All three protein systems were selected due to their key-role in the life-cycle of the SARS-CoV-2 virus (as discussed in §2). The protein structures were initially sourced from PDBs (see Table ). All mutations in the initial crystallographic structures were back-mutated using the "Rotamers" tool in UCSF Chimera. Following this, ligands and other unwanted molecules were removed from the structures. The 3-dimensional conformers of the selected ligands were sourced from PubChem () and inserted into the system. Five protein-ligand systems were built in total. All systems are detailed in Table and each of the proteins and ligands are shown visually in Figure . For each of our protocols and systems, the ligand was initially placed 20 A away from the surface of the protein. A distance of 20 A was chosen to minimise sampling bias that would arise from the initial position of the ligand due to long-range protein-ligand interactions. Thus, if the ligand was initially placed 3 A from the binding site, it would immediately form interactions with the protein in that region and therefore most likely bind to that site. By distancing the ligand we ensure that it stochastically diffuses around the protein before establishing its initial contact.