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Table 1 Restraints and statistics for the ensemble of 15 structures

From: A lack of peptide binding and decreased thermostability suggests that the CASKIN2 scaffolding protein SH3 domain may be vestigial

NOE restraints

 

Total

413

Intraresidue (|i – j| = 0)

204

Sequential (|i – j| = 1)

102

Medium range (1 < |i – j| < 5)

8

Long range (|i – j| ≥ 5)

99

Additional restraints

 

Hydrogen bond distance restraints

32

Backbone angle torsion angle restraints

74

RMS deviationsa

 

Bonds

0.0123 ± 0.0003

Angles

1.2827 ± 0.0363

Improper angles

1.6905 ± 0.1112

Dihedral angles

0.2015 ± 0.1411

RMS violations

 

NOE restraints > 0.5 Å

0.0 ± 0.0

NOE restraints > 0.3 Å

2.3 ± 1.2

NOE restraints > 0.1 Å

25.5 ± 4.1

Dihedral angles > 5°

6.2 ± 0.6

Ramachandran analysis for ordered residuesb

 

Most favored regions

95.2 %

Additional allowed regions

4.8 %

Generously allowed regions

0.0 %

Disallowed regions

0.0 %

  1. aAs reported by XPLOR-NIH 2.30 using the standard protein force field
  2. bAs reported by PROCHECK for residues 284–292, 298–312, 320–324, 334–343