Table 5. Data Collection and Refinement Statistics.
| SHP2·11c-9 | |
|---|---|
| crystal parameters | |
| space group | P1 |
| cell dimensions | |
| a (Å) | 40.0 |
| b (Å) | 40.9 |
| c (Å) | 48.9 |
| α (deg) | 94.6 |
| β (deg) | 109.2 |
| γ (deg) | 110.0 |
| data collection | |
| resolution range (Å) | 50.0–2.1 |
| no. of unique reflections | 12808 |
| completeness (%) | 82.3 |
| redundancy | 2.5 |
| Rmergea | 0.071 |
| refinement | |
| resolution range (Å) | 50.0–2.5 |
| no. of reflections used (F ≥ 2.0δ (F)) | 8843 |
| completeness (%) | 94.9 |
| no. of protein atoms | 2219 |
| no. of inhibitors | 1 |
| Rworkb/Rfreec | 18.7/22.1 |
| rms deviations from ideal geometry | |
| bond length (Å) | 0.0079 |
| bond angle (deg) | 1.33 |
a
Rmerge = ∑h ∑i|I(h)i – ⟨I(h)⟩|/∑h∑iI(h)i.
b
Rwork = ∑h|F(h)calcd – F(h)obsd|/∑hF(h)obsd, where F(h)calcd and F(h)obsd were the refined calculated and observed structure factors, respectively.
c
Rfree was calculated for a randomly selected 3.9% of the reflections that were omitted from refinement.