NMR and refinement statistics for unphosphorylated and phosphorylated peptides.
| Phosphorylated | Unphosphorylated | |
|---|---|---|
| NMR distance and dihedral constraints | ||
| Distance constraints | ||
| Total NOE | 161 | 117 |
| Intraresidue | 92 | 54 |
| Interresidue | ||
| Sequential (|i – j| = 1) | 56 | 53 |
| Medium-range (|i – j| < 4) | 13 | 10 |
| Structure statistics | ||
| Violations (mean and S.D.) | ||
| Distance constraints (Å) | 0.13 ± 0.19 | 0.09 ± 0.15 |
| Maximum distance constraint violation (Å) | 1.40 | 1.29 |
| Deviations from idealized geometry | ||
| Bond lengths (Å) | 1.29e-3 ± 0.18e-3 | 1.15e-3 ± 0.12e-3 |
| Bond angles (°) | 0.42 ± 0.01 | 0.45 ± 0.01 |
| Impropers (°) | 0.27 ± 0.003 | 0.27 ± 0.002 |
| Average pairwise r.m.s. deviation (Å) | ||
| Heavy (residues 5–10, 20 structures) | 0.84 ± 0.16 | 0.82 ± 0.34 |
| Backbone (residues 5–10, 20 structures) | 1.61 ± 0.16 | 1.69 ± 0.60 |