Table 1.
Data Collection and Refinement Statistics
| Data Set | Nup1201-757 SeMet |
|---|---|
| Data Collection | |
| Space group | P21212 |
| Cell dimensions | |
| a, b, c (Å) | 114.6, 153.7, 53.0 |
| α, β, γ (°) | 90.0, 90.0, 90.0 |
| No. of unique reflections | 35895 |
| Resolution (Å) | 50 - 3.0 (3.1-3.0) |
| Rsyma (%) | 5.1 |
| Completeness (%) | 99.8 (99.6) |
| Redundancy | 3.0 (3.0) |
| I/σ | 20.4 (1.8) |
| Refinement | |
| Resolution (Å) | 50 - 3.0 |
| No. of unique reflections | 35841 |
| No. atoms | |
| Protein | 5305 |
| Water | 0 |
| Rworkb | 24.4 |
| Rfreec | 29.9 |
| RMSD Bond lengths (Å) | 0.017 |
| RMSD Bond angles (°) | 1.915 |
| B factor (Å2) | |
| β-propeller | 114 |
| α-helical insertion bundle | 89 |
| α-helical domain | 83 |
| Ramachandran plot (%)d | |
| favored/allowed/outliers | 93.61/5.3/1.09 |
a
Rsym = |Ii − Ii|/Ii, where Ii is the intensity of the ith observation and Ii is the mean intensity of the reflection
b
Rwork = (||Fobs| − |Fcalc||/|Fobs|)
c
Rfree = R value for a randomly selected subset (5%) of the data that were not used for minimization of the crystallographic residual
d
Calculated using MolProbity