Utilizing tools in PyCPET, we examine the dynamics of 𝐸𝐸 "⃗ (𝑟𝑟) and contextualize them across these studies. We computed streamline distributions of 3-D 𝐸𝐸 "⃗ (𝑟𝑟) around the peptide C-N bond (Fig. ) along MD simulations of an HIV-1 protease (PDB 1KJ4). The four representative 𝐸𝐸 "⃗ (𝑟𝑟)s are shown in Figure , labeled HP-1, HP-2, HP-3, and HP-4 in the order of population. All four fields have a dominant direction perpendicular to the C-N bond, but PyCPET teases out changes in the field curvature. In HP-3 and HP-4, the field component along the C-N bond is not ubiquitous in the studied volume, and this component is not present at all in HP-1 and HP-2. Krzemińska and Robiero both showed that there is an overall 𝐸𝐸 "⃗ (𝑟𝑟) present in both directions observed in our 3-D analysis: the perpendicular one favoring electron transfer from the catalytic Asp residue to the C-N bond through a water molecule required for both gem-diol and oxyanionbased mechanisms, and the field along the C-N bond favoring the charge separation required for a concerted mechnism . Here we not only confirm this, but also show that 𝐸𝐸 "⃗ (𝑟𝑟) is not static across protein dynamics -a reality which traditional methods fail to capture. The change in 𝐸𝐸 "⃗ (𝑟𝑟) structure along dynamics supports the possibility of multiple mechanisms being favored in the enzyme, where HP-1 and HP-2 solely support charge transfer to the bond and likely a gem-diol/oxyanion based mechanism, while HP-3 and HP-4 sustain an electric field required for a cyclic concerted mechanism, where both charge transfer and C-N bond breaking are simultaneous . In addition, we find that these fields are heterogeneous across an entire 3-D field volume, highlighting the importance of a multidimensional approach to understanding electrostatic preorganization.