Table 3.
Data collection and refinement statistics
| EGFR L858R + Shc1 peptide | EGFR L858R + Optimal peptide | |
|---|---|---|
| Data collection | ||
| Space group | I23 | I23 |
| Cell dimensions | ||
| a, b, c (Å) | 143.9, 143.9, 143.9 | 144.6, 144.6, 144.6 |
| α, β, γ (°) | 90.0, 90.0, 90.0 | 90.0, 90.0, 90.0 |
| Resolution (Å) | 50.0–2.6 (2.69–2.6)a | 50.0–2.8 (2.9–2.8)a |
| Rmerge | 0.068 (0.477) | 0.062 (0.473) |
| I / σI | 13.8 (2.3) | 16.6 (2.2) |
| Completeness (%) | 99.0 (99.5) | 98.8 (99.3) |
| Redundancy | 3.4 (3.1) | 3.4 (3.1) |
| Refinement | ||
| Resolution (Å) | 38.5–2.6 | 34.1–2.8 |
| No. reflections | 15207 | 12361 |
| Rwork / Rfree | 0.182/0.266 | 0.192/0.222 |
| No. atoms | ||
| Protein | 2501 | 2495 |
| Water | 129 | 63 |
| B factors | ||
| Protein | 59.5 | 69.7 |
| Water | 61.3 | 65.9 |
| r.m.s. deviations | ||
| Bond lengths (Å) | 0.010 | 0.010 |
| Bond angles (°) | 1.180 | 1.146 |
a
Values in parentheses are for highest-resolution shell.