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 ANTIFUNGAL PROTEIN 11-MAY-15 2N2Q .
COMPND MOL_ID: 1; MOLECULE: DEFENSIN-LIKE PROTEIN 1; CHAIN: A; SYNONYM: CYSTE .
SOURCE MOL_ID: 1; ORGANISM_SCIENTIFIC: HEUCHERA SANGUINEA; ORGANISM_COMMON: C .
AUTHOR P.J.HARVEY,D.J.CRAIK,K.VRIENS .
54 1 4 4 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) .
3824.3 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) .
34 63.0 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 22.2 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 .
1 1.9 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 .
9 16.7 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES .
1 1.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES .
9 16.7 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+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 0 1 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 D 0 0 232 0, 0.0 2,-0.1 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 -67.2 16.3 -5.2 -12.6 A A
2 2 A G - 0 0 50 2,-0.0 2,-0.2 0, 0.0 0, 0.0 -0.545 360.0-168.6-152.4 76.9 13.6 -6.7 -10.5 A A
3 3 A V - 0 0 74 -2,-0.1 2,-0.8 1,-0.1 0, 0.0 -0.480 31.1-118.3 -67.2 136.3 13.8 -6.0 -6.8 A A
4 4 A K - 0 0 147 -2,-0.2 50,-3.2 2,-0.0 2,-0.4 -0.689 36.9-177.2 -86.4 109.2 11.4 -8.2 -4.9 A A
5 5 A L E -A 53 0A 52 -2,-0.8 2,-0.5 48,-0.2 48,-0.2 -0.881 15.3-147.4-109.6 140.4 8.8 -6.0 -3.2 A A
6 6 A a E -A 52 0A 47 46,-2.9 46,-2.5 -2,-0.4 2,-0.9 -0.924 12.8-135.4-110.2 124.6 6.1 -7.4 -1.0 A A
7 7 A D E -A 51 0A 63 -2,-0.5 44,-0.2 44,-0.2 43,-0.1 -0.716 28.8-171.6 -80.1 107.1 2.8 -5.6 -0.8 A A
8 8 A V E -A 50 0A 41 42,-3.3 42,-2.4 -2,-0.9 2,-0.1 -0.848 25.0-108.8-106.0 138.7 1.9 -5.5 2.8 A A
9 9 A P E -A 49 0A 80 0, 0.0 2,-0.3 0, 0.0 40,-0.2 -0.343 31.2-127.8 -67.2 142.2 -1.5 -4.3 4.1 A A
10 10 A S - 0 0 6 38,-1.4 38,-0.1 1,-0.1 17,-0.0 -0.645 18.4-169.3 -90.6 144.4 -1.7 -1.0 5.9 A A
11 11 A G S S+ 0 0 73 -2,-0.3 -1,-0.1 3,-0.1 0, 0.0 0.572 91.6 54.3 -99.9 -19.6 -3.2 -0.5 9.3 A A
12 12 A T S S+ 0 0 78 2,-0.0 2,-0.3 15,-0.0 -2,-0.0 0.942 102.0 59.6 -75.5 -54.6 -3.0 3.2 8.9 A A
