Table II.
X-ray data processing and refinement statistics
| Structure Refinement | TK Data |
|---|---|
| Cell constants (Å) | a = b = 136.4; c = 203.7 |
| Space group | P3121 |
| Resolution range (last shell) (Å) | 33.52-2.3 (2.42-2.3) |
| Reflections, unique | 91,552 |
| Multiplicity | 3.5 |
| Rmergea overall (last shell) | 0.12 (0.36) |
| Completeness (%) overall (last shell) | 93.8 (93.8) |
| Non-hydrogen protein atoms | 15,246 |
| Solvent molecules | 440 |
| Non-hydrogen ligand atoms | 78 |
| Non-hydrogen ion atoms | 3 |
| Rvalueb (%) overall (Rfree) | 16.6 (20.0) |
| Root mean square deviations from ideality | 0.008 Å (bonds), 1.46° (angles) |
| Average B valuec (Å2), protein | 24.6 |
| Average B value (Å2), ligand | 20.7 |
| Average B value (Å2), solvent | 23.5 |
| Average B value (Å2), ion | 16.6 |
| Φ, Ψ angle distribution for residuesd | |
| Most favored regions (%) | 88.9 |
| Additional allowed regions (%) | 11.1 |
a
Rmerge = Σhkl [(Σi |Ii - (I)| Σi Ii].
b
Rvalue = Σhkl ∥Fobs∥ - ∥Fcalc∥/Σhkl |Fobs| is the cross-validation R factor computed for the test set of 5% of unique reflections. c Temperature factors. d Ramachandran statistics as defined by PROCHECK (Laskowski et al., 1993).