Table 1.

Statistics on diffraction data and structure refinement

Data collection
Space group	P21
Unit cell (a, b, c, Å)	63.8, 78.7, 70.5, 90.0 92.5, 90.0
Resolution (Å)	1.55
Unique reflections	100,381
Fold of redundancy	6.7
Completeness (%)	99.5† (68.9)*
Average I/σ	14.0 (3.4)*
Rmerge	0.054 (0.22)*
Structure Refinement
R-factor	0.190
R-free	0.208 (10%)‡
Reflections	98144
RMS deviation for Bond (Å)	0.0043
Angle	1.1°
Average B-factor (Å2)
Protein	22.7 (5322)§
IBMX	43.1 (32)§
Waters	31.5 (501)§
Zn	17.0 (2)
Mg	15.1 (2)

^†The 99.5% completeness is calculated by including 4312 reflections in resolution shell 1.55 to 1.50 Å.

^*The numbers in parentheses are for the highest resolution shell.

^‡The percentage of reflections omitted for calculation of R-free.

^§The number of atoms in the crystallographic asymmetric unit.