Table 2.

Data refinement statistics

Refinement statistics	Values
Resolution range, Å	8.0–1.6
No. of unique reflections used for the refinement (F > 2σ)	8331
No. of protein atoms (Z > 1)	682
No. of water molecules	85
Rcryst.,* %	19.6
Rfree,† %	21.5
rms deviations from ideal values
Bond lengths, Å	0.012
Bond angles, °	2.75
Dihedral angles, °	24.0
Improper angles, °	1.56
Average temperature factors, Å2
Main chain	12.3
Side chain	16.5
Solvent	30.6

^*R_cryst. = Σ|F_obs(h) − F_calc(h)|/ΣF_obs(h), where F_obs and F_calc are the observed and calculated structure amplitudes of reflection h, respectively. The summation is over all reflections. 

^†R_free is equivalent to R_cryst. for a randomly selected 10% subset of reflections excluded from the target set for refinement.