Table 4.
Occupancies for hydrogen bond interactions between the three residues in 14-3-3γ that contributed most to the negative total enthalpic energy and the phosphate oxygens of Ser19 in the phosphorylated THp peptide fragments.
| 14-3-3γ residuea | Ser19 oxygenb | Hydrogen bond occupancy (%)c | |
|---|---|---|---|
| THp-(Phe14-Ala26) | THp-(Ala11-Asp22) | ||
| Arg132 (HH22) | O2P | 100.0 | 93.0 |
| Arg132 | (HH12) O1P | 100.0 | 92.9 |
| Arg132 (HH12) | O2P | 40.7 | 44.1 |
| Arg132 (HH22) | O1P | 24.7 | 16.1 |
| Arg57 (HH12) | O3P | 100.0 | 89.0 |
| Arg57 (HH22) | O1P | 100.0 | 89.4 |
| Arg57 (HH12) | O1P | 61.3 | 62.7 |
| Tyr133 (HH) | O2P | 100.0 | 93.0 |
a
Given in parentheses are hydrogens in the residue; HH12 and HH22 are amine hydrogens in the arginine side chain, whilst HH refers to the hydroxyl hydrogen in tyrosine
b
O1P, O2P and O3P correspond to the phosphate oxygens in THp-(Ser19)
c
Percentage of the last 50 ns of 14-3-3γ:THp simulation time in which the interaction partners formed a hydrogen bond interaction (characterized by a distance < 3.5 Å between the non-hydrogen atoms and a donor-hydrogen-acceptor angle > 120 degrees).