Introduction: Our previous studies on binding Gibbs free energies for WT,
I50V single mutant and
I50L/
A71V double mutant showed that
I50V decreases the binding affinity for TMC114, while the double m
Result: The distance between the flap tips (
Ile50Calpha and Ile50'Calpha) and the catalytic aspartates (
Asp25Calpha and
Asp25'Calpha) for WT-1T,
V32I-1T and
M46L-1T HIV-1-
pr/TMC114 shows that the distances in chain-A for all the three complexes are almost overlapped throughout the simulation with an average distance of 13.89, 14.05 and 14.05 A, respectively, which are slightly shorter than those of double binding for the two mutants.