Table 1. NMR constrains and refinement statistics.
| NOE restrains (total) | 1,349 |
|---|---|
| Intra-residue | 541 |
| Inter-residue | 808 |
| Sequential | 353 |
| Non-sequential | 455 |
| Medium range | 241 |
| Long range | 214 |
| Hydrogen bonds | 36 |
| Torsion angle restraints (total) | 198 |
| ϕ | 99 |
| ψ | 99 |
| Total restraints per residue | 13 |
| Total restraints per residue in structured residues* | 16 |
| Structure calculation statistics | |
| Violations | |
| Distance constraints (Å) | 0.0288±0.0024 |
| Dihedral angle constrains (°) | 0.2968±0.0453 |
| Max. dihedral angle violations (°) | 0.5 |
| Max. distance constraint violation (Å) | 5 |
| Average pairwise RMSD (Å) for all atoms | |
| Heavy atoms (Å) | 2.62±0.44 |
| Backbone atoms (Å) | 1.89±0.45 |
| Average pairwise RMSD (Å) for atoms in structured residues* | |
| Heavy atoms (Å) | 1.49±0.12 |
| Backbone atoms (Å) | 0.87±0.14 |
| Ramachandran analysis | |
| Most favoured regions | 93.1% |
| Additional allowed regions | 6.3% |
| Generously allowed regions | 0.5% |
| Disallowed regions | 0.2% |
*Structured Residues were considered the amino acids forming α-helices; K7-G30, A43-K65, G70-F87, D94-F111, I116- L119, a total of 87 amino acids from 122. NMR, muclear magnetic resonance; RMSD, root mean square deviation.