From: Structure of GlgS from Escherichia coli suggests a role in protein–protein interactions
Restraints for structure calculations | |
---|---|
Total restraints used | 421 |
Total NOE restraints | 289 |
Intraresidual | 59 |
Sequential (|i-j| = 1) | 96 |
Medium range (1<|i-j|<5) | 74 |
Long range (|i-j| ≥ 5) | 60 |
Hydrogen bond restraints | 29 |
Dihedral angles restraints | 103 |
Root mean square deviations from experimental restraints | |
Distance deviations (Å) | 0.041 ± 0.0020 |
Dihedral deviations (°) | 0.220 ± 0.0382 |
Deviations from idealized geometry | |
Bonds (Å) | 0.0040 ± 0.0001 |
Angles (°) | 0.5985 ± 0.0102 |
Impropers (°) | 0.3737 ± 0.0085 |
Root mean square deviations of the 15 structures from the mean coordinates (Å) | |
Backbone (residues Ser4-Met57) | 0.52 ± 0.20 |
Heavy atoms (residues Ser4-Met57) | 1.07 ± 0.21 |
Ramachandran plot statistics for residues Ser4-Met57 (%) | |
Residues in most favored regions | 93.9 |
Residues in additional allowed regions | 5.6 |
Residues in generously allowed regions | 0.5 |
Residues in disallowed regions | 0.0 |