DSSP OUTPUT
==== Secondary Structure Definition by the program DSSP, CMBI version 3.0.1 ==== DATE=2019-06-21 .
REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 .
HEADER TOXIN 26-JAN-00 1ED0 .
COMPND MOL_ID: 1; MOLECULE: VISCOTOXIN A3; CHAIN: A .
SOURCE MOL_ID: 1; ORGANISM_SCIENTIFIC: VISCUM ALBUM; ORGANISM_COMMON: EUROPEA .
AUTHOR S.ROMAGNOLI,R.UGOLINI,F.FOGOLARI,G.SCHALLER,K.URECH, M.GIANNATTASIO,L. .
46 1 3 3 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) .
2984.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) .
24 52.2 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES .
0 0.0 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES .
3 6.5 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES .
0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-5), SAME NUMBER PER 100 RESIDUES .
0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-4), SAME NUMBER PER 100 RESIDUES .
0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-3), SAME NUMBER PER 100 RESIDUES .
0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-2), SAME NUMBER PER 100 RESIDUES .
0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-1), SAME NUMBER PER 100 RESIDUES .
0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+0), SAME NUMBER PER 100 RESIDUES .
0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+1), SAME NUMBER PER 100 RESIDUES .
0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES .
2 4.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES .
16 34.8 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES .
2 4.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+5), SAME NUMBER PER 100 RESIDUES .
1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 *** HISTOGRAMS OF *** .
0 0 0 0 0 0 0 1 0 0 0 1 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 RESIDUES PER ALPHA HELIX .
0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 PARALLEL BRIDGES PER LADDER .
0 1 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 ANTIPARALLEL BRIDGES PER LADDER .
1 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 LADDERS PER SHEET .
# RESIDUE AA STRUCTURE BP1 BP2 ACC N-H-->O O-->H-N N-H-->O O-->H-N TCO KAPPA ALPHA PHI PSI X-CA Y-CA Z-CA CHAIN AUTHCHAIN
1 1 A K 0 0 78 0, 0.0 34,-2.5 0, 0.0 2,-0.2 0.000 360.0 360.0 360.0-175.6 2.4 0.6 -0.7 A A
