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 valuec2), 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 = ΣhklFobs∥ - ∥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).