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Table 1 Structure statistics of PrsA-PPIase

From: Solution structure of the parvulin-type PPIase domain of Staphylococcus aureus PrsA – Implications for the catalytic mechanism of parvulins

Total distance restraints

2161

   Short-range |i - j| ≤ 1

1081

   Medium-range, 1 < |i - j| < 5

379

   Long-range, |i - j| ≥ 5

764

   Restraints per residue

19.5

Violation statistics

   Maximum NOE restraint violation (Å)

0.16

   Number of NOE violations > 0.10 Å

3 ± 2

Energies

   Average restraint violation energy (kcal/mol ± SD)

9.55 ± 0.86

   Average AMBER energy (kcal/mol ± SD)

-3259.69 ± 8.55

RMS deviations from ideal covalent geometry

   Bond lengths (Å ± SD)

0.0096 ± 0.0001

   Bond angles (° ± SD)

1.93 ± 0.02

Atomic coordinate RMSD (Å ± SD) for residues 140–243 and (140–152, 160–243)

   Backbone atoms

0.55 ± 0.18 (0.31 ± 0.05)

   Heavy atoms

1.07 ± 0.20 (0.80 ± 0.06)

Ramachandran map regions (%)

   Residues in most favoured regions

93.9

   Additionally allowed regions

5.9

   Generously allowed regions

0.2

   Disallowed regions

0.0