Table 2 Statistics of X-ray diffraction data and structure refinement.
αMg+NADHγNADH | |
|---|---|
Data collection | |
Wavelength (Å) | 0.9785 |
Space group | P3121 |
a, b (Å) | 118.0 |
c (Å) | 142.1 |
Resolution (Å) | 50.0–2.40 (2.49–2.40)a |
Observed reflections | 449,533 |
Unique reflections (I/σ(I) > 0) | 45,428 |
Average redundancy | 9.9 (8.9) |
Average I/σ(I) | 22.6 (2.8) |
Completeness (%) | 100.0 (100.0) |
Rmerge (%)b | 12.1 (65.3) |
Refinement and structure model | |
No. of reflections (Fo > 0σ(Fo)) | 45,386 |
Working set | 43,063 |
Test set | 2,323 |
R factor/Rfree factor (%)c | 21.1/23.6 |
Total protein atoms | 5,048 |
Total ligand atoms | 89 |
Total solvent atoms | 94 |
Wilson B factor (Å2) | 54.3 |
Average B factor (Å2) | 64.5 |
Protein | 63.9 |
Mg (active site) | 52.6 |
NADH (active/allosteric site) | 129.3/70.8 |
Water | 54.3 |
RMS deviations | |
Bond lengths (Å) | 0.008 |
Bond angles (°) | 1.3 |
Ramachandran plot (%) | |
Most favored | 96.5 |
Allowed | 3.5 |
