Docking is a computationally inexpensive technique which generates a variety of configurations or poses by placing the ligand into a static structure of the apo-protein and subsequently scoring each generated candidate. It can be performed at high speeds by neglecting conformational changes in proteins which might normally occur on binding. This often results in sacrificing accuracy-making it difficult to distinguish binders from non-binders. Of course, there are also flexible docking approaches but these usually neglect protein strain and typically do not demonstrate dramatically better performances. Instead, docking can often be used to understand the conformational space of the ligand and provide some initial insight on how a ligand may fit in the binding site. Several studies have shown that docking does not reliably find experimental binding modes of ligands. In view of these limitations, here, we use docking to generate a variety of configurations to hopefully provide coverage of the entire binding site and all reasonable binding mode possibilities, and use these as starting points for our simulations.