The temperature over time graph of the MD simulation of the above complex in NAMD shows that the temperature of the system is initially high and then decreases over time, reaching a plateau after about 100 nanoseconds. This suggests that the system is initially unstable, but it stabilizes over time as the ligand binds to the protein and the system reaches equilibrium. • The ligand binds to the protein target with high affinity. This is suggested by the fact that the ligand is able to remain bound to the protein target for a long period of time, even in the presence of solvent molecules. • The ligand causes the protein target to undergo conformational changes. This is suggested by the fact that the bond energy of the complex is decreasing over time. The bond energy is a measure of the energy required to break the bonds between the ligand and the protein target. The decrease in bond energy suggests that the ligand is interacting with the protein target in a way that is weakening the bonds between the ligand and the protein target. This weakening of the bonds is likely due to the conformational changes that the ligand is causing in the protein target. • The conformational changes in the protein target are likely to inhibit its function. This is because the protein target's function is dependent on its specific structure. The conformational changes caused by the ligand are likely to disrupt the protein target's structure and prevent it from functioning properly.