Molecular recognition through the noncovalent association of biomolecules is of central importance in biology and pharmacology. Developing reliable computational methods for estimating binding thermodynamic parameters is therefore of great practical value. However, considerable uncertainty remains regarding the external entropy that is associated with the reduction in the external (positional and orientational) degrees of freedom upon complex formation. Here, we present a novel statistical mechanical method for computing the external entropy by extending the energetic approach we have developed for unimolecular processes to association processes. We find that, in contrary to what is postulated in most of the previous methods, intrinsic couplings between the internal and external degrees of freedom of bound complex cannot in general be neglected in the determination of the external entropy. Nevertheless, there exists the best choice of the external coordinates with which those couplings are minimized. With such a choice of the external coordinates, the lowest upper bound of the external entropy is obtained from a tractable expression, which serves as an estimate of the external entropy. Our method can be implemented in a straightforward manner with molecular dynamics simulations, and its applicability is demonstrated through the application to the barnase-barstar complex.