To explore which children of library B retained high-affinity docking to the spanish and European rat resistant mutants, the corresponding mutated amino acids were substituted into the wild-type rat VKORC1 amino acid sequence, alphafold modeled and the docked brodifacoum-cavity transferred from the crystal structure of human VKORC1 complex, as described in methods. DW docking by its "Dock Structures into Docking Cavity" subprogram were then performed by targeting the mutated VKORC1 models with the children of library B. The results were laydown into the same *.dwar file together with those from wild type rat for comparison. Multiple DW filters could be then applied using different thresholds for the rat-and for the human-VKORC1 targets.