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 13-JUL-01 1JKZ .
COMPND MOL_ID: 1; MOLECULE: DEFENSE-RELATED PEPTIDE 1; CHAIN: A; SYNONYM: PSD .
SOURCE MOL_ID: 1; ORGANISM_SCIENTIFIC: PISUM SATIVUM; ORGANISM_COMMON: PEA; O .
AUTHOR M.S.ALMEIDA,K.M.S.CABRAL,E.KURTENBACH,F.C.L.ALMEIDA, A.P.VALENTE .
46 1 4 4 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) .
3599.6 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) .
26 56.5 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 .
11 23.9 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 2.2 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 .
4 8.7 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 .
9 19.6 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 1 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 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 0 238 0, 0.0 45,-0.8 0, 0.0 2,-0.3 0.000 360.0 360.0 360.0 175.5 -10.9 -4.8 13.2 A A
2 2 A T E -A 45 0A 87 43,-0.2 2,-0.4 2,-0.0 43,-0.2 -0.979 360.0-148.0-132.4 144.2 -8.6 -3.1 10.7 A A
3 3 A a E -A 44 0A 34 41,-1.8 41,-1.4 -2,-0.3 2,-0.3 -0.929 9.0-155.5-115.7 134.8 -9.3 -1.4 7.3 A A
4 4 A E E -A 43 0A 93 -2,-0.4 2,-0.4 39,-0.2 39,-0.2 -0.808 6.5-162.1-108.2 148.1 -6.9 -1.3 4.4 A A
5 5 A H E -A 42 0A 106 37,-1.2 37,-3.2 -2,-0.3 2,-0.5 -0.988 16.1-131.0-133.3 141.1 -6.9 1.3 1.5 A A
6 6 A L E -A 41 0A 58 -2,-0.4 2,-0.4 35,-0.3 35,-0.2 -0.771 26.0-130.8 -91.4 125.9 -5.3 1.3 -1.9 A A
7 7 A A - 0 0 22 33,-1.4 33,-0.3 -2,-0.5 3,-0.2 -0.634 6.8-155.2 -81.1 128.5 -3.3 4.4 -2.8 A A
8 8 A D S S+ 0 0 158 -2,-0.4 2,-0.6 1,-0.2 -1,-0.1 0.580 87.0 70.6 -76.3 -10.6 -4.1 6.1 -6.1 A A
9 9 A T S S+ 0 0 89 2,-0.0 -1,-0.2 14,-0.0 2,-0.1 -0.503 73.4 122.5-107.4 63.3 -0.6 7.6 -6.2 A A
10 10 A Y S S- 0 0 41 -2,-0.6 3,-0.1 -3,-0.2 29,-0.0 -0.290 75.5-100.2-107.2-169.1 1.4 4.5 -6.9 A A
11 11 A R - 0 0 183 2,-0.2 2,-1.6 1,-0.1 -2,-0.0 0.017 52.4-116.3-107.0 27.4 3.8 3.5 -9.7 A A
12 12 A G S S+ 0 0 56 28,-0.0 2,-0.2 2,-0.0 -1,-0.1 -0.583 89.1 43.4 79.6 -87.5 1.3 1.4 -11.7 A A
13 13 A V S S- 0 0 73 -2,-1.6 2,-0.4 -3,-0.1 -2,-0.2 -0.529 74.0-136.5 -92.5 160.6 2.9 -2.0 -11.5 A A
14 14 A b + 0 0 14 -2,-0.2 3,-0.1 1,-0.1 25,-0.0 -0.917 24.9 167.2-118.5 143.5 4.6 -3.8 -8.5 A A
15 15 A F + 0 0 180 1,-0.4 2,-0.3 -2,-0.4 -1,-0.1 0.696 68.8 15.4-118.6 -46.1 7.8 -5.8 -8.4 A A
16 16 A T S >> S- 0 0 90 1,-0.1 3,-2.6 18,-0.0 4,-0.5 -0.971 73.8-111.8-136.2 151.2 8.7 -6.3 -4.7 A A
17 17 A N H 3> S+ 0 0 119 -2,-0.3 4,-1.5 1,-0.3 3,-0.4 0.736 114.1 67.4 -49.6 -26.3 6.8 -6.0 -1.4 A A
18 18 A A H 3> S+ 0 0 63 1,-0.2 4,-2.2 2,-0.2 5,-0.4 0.762 85.3 70.0 -68.1 -26.5 9.1 -3.0 -0.6 A A
