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
 TYR-131   GLY-132  13.5 13.2 -18.3 15.0 88.6 88.3 25.7
 GLY-132   PHE-133  12.2 11.6 -13.1 23.4 98.8 99.3 6.2
 PHE-133   ASP-134  8.5 8.0 12.7 -8.3 123.2 130.1 -21.3
 ASP-134   ASN-135  5.2 4.6 -5.9 16.3 133.5 130.7 58.2
 ASN-135   THR-136  2.7 2.5 8.3 -14.7 124.8 135.1 27.5
 THR-136   TYR-137  1.1 1.0 0.5 0.8 64.7 65.5 11.2

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
 PHE-238   PRO-239  4.2 3.9 -4.3 2.9 111.4 109.9 1.1
 PRO-239   PRO-240  2.0 1.3 4.9 -9.1 143.8 140.7 21.9
 PRO-240   TYR-241  2.4 2.5 -0.2 5.1 58.5 58.3 36.7

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