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. Author manuscript; available in PMC: 2009 May 1.
Published in final edited form as: J Thromb Haemost. 2008 Feb 25;6(5):837–845. doi: 10.1111/j.1538-7836.2008.02937.x

Table 4.

Crystallographic data for human thrombin bound to FM19 (PDB ID 3BV9)

Data collection
  Wavelength (Å) 0.9
  Space group P6122
  Unit cell dimension (Å) a = 80.9, b = 80.9, c = 183.7
  Molecules/asymmetric unit 1
  Resolution range (Å) 40.0–1.8
  Observations 247 117
  Unique observations 32 820
  Completeness (%) 96.9 (87.6)
  Rsym (%) 7.8 (24.1)
  I/σ(I) 19.8 (3.2)
Refinement
  Resolution (Å) 40.0–1.8
  |F|/σ(|F|) >0
  Rcryst, Rfree 0.190, 0.239
  Reflections (working/test) 31 172/1634
  Protein atoms 2323
  Solvent molecules 273
  Inhibitor atoms 47
  Glycerol/Na+/I− 2/1/3
  Rmsd bond lengths*(Å) 0.012
  Rmsd angles*(°) 1.7
  Rmsd ΔB (Å2) (mm/ms/ss) 3.40/3.99/5.46
  <B> protein (Å2) 26.8
  <B> solvent (Å2) 34.2
  <B> glycerol/Na+/I− (Å2) 52.8/22.5/29.7
Ramachandran plot
  Most favored (%) 99.2
  Generously allowed (%) 0.8
  Disallowed (%) 0.0

mm, main chain–main chain; ms, main chain–side chain; ss, side chain–side chain.

*

Root-mean-squared deviation (rmsd) from ideal bond lengths and angles and rmsd in B-factors of bonded atoms.