we also compare what we call the parallel polarizability α ∥ computed similarly as α iso but with α zz = 0. We immediately see that AmberFD, for all nucleobases, underestimates the parallel polarizability by between 19% -33% of the DFT value, even when only looking at the parallel components. Drude-2017 also systematically underestimates α components, however, their parameterization intentionally scales the polarizability by a factor of 0.85 to account for correlation effects. When accounting for this scaling factor, Drude-2017 deviates from the DFT α iso by no more than 14% and as little as 1%. AMOEBA also reproduces the polarizability exceptionally well for all nucleobases. This is not surprising, as the AMOEBA parameterization was explicitly fit to similar ωB97X-D/aug-cc-pVTZ calculations. While AmberFD underestimates α, it's first order response to electric fields, µ, is instead overestimated. As the sum of each of these two terms (multiplied by the electric fields) constitutes the total energy response, in a way, the inaccuracy in the dipole moment is compensated by a decrease in molecular polarizability. As the fitting procedure outlined in Figure scales the dipole moments prior to fitting polarization parameters, this compensation is indeed the case. Although the two properties themselves deviate from the DFT values, the RRMSE between DFT and AmberFD do perform similar to that from the Drude model (for the fields used here) and their difference narrow when only considering in-plane polarization energies. While Drude-2017 performs better than AmberFD for Adenine and Uracil, the opposite is true for Cytosine and Guanine where the dipole moments from Am-berFD are more accurate. For all cases, AMOEBA performs the best in RRMSE with the only exception being the parallel RRMSE for Guanine.