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Table 3 mCSM-PPI2 binding affinity change prediction upon residue mutation

From: Computer-aided molecular modeling and structural analysis of the human centromere protein–HIKM complex

Chain(s) Position Wild-type residues Mutant residues ΔΔGAffinity (Kcal/mol) Effect
H 219 LEU ALA  − 1.387 Decreasing affinity
H 225 VAL ALA  − 0.22 Decreasing affinity
H 233 LEU ALA  − 0.427 Decreasing affinity
H 234 LYS ALA  − 2.149 Decreasing affinity
H 238 LEU ALA  − 1.091 Decreasing affinity
M 94 LEU ALA  − 1.615 Decreasing affinity
M 163 LEU GLU  − 1.19 Decreasing affinity
  1. The wild-type structure is required as input, while the output displays the mutated chains, position of each mutated residue, the wild-type residues, mutants, binding free energy change in Kcal/mol and the effect of each mutation on the binding affinity of the protein to its interacting partner