13 13 A W + 0 0 50 35,-0.1 2,-0.3 10,-0.1 -3,-0.1 -0.579 67.8 165.2 -79.5 135.9 -4.9 3.5 5.6 A A
14 14 A S + 0 0 84 -2,-0.3 2,-0.8 2,-0.2 -3,-0.1 -0.968 42.2 29.7-146.4 157.9 -8.4 2.1 5.7 A A
15 15 A G S S- 0 0 57 -2,-0.3 2,-0.4 30,-0.1 30,-0.1 -0.820 109.2 -8.9 100.6-105.8 -11.5 2.3 3.4 A A
16 16 A H - 0 0 117 -2,-0.8 2,-0.7 29,-0.1 31,-0.2 -0.965 49.3-145.7-135.5 143.8 -10.6 2.8 -0.2 A A
17 17 A b + 0 0 3 29,-2.1 3,-0.1 -2,-0.4 -2,-0.1 -0.938 31.0 156.1-109.3 104.6 -7.3 3.4 -2.1 A A
18 18 A G + 0 0 64 -2,-0.7 2,-0.5 1,-0.2 -1,-0.1 0.647 65.5 49.0-102.2 -20.5 -8.1 5.6 -5.1 A A
19 19 A S > - 0 0 37 1,-0.1 4,-2.1 19,-0.0 -1,-0.2 -0.956 55.1-170.8-127.1 115.2 -4.7 7.1 -5.5 A A
20 20 A S H > S+ 0 0 68 -2,-0.5 4,-2.9 1,-0.2 17,-0.3 0.756 89.9 61.8 -73.2 -23.1 -1.6 5.0 -5.6 A A
21 21 A S H > S+ 0 0 79 2,-0.2 4,-2.2 1,-0.2 -1,-0.2 0.905 109.8 39.2 -68.9 -40.6 0.5 8.1 -5.5 A A
22 22 A K H > S+ 0 0 141 2,-0.2 4,-3.0 3,-0.2 -2,-0.2 0.853 113.9 55.8 -78.0 -34.2 -0.9 9.1 -2.1 A A
23 23 A c H X S+ 0 0 0 -4,-2.1 4,-2.5 2,-0.2 -2,-0.2 0.961 111.7 43.1 -56.9 -51.1 -0.9 5.5 -1.0 A A
24 24 A S H X S+ 0 0 23 -4,-2.9 4,-2.4 13,-0.4 5,-0.2 0.900 113.4 51.2 -64.2 -41.3 2.8 5.4 -1.8 A A
25 25 A Q H X S+ 0 0 107 -4,-2.2 4,-2.4 2,-0.2 5,-0.2 0.928 109.3 52.2 -59.8 -44.4 3.4 8.8 -0.1 A A
26 26 A Q H X S+ 0 0 15 -4,-3.0 4,-3.4 1,-0.2 5,-0.4 0.926 110.0 47.5 -56.9 -48.4 1.5 7.5 2.9 A A
27 27 A d H X S+ 0 0 0 -4,-2.5 4,-2.0 1,-0.2 6,-1.1 0.898 115.9 43.7 -63.4 -40.5 3.8 4.4 3.1 A A
28 28 A K H < S+ 0 0 102 -4,-2.4 -1,-0.2 2,-0.2 -2,-0.2 0.797 119.4 44.7 -72.9 -32.0 7.0 6.5 2.7 A A
29 29 A D H < S+ 0 0 92 -4,-2.4 -2,-0.2 -5,-0.2 -3,-0.2 0.916 120.0 37.6 -77.9 -47.7 5.7 9.1 5.1 A A
30 30 A R H < S+ 0 0 153 -4,-3.4 2,-0.2 -5,-0.2 -3,-0.2 0.928 128.2 4.0 -73.4 -46.6 4.3 6.8 7.8 A A
31 31 A E S < S- 0 0 92 -4,-2.0 0, 0.0 -5,-0.4 0, 0.0 -0.560 88.1 -80.9-131.7-167.4 7.0 4.1 7.7 A A
32 32 A H S S+ 0 0 190 -2,-0.2 2,-1.9 1,-0.1 -4,-0.2 0.072 76.6 127.4 -91.0 26.5 10.3 3.1 6.1 A A
33 33 A F > + 0 0 35 -6,-1.1 3,-2.0 1,-0.2 18,-0.2 -0.569 26.6 169.7 -88.3 78.6 8.6 1.9 2.9 A A
