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Table 2 BeAtMuSiC-predicted change in binding affinity as a result of mutation

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

Chain(s) Mutation(s) ΔΔGbind (kcal /mol) SA (in partners) SA (in complex)
H L219A 2.91 51.27% 0.52%
H V225A 0.42 42.55% 38.91%
H L233A 0.89 13.46% 13.46%
H K234A 1.70 44.29% 8.41%
H L238A 1.84 49.72% 9.84%
M L94A 1.85 36.25% 2.07%
M L163E 1.23 45.05% 20.71%
  1. With the main input being the protein–protein complex structures, the output reports the mutated chains, the specific mutations, change in binding free energy (Kcal/mol) and solvent accessibility, both in partner and in complex. Solvent accessibility depicts the solvent-accessible surface ratio in the structure, based on DSSP computation