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. 2019 May 21;75(Pt 6):439–449. doi: 10.1107/S2053230X19006599

Table 1. Diffraction data-collection and refinement statistics.

Values in parentheses are for the highest resolution shell.

Data collection
 Space group C2221
 Unit-cell parameters (Å) 65.1, 119.2, 72.8
 Resolution (Å) 20.49–1.90 (1.95–1.90)
 No. of reflections 90911 (5816)
 No. of unique reflections 22646 (1436)
 Completeness (%) 99.8 (100.0)
 Multiplicity 4.0 (4.1)
R merge (%) 4.5 (48.7)
R p.i.m. (%) 3.0 (33.8)
 CC1/2 0.999 (0.827)
 Average I/σ(I) 15.8 (2.5)
Refinement
R (%) 20.1 (25.0)
R free (%) 24.3 (30.9)
 No. of reflections in test set 1113 [4.9%]
 No. of protein molecules per asymmetric unit 1
 R.m.s.d., bond lengths (Å) 0.01
 R.m.s.d., bond angles (°) 0.98
 Average B factors2)
  Overall 37.3
  Protein molecules 36.2
  Water molecules 46.3
 Ramachandran plot: residues other than Gly and Pro in
  Most favored regions (%) 99.2
  Additional allowed regions (%) 0.8
  Disallowed regions (%) 0
 PDB code 6ncq

Calculated by BAVERAGE in the CCP4 suite (Winn et al., 2011).

Calculated using MolProbity (Chen et al., 2010).