Apolipoprotein A-I

(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  LEU-181   LYS-182  16.5 14.9 19.1 -21.1 26.3 75.2 -3.1  LYS-182   GLU-183  17.1 12.4 13.2 -21.9 63.5 22.2 -0.5  GLU-183   ASN-184  14.9 12.5 26.4 -15.3 108.2 81.8 -1.2  ASN-184   GLY-185  11.9 13.0 -12.6 -18.2 86.7 52.2 13.6  GLY-185   GLY-186  12.7 10.9 28.4 -34.7 38.9 79.7 -2.9  GLY-186   ALA-187  11.9 7.7 1.8 -30.3 89.0 30.8 -11.2  ALA-187   ARG-188  8.4 7.7 40.9 -4.3 113.1 88.2 -17.1  ARG-188   LEU-189  7.9 9.3 -18.9 -34.9 116.8 75.6 8.4  LEU-189   ALA-190  10.5 6.9 52.9 -22.4 50.7 62.4 21.4  ALA-190   GLU-191  7.8 3.9 -19.1 -45.6 66.3 126.7 12.7  GLU-191   TYR-192  6.6 5.9 -17.0 -85.0 90.7 75.7 -72.6  TYR-192   HIS-193  10.2 9.6 -34.7 -65.9 156.8 76.2 148.9 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