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  11.2 11.2 0.3 -7.5 94.0 95.7 -16.4
 LEU-235   LYS-236  8.1 8.1 -3.3 -38.6 51.5 47.3 122.8
 LYS-236   PRO-237  5.2 5.7 -60.8 1.4 60.5 77.4 -5.3
 PRO-237   GLY-238  3.2 2.8 -154.3 175.4 113.5 71.3 -1.2
 GLY-238   THR-239  1.8 2.0 175.7 -6.2 26.9 69.9 -443.6
 THR-239   HIS-240  1.9 5.1 141.7 25.7 92.3 37.5 270.5
 HIS-240   HIS-241  3.8 6.4 90.4 9.2 51.0 49.0 222.1
 HIS-241   THR-242  5.0 5.1 -31.9 15.7 98.6 114.8 -16.0
 THR-242   ILE-243  8.6 8.8 -10.3 0.0 152.2 145.6 -38.1

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  4.4 4.6 36.8 -31.6 48.1 56.5 -16.7
 LYS-309   THR-310  4.5 3.8 32.2 11.8 33.6 36.4 129.1
 THR-310   LEU-311  3.8 3.0 -12.6 -9.5 83.3 97.2 -5.5
 LEU-311   LEU-312  2.3 1.7 14.7 -5.0 88.7 83.6 -20.6
 LEU-312   ASN-313  1.5 2.8 -8.9 17.1 160.3 168.4 33.2
 ASN-313   ILE-314  2.0 2.5 -7.3 -6.6 120.2 125.5 -19.3
 ILE-314   GLU-315  2.2 2.1 10.8 -0.6 101.4 95.5 -15.3

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