At present, the rinrus-generated models do not outperform the others but there are several avenues that could be used to improve the former. These include addition of a second interaction sphere, or the use of a seed that is larger than just the ligand, containing some nearest-neighbor residues. A recent development in rinrus is an option to use a form of pairwise symmetryadapted perturbation theory (SAPT), as a means to decompose the interaction energy between a protein and individual residue main chains or side chains. (It is not entirely clear why the "functional group" version of SAPT is necessary in this capacity. Other pairwise forms of SAPT could probably be used instead. ) Thus, it is probably possible to further refine the rinrusbased construction of binding-site models.