Table III.
X-ray Data Collection and Refinement Statistics
| Data collection | |
| Space group | P21 |
| Cell dimensions (Å, °) | a = 102.8 |
| b = 293.9 | |
| c = 170.5 | |
| β = 92.4 | |
| Beamline | Photon factory BL5A |
| Resolution (Å)a | 50 – 2.30 (2.34 – 2.30) |
| Wavelength (Å) | 1.00000 |
| Rsym (%)ab | 8.5 (39.9) |
| <I>/<σI>a | 28.3 (3.6) |
| Completeness (%)a | 99.1 (99.0) |
| Observed reflections | 1,503,616 |
| Unique reflections | 439,066 |
| Multiplicitya | 3.4 (3.1) |
| Refinement and model quality | |
| Resolution range (Å) | 20 – 2.3 |
| No. of reflections | 433,754 |
| Rwork (%)c | 19.31 |
| Rfree (%)d | 22.62 |
| Total protein atoms | 65,983 |
| Total ligand atoms | 560 |
| Total water atoms | 2,064 |
| r.m.s.d. from ideal | |
| Bond lengths (Å) | 0.006 |
| Bond angles (°) | 0.911 |
| Dihedral angles (°) | 13.111 |
| Ramachandran plot | |
| Residues in favored regions (%) | 96.0 |
| Residues in allowed regions (%) | 4.0 |
| Residues in outlier regions (%) | 0 |
a
The values in parentheses refer to data in the highest resolution shell.
b
Rsym=ΣhΣi|Ih,I–<Ih>|/ΣhΣi|Ih,i|, where <Ih> is the mean intensity of a set of equivalent reflections.
c,d
R =Σ|Fobs–Fcalc|/ΣFobs, where Fobs and Fcalc are observed and calculated structure factor amplitudes, respectively. Rfree was calculated with a random 7% subset from all reflections which was not included in the refinement. Rwork was calculated with remaining reflections.