TABLE 2.
Data processing and refinement statistics
| Unit cell parameters | |
| a, b, and c (Å) | a = 48.3, b = 109.9, c = 105.9 |
| α, β, and γ (degrees) | α = 90.0, β = 97.8, γ = 90.0 |
| Space group: | P21 |
| Resolution range | 47.71–3.0 Å |
| No. of molecules/asymmetric unit | 2 |
| No. of reflections | |
| Observed | 90,279 (13,110) |
| Unique | 21,867 (3167) |
| I/σ (I) | 7.8 (2.6) |
| Completeness (%) | 100.0 (100.0) |
| Rmerge (%)a | 16.0 (61.0) |
| Multiplicity | 4.1 (4.1) |
| Rcryst (%)b | 25.5 |
| Rfree (%)b | 31.1 |
| No. of protein atoms | 7639 |
| No. of chains | 6 |
| Root mean square deviation from ideal geometry | |
| Bond length (Å) | 0.005 |
| Bond angles (degrees) | 1.150 |
| B values (Å2) | |
| Wilson B | 48.89 |
| Average B | 48.22 |
| Ramachandran plot (%) | |
| Residues in preferred regions | 89.31 |
| Residues allowed regions | 10.58 |
| Residues in disallowed regions | 0.1 |
a Rmerge = ΣhklΣi‖Ii(hkl) − (I(hkl))‖/ΣhklΣiIi(hkl), where Ii(hkl) is the ith observation of reflection hkl and (I(hkl)) is the weighted average intensity for all observations i of reflection hkl. Values in parentheses refer to the highest resolution shell.
b Rcryst and Rfree = (Σ‖Fo| − |Fc‖)/(Σ|Fo|), where |Fo| is the observed structure factor amplitude and |Fc| is the calculated structure factor amplitude.