**Table A1.**

*Predicted amino acid residues.*

#### **Figure A1.**

*(a) The* Z*-score of the modeled* Lm*TR (represented in dot) estimated to be 11.68 which is within the range of experimentally determined proteins by X ray method. (b) Verify 3D plot of the modeled protein structure,* Lm*TR. This shows 91.65% of its amino acid residues with an average 3D-1D score greater than or equal to 0.2, which is a positive inference to the expected 80% of amino acids with 3D-1D score above or equal to 0.2.*

#### **Figure A2.**

*Ramachandran plot of the modeled* Lm*TR protein structure. The percentage of residues in the most favored region (red) was 93.6% which is favorable for the protein's stereochemistry. The percentage of residues in the allowed region (yellow) was 6%. Only 0.2% of protein residues (Phe45) showed probable stereochemical hindrance or collision.*

#### **Figure A3.**

*A 3D geometry of the generated pharmacophore. The nitrogen on the bicyclic ring of CNQB with the oxygen from the nitro group on its purine ring derivative contributed a hydrogen bond acceptor HBA (red sphere). The oxygen from the nitrogen dioxide group on the conjugated benzene in addition to the nitrogen on the fivemember ring of PNTPC also contributed to HBA. Both had an aromatic ring (blue ring) as a common feature (blue ring in yellow 3D sphere) which contributed to hydrophobic interactions and the alkene feature shared amongst them generated the same hydrophobicity.*

#### **Figure A4.**

*(A) AUC score of 0.99 for the pharmacophore model. Determined at 1, 5, 10, and 100% of the selected database were the AUC and EF values as shown. The median is shown by dotted lines. If the curve is closer to the median it would suggest poor model. (B) AUC score of 0.702 generated for validating the docking system used. It verified the correlation between virtual screening performance and binding site descriptors of protein targets model (*Lm*TR).*

#### **Figure A5.**

*(a) 2D schematic diagram of co-crystallized FAD (PDB ID: 2JK6) and FAD docked in* Lm*TR superimposed together. Similar hydrogen bonding residues include Ser14, Gly15, Arg287, and Thr335. Similar hydrophobic residues in addition confirm the predicted active site. (b) Ligand alignment of co-crystalized FAD and FAD docked in* Lm*TR.*
