Table 3.
Comparison of the number of different amino acid residues making HHB and NNB contacts with the ligands in at least one of the FFR models’ snapshots during the docking simulations
| Model | Ligand | Best FEB (HHB) | Best FEB (NNB) | Residues sum (HHB+NNB) | Best Pose (HHB) | Best Pose (NNB) | Residues sum (HHB+NNB) |
|---|---|---|---|---|---|---|---|
| WT | ETH | 52 | 74 | 80 | 38 | 54 | 62 |
| TCL | 25 | 46 | 46 | 12 | 24 | 24 | |
| PIF | 23 | 35 | 35 | 22 | 32 | 34 | |
| I16T | ETH | 34 | 47 | 49 | 23 | 37 | 37 |
| TCL | 19 | 34 | 34 | 9 | 24 | 24 | |
| PIF | 23 | 28 | 28 | 17 | 22 | 22 | |
| I21V | ETH | 31 | 52 | 56 | 21 | 37 | 37 |
| TCL | 18 | 40 | 40 | 11 | 24 | 25 | |
| PIF | 22 | 20 | 22 | 21 | 22 | 24 | |
| 1ENY | ETH | 2 | 4 | 5 | 1 | 3 | 4 |
| TCL | 0 | 1 | 1 | 0 | 2 | 2 | |
| PIF | 2 | 2 | 2 | 0 | 2 | 2 | |
The total number of receptor residues that made HHB and NNB contacts with the ligands and the union of these residues (HHB+NNB) for the Best FEB (column 5) and for the reference or Best Pose (column 8).