TABLE 3.
NMR and refinement statistics
| NMR constraintsa | |
| Distance constraints | 771 |
| Intra-residue | 253 |
| Sequential (|i − j| = 1) | 180 |
| Interchain | 338 |
| Dihedral angle restraints | 120 |
| ϕ | 72 |
| χ1 | 48 |
| Structure statisticsb | |
| Violations (mean ± S.D.) | |
| Distance constraints | 0.07 ± 0.05 Å |
| Dihedral angle constraints | 1.86 ± 1.65° |
| Maximum dihedral angle violation | 4.97° |
| Maximum distance constraint violation | 0.244 Å |
| Deviations from idealized geometry | |
| Bond lengths | 0.0097 ± 0.0001 Å |
| Bond angles | 2.34 ± 0.04° |
| Average pairwise root mean square deviation, 15 structures | |
| Heavy | 0.68 Å |
| Backbone | 0.53 Å |
a Constraints observed were replicated by symmetry to all identical triplets between 2 and 9, see text for details.
b Statistics were calculated over the 72 restrained amino acids in the final structure.