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Table 4 mmCSM-PPI-predicted binding affinity change upon residue mutation

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

Chain(s) Mutation(s) Average distance (Å) Individual ΔΔGBinding (Kcal/mol) Predicted ΔΔGBinding (Kcal/mol) Effect
H L219A
V225A
L233A
9.75  − 1.39
 − 0.22
 − 0.43
 − 1.15 Decreasing affinity
H K234A
L238A
6.16  − 2.15
 − 1.09
 − 2.88 Decreasing affinity
M L94A
L163E
4.84  − 1.61
 − 1.19
 − 2.09 Decreasing affinity
  1. Using the 3D structure of the wild-type complex as input file, the tool display details about the mutated chains, mutated residues, average distance of the mutated residue from its closest interacting partner, individual binding free energy change in Kcal/mol, average (predicted) binding free energy change in Kcal/mol, and the impact of each mutation on the binding affinity of the complex