| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T197 |
0-198 |
Sentence |
denotes |
The integral extent of the residual dynamic criterion is achieved by assessing the variations arising from shifts of each of the protein residues that majorly feature the most flexible chain frames. |
| T198 |
199-324 |
Sentence |
denotes |
Hence, we validated the residual fluctuations by calculating the mean fluctuation for stable trajectories of each simulation. |
| T199 |
325-480 |
Sentence |
denotes |
The RMSF evaluation of all the protein residues were achieved in order to check the residues that may have tend towards an enhancement in the RMSD results. |
| T200 |
481-723 |
Sentence |
denotes |
Compelling fluctuations existed in terminal residues and in various loops along β sheets and coils of the spike protein (residues 852-1000) to about 0.47 nm and spike-rutin (residues 62–90, 400–520 and 675–730) to about 0.65 nm (Figure 2(B)). |
| T201 |
724-1043 |
Sentence |
denotes |
Similarly, in case of main protease and itself in complex with rutin showed fluctuations in the terminal residues and in some regions of β sheet with some coils and loops in main protease (residues 136-148) to about 0.37 nm and main protease-rutin (residues 39-52, 150-156) to about 0.37 nm, respectively (Figure 3(B)). |
| T202 |
1044-1279 |
Sentence |
denotes |
Also, we noticed that residues 270 to 350 in spike protein and 160 to 190 in main protease showed comparatively reduced discrepancy in RMSF values, which were the corresponding binding segment of both the complexes after MD simulation. |
| T203 |
1280-1562 |
Sentence |
denotes |
Interestingly, the binding region for spike-rutin and main protease-rutin before MD simulation were found to be the same after simulation, suggesting as a strong binding interaction of the rutin towards spike protein and main protease and indicating stability of both the complexes. |
