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. 2016 Jun 2;113(24):E3403–E3412. doi: 10.1073/pnas.1603269113

Table S1.

Statistics of crystallographic analyses

pSTING/IRF-3 pMAVS/IRF-3 pTRIF/IRF-3 IRF-3/CBP pNSP1/IRF-3 NSP1/IRF-3
Data collection
 Space group P2 P21 P3221 P21 P3221 P212121
Cell dimensions
a, b, c (Å) 60.08, 56.40, 75.55 38.80, 104.91, 66.27 72.81, 72.81, 127.60 85.23, 88.66, 92.81 72.98, 72.98, 127.55 67.77, 107.92, 135.65
 α, β, γ (°) 90.0, 104.64, 90.0 90.0, 106.13, 90.0 90.0, 90.0, 120.0 90.0, 113.09, 90.0 90.0, 90.0, 120.0 90.0, 90.0, 90.0
 Resolution, Å 2.00 (2.03–2.00) 2.40 (2.49–2.40) 1.60 (1.63–1.60) 2.50 (2.59–2.50) 1.72 (1.75 to1.72) 2.90 (2.95–2.90)
 Unique reflections 35,085 19,995 52,282 42,426 42,593 22,409
 Molecules per ASU 2 2 1 4 1 4
Rmerge (%) 10.8 (57.0) 9.9 (136) 5.6 (>100) 13.8 (155) 6.8 (>100) 14.0 (89.8)
Rp.i.m. (%) 6.6 (35.0) 4.0 (53.9) 1.7 (33.4) 8.5 (94.6) 2.2 (39.8) 5.6 (35.6)
 CC1/2 (0.817) (0.697) (0.818) (0.384) (0.823) (0.781)
II 14.0 (1.8) 14.3 (1.7) 45.2 (1.8) 6.2 (0.8) 44.5 (1.9) 15.7 (2.1)
 Completeness (%) 98.2 (83.7) 100 (100) 99.8 (99.5) 96.3 (85.9) 100 (100) 100 (99.9)
 Redundancy 3.6 (3.2) 7.2 (7.3) 11.9 (11.6) 3.5 (3.4) 11.8 (10.9) 7.1 (7.3)
Refinement
 Resolution (Å) 2.00 2.40 1.60 2.50 1.72 2.90
 No. reflections used 35,068 19,966 52,240 42,378 42,537 22,342
Rwork/Rfree (%) 17.6/23.7 18.8/25.1 16.8/18.7 19.2/24.2 17.4/19.0 21.0/25.0
 No. atoms 4,341 3,968 2,228 7,876 2,207 7,718
 Protein 3,669 3,678 1,851 7,650 1,885 7,386
 Ligand/ion 292 220 110 N.A. 102 332
 Water 380 70 267 226 220 0
B-factors
  Protein 33.6 64.9 32.7 62.8 39.4 46.3
  Ligand/ion 58.9 113.2 39.3 N.A. 60.4 63.9
  Water 37.5 52.9 42.2 52.3 46.3 N.A.
 Rmsd
  Bond lengths (Å) 0.007 0.002 0.006 0.003 0.007 0.002
  Bond angles (°) 1.004 0.605 1.039 0.624 0.999 0.589
PDB ID code 5JEJ 5JEK 5JEL 5JEM 5JEO 5JER

One crystal was used to collect each of the datasets. Values in parentheses are for the highest-resolution shells.