And so once we form these three individual chains these three individual chains are held together by disulfide bonds. And now the active side takes the proper confirmation and the oxyanine hole that is used to stabilize that tetrahedral intermediate takes on that perfect form so that once the active side is formed it can actually fit that substrate intermediate. And once the reaction takes place the tetrahedral intermediate can be stabilized by that fully formed oxyanion hole. So once again, we see that Trypsin cleaves the peptide between the peptide bond between the arginine 15 and the isolucine 16 producing this active pie Chimetrypsin. Now, this active Pychiamatripsin goes on, reacts with another pikmatripsin and that removes two dipeptides to produce a total of three individual chains. And these three chains, which are held together by disulfide bonds basically constitute that fully functional, fully active Chimotrypsin molecule we call Alpha Chimetrypsin.