Table 4: Cluster of hot spot residues on ABL1 interface of interaction.
| Chain | Residue | KFC2-A* | KFC2-B** | Partner |
| SH3 domain | ||||
| a | PHE 72 | 0.31 | 0.31 | RAD51a |
| a | GLU 98 | 1.37 | 0.07 | RAD51a |
| a | TRP 99 | 1.63 | 0.31 | RAD51a |
| a | TRP 110 | 0.92 | 0.29 | RAD51a |
| Tyrosine kinase domain | ||||
| a | LEU 327 | 0.34 | 0.32 | RAD51a |
| a | ARG 328 | 0.25 | 0.07 | RAD51a |
| a | TRP 430 | 1.34 | 0.20 | RAD51a |
| a | TYR 435 | 0.49 | 0.26 | RAD51a |
| a | MET 437# | 1.15 | 0.15 | RAD51a |
| a | ILE 443# | 1.20 | 0.19 | RAD51a |
| a | LEU 451# | 1.34 | 0.33 | RAD51a |
| a | TYR 456# | 1.77 | 0.38 | RAD51a |
| a | MET 458 | 0.81 | 0.14 | RAD51a |
| a | GLU 459 | 1.33 | 0.14 | RAD51a |
*Hot spot model based on shape specificity features; **Hot spot model based on biochemical features such as intermolecular hydrogen bonds; #Polymorphic residues that may greatly affect the free energy binding of FANCD2 to RAD51a.