We performed 50 ns MD simulations of all protein-ligand complexes of KPC-2 to evaluate the stability of protein-ligand interactions. The ligand 1 root mean square deviation (RMSD) (see the SI Fig. ) shows that the ligand stays bound to KPC-2 throughout the 50 ns MD simulation. Some of the earlier fluctuations of the RMSD are explained by the fact that the simulation starts with the ligand having π-π interactions with Trp105, which fluctuates for the first 10-15 ns. After this, the ligand settles into a π-π interaction with Trp105 for the duration of the MD simulation. Other ligand RMSDs are shown in SI Fig. . Generally, all ligands remain stably bound to the protein.