Utrophin Actin Binding Region

(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  SER-145   ASP-146  25.7 25.6 -0.8 0.9 130.9 130.5 -1.9  ASP-146   LEU-147  23.8 23.7 -7.1 -2.9 119.4 118.5 -242.2  LEU-147   GLN-148  24.4 24.6 -9.9 15.9 54.9 54.9 -224.3  GLN-148   GLN-149  23.2 24.4 -14.7 -8.4 85.9 81.2 -17.9  GLN-149   THR-150  19.7 20.6 10.0 0.4 51.6 36.5 196.1  THR-150   ASN-151  18.7 20.1 -78.6 89.8 88.4 108.8 72.2  ASN-151   SER-152  21.3 23.2 -64.7 4.3 30.0 47.1 1128.6  SER-152   GLU-153  22.3 24.4 -33.8 42.8 86.2 111.1 106.1  GLU-153   LYS-154  25.4 25.0 -29.1 -22.5 134.2 144.1 -886.5  LYS-154   ILE-155  26.5 26.1 28.5 -23.2 113.2 99.8 5.1  ILE-155   LEU-156  28.8 28.6 19.0 -9.4 119.2 119.9 9.5  LEU-156   LEU-157  30.1 30.1 3.0 -1.5 51.5 52.3 -3.5 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