Chaperone Protein Htpg

(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  GLN-118   LEU-119  23.6 12.9 1.3 -41.9 32.9 66.2 -33.9  LEU-119   ILE-120  23.0 15.3 167.6 -80.5 93.2 115.7 321.1  ILE-120   GLY-121  23.8 17.8 176.1 -163.2 131.5 55.4 -39.5  GLY-121   GLN-122  21.2 20.1 -171.1 -50.4 110.6 103.0 -61.9  GLN-122   PHE-123  18.0 23.8 -104.4 157.9 143.2 112.0 52.1  PHE-123   GLY-124  19.5 26.8 -15.1 125.0 95.7 165.1 -227.3  GLY-124   VAL-125  22.7 26.0 90.7 -71.6 88.6 57.4 6.3 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

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  LYS-226   ILE-227  7.0 4.1 -92.4 -17.1 49.6 33.1 73.4  ILE-227   ASN-228  9.3 7.0 87.4 -57.2 157.4 150.6 128.1  ASN-228   LYS-229  6.7 5.9 175.4 -36.3 106.7 153.6 -93.0 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