Fig 1.
Representative picture of modeled wild type MGMT protein docked to minor groove of DNA depicts a stable interaction between Ser151 of enzyme with thymine base, attaining stability with the help of two hydrogen bonds shown in the figure as dotted arrows.
Fig 2.
Illustrative representation of drastic conformational variability that a mutant structure (arrow specifies the site of an mutated residue) undergoes when compared wild type protein structure.
The snapshots were retrieved at every 5 ns interval along the 30 ns simulation.
Fig 3.
(a) Protein RMSDs for wt and Mu MGMT structures at 300 K. wt is shown in black and Mu in green.
(Insets A and B) shows the relative structures at the point of RMSD jump. (b) MGMT residue RMSF along the MDS and the arrow pointing out to the region showing maximum fluctuation. (c) The RMSD vs. Atomic units. Plot showing highly unstable Mu curve in red.
Fig 4.
MGMT protein shown with the domains assembled into functionally important clusters that surround the active site.
Fig 5.
Three dimensional time dependent Phi/Psi distribution showing the change in the Gibbs free energy by the mutation in the Clusters 3 and 4 (black = wt, Red = Mu).
Fig 6.
Intra protein hydrogen bond profile of wt and Mu MGMT protein over time at 300K.
Fig 7.
(a) The motion of principle EV overlaid sequentially.
Black and green colour represents wt and Mu respectively (b) RMSF of all atoms of both vectors.
Fig 8.
(a) Two dimensional representation of the motion of both structures along the first two principal eigenvectors, Black and green represent the wt and Mu MGMT respectively.
(b) FEL of both the motions generated separately. (c) Separate two dimensional representations of PCA of both wt and Mu MGMT with the inset of three most stable structures at different point of time.