. Author manuscript; available in PMC: 2019 Nov 19.

Published in final edited form as: J Med Chem. 2018 Dec 19;62(2):987–992. doi: 10.1021/acs.jmedchem.8b01723

Table 1.

Data collection and refinement statistics.

Data collection
Wavelength (Å)		0.9793
Resolution range (Å)		50.00 – 2.74 (2.79 – 2.74)^a
Space group		C 2
Unit cell	(a, b, c) (Å)	153.718 68.650 98.386
	(α, β, γ) (°)	90.000 120.727 90.000
Total reflections		114,299
Unique reflections		23,259 (1,186)
Multiplicity		4.9 (4.0)
Completeness (%)		100.00 (99.9)
<I>/(I)		17.86 (1.89)
Rmerge^b (%)		11.1 (68.0)
Wilson B-factor (Å²)		53.95
Refinement
Resolution range (Å)		48.65 – 2.74 (2.84 – 2.74)
Rwork/Rfree^c (%)		21.41 (29.57)/226.16 (36.72)
Number of non-hydrogen atoms^d		6208
protein		5864
ligands		265
waters		79
RMS (bonds, Å)		0.006
RMS (angles, °)		1.006
Ramachandran favored (%)		97.25
Ramachadran allowed (%)		2.75
Ramachandran outliers (%)		0.00
Average B-factor (Å²)		51.13
macromolecules		50.36
ligands		69.90
waters		45.25

RMS, Root Mean Square deviation from ideal values (crystallography).

Statistics for the highest-resolution shell are shown in parentheses.

Rmerge = 100Σ(h)Σ(i)|I(i)-<I>|/Σ(h)Σ(i)I(i), where I(i) is the ith intensity measurement of reflection h, and <I> is the average intensity from multiple observations.

Rfactor = Σ||Fobs|-|Fcalc||/Σ|Fobs|. Where Fobs and Fcalc are the structure factor amplitudes from the data and the model, respectively. 8.6 % reflections were used to calculate Rfree values.

Per asymmetric unit.