TABLE 1.

X-ray diffraction and model refinement statistics for the Z13e1-peptide complexa

StatisticData
Crystal
    Space groupP41212
    Unit cell constants (Å,°)a = b = 106.9; c = 88.8; α, β, γ = 90
Data set statistics
    Resolutionb (Å)30.0-1.80 (1.83-1.80)
    No. of observations690,654 (51,453)
    No. of unique reflections48,156 (3,528)
    Mosaicity (°)0.22
    Completeness (%)99.8 (100.0)
    Multiplicitiy14.3 (14.6)
    II32.2 (5.3)
    Rsym (%)4.7 (55.3)
Refinement statistics
    Rcryst (%)21.0
    Rfree (%)25.2
    No. of protein atoms3,210
    No. of peptide atoms83
    No. of water molecules230
    Wilson B value29.2
    Avg B value (Å2)40.4
        Light chain38.0
        Heavy chain43.0
        Peptide41.7
        Water38.8
    RMS deviation for bond
        lengths (Å)0.016
    RMS deviation for bond
        angles (°)1.55
Ramachandran plotc (%)97.0 (0.0)
  • a Rsym = Σ|Ii − <Ii>|/Σ|Ii|, where Ii is the scaled intensity of the ith measurement, and <Ii> is the mean intensity for that reflection. Rcryst = Σ‖Fobs|−|Fcalc‖/Σ|Fobs|, where Fcalc and Fobs are the calculated and observed structure factor amplitudes, respectively. Rfree = as for Rcryst, but for 5% of the total reflections chosen at random and omitted from refinement. RMS, root mean square.

  • b Statistics for the highest resolution shell are in parentheses.

  • c Percentage of residues in the favored region of the Ramachandran plot generated by MolProbity (21) (outliers are in parentheses).