Table 1.
Distance restraints | |
Intraresidue | 377 |
Sequential (|i-j| = 1) | 172 |
Medium range (2 ≤ |i-j| ≤ 4 | 76 |
Long range (4 < |i-j|) | 95 |
Hydrogen bond pairs (HN-O, N-O) | 42 |
Residual Dipolar Couplings | |
H-NH | 23 |
NOE violations | |
> 0.5 Å | 0.0 ± 0.0 |
> 0.3 Å | 18.0 ± 3.2 |
Dihedral angle restraintsb | |
φ/ψ angles for each amino acid | 57 |
Deviations from standard geometry (XPLOR-NIH) | |
Bonds | 0.0125 ± 0.0004 |
Angles | 1.4838 ± 0.0399 |
Impropers | 1.9898 ± 0.2513 |
Pairwise RMSD (Secondary structurec) | |
Backbone | 0.64 ± 0.11 Å |
All heavy atoms | 1.47 ± 0.16 Å |
Ramachandran Statisticsd | |
Most favored regions | 86.6 % |
Additional allowed regions | 12.0 % |
Generously allowed regions | 1.4 % |
Disallowed regions | 0.0 % |
aEnsemble of the top 20 structures with lowest overall energy and number of restraint violations.
bPredicted from chemical shifts using the PREDITOR web server.
cRMSD values for residues 58–69, 73–81, 88–94, 103–117.
dDetermined with PROCHECK-NMR for 10 lowest-energy structures.