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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.