Table 1.
NMR Structural Statistics for AIRE PHD Finger/H3K4me0 Complex
| Protein | |
|---|---|
| NMR distance and dihedral constraints | |
| Distance constraints | |
| Total NOE | 935 |
| Intraresidue | 442 |
| Interresidue | 493 |
| Sequential (|i − j| = 1) | 133 |
| Medium range (|i − j| < 4) | 129 |
| Long range (|i − j| > 5) | 231 |
| Protein-zinc restraints | 34 |
| Hydrogen bonds | 28 |
| Total dihedral angle restraints | |
| φ | 12 |
| ψ | 12 |
| Structure statistics | |
| Violations (mean ± SD) | |
| Distance constraints (Å) | 0.0311 ± 0.00266 |
| Dihedral angle constraints (°) | 0.238 ± 0.151 |
| Max. dihedral angle violation (°) | 0.557 |
| Max. distance constraint violation (Å) | 0.0367 |
| Deviations from idealized geometry | |
| Bond lengths (Å) | 0.0029 ± 0.00018 |
| Bond angles (°) | 0.487 ± 0.0214 |
| Impropers (°) | 0.401 ± 0.028 |
| Average pairwise rmsd (Å)a | |
| Heavy | 0.94 ± 0.093 |
| Backbone | 0.49 ± 0.064 |
a
Number of structures used in rmsd calculations is 20. Pairwise rmsd was calculated among 20 refined structures of the region with residues numbered 295–343.