simply placed the hevein such that its center-of-mass was about 14 Å away from the film surface, with its chitin-binding domain facing the PET residues. The protein topology was generated using CHARMM36m force field. The system was subsequently solvated in CHARMM with TIP3P water molecules and neutralized with a total ionic strength of 0.15 M of KCl, including counterions. Equilibration of the additive system, conversion to Drude, and production runs of additive and Drude systems were carried out as described below. For the Drude systems, the protein topology was generated using the latest Drude-2019 parameters.