Electrostatics plays an important role in regulating interactions between biological macromolecules. The electrostatic potential map of the protein-ligand complex BRAF-dabrafenib at pH 7 shows remarkable variations at different slicing depths within the binding pocket, whereas the values within protein stay rather constant (see Figure ). The dielectric constant map equally points out variations inside the binding pocket in contrast to the protein interior (compare Figure ). In particular, the tri-methyl moiety of dabrafenib is pointing outside the binding pocket and lies outside the cutoff where an epsilon value of 80 is reached (see Figure closeup on binding pocket). This indicates that it is completely solvent accessible and should be considered as solvated.