Chitin Oligosaccharide 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
 TYR-240   PRO-241  7.4 7.2 3.9 -4.1 45.3 48.5 3.2
 PRO-241   ALA-242  7.2 7.2 18.4 -5.7 76.1 70.8 15.2
 ALA-242   ALA-243  4.0 4.5 -5.0 8.0 135.9 130.3 11.4
 ALA-243   GLY-244  2.0 1.6 15.2 19.5 68.2 64.5 25.7
 GLY-244   THR-245  2.2 2.0 -40.7 -1.9 54.6 63.5 45.8
 THR-245   GLN-246  5.5 5.2 -7.4 1.4 63.6 66.4 -2.1

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
 VAL-482   MET-483  10.8 10.7 -11.5 12.2 102.9 100.2 2.1
 MET-483   SER-484  7.2 7.1 2.0 -0.6 133.5 133.2 0.2
 SER-484   GLY-485  3.9 3.8 18.9 23.2 47.5 49.5 54.3
 GLY-485   ALA-486  1.9 1.1 -24.8 29.0 77.2 98.5 9.6
 ALA-486   TRP-487  3.0 2.6 -10.8 -17.3 82.6 68.1 16.2
 TRP-487   MET-488  6.6 6.0 43.4 -31.1 31.7 34.4 17.5
 MET-488   TYR-489  8.1 8.3 -7.1 -5.7 77.1 78.8 5.9
 TYR-489   GLN-490  11.5 11.4 -7.2 1.5 143.6 144.9 -9.0

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