Before the details of the docking analysis are presented for the molecules there are some comments. Binding of a ligand to a protein is often quantified by a single number using docking software from a top scoring pose. The physical process of a ligand-protein interaction can not be defined by a single number, although being a good quantifier of interaction. The potential interaction energy well that a small molecule occupies geometrically when bound has structure: depth, width, and high dimensionality coming from the many body atomic interactions of atoms from 2 molecules (electrostatic, van der Waals, torsional rotations, longer range hydrogen bonding, electronic quantum structure, and so on). There are generally different and complicated high-dimensional well shapes of energy minima and, as a result, different bound states reflected in docking software by different ligand conformations and perturbations (wiggles) of these. The stability of these bound states is dictated by characteristics of the local potential well, translating to evaluation of the disassociation constant k_D. This information is required for accurate estimation of the on-/off-population of a ligand to a protein and its inhibitory effect.