34 34 A A T 3 S+ 0 0 73 -2,-1.9 -1,-0.2 1,-0.3 3,-0.1 0.667 72.3 65.1 -63.8 -18.0 10.7 3.9 0.5 A A
35 35 A Y T 3 S- 0 0 106 16,-0.7 2,-0.3 1,-0.3 -1,-0.3 0.464 99.6-145.9 -85.6 -1.7 9.3 1.8 -2.3 A A
36 36 A G < - 0 0 0 -3,-2.0 15,-2.5 -12,-0.2 -1,-0.3 -0.571 16.2 -97.5 82.5-131.3 5.9 3.3 -1.6 A A
37 37 A G E -B 50 0A 9 13,-0.3 -13,-0.4 -2,-0.3 2,-0.3 -0.956 21.9-134.2-178.6 173.1 2.8 1.3 -2.1 A A
38 38 A A E -B 49 0A 26 11,-2.8 11,-3.1 -2,-0.3 2,-0.8 -0.937 31.4 -97.0-144.1 163.3 0.0 0.6 -4.4 A A
39 39 A b E -B 48 0A 39 -2,-0.3 2,-0.4 9,-0.2 9,-0.2 -0.769 47.2-178.2 -87.3 114.2 -3.7 0.2 -4.3 A A
40 40 A H E -B 47 0A 94 7,-3.0 7,-3.0 -2,-0.8 2,-0.4 -0.912 27.1-115.7-119.5 139.9 -4.4 -3.5 -4.1 A A
41 41 A Y E +B 46 0A 157 -2,-0.4 2,-0.3 5,-0.3 5,-0.2 -0.623 44.0 155.2 -80.7 128.9 -7.8 -5.2 -4.1 A A
42 42 A Q - 0 0 81 3,-1.4 0, 0.0 -2,-0.4 0, 0.0 -0.860 49.7 -43.8-138.5 166.4 -8.7 -7.0 -1.0 A A
43 43 A F S S+ 0 0 182 -2,-0.3 3,-0.0 1,-0.3 4,-0.0 -0.693 123.2 2.7 -78.0 133.3 -12.0 -7.9 0.4 A A
44 44 A P S S- 0 0 90 0, 0.0 -1,-0.3 0, 0.0 2,-0.3 -0.987 129.4 -2.0-101.4 3.9 -14.1 -5.9 0.5 A A
45 45 A S S S- 0 0 52 -5,-0.1 -3,-1.4 -30,-0.1 2,-0.5 -0.918 79.4 -76.0-145.6 167.8 -12.4 -2.9 -1.3 A A
46 46 A V E - B 0 41A 37 -2,-0.3 -29,-2.1 -5,-0.2 -5,-0.3 -0.573 56.8-175.8 -66.9 119.4 -9.2 -1.6 -2.9 A A
47 47 A K E - B 0 40A 50 -7,-3.0 -7,-3.0 -2,-0.5 2,-0.4 -0.753 30.1 -96.4-119.8 161.8 -6.9 -0.9 -0.0 A A
48 48 A c E - B 0 39A 0 -2,-0.3 -38,-1.4 -9,-0.2 2,-0.5 -0.675 36.4-170.3 -82.2 126.2 -3.4 0.6 0.2 A A
49 49 A F E -AB 9 38A 13 -11,-3.1 -11,-2.8 -2,-0.4 2,-0.2 -0.987 15.2-138.0-120.7 124.1 -0.6 -1.9 0.3 A A
50 50 A d E -AB 8 37A 1 -42,-2.4 -42,-3.3 -2,-0.5 2,-0.8 -0.548 14.1-129.5 -83.4 141.6 2.9 -0.7 1.1 A A
51 51 A K E +A 7 0A 53 -15,-2.5 -16,-0.7 -44,-0.2 2,-0.3 -0.815 29.1 178.2 -97.2 109.1 5.8 -2.2 -0.8 A A
52 52 A R E -A 6 0A 124 -46,-2.5 -46,-2.9 -2,-0.8 2,-0.4 -0.731 33.1-108.7 -99.3 160.4 8.6 -3.4 1.4 A A
53 53 A Q E A 5 0A 87 -2,-0.3 -48,-0.2 -48,-0.2 -50,-0.0 -0.695 360.0 360.0 -89.6 137.6 11.6 -5.0 0.0 A A
54 54 A a 0 0 97 -50,-3.2 -1,-0.2 -2,-0.4 -49,-0.1 0.528 360.0 360.0-114.0 360.0 12.0 -8.6 0.6 A A