Table 1.
Data Collection and Refinement Statistics for R388A SrcKD Structure Determination
| Data Collection | Average (highest resolution shell) |
|---|---|
| Beamline | ALS 8.3.1 |
| Resolution (Å) | 50 − 2.2 (2.28 − 2.2) |
| Space group | P21 |
| Unit cell parameters (Å) | a = 59.65, b = 63.46, c = 83.86 |
| α = γ = 90° β = 91.45° | |
| Content of the assymteric unit | two kinase domains, two molecules of PP2 |
| Measured reflections (#) | 110199 |
| Unique reflections (#) | 31912 |
| Data Redundancy | 3.5 |
| Data completeness (%) | 98.7 (93.9) |
| Rsym (%)a | 9.4 (48.9) |
| I/sig | 13.5 (2.3) |
| Refinement | |
| R factor / R free | 22.6 % / 27.3 % |
| Number of protein atoms | 4356 |
| Number of non-protein atoms | 282 |
| Rmsd bond length (Å) | 0.0076 |
| Rmsd bond angle | 1.2° |
| Rmsd B factors (Å2) (mainchain / side-chain) | 1.5 / 2.1 |
| PDB entry | 3GEQ |
a
Rsym = Σ|I-<I>|/ ΣI, where I is the observed intensity of a reflection, and <I> is the average intensity of all the symmetry related reflections