Glutamate Receptor Ionotropic, Nmda 2A

(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
 THR-134   GLY-135  4.8 4.9 3.4 13.0 29.9 35.0 63.3
 GLY-135   ILE-136  2.7 2.5 19.2 -29.2 101.6 103.6 5.3
 ILE-136   SER-137  3.0 2.4 21.6 -23.0 121.3 117.4 36.3

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-232   THR-233  10.5 10.2 7.0 -4.5 158.4 158.0 -27.3
 THR-233   ILE-234  8.9 8.4 -13.6 -51.1 62.6 56.7 221.3
 ILE-234   GLY-235  10.9 10.1 -41.0 5.7 97.4 45.7 53.2
 GLY-235   SER-236  12.1 8.4 -4.3 -14.7 47.4 28.4 90.9
 SER-236   GLY-237  10.5 8.2 10.1 134.6 157.9 124.9 -557.2
 GLY-237   TYR-238  12.9 10.5 -112.1 24.7 52.2 25.2 456.7
 TYR-238   ILE-239  11.3 10.2 -8.8 -5.1 82.6 68.1 50.0
 ILE-239   PHE-240  7.6 8.5 -168.6 -44.5 9.7 82.6 -578.3
 PHE-240   ALA-241  6.2 4.9 9.5 -131.2 99.7 80.4 23.4
 ALA-241   THR-242  4.2 5.0 104.8 -27.5 43.4 28.5 318.2
 THR-242   THR-243  6.4 6.2 5.6 11.7 104.6 104.9 -20.4
 THR-243   GLY-244  7.2 6.6 -1.0 -2.2 156.2 148.6 -12.4

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