For globular proteins, interior atomic packing (arising from short-range, local interactions) of side-chains has been shown to be pivotal in the structural stabilization of the protein-fold. On the other hand, the electrostatic harmony (non-local, long-range) of the overall fold has also been shown to be essential for its stabilization. Packing anomalies include steric clashes, short contacts, holes and cavities while electrostatic disharmony refer to unbalanced partial charges in the protein core (particularly relevant for designed protein interiors). While the clash-score of [http://molprobity.biochem.duke.edu/ Molprobity] identifies steric clashes at a very high resolution, the Complementarity Plot combines packing anomalies with electrostatic imbalance of side-chains and signals for either or both.