Table 1.
Crystallographic data and refinement statistics§
| PDB ID | mutation | inhibitor | Resolution Range (Å) | Overall Rsym (outmost) | Completeness, % (outmost) | Rcryst/Rfree (%) | RMSD bond length/angle |
|---|---|---|---|---|---|---|---|
| 2itx* | Wild-Type | AMP-PNP | 25-3.0 | 0.089 (0.395) | 99.9 (100.0) | 18.8/26.1 | 0.016/1.75 |
| 2j6m* | Wild-Type | AEE788 | 25-3.1 | 0.073 (0.385) | 96.7 (83.8) | 19.9/24.9 | 0.010/1.57 |
| 2itw* | Wild-Type | AFN941 | 25-2.9 | 0.066 (0.395) | 100.0 (100.0) | 18.7/25.6 | 0.017/1.85 |
| 2ity | Wild-Type | gefitinib | 25-3.4 | 0.123 (0.398) | 99.7 (100.0) | 21.1/26.0 | 0.022/1.81 |
| 2itn | G719S | AMP-PNP | 25–2.4 | 0.065 (0.398) | 99.9 (100) | 19.7/26.7 | 0.017/1.71 |
| 2ito | G719S | gefitinib | 25-3.2 | 0.086 (0.387) | 99.9 (100) | 18.9/26.6 | 0.015/1.69 |
| 2itp* | G719S | AEE788 | 25-2.7 | 0.058 (0.367) | 99.9 (100) | 19.6/25.5 | 0.017/1.78 |
| 2itq* | G719S | AFN941 | 25-2.7 | 0.050 (0.382) | 98.8 (94.2) | 19.7/26.3 | 0.019/1.87 |
| 2itt | L858R | AEE788 | 25-2.7 | 0.053 (0.367) | 99.8 (99.8) | 20.8/26.2 | 0.018/1.81 |
| 2itu | L858R | AFN941 | 25-2.8 | 0.066 (0.394) | 99.9 (99.7) | 19.8/25.8 | 0.019/1.89 |
| 2itv | L858R | AMP-PNP | 25-2.4 | 0.055 (0.390) | 99.7 (100.0) | 19.5/24.2 | 0.016/1.70 |
| 2itz | L858R | gefitinib | 25-2.8 | 0.055 (0.334) | 93.9 (85.3) | 20.2/25.5 | 0.015/1.63 |
*
These structures were determined in potassium sodium tartrate buffer rather than PEG 400 as for the other structures(See Material and Methods for details).
§
PDB refers to the Protein Data Bank (www.pdb.org).
Rsym=Σ|Ii − <Ii>|/ΣIi, where Ii is the average intensity of symmetry-equivalent reflections.
Rcryst=Σ|Fo−Fc|/ΣFo where Fo and Fc are observed and calculated structure factor amplitudes, respectively.
Rfree is the Rcryst for reflections excluded from the refinement.