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Table 5 MutaBind2 mutation-induced change in binding affinity prediction

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

Chain(s) Mutation(s) ΔΔGBinding (Kcal/mol)
H L219A 1.95
H V225A 0.28
H L233A 0.8
H K234A 0.13
H L238A 2.18
M L94A 1.88
M L163E 0.7
  1. The input requires the PDB structure of the protein complex with a minimum of two distinct chains
  2. A negative and positive ΔΔGbind (kcal/mol) value correspond to stabilizing and destabilizing mutations, predicted to increase and decrease the binding affinity, respectively
  3. An all-positive value for the MutaBind2 output denotes a destabilizing effect on the protein–protein interaction