Table 1.
Data collection and refinement statistics (molecular replacement) of BceF kinase domain.
| BceF | |
|---|---|
| PDB accession code | 6Z0P |
| Beamline | ESRF ID23-2 |
| Date | 25 June 2016 |
| Data collection | |
| Space group | P 1 21 1 |
| Cell dimensions | |
| a, b, c (Å) | 44.27 90.48 61.34 |
| α, β, γ (°) | 90.0 111.1 90.0 |
| Wavelength (Å) | 0.8729 |
| Resolution (Å) | 90.5-1.85 (2.2-1.85) |
| R-factor observed (%) | 9.5 (47.3) |
| aRmeas (%) | 11.2 (55.1) |
| I / sigma | 9.6 (2.7) |
| Total reflections | 142,307 (58,228) |
| Unique reflections | 38,309 (15,478) |
| Completeness (%) | 99.4 (99.5) |
| Multiplicity | 3.7 (3.8) |
| b CC1/2 (%) | 99.7 (80.6) |
| Refinement | |
| Resolution (Å) | 48.4-1.85 (1.90-1.85) |
| Completeness (%) | 99.3 (96.6) |
| c No. reflections | 36413 |
| dRwork (%) | 18.3 (25.6) |
| Rfree (%) | 20.2 (23.5) |
| Rfree value test set size (%) | 5 |
| No. atoms | 3780 |
| Protein | 1836 (Chain A; 271 residues) 1839 (Chain B; 271 residues) |
| Ligand/ion | 54 (ADP) |
| Water | 51 |
| B-factors | |
| Protein | 26.3 (Chain A) 24.8 (Chain B) |
| Ligand/ion | 20.6 (ADP) |
| Water | 24.8 |
| R.m.s. deviations | |
| Bond lengths (Å) | 0.005 |
| Bond angles (°) | 1.272 |
| Clash score * | 4.6 (97th percentile) |
| Molprobity score * | 1.24 (99th percentile) |
| Number of xtals used for scaling | 1 |
Values in parentheses are for highest-resolution shell. (a) R-meas is a redundancy-independent R-factor defined in Reference [24]. (b) CC1/2 is the percentage of correlation between intensities from random half-datasets [25]. (c) Number of reflections corresponds to the working set. (d) Rwork corresponds to working set. * Calculated using Molprobity [26].