Glycine Receptor Subunit Alphaz1

(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
 SER-247   LEU-248  9.6 9.9 3.7 -2.8 101.3 98.2 -29.7
 LEU-248   LEU-249  9.5 9.8 1.2 13.0 34.9 30.7 155.3
 LEU-249   ILE-250  10.4 10.5 -19.0 12.1 128.1 117.8 -102.1
 ILE-250   VAL-251  7.4 7.4 -4.8 1.7 66.2 63.4 -42.7
 VAL-251   ILE-252  5.2 5.3 4.7 -2.9 77.7 76.0 -16.6
 ILE-252   LEU-253  8.2 8.0 3.2 10.9 22.0 29.1 255.5
 LEU-253   SER-254  7.1 6.5 -14.1 14.2 90.5 88.5 56.7
 SER-254   TRP-255  3.9 4.0 -6.6 8.7 76.6 79.2 121.2
 TRP-255   VAL-256  6.7 7.4 -15.1 -2.2 137.4 141.9 -321.9
 VAL-256   SER-257  8.9 9.2 -8.0 -1.5 126.4 128.0 -55.4
 SER-257   PHE-258  6.9 6.8 -7.3 11.5 73.6 78.5 -162.8
 PHE-258   TRP-259  9.5 9.0 -1.9 -2.1 111.2 117.1 -68.3

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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