Table 1. Diffraction data and structural refinement statistics.
Values in parentheses are for the highest resolution shell.
| Crystal data | |
| Space group | P21212 |
| Unit-cell parameters (Å) | a = 72.067, b = 185.573, c = 62.517 |
| Subunits per ASU | 2 |
| Data collection and refinement | |
| Temperature (K) | 100 |
| Wavelength (Å) | 0.9 |
| Resolution range (Å) | 30–2.0 (2.07–2.0) |
| No. of unique reflections | 56133 (4619) |
| Redundancy | 4.8 (4.4) |
| Completeness (%) | 97.7 (81.1) |
| Mean I/σ(I) | 16.1 (4.2) |
| Rmerge† (%) | 9.5 (23.5) |
| No. of protein atoms | 6080 |
| No. of water molecules | 462 |
| Mean B factor (Å2) | 28.40 |
| Mean B factor, main chains (Å2) | 26.5 |
| Mean B factor, side chains (Å2) | 29.9 |
| Mean B factor, waters (Å2) | 35.94 |
| Rwork‡/Rfree§ | 0.210/0.258 |
| Ramachandran plot (%) | |
| Most favoured | 89.7 |
| Additionally allowed | 9.4 |
| Generously allowed | 0.6 |
| Disallowed | 0.3 |
| PDB code | 1j3n |
R
merge =
, where Ii(hkl) and 〈I(hkl)〉 are the observed intensity of measurement i and the mean intensity of the reflection with indices hkl, respectively.
R
work =
, where F
obs and F
calc are the observed and calculated structure factors, respectively.
R free is the R factor for a subset of 5% of the reflections that were omitted from refinement.