. Author manuscript; available in PMC: 2015 Jul 15.

Published in final edited form as: J Mol Biol. 2014 May 17;426(14):2617–2631. doi: 10.1016/j.jmb.2014.05.006

Table 1.

Crystallographic data collection and refinement statistics.

Unit Cell and Space Group a, b = 51.2, c = 112.1 Å α, β = 90.0° γ = 120° P3₁
PDB ID Code: 4QAG		Refinement
		Resolution Range Used (Å)	28.6 – 1.71
Data Collection		Completeness in Range (%)	98.3
Resolution Limit (Å)	40 – 1.71	Sigma Cutoff	0.0
Unique Reflections	34856	R-factor/R_free(%) Cross-validated Coordinate	18.2/19.0
Completeness (%) / Multiplicity:		Error (Å)^48;49;50	0.23
All data	98.5 / 7.8	No. of Protein/Solvent Atoms	2076/174
2.03–2.15 Å Shell:	99.7 / 7.2	No. of Inhibitor/Cation Atoms	34/4
1.93–1.84 Å Shell:	99.3 / 5.3	RMS Bond Lengths (Å)⁵¹	0.008
1.84–1.77 Å Shell:	97.6 / 4.2	RMS Bond Angles (°)⁵¹	0.94
1.77–1.71 Å Shell:	89.5 / 2.9
		Average B-factors (Å²)
R_sym (%) / Average I/σ:		Protein/Solvent	55.5/70.3
All Data	8.8 / 27.1	Inhibitor/cations	61.5/46.0
2.03–2.15 Å Shell:	16.3 / 9.3
1.93–1.84 Å Shell:	31.0 / 4.8	Ramachandran Regions
1.84–1.77 Å Shell:	42.5 / 3.1	Most favored	98.1%
1.77–1.71 Å Shell:	45.1 / 2.4	Additional Allowed	1.9%
		Generous or disallowed	0%