Dynamic profiling and binding affinity prediction of NBTI antibacte-rials against DNA gyrase enzyme by multidimensional machine learning and molecular dynamics simulations

The chemical libraries used in this study comprised of 199 and 133 structurally diverse novel bacterial topoisomerase inhibitors (alias NBTIs), with experimentally determined in vitro antibacterial potencies against Staphylococcus aureus DNA gyrase (IC₅₀=0.007-50 µM) and Escherichia coli DNA gyrase (IC₅₀=0.020-100 µM), respectively (named as NBTI_SA and NBTI_EC), were compiled from the literature as *.sdf file format. The chemical structures comprising both NBTI libraries were initially sketched by using ChemDraw Professional 20.1.1 suite and subsequently energetically minimized utilizing Discovery Studio’s integrated Merck Molecular Force Field (MMFF) module. Moreover 4D ligands ensembles of both libraries ready to be used for multidimensional QSAR modeling are available, as well.