Table 1.

X-ray crystallography data collection and refinement statistics.

Beamline	14.1
Wavelength (Å)	1.22
Resolution range (Å)	15.0 – 1.15 (1.19 – 1.15)^a
Space group	P 2₁
Unit cell dimensions
a, b, c (Å)	31.5, 42.7, 65.7
α, β, γ (°)	90, 94.5, 90
Total reflections	172044
Unique reflections	62439 (6168)
Multiplicity	2.8 (2.7)^a
Completeness (%)	97.8 (97.6)^a
Mean I/σ(I)	15.4 (2.05)^a
Wilson B-factor	9.30
R_sym^b	0.065 (0.615)^a

Refinement

R_work^c	0.159 (0.241)^a
R_free^c	0.182 (0.249)^a
Number of total atoms	2099
protein molecule	1679
Ligands	112
Water	308
Total protein residues	208
RMS (bonds, Å)	0.018
RMS (angles, °)	1.64
Ramachandran favored (%)^d	98
Rotamer outliers (%)	0
Average B-factor	14.50
macromolecules	13.10
Ligands	11.10
Solvent	23.40

Data for highest resolution shell are given in brackets.

R_sym =∑_hkl ∑_i | I_i (hkl)- 〈I (hkl)〉|/∑_hkl ∑_i I_i (hkl) where I_i (hkl) is the i^th observation of the intensity of the reflection hkl.

R_work=∑_hkl || F_obs|-|F_calc||/∑_hkl |F_obs|, where F_obs and F_calc are the observed and calculated structure-factor amplitudes for each reflection hkl. R_free was calculated with 6% of the diffraction data that were selected randomly and excluded from refinement.

Calculated using MolProbity (Chen et al., 2010).