Table 1.

Data collection and refinement statistics

Resolution range, Å	30–2.97
Rsym*, %	10.6
I/σI overall (3.08–2.97 Å)	6.8 (2.3)
Completeness, % overall (3.08–2.97 Å)	92.8 (76.5)
Multiplicity	3.2
No. of reflections used in working set, %	158,002 (84.4)
No. of reflections used in test set, %	17,442 (9.3)
No. of nonhydrogen atoms with occupancy > 0 in the model	35,647
Protein atoms	35,264
Heterog. atoms	383
Solvent atoms	0
B factor from Wilson plot (Å2)	43.7
Rfree†, %	26.7
Rcryst‡, %	22.8
rms bond length, Å	0.008
rms bond angles, °	1.42

Diffraction data were collected from a single crystal at the beamline ID14EH3 (European Synchrotron Radiation Facility, Grenoble, France) at 4°C by using a wavelength of 0.931 Å. 

^*R_sym = ∑_i,hkl|〈I(hkl)〉 − I_i(hkl)|∑_i,hklI_i(hkl). 

^† R_free = ∑_(hkl)ɛT∥F_obs| − |F_calc∥/∑_(hkl)ɛT|F_obs|, where T is the test set (39). 

^‡ R_cryst = ∑_(hkl)∥F_obs| − |F_calc∥/∑_(hkl)|F_obs|.