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In the allosteric binding site, hydrophobic interaction was the main binding force. The Asn142, Val145, Leu146, Pro152, and Phe179 residues of Stp1 were found to play a critical role in the binding of corilagin with Stp1. In this study, we used MD simulation to reveal the ligand-protein interactions, providing a theoretical basis. This research work, thus, lays down the foundation for the development of new Stp1 inhibitors to be utilized in the future.We propose a method to maintain the symmetry condition of the refractive index with res