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Table 1 Crystallographic Statistics

From: Crystal structure of an FIV/HIV chimeric protease complexed with the broad-based inhibitor, TL-3

Unit Cell
Space group P3121
a, b, c (Å) 50.32 50.32 74.16
VM3/Da) 2.5
Solvent content (%) 49.7
Monomers/asymmetric unit 1
Data Collection
SSRL beam line BL 1-5
Wavelength (Å) 0.979
Resolution range (Å) 74.0 – 1.70
Observations 77,552
Reflections 12,424
Redundancy 6.2 (6.0)
Completeness (%)[1] 99.7 (99.6)
<I>/<σI> 15.7 (2.6)
Rsymm(I)[2] 0.070 (0.368)
Refinement
Reflections > 0.0 σF 12,396
R-factor[3] 0.184
Rfree (% of data) 0.233 (5.0)
R.m.s. deviation, bonds (Å) 0.011
R.m.s. deviation, angles (deg)[4] 1.47
Model
Protein Atoms <B-factor> (Å 2 )
Protein[5] 1,134 21.2/24.6[6]
TL-3 33 19.8
Water molecules 121 38.5
  1. [1] Values for highest resolution shell in parentheses.
  2. [2] Rsymm = ΣhklΣi|Ii(hkl) - I(hkl)|/ΣhklΣi(I(hkl)) where Ii(hkl) is the intensity of an individual measurement, and I(hkl) is the mean intensity of this reflection.
  3. [3] R-factor = Σhkl|Fobs| - |Fcalc|/Σhkl|Fobs|, where |Fobs| and |Fcalc| are observed and calculated structure factor amplitudes, respectively.
  4. [4] Ramachandran plot: 95.9% of residues in most favored regions; 3.1% in allowed regions, 1.0% in disfavored regions.
  5. [5] Includes residues with alternate conformations.
  6. [6] Average B-factors for main chain and side atoms, respectively.
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