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  4.3 4.2 6.5 9.9 29.7 36.4 74.1
 GLY-135   ILE-136  2.8 2.1 19.3 -26.9 100.7 104.4 -10.3
 ILE-136   SER-137  3.9 3.2 19.8 -14.7 121.8 120.1 33.8

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  11.4 10.9 6.0 4.9 158.5 163.8 -78.5
 THR-233   ILE-234  9.7 9.3 -19.7 -42.3 63.5 58.7 215.0
 ILE-234   GLY-235  11.7 11.2 -33.2 9.4 98.3 47.3 32.6
 GLY-235   SER-236  12.6 9.9 -11.6 -18.8 47.4 30.4 146.5
 SER-236   GLY-237  10.8 9.2 8.9 132.2 157.0 128.7 -524.3
 GLY-237   TYR-238  13.4 11.1 -106.8 22.4 51.2 23.7 422.5
 TYR-238   ILE-239  12.0 11.1 -14.0 -6.0 81.7 64.3 56.1
 ILE-239   PHE-240  8.2 9.3 -172.7 -37.0 9.5 84.2 -539.1
 PHE-240   ALA-241  6.9 5.7 14.1 -144.7 99.9 81.5 29.5
 ALA-241   THR-242  4.6 4.9 90.8 -16.6 42.8 32.7 281.8
 THR-242   THR-243  6.4 5.9 11.4 4.2 104.5 108.1 -27.8
 THR-243   GLY-244  6.7 6.0 -4.0 2.4 156.5 149.9 -5.7

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