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Beni-Suef University Journal of Basic and Applied Sciences

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
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