Attractive electrostatic protein-protein interactions (PPI) necessarily involve identifying oppositely charged regions of the protein surface that interact favorably. This cannot be done reliably if one only considers a single protein in isolation unless there are obvious charge "patches" that result in extreme molecular dipoles. Prior work [J. Pharm. Sci. 2019, 108, 120-132] identified three monoclonal antibodies (MAbs) that displayed experimental behavior ranging from net repulsive to strongly attractive electrostatic interactions. The present work provides a systematic computational approach for identifying the origin of diverse PPI, in terms of which sets of amino acids or individual amino acids are most influential, and determining if there are different patterns of pairwise amino acid interaction "maps" that result in different behaviors. The charge was eliminated computationally, one by one, for each charged residue in the wild-type sequences, which resulted in predicted changes in the second osmotic virial coefficient. The results highlight interaction "maps" that correspond to cases with qualitatively different net electrostatic PPI for the different MAbs and solution conditions, as well as key sets of residues that contribute to strongly attractive PPI. A more computationally efficient method is also proposed to identify key amino acids based on Mayer-weighted interaction energies.