Table 1.
X-ray Data Collection and Refinement Statistics
| Data collection | |
|---|---|
| Resolution (Å) | 50-2.6 |
| Observations | 890,683 |
| Unique reflections | 75,848 |
| Redundancy | 11.7 |
| Completeness (%) | 100.0 (100.0)1 |
| Rsym2 (%) | 9.8 (35.7)1 |
| <I/σI> | 10.0 (4.8)1 |
| Refinement | |
| Resolution (Å) | 50-2.6 |
| Reflections | 37,533 |
| Rcryst3 / Rfree (%) | 25.6 / 30.3 |
| Rmsd bond lengths (Å) | 0.007 |
| Rmsd bond angles (°) | 1.09 |
| Rmsd B-factors4 (Å2) (main/side chain) | 0.5 / 0.8 |
| Average B-factors (Å2) | |
| Protein (6322 atoms) | 37.4 |
| Phosphopeptide (320 atoms) | 40.0 |
| Solvent (78 atoms) | 35.3 |
1
Value in parentheses is for the highest resolution shell: 2.69-2.60 Å.
2
Rsym = 100 × Σ |I – 〈I〉| / Σ I.
3
Rcryst = 100 × Σ ∥Fo| – |Fc∥ / Σ |Fo|, where Fo and Fc are the observed and calculated structure factors, respectively. Rfree determined from 5% of the data.
4
For bonded protein atoms.