Mrna Capping Enzyme

(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
 LYS-234   LEU-235  10.9 11.0 4.3 8.7 108.6 108.0 -17.2
 LEU-235   LYS-236  10.1 10.0 -9.5 21.3 10.6 15.1 27.9
 LYS-236   PRO-237  8.4 8.3 -33.0 -25.9 65.9 65.9 67.3
 PRO-237   GLY-238  7.5 8.1 -149.0 -10.4 88.1 24.6 -267.0
 GLY-238   THR-239  4.5 7.1 -49.3 13.8 47.0 79.8 90.8
 THR-239   HIS-240  2.1 4.7 161.5 56.7 84.2 66.7 -234.0
 HIS-240   HIS-241  3.2 1.6 96.9 49.6 21.3 17.2 433.5
 HIS-241   THR-242  2.1 1.7 8.7 8.7 100.2 87.2 -10.0
 THR-242   ILE-243  5.2 5.3 -6.1 4.6 142.4 150.5 -2.7

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


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
 GLU-308   LYS-309  5.6 5.7 39.0 -39.5 74.8 82.4 -19.9
 LYS-309   THR-310  2.0 2.1 46.2 16.7 17.3 16.0 196.8
 THR-310   LEU-311  2.0 2.8 -20.1 -13.7 106.9 103.6 -66.4

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