TABLE 1

Data collection and refinement statistics for the FOX-4 crystal structures

ParameterCrystal structure
WTY150FY150F
LigandSFX
PDB entry5CGS5CGW5CGX
Data collection
    Resolution range (Å)20.0–1.620.0–1.420.0–1.2
    Wavelength (Å)0.9790.9790.979
    Space groupP21P21P21
    Unit cell dimensions (Å)
        a54.8553.2254.24
        b57.0956.6156.59
        c56.7554.1855.49
        α = γ (o)909090
        β (o)96.4596.2499.23
    No. of observed reflections137,328219,916355,116
    No. of unique reflections41,74862,56496,864
    Completeness (%)a96.5 (87.1)98.5 (93.8)95.4 (92.2)
    II7.6 (2.1)10.2 (2.5)6.4 (1.6)
    Rmerge (I)b0.080 (0.372)0.073 (0.496)0.070 (0.739)
Structural refinement
    Rcryst (%)c0.2010.1720.181
    Rfree (%)c0.2300.2070.205
    No. of protein nonhydrogen atoms2,7042,7812,797
    No. of water molecules220443379
    Average B-factor (Å2)17.214.011.4
RMSD from ideal valued
    Bonds (Å)0.0110.0090.012
    Angles (°)1.361.331.43
    Torsion angles (°)14.112.614.3
    Overall coordinate error (maximum-likelihood)0.210.150.16
Ramachandran statistics (for non-Gly/Pro residues) (%)
    Most favorable97.597.397.3
    Additional allowed2.52.72.7
  • a Values in parentheses indicate statistics for the high-resolution bin.

  • b Rmerge = ΣΣ j|Ij(hkl) − 〈I(hkl)〉|/ΣΣ j|〈I(hkl)〉|, where Ij is the intensity measurement for reflection j, and 〈I〉 is the mean intensity over j reflections.

  • c Rcryst/(Rfree) = Σ ||Fo(hkl)| − |Fc(hkl)||/Σ |Fo(hkl)|, where Fo and Fc are the observed and calculated structure factors, respectively. No σ-cutoff was applied. Five percent of the reflections were excluded from refinement and used to calculate Rfree.

  • d RMSD, root mean square deviation.