Table 2.
Crystallographic data collection and refinement statistics.
| Data set a | nNOS-4 | nNOS-5 | nNOS-6 | nNOS-7 | eNOS-7 |
|---|---|---|---|---|---|
| Data collection | |||||
| PDB code | 4IMS | 4IMT | 4IMU | 4IMW | 4IMX |
| Space group | P212121 | P212121 | P212121 | P212121 | P212121 |
| Cell dimensions | |||||
| a, b, c (Å) | 51.8 110.4 164.1 | 51.7 110.7 163.7 | 51.9 110.2 163.9 | 51.7 111.4 164.2 | 58.1 106.6 156.5 |
| Resolution (Å) | 2.15 (2.19–2.15) | 2.20 (2.24–2.20) | 2.03 (2.07–2.03) | 2.15 (2.19–2.15) | 2.25 (2.29–2.25) |
| Rsym or Rmerge | 0.093 (0.632) | 0.073 (0.723) | 0.067 (0.618) | 0.075 (0.674) | 0.063 (0.653) |
| I / σI | 18.0 (2.0) | 19.6 (1.8) | 21.8 (2.0) | 23.4 (2.2) | 21.7 (2.2) |
| No. unique reflections | 52,114 | 48,484 | 60,761 | 52,331 | 46,588 |
| Completeness (%) | 99.5 (99.8) | 99.6 (98.5) | 99.0 (96.5) | 99.6 (99.8) | 99.6 (99.8) |
| Redundancy | 3.5 (3.6) | 4.0 (3.9) | 3.6 (3.4) | 4.6 (4.5) | 3.6 (3.7) |
| Refinement | |||||
| Resolution (Å) | 2.15 | 2.20 | 2.03 | 2.20 | 2.25 |
| No. reflections used | 49,363 | 45,951 | 57,686 | 46,313 | 44,205 |
| Rwork / Rfree b | 0.183/0.235 | 0.199/0.248 | 0.184/0.225 | 0.213/0.273 | 0.176/0.222 |
| No. atoms | |||||
| Protein | 6679 | 6674 | 6682 | 6659 | 6446 |
| Ligand/ion | 163 | 189 | 193 | 185 | 211 |
| Water | 244 | 162 | 350 | 158 | 249 |
| R.m.s. deviations | |||||
| Bond lengths (Å) | 0.012 | 0.013 | 0.011 | 0.016 | 0.015 |
| Bond angles (deg) | 2.05 | 2.08 | 1.97 | 1.56 | 1.47 |
a
See Fig. 3 for the inhibitor chemical formula.
b
Rfree was calculated with the 5% of reflections set aside throughout the refinement. The set of reflections for the Rfree calculation were kept the same for all data sets of each isoform according to those used in the data of the starting model.