Table S1.

Crystallographic data measurement and refinement data

Data collection and refinementFBPS-N (native)FBPS-N (SeMet)FBPS-C (native)FBPS-C (SeMet)
Data collection
 Space groupP41212P41212P21P21
 Cell dimensions
  a, b, c, (Å)70.6, 70.6, 110.270.5, 70.5, 110.040.3, 103.6, 83.340.5, 104.1, 84.5
  α, β, γ, (°)90.0, 90.0, 90.090.0, 90.0, 90.090.0, 92.2, 90.090.0, 92.3, 90.0
PeakPeak
 Wavelength (Å)1.00000.97951.00000.9795
 Resolution* (Å)50.0–2.10 (2.18–2.10)50.0–2.80 (2.90–2.80)50.0–2.60 (2.69–2.60)50.0–2.90 (2.95–2.90)
 Rsys or Rmerge*0.084 (0.512)0.096 (0.497)0.115 (0.338)0.125 (0.539)
 I/σI*29.98 (3.76)25.46 (4.31)17.57 (2.98)15.23 (1.49)
 Completeness* (%)97.6 (90.0)100.0 (100.0)97.1 (79.4)88.2 (44.1)
 Redundancy*12.9 (10.2)15.2 (14.6)6.5 (3.7)6.3 (2.3)
 Total reflections214,164202,544137,03488,862
 Unique reflections16,62213,35021,05814,070
Refinement
 Resolution (Å)33.60–2.1038.61–2.60
 Rwork/Rfree0.216/0.2460.219/0.249
 No. atoms
  Protein2,1594,001
  Water12989
 B-factors
  Protein40.058.9
  Water39.058.5
 Rmsd
  Bond lengths (Å)0.0130.010
  Bond angles, degrees1.2151.315
 Ramachandran plot§
  Most favored region (%)86.891.6
  Additionally allowed region (%)12.08.2
  Generously allowed region (%)1.20.2
  Disallowed region (%)00
  • * Values for the outmost resolution shell are given in parentheses.

  • Rmerge = ΣiΣhkl | Ii-<I> | /ΣiΣhklIi, where Ii is the observed intensity and <I> is the average intensity from multiple measurements.

  • Rwork = Σ | | Fo |− | Fc | | /Σ | Fo |, where Fo and Fc are the structure-factor amplitudes from the data and the model, respectively. Rfree is the R factor for a subset (5%) of reflections that was selected before refinement calculations and was not included in the refinement.

  • § Ramachandran plots were generated by using the program PROCHECK.