. Author manuscript; available in PMC: 2018 Dec 11.

Published in final edited form as: J Mol Biol. 2016 Oct 7;428(23):4651–4668. doi: 10.1016/j.jmb.2016.10.005

Table 4.

Refinement statistics for the structure of the IFNLR1/ JAK1 complex

Resolution range (Å)	79.38 – 2.10 (2.15 – 2.10)^#
Completeness (%)	75.5 (20.6)
σ cutoff	none
No. of reflections, working set	30,056 (598)
No. of reflections, test set	1080 (26)
Final R_cryst	0.169 (0.190)
Final R_free	0.230 (0.248)
No. of non-H atoms
Protein	4036
Water	185
Total	4221
R.m.s. deviations
Bonds (Å)	0.018
Angles (°)	1.852
Average B-factors (Å²)
Protein (JAK1, IFNLR1)	50.7 (49.3, 68.3)
Water	45.8
Total	50.5
Ramachandran plot^§
Favored regions (%)	96.1
Additionally allowed (%)	3.9
Number of complexes in a.u.	1
PDB code	5l04

^§

Statistics were calculated with the Web-based version of MolProbity (http://molprobity.biochem.duke.edu/ [44])

Outermost shell