Table 1. X-ray Diffraction Data and Refinement Statistics.
| X-ray diffraction data | |
|---|---|
| beamline | Diamond I04 |
| wavelength (Å) | 0.9795 |
| space group | P3212 |
| cell parameters a,b,c (Å) | 161.6, 161.6, 139.1 |
| molecules per asymmetric unit | 2 |
| resolution (Å) | 29.2–2.60 |
| high resolution shell (Å) | 2.74–2.60 |
| Rmergea (%) | 6.0 (66.8) |
| total observations | 298633 |
| unique reflections | 63561 |
| I/σ(I)a | 16.1 (1.7) |
| completenessa (%) | 99.6 (99.6) |
| multiplicitya | 4.7 (4.7) |
| refinement | |
|---|---|
| resolution range (Å) | 29.16–2.60 |
| unique reflections | 60392 |
| Rcryst (%) | 21.3 |
| Rfree (%) | 24.0 |
| No. of non-hydrogen atoms | 8845 |
| protein | 8737 |
| solvent | 108 |
| rmsd bonds (Å) | 0.006 |
| rmds angles (deg) | 1.0 |
| B-factors | |
| wilson (Å2) | 70.6 |
| average (Å2) | 69.2 |
| protein (Å2) | 69.1 |
| solvent (Å2) | 74.1 |
| rmsd B-factors | 1.3 |
| ramachandran plotb | |
| favored (%) | 96.9 |
| allowed (%) | 3.1 |
| disallowed (number) | 0 |
| score, percentilec | 1.65, 99th |
a
Numbers in parentheses refer to the high resolution shell.
b
Ramachandran analysis of backbone dihedral angles was done using Molprobity (molprobity.biochem.duke.edu).
c
The Molprobity score provides, on a scale of X-ray resolution, an overall assessment of the quality of the protein geometry relative to a set of reference structures; the 100th percentile is among the best, the 0th percentile among the worst structures at comparable resolution (N = 6237; 2.6 Å ± 0.25 Å).