## 3 Results and Discussion
### Normal Mode Analysis  
Normal mode analysis (NMA) was conducted utilizing the iMODS server to assess the stability and mobility of atoms within the complex. The deformability of the target under investigation relies on the potential for deformation at any of its amino acid residues. Each normal mode is linked to an eigenvalue that characterizes the rigidity of motion, with its magnitude directly linked to the energy needed to alter the structure. Lower eigenvalues indicate greater ease of deformation [25; 32; 51; 72; 73]. The B-factor corresponds to the root mean square deviation (RMSD) because B-factors reflect how different parts of the structure vibrate relative to each other. Low B-factors for atoms signify their membership in the stable regions of the structure, while atoms in the flexible portions exhibit higher B-factors [74; 75]. The NMA results are shown in the figure below. The variance is indicated by purple-colored bars and cumulative variance by green-colored bars, it is inversely related to the eigenvalue. The outcomes for both Mol3/Mol5/RXB-Ca3 docking complexes can be seen in Figure 7A. Figure 7B displays the deformability graph for these complexes, with the peaks on the graph corresponding to areas of deformability within the complexes.  
Figure 6: The 3D structure shows the most favorable AKT1 complexes after docking, with the inhibitors (Mol3 and Mol5) displayed in stick form and colored using default atom colors.  
Figure 7: _Cont_.  
Significantly, both Mol3 and Mol5 yielded comparable outcomes when interacting with the Ca3 target. Therefore, only one set of results is presented for both in Figure 7. In Figure 7C, the B-factor of the complex provides an average root mean square value, reflecting the motion of individual atoms within the complex. The majority of Ca3 atoms, in the presence of Mol3 and Mol5, exhibited B-factor values around 0.2, indicating a higher likelihood of rigid segments and affinity compared to RXB, where the B-factor line exceeded 0.2. The eigenvalues for the RXB-Ca3 complex were notably higher in comparison to those of the Mol3/Mol5-Ca3 complexes, as shown in Figure 7E. This suggests that more energy would be required to deform the RXB-Ca3 complex when compared to the Mol3/Mol5-Ca3 complexes. This finding is a positive indicator, suggesting a potential swift clearance of Mol3 and Mol5 from the body. The variance map exhibited minimal variances at the individual level and substantial cumulative variances for both scenarios. In the complex depicted in Figure 7G, the covariance map reveals the interactions between pairs of residues, indicating whether they undergo correlated (red), uncorrelated (white), or anti-correlated (blue) motions. It isewident that the Mol3/Mol5-Ca3 complexes exhibit a higher degree of correlation in comparison to the RXB case. The elastic network model establishes connections between atom pairs using springs, with each dot on the graph symbolizing a spring connecting a specific pair of atoms. These dots are shaded to reflect their stiffness, with darker gray indicating stiffer springs, as seen in Figure 7F. The findings from the elastic network analysis reveal a greater number of strongly connected atom pairs in comparison to the RXB case. The results from the iMODS simulation imply that the Mol3/Mol5-Ca3 complexes exhibit stability.