Table 1 Data collection and refinement statistics. RMS, root mean square.

Values in parentheses are those for the highest resolution shell.

Protein“Pseudo-apo”–Sestrin2
  OrganismHomo sapiens
  PDB ID5T0N
Data collection
  Space groupI23
    a, b, and c (Å)292.26, 292.26, and 292.26
    α, β, and γ (°)90.0, 90.0, and 90.0
  Wavelength (Å)0.9792
  Resolution range (Å)200.0–3.0 (3.05–3.00)
  Completeness (%)100 (100)
  Redundancy40.7 (41.9)
  Rmeas (%)28.0 (>100)
  Rpim (%)4.4 (37.8)
  I19.5 (2.0)
Refinement
  Resolution range (Å)103.3–3.0
  Rwork (%)18.9
  Rfree (%)22.5
  Number of reflections
    Total82,205
    Rfree reflections1,637
  Number of nonhydrogen atoms14,648
    Protein atoms14,648
  RMS deviations
    Bond lengths (Å)0.010
    Bond angles (°)1.037
  Average B-factor (Å2)
    Protein49.0
  Ramachandran (%)
    Favored96.4
    Allowed3.0
    Outlier0.7