2 2 A S E -A 34 0A 17 32,-0.2 2,-0.5 44,-0.1 32,-0.2 -0.567 360.0-151.6 -79.6 145.8 4.8 3.5 -1.5 A A
3 3 A a E +A 33 0A 1 30,-3.1 30,-2.2 -2,-0.2 43,-0.1 -0.955 17.2 175.9-135.9 104.0 3.1 6.8 -2.5 A A
4 4 A b - 0 0 0 -2,-0.5 42,-1.5 40,-0.3 28,-0.1 -0.871 31.6-135.1-118.8 145.1 4.9 9.3 -4.8 A A
5 5 A P S S+ 0 0 40 0, 0.0 2,-0.3 0, 0.0 -1,-0.1 0.841 82.7 7.7 -65.9 -39.5 3.6 12.6 -6.3 A A
6 6 A N S > S- 0 0 98 38,-0.1 4,-2.4 1,-0.1 5,-0.1 -0.883 72.7-105.9-143.0 167.0 4.8 12.0 -9.8 A A
7 7 A T H > S+ 0 0 76 -2,-0.3 4,-2.6 2,-0.2 5,-0.1 0.901 121.4 54.0 -61.0 -43.8 6.4 9.6 -12.3 A A
8 8 A T H > S+ 0 0 111 2,-0.2 4,-2.2 1,-0.2 -1,-0.2 0.853 109.5 48.1 -60.8 -36.0 9.7 11.6 -12.0 A A
9 9 A G H > S+ 0 0 11 2,-0.2 4,-2.9 1,-0.2 -2,-0.2 0.905 110.1 50.7 -71.6 -43.4 9.5 11.2 -8.2 A A
10 10 A R H X S+ 0 0 41 -4,-2.4 4,-2.4 1,-0.2 -2,-0.2 0.897 111.1 51.6 -54.9 -41.5 8.8 7.4 -8.5 A A
11 11 A N H X S+ 0 0 89 -4,-2.6 4,-2.1 2,-0.2 -2,-0.2 0.924 113.2 41.4 -65.6 -47.4 11.9 7.3 -10.9 A A
12 12 A I H X S+ 0 0 67 -4,-2.2 4,-2.7 2,-0.2 5,-0.2 0.942 115.0 51.4 -68.3 -45.3 14.2 9.1 -8.4 A A
13 13 A Y H X S+ 0 0 7 -4,-2.9 4,-2.3 1,-0.2 -2,-0.2 0.908 113.3 46.9 -50.3 -46.7 12.8 7.1 -5.5 A A
14 14 A N H X S+ 0 0 70 -4,-2.4 4,-2.7 -5,-0.2 -1,-0.2 0.836 110.0 51.3 -67.7 -37.2 13.4 3.9 -7.5 A A
15 15 A A H X S+ 0 0 42 -4,-2.1 4,-2.0 2,-0.2 -2,-0.2 0.891 110.3 49.6 -70.2 -39.6 17.0 5.0 -8.5 A A
16 16 A c H <>S+ 0 0 13 -4,-2.7 5,-1.9 2,-0.2 -2,-0.2 0.969 114.3 45.6 -57.9 -54.5 17.8 5.6 -4.9 A A
17 17 A R H ><5S+ 0 0 97 -4,-2.3 3,-1.6 1,-0.2 -2,-0.2 0.908 110.6 52.1 -54.6 -49.5 16.4 2.2 -3.9 A A
18 18 A L H 3<5S+ 0 0 143 -4,-2.7 -1,-0.2 1,-0.3 -2,-0.2 0.852 102.0 60.4 -64.1 -34.6 18.2 0.4 -6.8 A A
19 19 A T T 3<5S- 0 0 105 -4,-2.0 -1,-0.3 -5,-0.1 -2,-0.2 0.048 125.1-104.6 -79.7 27.4 21.5 1.9 -5.8 A A
20 20 A G T < 5S+ 0 0 68 -3,-1.6 -3,-0.2 1,-0.2 -2,-0.2 0.672 71.9 147.6 64.8 23.4 21.0 0.1 -2.4 A A
21 21 A A < - 0 0 26 -5,-1.9 -1,-0.2 -6,-0.2 -2,-0.0 -0.672 54.3 -93.3 -93.2 146.4 20.0 3.2 -0.4 A A
22 22 A P > - 0 0 75 0, 0.0 4,-2.1 0, 0.0 5,-0.2 -0.225 30.1-116.8 -70.4 148.6 17.5 2.8 2.5 A A
23 23 A R H > S+ 0 0 109 1,-0.2 4,-2.6 2,-0.2 5,-0.1 0.829 108.0 46.8 -52.4 -52.5 13.7 3.4 2.0 A A
