Figure S1. Two dimensional representation ofthe residues interacting to heme in binding site of (A) Tt,(B) Ns, (C) Secondary structure assignment of Tt (in1U55.pdb), (D) Ns (in 2O0C.pdb).

Figure S2. RMS plots from MD simulations. RMSDof (A) apo Ns, (B) Ns complexed to heme, (C)Ns complexed to BAY 58-2667, (D) apo Tt, (E)Tt complexed to BAY 58-2667, (F) apo sGC Homosapiens, (G) Homo sapiens complexed to Heme, (H)Overlaid RMSF of 70 ns MD simulation of apo sGC Homosapiens (straight line) on the sGC Homo sapienscomplexed to Heme (dashed line), (I) Overlaid RMSF of time frameswithin 0–20 ns (black), 20–40 ns (red),25–45 ns (green), and 50–70 ns (blue) from MDsimulation of apo sGC, (J) Overlaid RMSF of 0–20 ns(black), 20–40 ns (red), 25–45 ns (green),and 50–70 ns (blue) time frames from MD simulation ofsGC complexed to heme.

Figure S3. Sequence alignment of two sGChomolog of Ns and Tt.

Figure S4. Distance variations between centersof mass of the group of residues numbered 4–8 (black),30–45 (red) and 135–150 (green) from the H6 (with aminoacids 100–115) in sGC Homo sapiens.

Figure S5. Solvent accessible surface area(SASA) and volume of heme binding site varies during 20 ns MDsimulation.

Table S1. The interacting residues of hemebinding site with the ligands obtained from docking experiments,*Metabolite, Italic protonated ligand.

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