Table 1.
NMR and refinement statistics for protein structures
| Protein | |
|---|---|
| NMR distance and dihedral constraints | |
| Distance constraints | |
| Total NOE | 2380 |
| Intra-residue | 1117 |
| Inter-residue | 1263 |
| Sequential (∣i−j∣=1) | 581 |
| Medium range (∣i−j∣<4) | 311 |
| Long range (∣i−j∣>5) | 371 |
| Hydrogen bonds | 112 |
| Total dihedral angle restraints | |
| φ | 131 |
| ψ | 131 |
| Structure statistics | |
| Violations (mean and s.d.) | |
| Distance constraints (Å) | 0.0779±0.0008 |
| Dihedral angle constraints (deg) | 0.7545±0.0703 |
| Maximum dihedral angle violation (deg) | 7.718 |
| Maximum distance constraint violation (Å) | 0.478 |
| Deviations from idealized geometry | |
| Bond lengths (Å) | 0.0044±0.0001 |
| Bond angles (deg) | 0.6595±0.0055 |
| Impropers (deg) | 0.4181±0.0067 |
| Average pairwise r.m.s.d. between 10 structures (Å) | |
| Heavya | 1.38±0.22 |
| Backbonea | 0.71±0.14 |
| Heavyb | 1.26±0.20 |
| Backboneb | 0.55±0.11 |
| Ramachandran plot appearance | |
| Most favoured regions (%) | 71.5 |
| Additional allowed (%) | 25.9 |
| Generously allowed (%) | 2.3 |
| Disallowed regions (%) | 0.2 |
| aThese calculations included residues 221–242 and 258–379. | |
| bThese calculations included residues 221–228, 231–232, 240–242, 258–269, 276–283, 291–300, 305–311, 322–331, 333–338, 340–350 and 364–379. | |