A set of 117 structurally distinct compounds reported as chymase inhibitors with their diverse experimentally known inhibitory activity (IC 50 ) data was compiled from the literature such as life science journals [14] [15] [16] [17] [18] [19] [20] 55, [66] [67] [68] . All of the inhibitory activities were obtained using the same biological assay method [14] . To form a training set, 20 compounds with distinctive structural motif and wide activity range (0.46 to 5900 nM) were selected. For all compounds in the training set, energy minimization process was performed with CHARMM forcefield. Poling algorithm was applied to generate a maximum of 255 diverse conformations with the energy threshold of 20 kcal·mol −1 above the calculated energy minimum for every compound in the dataset. These conformers were generated using Diverse Conformer Generation protocol running with Best/Flexible conformer generation option as available in Accelrys Discovery Studio v2.5 (DS), Accelrys, San Diego, CA, USA. This method ensures the best coverage of conformational space by performing a more rigorous energy minimization in both torsional and cartesian space by using poling algorithm.