File:Mutated Phage 327 on Peptidoglycan.png

In an attempt to decrease the binding affinity value between Phage P2 and S. pyogenes, we used MODELLER to model 450 different versions of Phage P2. MODELLER is used to predict a protein’s three-dimensional structures when the program is provided with an alignment of known sequences. The program then calculates many models that satisfies its restraints. MODELLER created 450 different probable models of the mutated Phage P2. Thereafter, we docked all 450 versions with the receptor of S. pyogenes via Autodock Vina. The average binding affinity was -4.90 kcal/mol, the maximum was -3.51 kcal/mol, and the minimum was -6.60 kcal/mol; the minimum occurred at Phage P2 Mutant #327, indicating that though it may not bind to S. pyogenes as well as it would to L. lactis, it has significantly improved its binding affinity from the natural form of Phage P2.