Considering the top-scoring results (from both the Vinardo and dkoes scoring functions) in the presence of the heme cofactor, the 5XE1 and 5EK2 protein targets appear most frequently in the two tables above. Unfortunately, selfdocking of the native ligands deviates somewhat from their corresponding crystallographic coordinates. For 5XE1, both Vinardo and dkoes produce a heavy-atom RMSD of approximately 1.0 Å relative to the crystallographic pose, with approximate binding energies of -10.24 kcal/mol (Vinardo) and -7.76 kcal/mol (dkoes). I consider these deviations relatively large, suggesting that the calculated binding energies for the self-docked native ligands may be inaccurate and likely underestimate the true binding affinities.