Putative Groel-Like Chaperonine 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
 GLU-184   GLN-185  7.6 7.9 -20.3 8.8 45.4 44.7 35.6
 GLN-185   THR-186  5.2 5.5 3.2 5.2 144.3 140.9 21.1
 THR-186   THR-187  6.3 6.4 -9.5 -5.4 48.2 63.1 49.1
 THR-187   GLY-188  5.8 6.1 34.2 -45.6 133.8 154.1 23.5
 GLY-188   ARG-189  4.8 5.0 -12.4 17.6 73.9 71.7 -10.4
 ARG-189   THR-190  2.8 2.7 -4.0 0.4 77.0 69.9 12.4
 THR-190   ILE-191  5.7 5.4 23.7 -27.0 154.8 157.9 8.5

Downloading Image

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-386   ARG-387  3.8 3.6 -12.7 10.7 40.4 40.0 3.2
 ARG-387   GLY-388  4.9 4.9 22.7 -60.4 141.4 142.9 115.2
 GLY-388   LYS-389  2.3 2.7 -14.2 26.8 59.5 74.4 -7.3
 LYS-389   LEU-390  1.2 0.8 43.6 -23.0 110.7 108.7 -31.1
 LEU-390   ILE-391  3.0 3.5 2.6 -9.4 158.3 162.8 26.6

Downloading Image

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