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  VAL-208   GLU-209  4.4 4.0 -1.4 2.4 38.2 39.6 -4.6  GLU-209   ILE-210  3.0 2.8 -3.0 4.8 31.6 31.4 -11.4  ILE-210   GLU-211  3.1 2.7 0.3 19.1 131.5 128.7 -132.3  THR-220   VAL-221  8.7 6.3 48.2 -23.8 13.0 59.4 37.2  THR-220   VAL-221  8.7 6.3 48.2 -23.8 13.0 59.4 37.2 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  THR-220   VAL-221  8.7 6.3 48.2 -23.8 13.0 59.4 37.2  THR-220   VAL-221  8.7 6.3 48.2 -23.8 13.0 59.4 37.2  VAL-221   ILE-222  9.1 8.5 33.0 10.8 63.0 43.8 415.6  ILE-222   SER-223  6.5 8.1 -66.0 14.3 152.1 142.9 -519.1  SER-223   TRP-224  7.2 7.8 -17.0 -5.4 120.3 120.4 -166.9  TRP-224   GLU-225  5.0 5.6 6.9 -23.9 71.8 73.4 -67.4  GLU-225   LYS-226  6.7 6.8 -14.5 13.5 138.5 125.5 92.5  LYS-226   ILE-227  7.1 7.0 -14.3 3.7 78.8 73.3 15.2  ILE-227   ASN-228  9.0 8.5 -38.0 66.2 114.5 127.3 166.7  ASN-228   LYS-229  11.5 10.7 -9.2 -0.1 94.8 91.8 -47.7  LYS-229   ALA-230  13.5 13.2 -6.2 0.9 155.3 155.4 -57.1 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