TABLE 1.
Selected crystallographic data
| Parameter | Value(s) for nmrGRβ (F598S)/RU-486a |
|---|---|
| Data collection | |
| Space group | P61 |
| Cell dimensions | |
| a, b, c (Å) | 48.4, 48.4, 385.8 |
| α, β, γ (°) | 90, 90, 120 |
| Wavelength (Å) | 1.0 |
| X-ray source | APS SER-CAT 22ID |
| Resolution (Å) | 50–2.35 (2.39–2.35) |
| No. of reflections | 120,449 |
| No. of unique reflections | 20,767 |
| Completeness (%) | 97.7 (84.3) |
| Rmerge (%)b | 6.9 (45.3) |
| I/σ | 28.6 (2.5) |
| Redundancy | 5.8 (3.3) |
| Refinement | |
| Resolution (Å) | 35.0–2.35 (2.47–2.35) |
| No. of molecules/AUc | 2 |
| No. of amino acids/AU | 414 |
| No. of RU-486 molecules/AU | 2 |
| No. of waters/AU | 18 |
| Rwork (%)d | 21.0 |
| Rfree (%)e | 24.1 |
| Average B-factors (Å2) | |
| Protein | 60.3 |
| RU-486 | 50.9 |
| Water | 53.8 |
| RMSD from ideal | |
| Bond lengths (Å) | 0.002 |
| Bond angles (°) | 0.501 |
| Ramachandran plot (%) | |
| Favored | 98.26 |
| Allowed | 1.74 |
| Outlier | 0 |
a
PDB ID 5UC1. Values in parentheses are for the highest-resolution shell.
b
Rmerge = ∑∑|I − <I>|/∑∑|I|, where I is the observed intensity and <I> is the average intensity.
c
AU, asymmetric unit.
d
Rwork = ∑||Fo| − |Fc||/∑|Fo|, where Fo and Fc are the observed and calculated structure factors, respectively.
e
Rfree = ∑||Fo| − |Fc||/∑|Fo| for 5% of the data not used at any stage of the structural refinement.