Table 6.
Contribution of the IFN-γ residues/molecules.
| Hydrophobic InteractionsHydrophobic Interactions | |||||||
|---|---|---|---|---|---|---|---|
| Index | Residue | AA | Distance | Ligand Atom | Protein Atom | ||
| 1 | 108 B | ALA | 3.27 | 3929 | 3325 | ||
| 2 |
111 B |
ASP |
2.93 |
3924 |
3379 |
||
| Hydrogen Bonds | |||||||
| Index |
Residue |
AA |
Distance H-A |
Distance D-A |
Donor Angle |
Donor Atom |
Acceptor Atom |
| 1 | 47 A | LYS | 2.14 | 3.05 | 145.92 | 361 [N3+] | 3967 [O3] |
| 2 | 115 B | SER | 1.64 | 2.63 | 159.69 | 3439 [O3] | 3917 [O3] |
| 3 | 115 B | SER | 2.60 | 3.25 | 121.23 | 3957 [O3] | 3437 [O2] |
| 4 |
118 B |
LYS |
2.63 |
3.11 |
108.26 |
3482 [N3+] |
3958 [O3] |
| Salt Bridges | |||||||
| Index |
Residue |
AA |
Distance |
Ligand Group |
Ligand Atoms |
||
| 1 | 55 A | ARG | 5.08 | Carboxylate | 3940, 3965 | ||
| 2 | 118 B | LYS | 3.09 | Carboxylate | 3971, 3960 | ||