Table 1.

Crystallographic structure determination statistics

Data collection details
Collection site	BL4 ESRF, 1995
Wavelength, Å	0.995
Collimation, mm	0.05 × 0.05
No. of crystals	1
Unit cell dimensions, Å	136.8 × 109.4 × 72.0 (cell form E)
Data processing details	All data	Outer shell
Resolution range, Å	20–2.65	2.74–2.65
No. of observations	83.791	5,304
Unique reflections	27,792	2,086
Completeness, %	86.8	69.0
Reflections with F/σ(F) > 3	24,040	1,133
Rmerge, %*	10.3	43.9
Refinement statistics
Resolution range, Å	20–2.65
Unique reflections	27,792
R factor, %†	0.222
No. of protein atoms	7765
No. of inhibitor atoms	32
No. of water molecules	72
rms bond length deviation, Å	0.006
rms bond angle deviation, °	1.3
Mean B factors, Å2‡	43/50/29/74
rms B factor deviation, Å2§	4.7

rms, root-mean-square. 

^*R_merge = ∑|I − <I>|/∑<I>. 

^†R factor = ∑|F_obs − F_calc|/∑F_obs. 

^‡Mean B factors for main chain, side chain, water, and inhibitor atoms, respectively. 

^§rms deviation between B factors for bonded main chain atoms.