Table 1.
Summary of structural statistics for the human β4a-A domain, ensemble of the 15 lowest energy structures
| NOE upper distance limits | 963 |
| Intraresidue | 472 |
| Sequential | 196 |
| Medium range (1 < |i − j| ≥ 4) | 87 |
| Long range (|i − j| > 4) | 208 |
| Dihedral angle constraints | 143 |
| φ | 52 |
| ψ | 52 |
| χ | 39 |
| Hydrogen bonds | 2 × 25 |
| RMSD from experimental constraints | |
| Distances (Å) | 0.0339 ± 0.001 |
| Dihedrals (°) | 0.7455 ± 0.134 |
| Average number of NOE distance constraint violations | |
| >0.5 Å | 0.00 ± 0.00 |
| >0.2 Å | 2.27 ± 1.39 |
| RMSD from idealized covalent geometry | |
| Bonds (Å) | 0.0054 ± 0.0003 |
| Angles (°) | 0.6689 ± 0.0333 |
| Impropers (°) | 0.6105 ± 0.0426 |
| Atomic RMSD values (Å) for β4a-A domain residues 1–55 | |
| Backbone atoms | 0.74 ± 0.11 Å |
| All atoms | 1.35 ± 0.17 Å |
| Ramachandran plot (%)a,b | |
| Most favored regions | 79.0% |
| Additional allowed regions | 16.3% |
| Generously allowed regions | 4.7% |
| Disallowed regions | 0.0% |
Structure statistics are reported as averages of the 15 lowest energy structures calculated from the CNS program.
a Glycines and prolines are excluded.
bResidues 1–11, 19–22, and 27–55.