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 PLANT TOXIN 29-JUL-92 1GPS .
COMPND MOL_ID: 1; MOLECULE: GAMMA-1-P THIONIN; CHAIN: A; ENGINEERED: YES .
SOURCE MOL_ID: 1; ORGANISM_SCIENTIFIC: TRITICUM TURGIDUM; ORGANISM_TAXID: 457 .
AUTHOR M.BRUIX,M.A.JIMENEZ,J.SANTORO,C.GONZALEZ,F.J.COLILLA,E.MENDEZ,M.RICO .
47 1 4 4 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) .
3544.3 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) .
39 83.0 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 .
12 25.5 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES .
1 2.1 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 .
13 27.7 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES .
1 2.1 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES .
9 19.1 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 0 0 1 0 0 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 0 0 0 2 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 .
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 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 0 177 0, 0.0 46,-1.5 0, 0.0 2,-0.6 0.000 360.0 360.0 360.0 123.0 11.6 4.5 10.7 A A
2 2 A I E -A 46 0A 113 44,-0.2 2,-0.6 42,-0.0 44,-0.2 -0.960 360.0-154.5-104.6 116.3 9.2 2.4 8.8 A A
3 3 A a E +A 45 0A 25 42,-3.2 42,-1.7 -2,-0.6 2,-0.2 -0.942 16.6 175.2 -96.7 110.7 6.2 4.2 7.4 A A
4 4 A R E +A 44 0A 113 -2,-0.6 2,-0.3 40,-0.2 40,-0.2 -0.691 19.3 153.8-118.9 73.7 3.4 1.8 6.9 A A
5 5 A R E -A 43 0A 176 38,-1.5 38,-3.0 -2,-0.2 2,-0.3 -0.744 42.3-105.8-108.5 154.7 0.4 3.9 5.9 A A
6 6 A R E -A 42 0A 147 -2,-0.3 2,-0.5 36,-0.2 36,-0.2 -0.612 39.3 -98.0 -88.0 136.9 -2.7 3.1 3.8 A A
7 7 A S - 0 0 19 34,-2.6 2,-1.2 -2,-0.3 34,-0.2 -0.317 27.0-163.4 -53.9 101.0 -3.2 4.2 0.2 A A
8 8 A A S S+ 0 0 92 -2,-0.5 -1,-0.1 1,-0.2 3,-0.1 -0.776 87.7 37.2 -84.5 93.0 -5.4 7.4 0.1 A A
9 9 A G S S+ 0 0 60 -2,-1.2 2,-1.3 1,-0.1 -1,-0.2 -0.304 89.8 93.3 154.7 -48.7 -6.3 7.0 -3.6 A A
10 10 A F - 0 0 60 31,-0.1 2,-0.8 10,-0.1 31,-0.3 -0.514 60.7-167.0 -78.8 90.3 -6.7 3.2 -4.0 A A
11 11 A K - 0 0 203 -2,-1.3 -3,-0.1 -3,-0.1 -1,-0.0 -0.781 48.2 -16.8 -86.7 101.5 -10.4 2.8 -3.5 A A
12 12 A G S S+ 0 0 36 -2,-0.8 2,-0.7 29,-0.0 29,-0.1 -0.610 107.3 14.4 114.1-155.6 -11.3 -0.8 -3.0 A A
13 13 A P - 0 0 84 0, 0.0 26,-0.3 0, 0.0 27,-0.1 -0.509 43.7-175.1 -66.1 106.4 -9.9 -4.4 -3.5 A A
14 14 A b - 0 0 3 25,-1.1 2,-2.6 -2,-0.7 6,-0.2 0.691 15.6-173.4 -65.7 -31.1 -6.1 -4.2 -4.2 A A
15 15 A M + 0 0 114 23,-2.5 2,-0.3 22,-0.1 -1,-0.1 -0.081 57.9 38.0 64.6 -33.9 -6.2 -8.0 -4.8 A A
16 16 A S S > S- 0 0 42 -2,-2.6 4,-1.9 1,-0.1 5,-0.1 -0.990 76.6-123.9-145.4 142.8 -2.4 -8.5 -5.1 A A
17 17 A N H > S+ 0 0 86 -2,-0.3 4,-3.1 2,-0.2 5,-0.2 0.922 112.4 57.5 -42.1 -43.0 0.7 -7.0 -3.5 A A
18 18 A K H > S+ 0 0 139 1,-0.2 4,-2.3 2,-0.2 -1,-0.2 0.894 104.9 48.9 -64.2 -46.7 1.9 -6.0 -6.9 A A
19 19 A N H > S+ 0 0 81 -5,-0.2 4,-1.6 2,-0.2 -1,-0.2 0.931 114.6 45.9 -57.5 -47.5 -1.2 -3.8 -7.7 A A
