TABLE 1.
Data collection and refinement statistics
| apo-MtbGpgP | MtbGpgP -VO3 | MtbGpgP -PO4 | |
|---|---|---|---|
| Data collection | |||
| Wavelength (Å) | 0.97930 | 1.03935 | 1.00000 |
| Resolutiona | 50.00–1.95 (1.98–1.95) | 50.00–2.30 (2.34–2.30) | 50.00–1.77 (1.80–1.77) |
| Space group | P212121 | P212121 | P212121 |
| Unit cell dimensions | |||
| a, b, c (Å) | 46.3, 77.0, 126.5 | 46.3, 82.8, 131.3 | 55.4, 76.9, 106.0 |
| α, β, γ (°) | 90.0, 90.0, 90.0 | 90.0, 90.0, 90.0 | 90.0, 90.0, 90.0 |
| Rmerge (%)a,b | 6.2 (41.1) | 5.5 (27.0) | 6.7 (32.8) |
| I/σIa | 31.2 (5.3) | 46.4 (8.9) | 29.5 (5.6) |
| Completeness (%)a | 97.1 (100) | 96.5 (100) | 99.3 (89.5) |
| Redundancya | 6.7 (7.1) | 7.0 (7.0) | 6.7 (4.8) |
| Total reflections | 223,942 | 156,449 | 295,755 |
| Unique reflections | 33,241 | 22,409 | 44,306 |
| Refinement statistics | |||
| Resolution (Å) | 48.90–1.95 | 35.01–2.30 | 36.14–1.78 |
| No. atoms | |||
| Protein | 3,227 | 3,151 | 3,250 |
| Water | 302 | 117 | 386 |
| Ligand | 0 | 8 | 10 |
| B-factor | |||
| Protein | 29.25 | 46.41 | 23.73 |
| Water | 32.87 | 38.73 | 32.47 |
| Ligand | N/A | 35.42 | 17.58 |
| Rwork/Rfreec | 20.3/23.9 | 19.20/24.48 | 18.2/21.9 |
| RMSDs | |||
| Bond lengths (Å) | 0.007 | 0.012 | 0.007 |
| Bond angles (°) | 1.158 | 1.232 | 1.172 |
| Observed residues | |||
| Chain A | 2–215 | 3–215 | 3–219 |
| Chain B | 3–216 | 3–215 | 2–218 |
| Ramachandran plot (%)d | |||
| Favored | 98.05 | 96.25 | 99.04 |
| Allowed | 1.95 | 3.00 | 0.24 |
| Outliers | 0 | 0.50 | 0.72 |
| MOLPROBITY scored | 1.75 | 2.12 | 1.66 |
a The numbers in parentheses are for the highest resolution shell.
b Rmerge = Σ|I − <I>|/Σ<I>, where I is the observed intensity, and <I> is the average intensity of multiple observations of symmetry related reflections.
c Rwork/Rfree = Σ||Fo| − |Fc||/Σ|Fo|, where Fo and Fc are the observed and calculated structure factors, respectively.
d The Ramachandran plot and MOLPROBITY score were calculated with MOLPROBITY.