Table 1.
Diffraction Data and Crystallographic Refinement Statistics
| Space Group | C2 |
| Cell dimensions (Å, °) | a = 162.5, b = 82.2, c = 91.1 β = 117.8 |
| Wavelength (Å) | 1.0 |
| Resolution (Å) | 80.6 – 1.9 |
| Average redundancya | 3.4 (2.9) |
| Rmergeb (%)a | 4.5 (17.5) |
| Completeness (%)a | 98.7 (90.8) |
| <I>/σIa | 16.9 (4.8) |
| Number of reflections (working/test) | 78352/4105 |
| Number of protein atoms/heteroatomsc | 6648/103 |
| Number of water molecules | 778 |
| Rcryst/Rfree (%)d | 16.3/19.7 |
| RMS deviation from ideal values | |
| Bond length (Å) | 0.014 |
| Bond angle (°) | 1.4 |
| Average B factor (Å2) | |
| Proteins | 16.4 |
| Ligands (ADP and MTR) | 16.4 |
| Magnesium ions | 18.0 |
| Chloride ions | 20.7 |
| Water molecules | 25.3 |
| Ramachandran Plote | |
| Total Favoured (%) | 97.8 |
| Total Allowed (%) | 100 |
| DPIf coordinate error based on Rfree (Å) | 0.13 |
aValues in parentheses corresponds to the value in highest resolution shell (1.97–1.90Å).
bRmerge = ∑∑|I (k) - <I>|/∑I (k) where I (k) and <I> represent the diffraction intensity values of the individual measurements and the corresponding mean values. The summation is over all unique measurements.
cHeteroatoms include ADP, MTR, ethylene glycol, magnesium and chloride ions.
dRcryst = ∑|Fobs - Fcalc|/∑|Fobs|; Rfree is Rcryst for the 5% cross validated test data.
eAs defined by the Ramachandran plot in MolProbity [53].
fCruickshank's diffraction component precision index (DPI) [54] as an estimate of coordinate error.