As the modelled change in active state probability can be related to local changes in ligand binding site conformations, the seeded MD trajectories can be mined to select protein conformations associated with functional states. In turn, the resulting conformations can be used for further virtual screening, to find ligands that could induce the same binding site rearrangements. For example, the increased activity of compound 1 over compound 2 was related to differences in the preferred conformations of F280 during the MD simulations. This insight was not apparent from available X-ray crystallographic data since in existing crystal structures for 1 and 2 this residue is modelled in the "down" conformation (PDB IDs: 1T4J and 1T48 respectively) . The simulations carried out here revealed an alternative "up" rotamer, which is predominantly adopted in inactive states of PTP1B. Therefore targeting the F280 "up" rotamer offers a potential focus for further drug discovery campaigns.