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 12-MAY-15 2N2R .
COMPND MOL_ID: 1; MOLECULE: DEFENSIN-LIKE PROTEIN 2; CHAIN: A; SYNONYM: CYSTE .
SOURCE MOL_ID: 1; ORGANISM_SCIENTIFIC: RAPHANUS SATIVUS; ORGANISM_COMMON: RAD .
AUTHOR P.J.HARVEY,D.J.CRAIK,K.VRIENS .
51 1 4 4 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) .
3489.1 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) .
34 66.7 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 .
13 25.5 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 .
1 2.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-3), SAME NUMBER PER 100 RESIDUES .
1 2.0 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 .
8 15.7 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES .
1 2.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES .
9 17.6 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES .
1 2.0 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 1 0 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 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 Q 0 0 177 0, 0.0 2,-0.2 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 130.0 9.6 -6.0 -10.1 A A
2 2 A K - 0 0 158 47,-0.1 49,-3.3 0, 0.0 2,-0.5 -0.738 360.0 -87.0-134.0-173.5 5.8 -6.0 -9.9 A A
3 3 A L E -A 50 0A 82 -2,-0.2 2,-0.4 47,-0.2 45,-0.0 -0.899 33.3-168.7-108.2 127.8 3.4 -4.9 -7.2 A A
4 4 A a E -A 49 0A 38 45,-3.1 45,-3.2 -2,-0.5 2,-0.3 -0.904 21.8-127.4-108.9 141.8 2.3 -7.2 -4.5 A A
5 5 A Q E +A 48 0A 100 -2,-0.4 43,-0.2 43,-0.2 29,-0.0 -0.665 27.6 172.8 -96.7 144.1 -0.5 -6.2 -2.3 A A
6 6 A R E -A 47 0A 113 41,-2.7 41,-2.2 -2,-0.3 -2,-0.0 -0.917 10.3-171.0-147.6 114.2 -0.5 -6.1 1.5 A A
7 7 A P + 0 0 54 0, 0.0 2,-0.4 0, 0.0 4,-0.3 0.869 64.0 72.2 -75.4 -39.0 -3.5 -4.6 3.4 A A
8 8 A S + 0 0 84 1,-0.1 2,-0.1 2,-0.1 4,-0.1 -0.656 65.7 69.0 -94.4 139.4 -2.2 -4.6 6.9 A A
9 9 A G S S- 0 0 52 2,-0.7 -1,-0.1 -2,-0.4 16,-0.0 -0.575 115.4 -4.6 164.7 -86.3 0.4 -2.3 8.2 A A
10 10 A T S S+ 0 0 35 -3,-0.1 2,-0.1 -2,-0.1 -2,-0.1 0.770 113.1 87.5-101.3 -33.7 -0.7 1.3 8.5 A A
11 11 A W + 0 0 33 -4,-0.3 -2,-0.7 34,-0.1 2,-0.2 -0.395 40.4 155.4 -72.7 140.3 -4.1 1.0 6.9 A A
12 12 A S + 0 0 115 2,-0.2 2,-0.4 -4,-0.1 -4,-0.0 -0.719 56.4 17.5-160.5 110.4 -7.2 0.1 9.0 A A
13 13 A G S S- 0 0 49 -2,-0.2 2,-0.2 32,-0.1 -2,-0.0 -0.972 101.3 -18.8 138.2-121.1 -10.7 1.1 7.8 A A
14 14 A V - 0 0 114 -2,-0.4 2,-1.0 30,-0.1 30,-0.2 -0.667 62.0-100.5-120.7 171.1 -11.8 2.2 4.3 A A
15 15 A b + 0 0 18 28,-1.4 3,-0.2 -2,-0.2 28,-0.1 -0.844 45.5 166.8 -96.4 99.2 -10.1 3.5 1.2 A A
16 16 A G - 0 0 55 -2,-1.0 2,-0.4 1,-0.3 -1,-0.2 0.986 65.3 -0.3 -74.3 -71.3 -10.7 7.2 1.4 A A
17 17 A N > - 0 0 117 1,-0.2 4,-2.2 18,-0.0 5,-0.3 -0.989 60.5-140.9-127.5 133.5 -8.4 8.6 -1.2 A A
18 18 A N H > S+ 0 0 81 -2,-0.4 4,-2.2 1,-0.2 5,-0.2 0.936 103.7 43.6 -53.4 -56.8 -6.0 6.7 -3.4 A A
19 19 A N H > S+ 0 0 113 1,-0.2 4,-2.2 2,-0.2 -1,-0.2 0.819 111.6 56.2 -63.4 -34.3 -3.1 9.1 -3.2 A A
20 20 A A H > S+ 0 0 53 2,-0.2 4,-2.4 1,-0.2 -2,-0.2 0.978 114.9 33.0 -64.3 -60.0 -3.6 9.7 0.5 A A
21 21 A c H X S+ 0 0 7 -4,-2.2 4,-2.7 2,-0.2 -2,-0.2 0.785 114.3 61.7 -74.1 -23.5 -3.2 6.1 1.7 A A
