Table 1.
NMR and refinement statistics
| AfCcdA(AA) | |
|---|---|
| NMR distance and dihedral constraints | |
| Distance constraints | |
| Total NOE | 622 |
| Intraresidue | 125 |
| Inter-residue | 497 |
| Sequential (|i - j| = 1) | 232 |
| Medium range (2 ≤ |i - j| ≤ 4) | 164 |
| Long range (|i - j| ≥ 5) | 101 |
| Total dihedral-angle restraints | 238 |
| ϕ | 119 |
| ψ | 119 |
| Structure statistics | |
| Violations (mean ± s.d.) | |
| Distance constraints (Å) | 0.147 ± 0.006 |
| Dihedral-angle constraints (°) | 0.352 ± 0.026 |
| Max. dihedral-angle violation (°) | 1.80 |
| Max. distance-constraint violation (A) | 1.07 |
| Deviations from idealized geometry | |
| Bond lengths (Å) | 0.006 ± 0.000 |
| Bond angles (°) | 0.863 ± 0.023 |
| Impropers (°) | 0.704 ± 0.027 |
| Average pairwise r.m.s. deviation (Å)a | |
| Heavy | 1.553 |
| Backbone | 0.971 |
a
Statistics are calculated and averaged over an ensemble of the 15 lowest-energy structures out of 75 calculated structures. The precision of the atomic coordinates is defined as the average r.m.s. difference between the 15 final structures and their mean coordinates. The calculation includes only the structured regions of the protein: residues 4–12, 31–49, 58–77, 84–94, 108–117, 120–130, 137–156 and 165–183.