The three figures below illustrate the most important intermolecular interactions between the 8ABX protein target and the top-scoring, low-toxicity natural compound CNP0211967.1. The first figure depicts hydrogen bonding interactions between the ligand and the ARG334 residue. DiscoveryStudio, the program that I often use for visualizations, suggests a suboptimal interaction involving the hydroxyl proton of the ligand and an N-H proton of ARG334, that arising from the ligand's internal hydrogen bonding orientation in isolation. This underscores the potential value of local refinements with flexible geometries at higher levels of theory to correct the rigid-body-based docking approach. For instance, the ligand's hydroxyl groups could reorient their protons to form new internal hydrogen bond, while positioning the two oxygens in proximity to the residue's N-H groups without any undesired steric or electronic clashes of the hydrogens. Such local geometric refinements would further enhance protein-ligand binding.