Aspartate Carbamoyltransferase (Aspartate Transcarbamylase) 3 (T State) (E.C.2.1.3.2)

(All numbering and residues are taken from first PDB file)

Bending Residue Dihedral Analysis

Residue i Residue i+1 Distance of hinge axis to residue i in conformer 1 (A) Distance of hinge axis to residue i in conformer 2 (A) Change in psi (i) (deg) Change in phi (i+1) (deg) Angle of psi(i) axis to hinge axis conformer 1 (deg) Angle of psi(i) axis to hinge axis conformer 2 (deg) Percentage Progress  ILE-224   LEU-225  6.4 6.4 -9.9 3.1 100.1 103.2 -0.1  LEU-225   TYR-226  2.8 2.8 6.7 -0.3 125.3 133.4 -9.8  TYR-226   MET-227  2.6 2.6 -16.8 21.4 89.1 82.6 21.1 Graph shows rotational transition at bending residues and can be used to identify hinge bending residues. Probably only informative for interdomain rotations greater than 20 degrees

Residue i Residue i+1 Distance of hinge axis to residue i in conformer 1 (A) Distance of hinge axis to residue i in conformer 2 (A) Change in psi (i) (deg) Change in phi (i+1) (deg) Angle of psi(i) axis to hinge axis conformer 1 (deg) Angle of psi(i) axis to hinge axis conformer 2 (deg) Percentage Progress  ARG-250   ALA-251  11.0 10.9 12.9 0.0 99.9 97.9 12.4  ALA-251   SER-252  11.9 12.0 -13.3 -9.0 39.7 32.9 85.4  SER-252   ASP-253  14.8 14.6 40.3 -23.6 149.9 151.1 -87.3 Graph shows rotational transition at bending residues and can be used to identify hinge bending residues. Probably only informative for interdomain rotations greater than 20 degrees