Supplementary molecular docking tables and figures for Neisseria gonorrhoeae carbonic anhydrases: binding affinities, interaction profiles, MD stability metrics, and normal mode analyses

This deposit contains the supplementary tables and figures supporting the molecular docking and post-docking analyses of a certain thesis. The materials summarise docking outcomes, short molecular dynamics (MD) sanity checks, interaction profiling, and normal mode analyses for phytochemical ligands screened against Neisseria gonorrhoeae carbonic anhydrases across orthosteric and candidate allosteric binding sites. The docking workflow focused on a 10% representative ligand panel selected from a larger phytochemical library and evaluated against three binding contexts: the 1KOQ orthosteric site, the 3KS3 orthosteric site, and a 3KS3 candidate allosteric pocket. Docking was performed using AutoDock Vina, with downstream analyses used to contextualise binding affinity, selectivity, and stability trends. Contents Supplementary Tables ST1: Summary statistics of the docked 10% ligand panel, including ligand counts per site and mean/median binding free energies (ΔG_dock, kcal/mol). ST2: MD-based stability metrics for the simulated 3KS3 binding pockets, reporting mean and maximum Cα RMSD (nm) and final potential energy (kJ/mol). ST3: Mean counts of key non-covalent interaction types (hydrogen bonding, hydrophobic, π–π, cation–π, ionic, π–anion, van der Waals) derived from short MD trajectories of top-ranked ligand–site complexes. ST4: First three normal mode eigenvalues (eig1–eig3) for top-ranked ligand–site complexes, reflecting relative flexibility and collective motions. Supplementary Figures SF1: Orthosteric and allosteric affinity and selectivity plots, including cross-site ΔG comparisons and distribution summaries. SF2: Representative docking poses of selected ligand–site complexes across 1KOQ and 3KS3 binding sites, visualising key interaction patterns. SF3: MD-based stability visualisations for 3KS3 binding pockets (mean Cα RMSD and final potential energy). SF4: Normal mode eigenvalue profiles per binding site, summarising relative flexibility trends. These supplementary materials are intended to support transparency, interpretation, and reuse of the docking analyses, and they complement the full raw docking datasets and scripts archived separately.