These findings seem to be in good agreement with the inhibitor binding modes reported in KLIFS (Table in the original publication, 7 see also Table ). The majority of ligands are in both approaches described to be front cleft binders, occupying mostly AP-GA and AP-FP subpockets (since SE is not defined in KLIFS, AP-SE and FP-SE connections are part of the KLIFS equivalent of the AP and FP subpockets). In contrast, back cleft binders that describe ligands that occupy the back pockets (AP-GA-B1/2 combinations) occur by far less often. While the KLIFS binding mode annotation is based on kinase-ligand interaction fingerprints, the analysis reported here shows that KinFragLib's automated subpocket-based procedure generates reasonable fragments.