The distributions found by large sampling with random initial conditions from docking software can be useful in reducing the dimensionality of the dihedral angles of a ligand to protein in optimistic binding goals. A primary smeared peak in the energy density of states points to a reduction in the degrees of freedom in describing the ligand and its conformations near that point, such as at 68 and 46. In the case of the peak at 68, 5 of the 9 rotatable dihedral angles do not change much, and also perhaps 2 others. The 'lower half' of the molecule flip flops substantially in several different orientations within this set, and is due to only one degree of freedom angle. This is found by visualizing many of these molecules at ~68 docked score values.