Udp-N-Acetylmuramate-L-Alanine Ligase

(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
 ALA-318   ASP-319  5.3 5.5 7.1 9.4 99.4 103.3 -17.3
 ASP-319   PHE-320  3.2 3.7 -57.5 69.1 85.1 91.8 15.7
 PHE-320   GLN-321  0.5 0.1 19.3 -8.5 48.7 66.1 6.7
 GLN-321   GLY-322  4.0 3.7 -175.2 172.9 103.5 117.9 19.3
 GLY-322   ALA-323  6.5 5.3 167.1 -171.9 125.1 123.5 3.8
 ALA-323   GLY-324  8.8 8.9 99.1 141.9 68.2 63.1 -95.6
 GLY-324   ARG-325  11.3 11.8 -56.4 159.3 125.2 144.5 237.4
 ARG-325   ARG-326  12.2 13.4 -48.2 -8.5 154.1 125.0 -83.9
 ARG-326   PHE-327  9.7 10.5 -35.4 -7.3 103.8 114.5 -2.5
 PHE-327   ASP-328  8.4 8.6 8.3 -11.7 130.8 125.6 16.1

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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