22 22 A K H X S+ 0 0 45 -4,-2.2 4,-2.5 -5,-0.3 9,-0.2 0.986 110.7 40.1 -55.5 -57.0 -0.8 5.4 -1.1 A A
23 23 A N H X S+ 0 0 64 -4,-2.2 4,-2.4 1,-0.2 -2,-0.2 0.872 113.3 56.0 -60.4 -41.4 1.5 8.0 0.4 A A
24 24 A Q H X S+ 0 0 76 -4,-2.4 4,-2.8 2,-0.2 5,-0.4 0.897 108.9 46.6 -60.1 -41.7 0.6 6.8 3.9 A A
25 25 A d H X>S+ 0 0 0 -4,-2.7 5,-2.3 2,-0.2 4,-1.3 0.995 112.1 49.7 -62.9 -56.5 1.7 3.3 3.1 A A
26 26 A I H <5S+ 0 0 52 -4,-2.5 -2,-0.2 4,-0.3 -1,-0.2 0.781 117.9 41.1 -53.2 -36.9 4.9 4.4 1.5 A A
27 27 A R H <5S+ 0 0 163 -4,-2.4 -1,-0.3 -5,-0.2 -2,-0.2 0.915 125.5 30.3 -78.9 -41.6 5.7 6.6 4.5 A A
28 28 A L H <5S+ 0 0 103 -4,-2.8 -3,-0.2 -5,-0.2 -2,-0.2 0.986 138.2 13.8 -89.7 -62.7 4.6 4.2 7.3 A A
29 29 A E T <5S- 0 0 32 -4,-1.3 -3,-0.2 -5,-0.4 -4,-0.1 0.561 104.3-121.7 -93.9 -6.9 5.1 0.7 6.3 A A
30 30 A K < + 0 0 142 -5,-2.3 -4,-0.3 -6,-0.3 2,-0.2 0.993 48.4 165.2 64.2 66.8 7.2 1.8 3.4 A A
31 31 A A - 0 0 0 -9,-0.2 18,-0.3 -8,-0.1 3,-0.1 -0.393 42.2-127.6 -94.7-178.9 5.4 0.4 0.5 A A
32 32 A R S S- 0 0 132 16,-2.8 2,-0.3 1,-0.3 17,-0.2 0.727 85.1 -6.9-102.8 -29.5 6.0 1.3 -3.1 A A
33 33 A H E -B 48 0A 63 15,-2.7 15,-3.0 2,-0.0 -1,-0.3 -0.840 59.4-167.7-152.6 179.5 2.4 2.1 -4.0 A A
34 34 A G E +B 47 0A 0 13,-0.3 2,-0.3 -2,-0.3 -12,-0.3 -0.838 15.0 155.3-177.1 139.6 -1.1 1.8 -2.5 A A
35 35 A S E -B 46 0A 19 11,-2.2 11,-2.9 -2,-0.3 2,-1.0 -0.971 50.7 -70.3-161.5 173.7 -4.6 2.1 -3.8 A A
36 36 A b E -B 45 0A 31 -2,-0.3 2,-0.5 9,-0.2 9,-0.2 -0.656 49.6-171.9 -75.1 102.2 -8.3 1.3 -3.4 A A
37 37 A N E -B 44 0A 46 7,-2.7 7,-1.9 -2,-1.0 2,-1.4 -0.871 23.5-126.7 -99.5 132.9 -8.4 -2.4 -4.2 A A
38 38 A Y E +B 43 0A 137 -2,-0.5 2,-0.4 5,-0.2 5,-0.2 -0.688 39.6 163.4 -85.3 92.6 -11.8 -3.8 -4.5 A A
39 39 A V E > -B 42 0A 48 -2,-1.4 3,-1.5 3,-0.7 -2,-0.0 -0.862 54.4 -51.8 -99.6 144.4 -12.0 -6.7 -2.3 A A
40 40 A F T 3 S+ 0 0 183 -2,-0.4 -1,-0.0 1,-0.3 -2,-0.0 -0.386 121.3 3.4 -62.3 134.6 -15.5 -7.9 -1.5 A A
41 41 A P T 3 S+ 0 0 81 0, 0.0 -1,-0.3 0, 0.0 2,-0.3 -0.940 126.1 6.5-107.0 19.0 -17.5 -6.0 -0.4 A A
42 42 A A E < S- B 0 39A 45 -3,-1.5 -3,-0.7 -5,-0.1 -5,-0.1 -0.998 74.4 -85.5-159.6 151.3 -15.8 -2.6 -0.5 A A
43 43 A H E - B 0 38A 99 -2,-0.3 -28,-1.4 -5,-0.2 2,-0.3 -0.299 43.8-178.1 -59.8 132.9 -12.6 -0.7 -1.5 A A
44 44 A K E - B 0 37A 53 -7,-1.9 -7,-2.7 -30,-0.2 2,-1.0 -0.923 35.7-104.3-131.4 152.3 -9.8 -0.8 1.0 A A
45 45 A c E - B 0 36A 2 -2,-0.3 2,-0.5 -9,-0.2 -9,-0.2 -0.718 41.6-173.7 -79.3 105.0 -6.4 0.8 0.9 A A
46 46 A I E - B 0 35A 3 -11,-2.9 -11,-2.2 -2,-1.0 2,-0.3 -0.915 18.7-133.8-103.5 129.8 -4.1 -2.0 0.1 A A
47 47 A d E -AB 6 34A 0 -41,-2.2 -41,-2.7 -2,-0.5 2,-0.6 -0.643 15.7-144.2 -84.6 136.9 -0.5 -1.1 0.2 A A
48 48 A Y E -AB 5 33A 34 -15,-3.0 -16,-2.8 -2,-0.3 -15,-2.7 -0.916 15.0-170.4-110.4 123.4 1.6 -2.3 -2.7 A A
49 49 A F E -A 4 0A 33 -45,-3.2 -45,-3.1 -2,-0.6 2,-0.6 -0.689 35.4 -93.7-106.0 157.7 5.0 -3.5 -2.2 A A
50 50 A P E A 3 0A 58 0, 0.0 -47,-0.2 0, 0.0 -45,-0.0 -0.654 360.0 360.0 -77.4 116.1 7.6 -4.3 -4.9 A A
51 51 A a 0 0 97 -49,-3.3 -48,-0.1 -2,-0.6 -46,-0.1 -0.647 360.0 360.0-137.5 360.0 7.6 -7.9 -5.7 A A