Figure 1: Redock alignment CHIKV macrodomain with ligand ADP ribose - substrate - in sticks (left) and SARS-Cov2 macrodomain (right)
Table 1
Table 1: Docking studies with CHIKV nsp3 Macrodomain
Table 1: Docking studies with CHIKV nsp3 Macrodomain
Table 2: Molecular Dynamic studies with CHIKV nsp3 Macrodomain
Table 3: Virtual Hits obtained in nsp3 macrodomain docking studies
Table 4: Frequency of identified h-bond in the Clustered complex along the 100ns of simulation
The non-interacting residues were kept hidden. Symbols in table: y = hydrophobic interactions; h = H-bonds; s = salt-bridges;a = aromatic interactions; hal = halogen interactions.
Supplementary Table 2: Interacting residues from the 5 top scored molecules by subset in CHIKV macrodomain
Figure 1: Redock alignment CHIKV macrodomain with ligand ADP ribose - substrate - in sticks (left) and SARS-Cov2 macrodomain (right)
Figure 2: Up - ADPr site 2D representation with ligand at the center of picture, surrounded with interacting (labed) residues by PoseView in ProteinPlus server. Left: ADPr-macrodomain (CHIKV); Right ADPr-macrodomain (SARS-Cov2)/ Down - Sequence alignment of CHIKV and SARS-Cov2 nsp3 using structural information
Sharma18-Miltefosine (in CHIKV macrodomain)
Henß16-Suramin (in CHIKV macrodomain)
Molecular Dynamics (MD)
Figure 3: 2D protein-ligand interaction profile representation of top scored molecules from docking calculations.
Figure 4: RMSD (root mean square deviation) trajectory of receptor heavy chain atoms in 100ns Molecular Dynamics simulation
Figure 5: RMSF (root mean square fluctuation) trajectory of receptor heavy chain atoms in 100ns Molecular Dynamics simulation
Figure 6: Left: Hydrophobic surface representation of NothiasScaglia15-18 in the receptor binding pocket (by Chimera). Right: The interacting residues (by PLIP).
Tables at a glance
Figures at a glance