Molybdopterin Biosynthesis Protein Moea

(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-41   SER-42  31.5 32.1 5.1 -13.9 83.8 83.2 16.3
 SER-42   ASP-43  32.8 33.7 -26.7 34.8 26.9 25.8 -92.9
 ASP-43   VAL-44  35.0 36.0 -6.1 2.9 55.5 56.4 163.2
 VAL-44   VAL-45  33.2 34.2 14.6 -18.1 114.9 113.5 11.4
 VAL-45   SER-46  34.7 36.0 10.2 -11.7 134.6 130.5 -119.1
 SER-46   PRO-47  34.2 35.4 -9.3 36.7 97.4 98.4 26.4
 PRO-47   LEU-48  33.3 34.6 -56.9 24.0 28.0 30.5 386.5
 LEU-48   ASP-49  33.6 34.7 37.1 -25.9 123.3 132.2 -513.6
 ASP-49   VAL-50  35.9 36.1 -23.8 58.8 46.9 49.1 -312.6
 VAL-50   PRO-51  34.7 34.5 154.8 9.1 138.1 168.6 583.9
 PRO-51   GLY-52  34.3 35.2 -176.8 133.7 117.3 88.4 -546.7
 GLY-52   PHE-53  33.8 35.6 -66.0 52.9 52.3 47.2 203.1
 PHE-53   ASP-54  35.5 35.2 -66.5 36.3 34.8 36.8 384.7
 ASP-54   ASN-55  37.4 37.2 8.7 -6.0 132.3 144.1 -200.7
 ASN-55   SER-56  34.8 35.0 -7.6 5.4 39.3 41.4 31.1

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
 ASN-135   ILE-136  39.7 39.4 -9.7 12.1 47.4 53.8 147.5
 ILE-136   ARG-137  39.4 39.3 8.0 -4.3 151.3 151.8 -193.0
 ARG-137   ARG-138  38.4 38.5 -14.2 7.2 49.2 47.9 68.9
 ARG-138   ARG-139  40.0 40.6 -0.5 -11.9 27.9 23.9 262.0
 ARG-139   GLY-140  38.5 39.4 25.7 -2.9 133.6 128.9 -340.5
 GLY-140   GLU-141  39.2 40.8 -7.9 -15.8 105.1 102.2 2.3
 GLU-141   ASP-142  40.8 41.9 -6.4 -7.9 67.6 67.9 199.4
 ASP-142   ILE-143  38.5 39.5 26.2 47.9 177.1 161.0 -1337.7
 ILE-143   SER-144  38.0 38.8 141.1 161.0 106.7 122.0 729.7
 SER-144   ALA-145  39.7 41.3 -37.6 -4.8 36.2 34.1 600.9
 ALA-145   GLY-146  37.9 39.5 1.1 -13.1 144.2 148.1 120.6
 GLY-146   ALA-147  38.9 40.2 48.1 -24.5 102.8 97.5 -218.2
 ALA-147   VAL-148  39.8 40.9 -4.7 1.3 65.3 55.6 50.9
 VAL-148   VAL-149  38.5 40.0 -40.8 30.9 137.8 129.8 -106.8
 VAL-149   PHE-150  36.9 38.3 -8.3 8.0 74.1 69.4 -76.8
 PHE-150   PRO-151  36.5 37.5 -5.0 3.7 5.5 10.5 111.1
 PRO-151   ALA-152  37.9 38.7 2.3 8.9 119.4 113.8 22.4
 ALA-152   GLY-153  36.0 36.6 10.2 -20.0 90.9 88.9 -55.0
 GLY-153   THR-154  36.9 37.2 17.3 -8.2 28.5 23.4 21.0
 THR-154   ARG-155  36.4 36.8 8.4 -5.3 80.9 77.7 98.9
 ARG-155   LEU-156  34.8 35.2 -7.6 -6.9 151.8 150.5 -165.0

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