Overall, the AmberFD model is able to reproduce EDA polarization and charge transfer energies, as well as frozen electrostatic, dispersion, and Pauli repulsion energies, exceptionally well, and is able to replicate fundamental differences in stacking and hydrogen bonding interactions. Additionally, the AmberFD model was compared against the CHARMM Drude-2017 and AMOEBA force fields for nucleic acids for various h-bonded, stacked, and multiplet NMR resolved geometries from the Protein Data Bank. This analysis revealed that, while a variety of molecular properties dictate the reproducibility of interaction energies, extra attention should be paid to how one defines frozen electrostatics in a molecular mechanics model in order to be consistent with EDA computations. Finally, our results also reveal that not only can a fluctuating density model mimic DFT polarization and change transfer energies but the sources of these interactions via changes in electron density can also be replicated within the AmberFD model. approximations made in the AmberFD model and a list of all parameters determined by the fitting procedure. Additionally, we include a partitioned list of PDB IDs and residues used in the EDA comparison between force fields, as well as additional violin plots of this analysis for each of the aforementioned PDB query criteria. We also include a secondary example of density differences in AmberFD and DFT for a small duplex simulation in solvent using AmberFD derived forces.