TABLE 1.
BAP data collection and refinement statistics
| Statistic | Value |
|---|---|
| Data collection | |
| Space group | P21 |
| Cell dimensions | |
| a, b, c (Å) | 118.4, 108.1, 120.4 |
| β (deg) | 95.1 |
| Temperature (K) | 100 |
| Radiation source | 19-ID |
| Wavelength (Å) | 0.9793 |
| Resolution (Å)a | 30.00–2.10 (2.14–2.10) |
| Unique reflections | 176,530 (8826) |
| Rmergeb | 0.137 (0.570) |
| 〈I〉/〈σI〉 | 9.0 (1.9) |
| Completeness (%) | 99.8 (99.8) |
| Redundancy | 3.2 (3.0) |
| Refinement | |
|---|---|
| Resolution (Å) | 29.69–2.10 |
| No. of reflections work/test set | 173,579/2166 |
| Rwork/Rfreec | 0.205/0.229 |
| No. of atom proteins/ligands/water | 19,666/130/1124 |
| Average B factor protein/ligands/water (Å2) | 24.4/36.2/23.8 |
| Rmsd | |
| Bond lengths (Å) | 0.008 |
| Bond angles (deg) | 0.73 |
| Ramachandran plot | |
| Most favored (%) | 95.9 |
| Outliers (%) | 0.25 |
| MolProbity score | 1.26 |
| Clash score | 1.39 |
a
Values in parentheses correspond to the highest-resolution shell.
b
Rmerge = ΣhΣj|Ihj − 〈Ih〉|/ΣhΣjIhj, where Ihj is the intensity of observation j of reflection h.
c
Rwork = Σh|Fo| − |Fc|/Σh|Fo| for all reflections, where Fo and Fc are observed and calculated structure factors, respectively. Rfree is calculated analogously for the test reflections, randomly selected, and excluded from the refinement.