TABLE 1.
NMR refinement statistics for the HR domain (OutC-HRF3)
| NMR distance and dihedral constraints | |
| Distance constraints | |
| Total NOE | 1954 |
| Intra-residue | 652 |
| Inter-residue | |
| Sequential (|i − j| = 1) | 381 |
| Medium range (|i − j| ≥ 2 ≤ 4) | 170 |
| Long range (|i − j| ≥ 5) | 751 |
| Hydrogen bonds (experimental measured) | 28 |
| Hydrogen bonds(observed in >50% of structures) | 64 |
| Total dihedral angle restraints (TALOS) | 76 |
| ϕ | 38 |
| ψ | 38 |
| Structure statistics | |
| Violations (mean ± S.D.) | |
| Distance constraints (>0.5) (Å) | 0 |
| Dihedral angle constraints (>5) (°) | 0 |
| Deviations from idealized geometry | |
| Bond lengths (Å) | 0.005 ± 0.0001 |
| Bond angles (°) | 0.671 ± 0.011 |
| Impropers (°) | 0.748 ± 0.024 |
| Average pairwise r.m.s.d. (Å)a | |
| Backbone | 0.46 ± 0.11 |
| Heavy | 1.26 ± 0.20 |
| R.m.s.d. from the mean structure (Å)a | 0.33 ± 0.07 |
| Residues in allowed regionsb | 98.3% |
| Residues in disallowed regions | 1.7% |
a Pairwise r.m.s.d. and r.m.s.d. from the mean structure were calculated among the 20 lowest energy structures from 50 refined structures (amino acid residues 91 to 157).
b Structure quality was analyzed with MolProbability over structured regions (amino acid residues 91–157). One residue in a tight β-turn between β5 and β6 (Pro140) is in a disallowed region.