Ubiquitin-Activating Enzyme E1c

(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
 VAL-211   ASN-212  18.5 17.6 31.2 -37.2 161.4 164.3 95.8
 ASN-212   PHE-213  20.2 19.3 -27.5 12.1 87.5 93.1 2.1
 PHE-213   PRO-214  21.7 21.5 28.9 16.5 131.3 132.0 -366.0
 PRO-214   MET-215  25.2 25.1 5.5 -1.9 129.8 143.0 49.3
 MET-215   ALA-216  24.8 25.5 3.4 -33.2 87.1 85.3 -38.5
 ALA-216   THR-217  28.3 28.5 13.7 5.7 63.0 58.0 132.4

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


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
 LYS-286   ARG-287  6.9 6.8 -14.5 6.1 45.8 43.6 127.1
 ARG-287   ILE-288  9.2 9.2 8.3 -5.0 128.4 134.0 18.3
 ILE-288   ILE-289  6.1 6.3 -19.1 12.1 22.4 22.9 56.7
 ILE-289   PRO-290  6.2 7.0 0.7 6.9 121.1 123.9 -129.4
 PRO-290   ALA-291  3.6 4.6 -0.3 -9.8 72.5 73.3 24.5

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