Table 1 Data collection and refinement statistics.

From: Molecular basis of the interaction of the human tyrosine phosphatase PTPN3 with the hepatitis B virus core protein

 

PTPN3-PDZ/ PBM-HBc

Data collection

Space group

P 31 2 1

Unit cell (a, b, c) (Å)

75.58, 75.58, 46.59

α, β, γ (°)

90.00, 90.00, 120.00

Resolution (Å)

46.59–1.86 (1.96–1.86)

No. of reflections (total/unique)

67,510/13,198

Redundancy

5.1 (5.0)

Completeness (%)

99.4 (97.8)

I/σ (I)

17.38 (2.70)

R-meas (%)

5.6 (57.5)

CC(1/2)

99.9 (97.7)

Refinement

Resolution (Å)

29.35–1.86

No. reflections

13,066

Rwork†/Rfree‡

0.197/0.236

No. of protein atoms/ligand atoms

749/63

No. of solvent/hetero-atoms

68/1

Rmsd bond lengths (Å)

0.007

Rmsd bond angles (°)

0.836

Wilson B-factors

28.6

Ramachandran plot (favored/disallowed)*

96.9/0.0

PDB code

6T36

  1. Values in parenthesis correspond to the highest resolution shell.
  2. Rmeas = Σh(n/n−1)1/2Σi |Ii(h)—<I(h)>|/ΣhΣi Ii(h), where Ii(h) and <I(h)> are the ith and the mean measurement, respectively, of the intensity of reflection h.
  3. †Rwork = Σh||Fobs(h)|−|Fcalc(h)||/Σh|Fobs(h)|, where Fobs(h) and Fcalc(h) are the observed and calculated structure factors, respectively. No I/σ cut-off was applied.
  4. ‡Rfree is the R-value obtained for a test set of reflections consisting of a randomly selected 5% subset of the data set excluded from refinement.
  5. *Categories were defined by MolProbity.
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