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

Beni-Suef University Journal of Basic and Applied Sciences

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

Chain(s)	Position	Wild-type residues	Mutant residues	ΔΔG^Affinity (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

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