Comprehensive Data on Molecular Dynamics, Docking Results, and Free Energy Decomposition for β-Lactamase Enzyme Complexes

This dataset provides a comprehensive collection of results from molecular dynamics simulations, docking studies, and free energy decomposition for β-lactamase enzymes. It includes:<b>Plots, Tables, and Charts</b>: Detailed visualizations of the molecular dynamics analyses for the 1HTZ, 4S2I, and 4ZAM β-lactamase complexes. These include Root Mean Square Fluctuation (RMSE), Solvent Accessible Surface Area (SASA), Radius of Gyration, and Root Mean Square Deviation (RMSD), offering insights into the stability and flexibility of the enzymes when bound to study compounds.<b>Docking Results</b>: Molecular docking data showing the interactions between various inhibitors and the β-lactamase enzymes (1HTZ_TEM, 4S2I_CTX-M, 4ZAM_SHV). These results provide insights into the binding affinity and effectiveness of inhibitors designed to counteract β-lactamase-mediated antibiotic resistance.<b>Free Energy Decomposition</b>: A detailed table breaking down the free energy components for the 1HTZ_TEM, 4S2I_CTX-M, and 4ZAM_SHV β-lactamase complexes, contributing to understanding the binding energetics of inhibitors.<b>Supplementary Tables</b>: Additional data tables providing further statistical analyses and supplementary information to support the molecular dynamics and docking studies.