The structural changes that occurred per complex because of ligand binding were further investigated. Thus, the root means square fluctuation (RMSF) was adopted to calculate the residues' dynamic mobility structures following docking. According to the RMSF trajectory plot (Figure ), the protein amino acid residues of the docked complexes are moderately similar in their fluctuation pattern during the simulation. However, Sotorasib (control) showed the highest fluctuation with an RMSF value > 5.6 nm, suggesting that all the selected docked ligands are more stable than the control in the active site of the target receptor. On this plot, peaks indicate areas of the protein that fluctuate the most during the simulation. Particularly, the tails of protein chains (i.e., N-and C-terminal) tend to fluctuate more while observing overall protein parts. In contrast, the secondary structure elements, which includes alpha helices and beta strands, fluctuate less than the loop regions because they are more rigid than the unstructured parts of the protein.