Table 2.
Data Collection and Refinement Statistics for X-ray Crystal Structures of hRRM1 Bound with Compound 4
| Cell Dimensions | |
|---|---|
| space group | P212121 |
| a, b, c, (Å) | 72.21, 112.11, 218.27 |
| wavelength (Å) | 0.98 |
| resolution (Å) | 200.00–3.70 |
| monomer per asymmetric unit | 2 |
| unique reflections | 19896 |
| Rsyma | 21.8 (89.7)c |
| I/σ(I) | 28.8 (4.4) |
| (%) completeness | 95.5 (95.7) |
| redundancy | 3.2 (3.0) |
|
| |
| refinement | |
|
| |
| number of reflections | 18327 |
| Rwork/Rfreeb | 23.2/28.9 |
| number of atoms | 11384 |
| protein | 11296 |
|
| |
| RMS deviation from ideal | |
|
| |
| bond length (Å) | 0.009 |
| bond angle (deg) | 1.78 |
|
| |
| Ramachandran plot, residues in (%) | |
|
| |
| core regions | 80.6 |
| allowed regions | 17.5 |
| generously allowed regions | 1.5 |
a
Rsym = ΣhklΣi/Ii(hkl) − 〈I(hkl)〉/ΣhklΣiIi(hkl), where Ii(hkl) is the ith observation of reflection hkl, and 〈I(hkl)〉i is the weighted average intensity for all observations i of reflection hkl.
b
Rwork and Rfree = Σ||Fo| − |Fc||/Σ|Fo|, where Fo and Fc are the observed and calculated structure factor amplitudes, respectively. For the calculation of Rfree, 5% of the reflection data were selected and omitted from refinement.
c
Values in parentheses are used for the highest-resolution shell.