T4L99A is an extensively studied test system with a wealth of experimental data, commonly used in the development of free energy methods. A point mutation (L99A) results in a protein cavity which binds a range of small aromatic ligands. The T4L99A system, while relatively simple, does have some complexities that make it particularly interesting for the testing of enhanced sampling methods. For example, as the binding site is completely occluded from the solvent, MSMD simulations struggle to map the site using classical MD owing to the timescales required for diffusion. Secondly, some ligands, such as toluene, bind to T4L99A in multiple orientations with a significant kinetic barrier preventing them from readily interchanging. Here, using benzene as a probe, we first test GCNCMC as a site finding tool and compare its ability to map the occluded binding pocket to classical MSMD simulations.