TABLE 1.
Data collection and refinement statistics
| Erv1CTD | Erv1FL | |
|---|---|---|
| Data collection | ||
| Space group | P22121 | P21221 |
| Unit cell (90°, Å) | 38.55, 46.60, 58.88 | 63.28, 77.68, 116.23 |
| Resolution range (Å)a | 50.00–2.00 (2.07–2.00) | 49.06–3.00 (3.16–3.00) |
| Unique reflections | 7,532 (727) | 11,892 (1,688) |
| Completeness (%) | 99.7 (100.0) | 99.2 (98.6) |
| <I/σ(I)> | 30.88 (10.68) | 11.00 (3.80) |
| Rmerge (%)b | 6.4 (23.8) | 12.6 (41.1) |
| Average redundancy | 10.4 | 5.7 |
| Structure refinement | ||
| Resolution range (Å)a | 50.00–2.00 (2.06–2.00) | 46.53–3.00 (3.08–3.00) |
| R factorc/Rfreed (%) | 19.2/22.9 | 25.5/30.4 |
| Number of protein atoms | 890 | 3250 |
| Number of water atoms | 21 | 0 |
| RMSD bond lengths (Å)e | 0.017 | 0.005 |
| RMSD bond angles (°) | 1.753 | 0.902 |
| Mean B factors (Å2) | 35.15 | 50.73 |
| Ramachandran plotf | ||
| Most favored (%) | 98.1 | 95.8 |
| Additional allowed (%) | 1.9 | 3.7 |
| Outliers (%) | 0 | 0.5 |
| Protein Data Bank entry | 4E0H | 4E0I |
a The values in parentheses are for the highest resolution shell.
b Rmerge = ΣhklΣi|Ii(hkl)−<I(hkl)>|/ΣhklΣi|Ii(hkl)|, where Ii(hkl) is the intensity of an observation, and <I(hkl)> is the mean value for its unique reflection. Summations are over all reflections.
c R factor = Σh‖Fo(h)| − |Fc(h)‖/Σh|Fo(h)|, where Fo and Fc are the observed and calculated structure-factor amplitudes, respectively.
d Rfree was calculated with 5% of the data excluded from the refinement.
e Root mean square deviation from ideal values.
f Categories as defined by MolProbity.