Noncovalent interactions play a significant role in determining the Structures of DNA, RNA, and proteins. Among the most prevalent are pi-pi interactions, which Occur as favorable forces between the aromatic Subunits of biochemical molecules. The aromatic side chains of amino acids tryptophan and phenylalanine are commonly modeled with indole and benzene, respectively. We have utilized the MP2 and SCS-MP2 methods with the aug-cc-pVDZ basis Set to Compute several T-shaped interaction energies and parallel displaced (PD) three-dimensional potential energy Surfaces (PESs) at 3.4, 3.6, and 3.8 angstrom vertical separations. At selected minima, CCSD(T) results extrapolated to the complete-basis-set (CBS) limit were obtained. The trend of the T-shaped interactions has been rationalized by considering electrostatic potential maps and symmetry-adapted perturbation theory (SAPT) results. The global minimum has been verified to be the N-H/pi T-shaped configuration with a CCSD(T)/CBS interaction energy of -5.62 kcal mol(-1). For the PD PESs, the MP2 and SCS-MP2 methods predict different minimum configurations. The CCSD(T) method favors the SCS-MP2 PD configuration over the MP2 PD Configuration by 0.18 kcal mol(-1). Among the approximate methods considered here, the SCS-CCSD method extrapolated to the CBS limit incurs only around 2% error compared to CCSD(T)/CBS results and is the most reliable for the interaction energies of the indole-benzene complex. Overall, the extension of aromaticity and the highly positive hydrogen of the N-H bond, both exhibited by indole, enhance the strength of nonbonded interactions with benzene compared to those in the benzene dimer or in the pyridine-benzene complex.