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The anisotropic feature of charge transfer reactions in realistic proteinscannot be ignored, due to the highly complex chemical structure ofbio-molecules. In this work, we have performed the first large-scalequantitative assessment of charge transfer preference in protein complexes bycalculating the charge transfer couplings in all 20*20 possible amino acid sidechain combinations, which are extracted from available high-quality structuresof thousands of protein complexes. The charge transfer database quantitativelyshows distinct features of charge transfer couplings among millions of aminoacid side-chains combinations. The knowledge graph of charge transfer couplingsreveals that only one average or representative structure cannot be regarded asthe typical charge transfer preference in realistic proteins. This data drivenmodel provides us an alternative route to comprehensively understand thepairwise charge transfer coupling parameters based structural similarity,without any require of the knowledge of chemical intuition about the chemicalinteractions.

Charge Transfer Database for Bio-molecule Tight Binding Model Derived from Thousands of Proteins