24 24 A P H > S+ 0 0 91 0, 0.0 4,-1.7 0, 0.0 -1,-0.2 0.909 112.8 50.3 -62.9 -42.2 13.1 6.4 4.3 A A
25 25 A T H > S+ 0 0 88 1,-0.2 4,-2.2 2,-0.2 -2,-0.2 0.926 114.5 44.4 -59.6 -45.3 16.1 8.3 3.0 A A
26 26 A c H X S+ 0 0 0 -4,-2.1 4,-2.4 1,-0.2 6,-0.3 0.881 108.0 59.2 -64.8 -40.3 14.9 7.7 -0.6 A A
27 27 A A H X>S+ 0 0 4 -4,-2.6 4,-1.7 1,-0.2 5,-1.4 0.845 112.9 38.4 -57.9 -37.1 11.3 8.6 0.4 A A
28 28 A K H <5S+ 0 0 136 -4,-1.7 -2,-0.2 2,-0.2 -1,-0.2 0.780 110.5 57.6 -90.7 -27.1 12.5 12.1 1.4 A A
29 29 A L H <5S+ 0 0 115 -4,-2.2 -2,-0.2 -5,-0.2 -3,-0.2 0.907 122.6 29.8 -58.3 -42.2 15.0 12.5 -1.4 A A
30 30 A S H <5S- 0 0 20 -4,-2.4 -2,-0.2 -5,-0.1 -1,-0.2 0.772 107.4-122.5 -83.8 -34.7 12.0 11.9 -3.7 A A
31 31 A G T <5 + 0 0 37 -4,-1.7 -3,-0.2 -5,-0.2 -4,-0.1 0.589 65.1 140.0 84.0 17.6 9.2 13.4 -1.4 A A
32 32 A b < - 0 0 0 -5,-1.4 2,-0.3 -6,-0.3 -1,-0.2 -0.286 34.6-159.2 -73.4 171.8 7.4 10.0 -1.5 A A
33 33 A K E -A 3 0A 81 -30,-2.2 -30,-3.1 11,-0.1 2,-0.4 -0.881 10.8-120.1-149.4 173.0 5.7 8.5 1.6 A A
34 34 A I E +A 2 0A 73 -2,-0.3 2,-0.3 -32,-0.2 -32,-0.2 -0.984 26.2 168.9-133.3 128.5 4.5 5.1 2.7 A A
35 35 A I - 0 0 68 -34,-2.5 5,-0.0 -2,-0.4 -2,-0.0 -0.825 39.8-127.4-123.0 170.2 1.2 3.5 3.7 A A
36 36 A S S S+ 0 0 127 -2,-0.3 -1,-0.1 3,-0.0 -34,-0.1 0.814 78.2 109.4 -75.3 -38.3 -0.2 -0.0 4.3 A A
37 37 A G S S- 0 0 34 1,-0.1 -2,-0.2 -36,-0.1 0, 0.0 -0.105 73.8-132.7 -52.9 133.4 -3.0 0.7 1.9 A A
38 38 A S S S+ 0 0 116 2,-0.0 2,-0.3 -37,-0.0 -1,-0.1 0.862 94.5 36.6 -54.3 -44.7 -2.9 -1.2 -1.4 A A
39 39 A T S S- 0 0 114 -38,-0.1 7,-0.1 -36,-0.0 -36,-0.1 -0.843 81.8-135.5-110.8 151.9 -3.7 2.1 -3.3 A A
40 40 A a - 0 0 13 5,-0.4 -38,-0.1 -2,-0.3 -2,-0.0 -0.508 35.0 -83.1 -95.4 164.0 -2.4 5.6 -2.4 A A
41 41 A P > - 0 0 61 0, 0.0 3,-1.2 0, 0.0 -1,-0.2 -0.185 46.4 -99.0 -65.4 165.3 -4.5 8.9 -2.4 A A
42 42 A S T 3 S+ 0 0 126 1,-0.3 -2,-0.0 2,-0.2 0, 0.0 0.648 122.0 54.6 -61.3 -21.9 -5.1 10.9 -5.6 A A
43 43 A D T 3 S+ 0 0 87 1,-0.2 -1,-0.3 2,-0.1 3,-0.1 0.674 120.2 28.8 -89.6 -20.6 -2.2 13.3 -4.7 A A
44 44 A Y S < S+ 0 0 64 -3,-1.2 -40,-0.3 1,-0.1 -1,-0.2 -0.360 76.9 144.3-129.7 53.6 0.5 10.6 -4.3 A A
45 45 A P 0 0 56 0, 0.0 -5,-0.4 0, 0.0 -1,-0.1 0.778 360.0 360.0 -68.8 -31.7 -0.8 7.8 -6.7 A A
46 46 A K 0 0 91 -42,-1.5 -44,-0.1 -3,-0.1 -43,-0.1 0.924 360.0 360.0 -75.2 360.0 2.5 6.5 -8.1 A A