Molecular docking analysis was implemented using the Surflex-Dock module in Sybyl-X2.2.1 (Tripos Inc, St Louis, MO, USA) with the known crystal structure of AXL complexed with ligands (PDB ID: 5U6B). To prepare the protein, hydrogen was added and energy was minimized using Powell's method with the Tripos force field until the root-mean-square derivation (RMSD) values were < 0.05 Kcal/mol·Å. Initial optimization and termination of minimization were set as simplex and gradient, respectively. The new ligands were prepared using Chem3D (PerkinElmer, Waltham, MA, USA). Molecular docking simulations were conducted using the Surflex-Dock mode with the extraction of the original ligand. To generate the active site, a threshold of 0.5 Å and bloat of 0 Å were applied based on the original ligand in the crystal structure. Other parameters were used as default. The results of the docking simulation were validated by comparing the redocked structure to the original pose of the ligand. Molecular interactions between proteins and ligands were further analyzed using Discovery Studio 4.0 Visualizer (BIOVIA, San Diego, CA, USA).

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