20 20 A c H X S+ 0 0 0 -4,-1.9 4,-2.2 -6,-0.2 3,-0.3 0.974 112.6 50.7 -56.8 -55.6 -0.9 -2.1 -4.3 A A
21 21 A A H X S+ 0 0 14 -4,-3.1 4,-2.4 11,-0.7 -2,-0.2 0.790 106.2 55.6 -54.4 -37.4 2.8 -1.5 -4.7 A A
22 22 A Q H X S+ 0 0 123 -4,-2.3 4,-1.6 2,-0.2 -1,-0.2 0.950 109.6 44.0 -65.8 -47.3 2.4 0.0 -8.2 A A
23 23 A V H X S+ 0 0 29 -4,-1.6 4,-2.4 -3,-0.3 -2,-0.2 0.881 113.1 54.0 -63.5 -41.1 -0.0 2.8 -7.0 A A
24 24 A d H <>S+ 0 0 0 -4,-2.2 5,-2.9 2,-0.2 -2,-0.2 0.910 102.9 54.7 -65.0 -36.6 2.2 3.4 -3.9 A A
25 25 A Q H ><5S+ 0 0 121 -4,-2.4 3,-0.8 1,-0.2 -1,-0.2 0.898 112.4 45.2 -62.8 -36.5 5.3 3.9 -6.1 A A
26 26 A Q H 3<5S+ 0 0 153 -4,-1.6 -2,-0.2 1,-0.2 -1,-0.2 0.924 111.5 53.9 -63.9 -44.3 3.2 6.6 -7.9 A A
27 27 A E T 3<5S- 0 0 71 -4,-2.4 -1,-0.2 -5,-0.1 -2,-0.2 0.121 127.7 -92.0 -89.1 19.3 2.0 8.0 -4.5 A A
28 28 A G T < 5S+ 0 0 55 -3,-0.8 2,-0.4 1,-0.3 -3,-0.2 0.430 85.5 125.6 88.5 10.5 5.5 8.5 -3.0 A A
29 29 A W < - 0 0 58 -5,-2.9 -1,-0.3 -6,-0.1 16,-0.2 -0.785 61.8-134.8-103.9 143.5 6.0 5.1 -1.3 A A
30 30 A G S S- 0 0 56 14,-0.5 2,-0.3 -2,-0.4 15,-0.2 0.534 79.9 -38.3 -68.2 -15.9 8.9 2.7 -1.8 A A
31 31 A G E -B 44 0A 8 13,-1.3 13,-0.7 -7,-0.1 2,-0.3 -0.959 59.7-145.9 176.1-169.0 6.5 -0.3 -2.0 A A
32 32 A G E -B 43 0A 9 11,-0.3 -11,-0.7 -2,-0.3 2,-0.3 -0.902 5.2-141.3 178.5 151.8 3.3 -1.8 -0.6 A A
33 33 A N E -B 42 0A 49 9,-2.9 9,-2.7 -2,-0.3 2,-0.7 -0.900 25.2-119.9-123.4 154.9 1.4 -4.9 0.4 A A
34 34 A b E -B 41 0A 7 -2,-0.3 7,-0.2 7,-0.2 4,-0.2 -0.798 39.9-143.8-101.6 106.0 -2.3 -5.8 0.1 A A
35 35 A D E >> -B 40 0A 69 5,-3.4 4,-1.0 -2,-0.7 5,-0.6 -0.514 45.1 -24.3 -89.7 139.2 -3.6 -6.5 3.6 A A
36 36 A G T 45S+ 0 0 51 1,-0.2 2,-0.7 -2,-0.2 -2,-0.1 -0.419 133.7 2.5 75.0-129.4 -6.1 -8.9 5.1 A A
37 37 A P T 45S- 0 0 95 0, 0.0 -1,-0.2 0, 0.0 -22,-0.1 -0.133 117.3 -91.9 -76.6 35.4 -8.7 -10.3 2.6 A A
38 38 A F T 45S+ 0 0 95 -2,-0.7 -23,-2.5 -4,-0.2 -24,-0.3 0.719 103.1 103.2 60.1 33.1 -6.8 -8.2 -0.1 A A
39 39 A R T <5 + 0 0 95 -4,-1.0 -25,-1.1 -26,-0.3 2,-0.2 0.846 62.1 68.7 -96.5 -62.9 -8.8 -4.9 0.2 A A
40 40 A R E < - B 0 35A 129 -5,-0.6 -5,-3.4 -27,-0.1 2,-0.8 -0.354 68.3-151.0 -69.3 119.7 -6.6 -2.5 2.2 A A
41 41 A c E - B 0 34A 7 -31,-0.3 -34,-2.6 -7,-0.2 2,-0.5 -0.864 16.3-173.9 -91.3 106.8 -3.4 -1.4 0.4 A A
42 42 A K E -AB 6 33A 51 -9,-2.7 -9,-2.9 -2,-0.8 2,-0.4 -0.948 11.4-151.7-111.8 121.4 -0.8 -0.7 3.1 A A
43 43 A d E -AB 5 32A 0 -38,-3.0 -38,-1.5 -2,-0.5 -11,-0.3 -0.790 5.2-135.4-113.4 144.3 2.4 0.8 1.9 A A
44 44 A I E +AB 4 31A 61 -13,-0.7 -13,-1.3 -2,-0.4 -14,-0.5 -0.603 29.2 148.7 -98.6 143.6 6.0 0.9 2.9 A A
45 45 A R E -A 3 0A 124 -42,-1.7 -42,-3.2 -2,-0.3 2,-0.7 -0.956 44.7-111.6-161.1 158.7 8.5 3.7 3.1 A A
46 46 A Q E A 2 0A 128 -2,-0.3 -44,-0.2 -44,-0.2 -2,-0.0 -0.906 360.0 360.0-100.2 107.5 11.6 4.7 5.1 A A
47 47 A a 0 0 118 -46,-1.5 -2,-0.0 -2,-0.7 0, 0.0 -0.770 360.0 360.0 -85.0 360.0 10.8 7.7 7.3 A A