Computational dataset for: Mechanism of human hexokinase-2 inhibition by flavonoids - substrate- and product-site discrimination revealed by enzyme kinetics, molecular docking, and molecular dynamics

Supporting computational data for the article: Mechanism of human hexokinase-2 inhibition by flavonoids - substrate- and product-site discrimination revealed by enzyme kinetics, molecular docking, and molecular dynamics. Target macromolecule: human hexokinase-2 (UniProt P52789; 917 residues; 102.4 kDa). Receptor conformations derive from PDB entries 2NZT, 5HG1 and 5HEX (chain A, protein only). The archive contains: (1) per-replicate molecular-dynamics analysis arrays for 14 systems, each simulated in 3 independent replicates of 300 ns, giving 12.6 microseconds of all-atom simulation in total; (2) the analysis scripts that produced every derived figure and table; (3) the docked and induced-fit starting structures, one per simulated system; (4) the numerical source of Tables 1-6 and S1-S10; and (5) the experimental enzyme-kinetics measurements. Simulations used the CHARMM36m force field with TIP3P water at 310.15 K, 100 ns of equilibration followed by 300 ns of production per replicate. MM-GBSA rescoring was repeated at interior dielectric constants of 1, 2, 4 and 5. A full file listing and md5 manifest are included in README.md inside the archive.