A potentially stronger interaction between the ligand and the protein arises from numerous dispersion contacts. As shown in Fig3-4 above, the apolar ring of the ligand is "sandwiched" by three aromatic residues (PHE212, PHE268, and HIE337), while other apolar regions form additional dispersion interactions with PHE161, PHE224, and other nearby residues. Together, these contacts confer a relatively strong binding affinity of approximately -11.71 kcal/mol, already accounting for the ligand's DFT-based conformational strain energy.