TABLE 1.
X-ray crystallographic data and refinement statistics for CtFabI·NADH·AFN1252 complex (Protein Data Bank entry 4Q9N)
| Crystal | CtFabI·NADH· AFN-1252 |
|---|---|
| Data collection | |
| Space group | P43 |
| Wavelength (Å) | 1.0 |
| Unit cell dimensions | |
| a (Å) | 96.15 |
| b (Å) | 96.15 |
| c (Å) | 263.08 |
| α, β, γ (degrees) | 90, 90, 90 |
| Molecules/ASUa | 8 |
| Resolution (Å) b | 1.8 (1.85–1.80)d |
| Completeness (%)b | 98.8 (95.1) |
| Redundancyb | 6.3 (3.4) |
| No. of total reflections | 335,128 |
| No. of unique reflections | 221,426 |
| I/σb | 15.5 (1.57) |
| Rsymb,c | 12.2 (61.6) |
| Refinement statistics | |
| Resolution (Å) | 1.8 |
| No. of reflections | 218,306 |
| Rwork/Rfree (%)d,e | 0.1863/0.2292 |
| No. of atoms | 19,232 |
| Protein | 17,700 |
| Ligand/ion | 576 |
| Water | 956 |
| B-Factors (Å2) | |
| Protein | 25.4 |
| Ligand/ion | 22.7 |
| Water | 28.2 |
| Root mean square deviations | |
| Bond length (Å) | 0.006 |
| Bond angle (degrees) | 1.057 |
| Ramachandran analysis | |
| Most favored (%) | 97.5 |
| Allowed (%) | 3.3 |
| Disallowed (%) | 0.2 |
a Asymmetric unit.
b Values in parentheses are for the highest resolution shell.
c Rsym = Σ|I − 〈I〉|/Σ〈I〉, where I is the observed intensity, and 〈I〉 is the average intensity of multiple observations of symmetry-related reflections.
d r = Σhkl‖Fo| − |Fc‖/Σhkl|Fo|.
e Rfree is calculated from 5% of the reflections excluded from refinement.