International
Tables for
Crystallography
Volume C
Mathematical, physical and chemical tables
Edited by E. Prince

© International Union of Crystallography 2006
International Tables for Crystallography (2006). Vol. C. ch. 8.3, p. 701

Table 8.3.2.3 

E. Prince,a L. W. Fingerb and J. H. Konnertc

a NIST Center for Neutron Research, National Institute of Standards and Technology, Gaithersburg, MD 20899, USA,bGeophysical Laboratory, Carnegie Institution of Washington, 5251 Broad Branch Road NW, Washington, DC 20015-1305, USA, and cLaboratory for the Structure of Matter, Code 6030, Naval Research Laboratory, Washington, DC 20375-5000, USA

Table 8.3.2.3 | top | pdf |
Typical values of standard deviations for use in determining weights in restrained refinement of protein structures (after Hendrickson, 1985[link])

Interatomic distances
  Nearest neighbour (bond) σd = 0.02 Å
  Next-nearest neighbour (angle) 0.03 Å
  Intraplanar distance 0.05 Å
  Hydrogen bond or metal coordination 0.05 Å
Planar groups
  Deviation from plane σp = 0.02 Å
Chiral centres
  Chiral volume σc = 0.15 Å3
Nonbonded contacts
  Interatomic distance σn = 0.50 Å
Torsion angles
  Specified (e.g. helix φ and ψ) σt = 15°
  Planar group 3°
  Staggered 15°

Thermal parameters Anisotropic Isotropic
  Main-chain neighbour σv = 0.05 Å σB = 1.0 Å2
  Main-chain second neighbour 0.10 Å 1.5 Å2
  Side-chain neighbour 0.05 Å 1.5 Å2
  Side-chain second neighbour 0.10 Å 2.0 Å2