. Author manuscript; available in PMC: 2016 May 26.

Published in final edited form as: Biochemistry. 2015 May 12;54(20):3183–3196. doi: 10.1021/acs.biochem.5b00106

Table 4.

Crystallographic Data Collection and Refinement Statistics

data set	VIM-2:CS319
processing	XDS/SCALA
beamline	DLS I04-1
space group	P2₁
cell dimensions	a = 52.89 Å, b = 61.40 Å, c = 68.92 Å, β = 100.9°
wavelength (Å)	0.9200
resolution (Å)^a	29.64–1.25 (1.32–1.25)
total no. of reflections^a	302755 (38004)
no. of unique reflections^a	115461 (15946)
completeness (%)^a	96.7 (91.8)
redundancy^a	2.6 (2.4)
I/(σI)^a	11.1 (2.3)
Rmerge (%)^a	0.040 (0.395)
refinement	REFMAC5
total no. of reflections	109653
resolution (Å)	29.64–1.25
Rcryst (%)	14.5
R_free (%)^b	16.4
root-mean-square deviation for bond lengths (Å)	0.0064
root-mean-square deviation for bond angles (deg)	1.4591
no. of protein atoms	3578
no. of water molecules	355
% residues in Ramachandran regions (favored/allowed/disallowed)	98.5/1.5/0
Wilson B factor	11.3
B factors (protein)	15.6 (15.4, 16.0)^c
B factors (ligand)	26.7,^d 22.7,^e 14.7^f
B factors (water molecules)	27.6
PDB entry	4UA4

Data for the highest-resolution shell are in parentheses.

R_free was calculated with 5% of the reflections omitted.

Values for chains A and B, respectively.

Major conformation, chain B (occupancy of 0.6).

Minor conformation, chain B (occupancy of 0.3).

Dimer, chain A.