We have already seen ∆G direct results for the different systems in previous sections. Now, we directly compare them to ∆G ESM ACS results obtained through the ESMACS protocol for ADRP-tofacitinib system. The standard ESMACS protocol (denoted as "ESMACS-s" and involves performing an ensemble typically of 25 MD simulations of 4 ns duration starting from a chosen conformation) has been extensively applied to a diverse range of protein-ligand systems and shown to rank ligands with very high precision. In this study, we chose the most stable binding pose (the one with the least RMSD) from the different sub-replicas of the splitting protocol at each binding site as the starting structure for our standard ESMACS calculations. Table and Figure show a comparison of ∆G direct and ∆G ESM ACS-s . We find that both methods achieve strongly correlated results with a correlation coefficient of 0.87.