International
Tables for
Crystallography
Volume F
Crystallography of biological macromolecules
Edited by M. G. Rossmann and E. Arnold

© International Union of Crystallography 2006
International Tables for Crystallography (2006). Vol. F. ch. 20.1, p. 488   | 1 | 2 |

Table 20.1.3.4 

U. Stockera and W. F. van Gunsterena

aLaboratory of Physical Chemistry, ETH-Zentrum, 8092 Zürich, Switzerland

Table 20.1.3.4 | top | pdf |
Number of protein-backbone dihedral-angle transitions per 100 ps for the different molecules using different time periods

Dihedral angles with threefold and sixfold potential-energy wells are distinguished. The bottom rows show the averages over all protein molecules.

(a) 120° transitions

Molecule 400–800 ps 400–1200 ps 400–2000 ps
1 46.5 45.4 47.7
2 40.5 41.5 47.3
3 50.5 57.1 51.3
4 44.8 46.4 46.4
All 45.6 47.6 48.2

(b) 60° transitions

Molecule 400–800 ps 400–1200 ps 400–2000 ps
1 245.5 246.6 289.3
2 271.5 272.1 261.3
3 381.5 381.0 348.3
4 356.8 325.4 325.4
All 313.8 306.3 306.1

(c) All transitions

Molecule 400–800 ps 400–1200 ps 400–2000 ps
1 292.0 292.0 336.9
2 312.0 313.7 308.6
3 432.0 438.1 399.6
4 401.5 371.8 371.8
All 359.4 353.9 354.2