Table 1. Summary of diffraction data and structure refinement statistics.
| Se-NosA1-111 | |
|---|---|
| Summary of diffraction data | |
| Wavelength (Å) | 0.9794 |
| Space group | P4132 |
| Cell parameters | |
| a = b = c (Å) | 143.3 |
| Resolution (Å) | 50.0-2.4 (2.59-2.40)a |
| Observed reflections | 1,483,177 |
| Unique reflections (I/σ(I) > 0) | 18,105 |
| Average redundancy | 81.9 (81.8) |
| Average I/σ(I) | 90.0 (17.6) |
| Completeness (%) | 100.0 (100.0) |
| Rmerge (%)b | 9.2 (46.4) |
| Refinement and structure model | |
| Reflections (Fo ≥ 0σ(Fo)) | |
| Working set | 17,056 |
| Test set | 915 |
| R factor/Free R factor (%)c | 17.9/21.5 |
| No. of protein atoms | 2,207 |
| No. of water atoms | 128 |
| Average B factor (Å2) | |
| All atoms | 48.4 |
| Main chain/side chain | 46.6/51.4 |
| Water | 40.3 |
| RMS deviations | |
| Bond lengths (Å) | 0.007 |
| Bond angles (°) | 1.0 |
| Ramachandran plot (%) | |
| Most favoured regions | 96.6 |
| Allowed regions | 3.4 |
| Generously allowed regions | 0.0 |
aNumbers in parentheses represent the highest resolution shell.
bRmerge = ∑hkl∑i|Ii(hkl)i− < I(hkl) > |/∑hkl∑iIi(hkl).
cR = ∑hkl||Fo|−|Fc||/∑hkl|Fo|.