TABLE 1.
Summary of structural statistics and restraints
Structural statistics were calculated using the Protein Structure Validation Suite (43).
| Distance restraints | |
| Total NOE | 755 |
| Intra-residue | 172 |
| Inter-residue | 583 |
| Sequential (|i − j| = 1) | 253 |
| Medium-range (|i − j|<5) | 329 |
| Long-range (|i − j|>5) | 1 |
| H-Bond Restraints (|i − j|<5) | 27 |
| Total dihedral angle restraints | 104 |
| φ | 51 |
| ψ | 53 |
| 3J HNHA coupling constant restraints | 36 |
| Total restraints | 922 |
| Total no. of restricting constraints per restrained residuea | 15.4 |
| Structure statisticsb | |
| Violations | |
| r.m.s.d. of distance violation/constraint (Å) | 0.06 |
| r.m.s.d. of dihedral angle violation/constraint | 0.22° |
| Max dihedral angle violation | 3.3° |
| Max distance constraint violation (Å) | 0.47 |
| r.m.s.d. from ideal geometry | |
| Bond length (Å) | 0.021 |
| Bond angles | 1.1° |
| Average pairwise r.m.s.d (Å) | |
| Ordered backbonec | 0.6 |
| All Backbone | 3.6 |
| Ordered heavy atomsc | 1.1 |
| All heavy atoms | 4.0 |
| Ramachandran statisticsd | |
| Most favored regions | 99.8% |
| Allowed regions | 0.2% |
| Disallowed regions | 0% |