Bifunctional Purine Biosynthesis Protein Purh

(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
 LEU-103   TYR-104  9.7 9.5 26.8 2.4 86.0 64.1 184.9
 TYR-104   PRO-105  8.9 7.1 3.9 -5.4 150.9 135.7 48.1
 PRO-105   PHE-106  9.1 9.0 -51.1 -7.4 94.1 64.0 158.5
 PHE-106   VAL-107  6.2 6.6 -20.7 5.1 80.4 52.4 129.3
 VAL-107   LYS-108  9.2 9.1 -4.9 -0.9 146.3 114.2 -89.4
 LYS-108   THR-109  10.9 11.9 -15.9 12.1 126.2 112.6 -87.6
 THR-109   VAL-110  8.0 10.1 1.2 -12.1 105.7 126.8 99.5
 VAL-110   ALA-111  9.5 10.1 23.3 -0.9 83.4 119.2 -90.2
 ALA-111   SER-112  13.0 13.4 -27.5 16.1 161.6 128.9 -138.9
 SER-112   PRO-113  12.9 14.9 22.3 -12.1 84.7 92.7 64.4
 PRO-113   GLY-114  15.7 17.5 -11.0 -12.0 111.7 114.8 -160.4
 GLY-114   VAL-115  15.4 16.7 45.1 -3.3 95.0 70.5 36.8
 VAL-115   THR-116  11.8 12.9 16.5 -30.8 133.1 99.0 127.5
 THR-116   VAL-117  12.2 12.1 -7.2 1.5 53.5 76.8 5.7
 VAL-117   GLU-118  10.5 9.8 9.0 4.4 59.6 37.1 167.5
 GLU-118   GLU-119  9.7 8.9 -7.4 3.4 126.3 100.0 -126.0
 GLU-119   ALA-120  7.8 7.7 -17.5 6.7 57.9 49.9 51.1
 ALA-120   VAL-121  6.2 6.1 -1.7 5.8 77.5 96.7 -64.7
 VAL-121   GLU-122  4.9 4.1 4.4 -4.9 39.3 38.9 -1.4
 GLU-122   GLN-123  4.3 2.8 -3.2 -2.9 98.2 79.4 -1.5
 GLN-123   ILE-124  1.3 3.2 4.0 -19.4 136.7 135.8 169.1
 ILE-124   ASP-125  0.9 1.4 -12.2 -5.0 113.1 119.0 -134.2
 ASP-125   ILE-126  4.4 4.9 9.7 -4.6 115.2 113.5 13.0
 ILE-126   GLY-127  7.3 7.1 -0.5 -7.9 101.5 98.6 -85.4
 GLY-127   GLY-128  10.1 10.2 7.1 3.7 110.5 110.1 -37.0
 GLY-128   VAL-129  10.5 10.7 -1.2 -4.6 14.0 17.1 82.3
 VAL-129   THR-130  10.1 10.4 9.0 -11.0 96.3 97.9 -16.5

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


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
 THR-182   ALA-183  9.7 10.0 3.7 -7.6 143.3 141.7 40.6
 ALA-183   GLN-184  8.5 8.7 7.9 -2.3 85.2 89.8 -15.6
 GLN-184   TYR-185  7.9 8.4 -7.9 8.8 136.6 134.1 -11.6
 TYR-185   ASP-186  5.9 6.6 -5.8 -2.7 70.5 74.3 -0.4

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