The backbone conformation of a protein is represented by the (phi , psi, omega) torsion angles of its residues. These angles are grouped into seven domains called A, C, B, P, G, E and O. Domain O (not shown) groups all cis-conformations (omega = 0°). The other six domains correspond to trans-conformations (omega = 180°); A groups alpha-helical and C 3-10-helical structures, B corresponds to beta-like and P to polyproline-like extended conformations and G and E have negative phi angles, mirror-symetrical with A/C and B/P, respectively.

The table below gives, for each amino acid and for each domain the values of the three torsion angles phi psi and omega.
These are the values which are used by PRELUDE to build the predicted structures .

  confos
Ala  
A -62.99 -40.62 180.00
C -81.98 -6.08 180.00
B -129.24 141.62 180.00
P -67.56 138.13 180.00
G 69.33 27.67 180.00
E 124.29 -180.07 180.00
 
Cys 
A -66.57 -41.49 180.00
C -86.18 -6.86 180.00
B-122.25 142.37 180.00
P -71.68 137.12 180.00
G 71.00 31.75 180.00
E 159.50 -182.00 180.00
 
Asp 
A -66.54 -41.22 180.00
C -90.16 1.11 180.00
B-119.50 129.16 180.00
P -71.75 131.32 180.00
G 60.50 38.67 180.00
E 98.50 -177.20 180.00
O -99.00 210.00 0.00
Glu 
A -65.63 -40.90 180.00
C -83.35 -6.32 180.00
B-120.71 136.01 180.00
P -67.76 132.07 180.00
G 60.00 36.62 180.00
E 124.62 -182.00 180.00
 
Phe 
A-62.99 -44.51 180.00
C -91.84 1.34 180.00
B -125.17 137.46 180.00
P -72.45 134.57 180.00
G 61.78 30.44 180.00
E 179.00 -202.00 180.00
 
Gly 
A -65.67 -43.68 180.00
C -85.77 1.73 180.00
B-134.58 167.71 180.00
P-72.89 157.18 180.00
G 85.44 9.80 180.00
E105.54 -171.71 180.00
O-89.00 210.00 0.00
His 
A -67.48 -42.86 180.00
C -96.70 -0.65 180.00
B -129.14 137.86 180.00
P -69.71 134.71 180.00
G 59.38 39.08 180.00
E 132.67 -215.67 180.00
 
Ile 
A -65.19 -44.98 180.00
C -88.15 -5.38 180.00
B-118.70 132.65 180.00
P -73.39 129.79 180.00
E 72.50 -168.00 180.00
 
 
Lys 
A -64.89 -41.63 180.00
C -85.39 -6.48 180.00
B -119.89 141.30 180.00
P -70.78 133.27 180.00
G 65.94 34.94 180.00
E 110.83 -174.25 180.00
 
Leu 
A -65.39 -41.96 180.00
C -85.39 -5.06 180.00
B -117.18 134.20 180.00
P -72.69 135.93 180.00
G 74.38 36.85 180.00
E 80.50 -194.50 180.00
 
Met 
A -66.15 -40.24 180.00
C -88.04 -4.36 180.00
B -126.36 138.63 180.00
P -68.93 130.93 180.00
G 48.75 42.50 180.00
E 114.00 -189.00 180.00
 
Asn 
A -65.79 -41.91 180.00
C -95.82 5.26 180.00
B-121.34 131.40 180.00
P -73.60 130.31 180.00
G 60.05 34.44 180.00
E 79.14 -180.71 180.00
 
Pro 
A -55.68 -38.42 180.00
C -67.59 -9.61 180.00
B -106.20 148.80 180.00
P -63.43 143.52 180.00
G 106.00 65.00 180.00
O -78.57 127.26 0.00
 
Gln 
A -65.41 -40.70 180.00
C -85.21 -6.51 180.00
B -122.35 142.72 180.00
P -72.20 137.59 180.00
G 56.69 39.62 180.00
E 80.25 -206.75 180.00
 
Arg 
A -64.11 -42.92 180.00
C -88.39 -5.79 180.00
B-126.38 133.86 180.00
P -68.87 133.18 180.00
G 60.36 40.79 180.00
E 92.80 -157.80 180.00
 
Ser 
A -64.87 -40.48 180.00
C -85.17 -4.96 180.00
B -127.22 146.43 180.00
P -70.17 143.72 180.00
G 74.53 27.80 180.00
E 108.93 -174.71 180.00
 
Thr 
A -66.17 -42.24 180.00
C -93.19 -2.55 180.00
B -120.61 144.94 180.00
P -73.22 142.94 180.00
G 65.20 39.00 180.00
E 132.17 -163.83 180.00
O -106.00 112.00 0.00
Val 
A -67.46 -42.91 180.00
C -92.25 -5.72 180.00
B -119.95 133.71 180.00
P -74.31 129.00 180.00
G 56.33 25.00 180.00
E 129.00 -221.00 180.00
 
Trp 
A -62.96 -41.89 180.00
C -86.32 -3.29 180.00
B -125.36 145.33 180.00
P -73.91 138.36 180.00
G 71.00 33.00 180.00
 
 
Tyr 
A -66.11 -43.75 180.00
C -93.94 -3.59 180.00
B -125.72 140.55 180.00
P -71.79 134.35 180.00
G 78.54 25.92 180.00
E 174.00 -187.00 180.00
O -114.50 164.00 0.00

null About... (A propos de...) | Crédits | ©2005-2011 J.M. K.