TABLE 1.

X-ray data and refinement statistics

	Data set
	High resolution	MAD
Data collection
Space group	P1	P1
Cell dimensions
a, b, c	50.6, 75.3, 84.1 Å	50.7, 75.6, 84.3 Å
α, β, γ	114.9, 94.8, 90.2°	115.1, 94.9, 90.3°

		Peak	Inflection	Remote
Wavelength	0.97939	0.97939	0.97951	0.91162
Resolutiona	43.9 to 2.00 Å (2.1 to 2.00 Å)	50.4 to 2.55 Å (2.69 to 2.55 Å)	50.4 to 2.55 Å (2.69 to 2.55 Å)	50.4 to 2.37 Å (2.50 to 2.37 Å)
Completenessa	96.2% (95.0%)	97.4% (95.9%)	97.4% (95.6%)	97.3% (95.6%)
Average I/σIa	13.2 (3.0)	14.8 (3.9)	14.8 (3.7)	12.0 (2.4)
Unique reflectionsa	72,902 (10,538)	35,814 (5178)	35,817 (5179)	44,562 (6393)
Redundancya	3.7 (3.7)	3.8 (3.8)	3.8 (3.8)	3.8 (3.8)
Rsyma,b	8.4% (55.9%)	6.8% (28.8%)	6.9% (30.2%)	8.5% (46.9%)
Refinement
Resolution range	42.6 to 2.0 Å
No. of reflections	72,482
No. of atoms
Protein	6930
Ligand/ions	12
Water	455
R-factorc	0.194
Rfreed	0.228
Wilson B-factor	24.5
Average B-factors (Å2)
Protein	37.0
N-terminal A	30.7
N-terminal B	33.6
C-terminal B	76.4
Ligand/ions	39.8
Water	39.9
R.m.s.d.
Bond lengths	0.018 Å
Bond angles	1.645°
Ramachandran analysis (%)e
Most favored	96.2
Additionally allowed	3.6
Outliers	0.2

^a Data in parentheses are for the outermost data shell.

^b R_sym = Σ_hΣ_j|I(h;j) − Σ(h)|/Σ_hΣ_jI(h), where I(h;j) is the jth measurement of the intensity of the unique reflection h, and I(h) is the mean over all symmetry-related measurements.

^c R-factor = Σ|F_obs − F_calc|/F_obs, where F_obs and F_calc are the observed and calculated structure-factor amplitudes, respectively.

^d R_free is the R-factor of the 5% of data (selected randomly) not used in refinement.

^e Data are according to the definitions of Lovell et al. (49).