(i) AP fragments generally have a higher number of HBD and HBA, as this part of the inhibitor usually forms hydrogen bonds to the hinge region and acts as anchor to position the ligand. 9 (ii) The logP values vary widely in all subpocket pools. X, FP, and SE fragments have the lowest median logP, i.e. they tend to be more hydrophilic. For SE, this can be explained by the solvent-exposure of this part of the kinase binding site. The same holds for FP, which is also partially solvent-exposed. While the AP fragments usually do provide the hydrogen bonds as anchor, they are often surrounded by a hydrophobic pocket, which could explain the comparatively high logP of these fragments. (iii) AP, FP, and SE fragments tend to be larger in terms of the number of heavy atoms, with AP having the highest median value.