Glycine Betaine/carnitine/choline-Binding Protein

(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  ASN-115   THR-116  0.8 0.6 -3.8 2.3 121.5 120.3 4.1  THR-116   TYR-117  3.6 3.6 4.0 -4.9 33.6 33.6 43.4  TYR-117   ALA-118  4.8 4.8 -0.7 1.6 127.1 126.2 20.7 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  LEU-146   GLY-147  9.0 9.0 -1.9 4.4 125.5 122.8 -97.7  GLY-147   VAL-148  9.6 9.7 -4.6 16.4 156.1 157.2 133.1  VAL-148   ASP-149  10.3 10.4 -2.2 10.6 129.2 130.3 75.7  ASP-149   ASN-150  11.9 11.7 -4.3 0.0 89.7 90.6 16.4  ASN-150   TYR-151  15.6 15.5 0.7 -7.6 56.7 53.0 -108.8  TYR-151   TRP-152  15.4 15.2 2.3 -3.7 111.0 105.8 -1.6  TRP-152   MET-153  13.6 13.5 2.1 -10.2 129.6 121.3 76.1  MET-153   LYS-154  16.1 16.3 8.3 18.0 62.2 57.8 191.0  LYS-154   LEU-155  18.9 18.9 0.3 -10.5 32.3 44.8 -59.3  LEU-155   LYS-156  17.1 17.4 -4.3 3.3 86.9 71.8 -123.4  LYS-156   GLY-157  19.3 20.1 1.3 -8.1 81.1 83.2 -163.9  GLY-157   ASN-158  17.3 18.0 -24.4 38.8 38.2 51.5 51.5  ASN-158   GLY-159  14.7 15.0 -1.0 2.3 55.9 38.3 -131.5  GLY-159   TYR-160  14.9 15.4 -0.4 -0.4 20.5 17.0 72.9  TYR-160   GLN-161  15.4 15.5 -5.0 -1.3 77.1 73.2 43.5  GLN-161   ASP-162  19.0 19.1 9.3 1.2 84.4 78.9 -51.4 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  TYR-221   ASP-222  5.7 5.6 -0.2 -3.3 127.5 127.1 -46.7  ASP-222   CYS-223  4.6 4.4 3.2 0.7 56.4 56.3 30.2  CYS-223   SER-224  1.6 1.5 1.0 -1.7 14.0 12.0 3.6 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