Table 1.
NMR and refinement statistics for protein structures.
| Bcd1p120–303 | |
|---|---|
| NMR distance and dihedral constraints | |
| Distance constraints | |
| Total NOE | 4186 |
| Intraresidue | 1115 |
| Inter-residue | 3071 |
| Sequential (|i – j| = 1) | 1087 |
| Medium range (|i – j| ≤ 4) | 694 |
| Long range (|i – j| ≥ 5) | 1290 |
| Total dihedral angle restraints | 280 |
| ϕ | 138 |
| ψ | 142 |
| Total RDCs | 111 |
| Structure statistics | |
| Violations (mean and s.d.) | |
| Distance constraints (Å) | 0.039 ± 0.036 |
| Dihedral angle constraints (°) | 0.889 ± 0.699 |
| Max. distance constraint violation (Å) | 0.24 ± 0.04 |
| Max. dihedral angle violation (°) | 2.79 ± 0.48 |
| Deviations from idealized geometry | |
| Bond lengths (Å) | 0.0114 ± 0.0003 |
| Bond angles (°) | 1.2036 ± 0.0305 |
| Impropers (°) | 1.3914 ± 0.0716 |
| Average pairwise r.m.s. deviationa (Å) | |
| Backbone | 0.74 ± 0.16 |
| Heavy | 1.36 ± 0.20 |
aPairwise r.m.s. deviation (residues 123–301) was calculated among 20 refined structures.