Alongside using long equilibrium datasets to reweight binding affinities from docking, augmenting simulations using spectroscopic methods has been a method that has gained considerable attention. Tightly integrating spectroscopic methods and MD simulations allows a practitioner a complete structural and dynamical view of a protein's conformational ensemble. Successful use of these methods has been long demonstrated using X-ray Crystallography , and has recently been extended to consider NMR and FRET .