Table 1. X-ray data-collection and refinement statistics.

Values in parentheses are for the highest resolution shell.

Data collection
X-ray source	SRS PX10.1
Wavelength (Å)	1.117
Space group	C2221
Unit-cell parameters (Å, °)	a = 83.4, b = 152.04, c = 118.55, α = β = γ = 90
Matthews coefficient (Å3 Da−1)	2.46
Solvent content (%)	50.0
Wilson B factor (Å2)	17.2
No. of unique reflections	62507 (4944)
Rmerge†	0.066 (0.238)
Redundancy	4.5 (2.9)
Completeness (%)	97.1 (78.1)
I/σ(I)	13.5 (4.2)
Refinement
Resolution (Å)	20–1.85
R factor/Rfree‡ (%)	0.171 (0.198)
No. of protein atoms	5328
No. of ligand atoms	96
No. of water atoms	348
R.m.s. deviations from ideality
Bond lengths (Å)	0.016
Bond angles (°)	1.5
Ramachandran plot (%)
Most favoured regions	91.8
Additional allowed regions	7.9
Generously allowed regions	0.3
Average B values (Å2)
Overall	18.8
Protein atoms	18.4
Ligand atoms	20.9

^† R _merge = , where I _i(hkl) is the intensity of the ith measurement of reflection hkl and 〈I(hkl)〉 is the average value over multiple measurements.

^‡ R factor = , where F _obs and F _calc are the observed and calculated structure factors, respectively. R _free was calculated for 5% of the reflections removed randomly from the refinement.