<p>Reproducible molecular dynamics simulations and binding free energy analysis of the CZS-241–FABP5.</p>

(F) RMSD profiles from duplicate molecular dynamics (MD) simulations showing that the CZS-241–FABP5 complex remained stable with fluctuations below 3 Å throughout the simulation. (G) Rg analysis indicating stable global compactness of the CZS-241–FABP5 complex with only minor conformational fluctuations during MD simulations.

(H) SASA analysis showing slight variations, suggesting limited changes in the binding microenvironment upon ligand association. (I) Time-dependent evolution of the distance between CZS-241 and the key interacting residue THR56, illustrating transient fluctuations followed by convergence to a stable binding distance. (J) Hydrogen bond analysis demonstrating persistent intermolecular hydrogen bonding between CZS-241 and FABP5, with an average of approximately three hydrogen bonds maintained during the simulation.(K–L) RMSF profiles indicating low residue-level flexibility (<3 Å for most residues), consistent with a stable ligand–protein complex.