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I have developed a homology model of a protein with only 15% sequence similarity. Consequently, the AlphaFold homology model lacks high accuracy. To gain insight into the protein’s behavior, I conducted a 1000 ns molecular dynamics (MD) simulation on this model. However, I noticed that the root mean square deviation (RMSD) values consistently hover around ~1.2 nm throughout the simulation, which is relatively high. This suggests that the AlphaFold model may not have accurately captured the true conformation due to the low sequence identity.
For RMSD calculation, I used the following commands:
gmx trjconv -s md_0_1.tpr -f md_0_1.xtc -o md_0_1_noPBC.xtc -pbc mol -center (I selected group 1 (“Protein”) as the group to be centered and group 0 (“System”) for output.)
gmx rms -s md_0_1.tpr -f md_0_1_noPBC.xtc -o rmsd.xvg -tu ns (I chose backbone atoms for both the least-squares fit and the group for RMSD calculation.)
Please suggest what steps I should take next to effectively analyze the simulated protein. Am I going in the right direction?
rmsd_new400.xvg (2.5 MB)