MOESM1 of Homology modelling, molecular docking, and molecular dynamics simulations reveal the inhibition of Leishmania donovani dihydrofolate reductase-thymidylate synthase enzyme by Withaferin-A

Additional file 1: Figure S1. The structures of ligands: (A) Withaferin-A, (B) Methotrexate, (C) DHFA drawn using Chemdraw ultra version 12.0 software. Figure S2. Sequence identity between Hu DHFR and Ld DHFR-TS. Asterisks indicate identical amino acids. Dots and colons indicate conserved amino acid substitutions. Dashes indicate gaps. Figure S3. Sequence identity between Hu TS and Ld DHFR-TS. Asterisks indicate identical amino acids. Dots and colons indicate conserved amino acid substitutions. Dashes indicate gaps. Figure S4. Sequence identity between Ld DHFR-TS and T.cruzichain A. Asterisks indicate identical amino acids. Dots and colons indicate conserved amino acid substitutions. Dashes indicate gaps. Figure S5. Ramachandran Plot: (A) Modelled Ld DHFR-TS and (B) reference T. cruzi DHFR-TS obtained using PROCHECK. Figure S6. Local quality estimate of (A) modelled Ld DHFR-TS and (B) reference T.cruzi DHFR-TS obtained from Swiss model. Figure S7. Secondary structures of (A) modelled Ld DHFR-TS and (B) reference T.cruzi DHFR-TS obtained from PDB sum. Table S1. Features of the generated Ld DHFR-TS model from Swiss model. Table S2. Ramachandran plot Statistics from PROCHECK results for modelled Ld DHFR-TS protein and reference T. cruzi DHFR-TS protein. Table S3. Drug likeness properties of WA from molsoft