TABLE 1.
Data collection and refinement statistics
AU, asymmetric unit; r.m.s.d., root mean square deviation; PDB, Protein Data Bank.
| Resolution (highest shell; Å) | 2.50 (2.59–2.50) |
| Space group | P61 |
| Unit cell dimensions | a = 104.4, b = 104.4, c = 143.9 Å; α = β = 90.0°, γ = 120.0° |
| No. of reflections | 30,710 |
| Rsym (highest shell)a | 7.7% (42.2%) |
| Completeness (highest shell) | 99.90% (98.96%) |
| Average redundancy (highest shell) | 8.0 (7.9) |
| I/σ | 29.3 (5.3) |
| Monomers/AU | 2 |
| No. of protein atoms/AU | 4195 |
| No. of ligand atoms/AU | 85 |
| No. of waters/AU | 151 |
| Rworkingb (Rfree)c | 20.5 (25.5) |
| Average B-factors (Å2) | |
| Protein | 45.0 |
| Ligand | 53.5 |
| Water | 45.5 |
| r.m.s.d. | |
| Bond lengths (Å) | 0.005 |
| Bond angles | 1.078° |
| PDB code | 4E2J |
a Rsym = Σ|I − 〈I〉|/Σ|I|, where I is the observed intensity, and 〈I〉 is the average intensity of several symmetry-related observations.
b Rworking = Σ‖Fo| − |Fc‖/Σ|Fo, where Fo and Fc are the observed and calculated structure factors, respectively.
c Rfree = Σ‖Fo| − |Fc‖/Σ|Fo for 7% of the data not used at any stage of the structural refinement.