19 19 A S H <> S+ 0 0 23 -3,-2.6 4,-1.6 1,-0.2 -1,-0.2 0.914 106.5 36.7 -58.9 -44.5 7.5 -1.0 -3.4 A A
20 20 A c H X S+ 0 0 0 -4,-0.5 4,-4.7 -3,-0.4 5,-0.3 0.899 114.2 56.7 -74.6 -42.6 4.2 -0.6 -1.4 A A
21 21 A D H X S+ 0 0 43 -4,-1.5 4,-3.2 12,-0.3 5,-0.3 0.973 114.3 36.8 -51.7 -64.2 5.9 -0.3 2.0 A A
22 22 A D H X S+ 0 0 79 -4,-2.2 4,-3.3 1,-0.2 5,-0.3 0.953 120.0 51.3 -51.4 -54.1 8.0 2.7 1.1 A A
23 23 A H H X S+ 0 0 10 -4,-1.6 4,-4.3 -5,-0.4 5,-0.4 0.939 113.3 42.8 -47.8 -60.9 5.2 4.0 -1.0 A A
24 24 A d H X S+ 0 0 0 -4,-4.7 4,-2.8 2,-0.2 -2,-0.2 0.959 115.2 49.0 -52.6 -58.8 2.6 3.7 1.8 A A
25 25 A K H < S+ 0 0 93 -4,-3.2 -1,-0.2 -5,-0.3 -2,-0.2 0.870 121.4 36.5 -48.9 -44.3 5.0 5.1 4.4 A A
26 26 A N H < S+ 0 0 113 -4,-3.3 3,-0.3 -5,-0.3 -1,-0.2 0.864 127.2 35.9 -79.4 -39.7 5.8 8.0 2.1 A A
27 27 A K H < S+ 0 0 120 -4,-4.3 2,-0.4 -5,-0.3 -3,-0.2 0.957 137.3 14.0 -78.8 -55.0 2.3 8.5 0.6 A A
28 28 A A S < S- 0 0 39 -4,-2.8 2,-1.6 -5,-0.4 -1,-0.2 -0.790 84.8-132.7-127.8 85.2 0.2 7.7 3.6 A A
29 29 A H + 0 0 172 -2,-0.4 -4,-0.2 -3,-0.3 2,-0.2 -0.055 59.3 133.7 -38.6 72.0 2.4 7.7 6.8 A A
30 30 A L - 0 0 48 -2,-1.6 14,-0.1 -6,-0.2 3,-0.1 -0.459 69.2 -93.7-115.8-173.3 1.0 4.4 8.1 A A
31 31 A I S S- 0 0 99 12,-0.9 2,-0.3 1,-0.2 13,-0.1 0.943 89.9 -22.7 -73.0 -51.2 2.6 1.2 9.5 A A
32 32 A S - 0 0 57 11,-0.4 11,-2.5 -8,-0.1 2,-0.3 -0.986 48.4-162.0-157.9 166.1 2.9 -1.0 6.4 A A
33 33 A G E -B 42 0A 8 -2,-0.3 -12,-0.3 9,-0.3 9,-0.2 -0.953 8.4-168.9-157.2 134.0 1.6 -1.7 2.9 A A
34 34 A T E -B 41 0A 52 7,-1.2 7,-2.4 -2,-0.3 2,-0.5 -0.678 31.3 -92.9-119.3 173.7 1.8 -4.7 0.5 A A
35 35 A b E -B 40 0A 28 -2,-0.2 2,-0.4 5,-0.2 5,-0.3 -0.765 36.5-179.5 -92.3 128.1 1.0 -5.4 -3.2 A A
36 36 A H E > S-B 39 0A 68 3,-3.6 3,-2.7 -2,-0.5 -2,-0.0 -0.988 73.3 -17.6-128.4 121.1 -2.4 -6.8 -4.2 A A
37 37 A N T 3 S- 0 0 142 -2,-0.4 -1,-0.1 1,-0.3 3,-0.1 0.873 129.4 -53.3 52.3 37.9 -3.3 -7.6 -7.8 A A
38 38 A W T 3 S+ 0 0 173 1,-0.3 -1,-0.3 -25,-0.1 2,-0.2 0.509 124.2 107.7 74.4 5.9 -0.3 -5.5 -8.8 A A
39 39 A K E < - B 0 36A 113 -3,-2.7 -3,-3.6 -26,-0.1 2,-0.5 -0.658 69.8-116.3-109.7 166.9 -1.8 -2.6 -6.7 A A
40 40 A c E - B 0 35A 0 -33,-0.3 -33,-1.4 -5,-0.3 2,-0.4 -0.915 25.6-176.5-111.8 129.3 -0.7 -1.2 -3.3 A A
41 41 A F E -AB 6 34A 54 -7,-2.4 -7,-1.2 -2,-0.5 -35,-0.3 -0.948 11.9-150.2-120.4 138.8 -2.8 -1.3 -0.2 A A
42 42 A d E -AB 5 33A 9 -37,-3.2 -37,-1.2 -2,-0.4 2,-0.6 -0.657 17.0-117.1-106.2 163.6 -1.8 0.3 3.1 A A
43 43 A T E +A 4 0A 35 -11,-2.5 -12,-0.9 -2,-0.2 2,-0.4 -0.897 35.9 169.6-106.5 119.8 -2.7 -0.7 6.7 A A
44 44 A Q E -A 3 0A 82 -41,-1.4 -41,-1.8 -2,-0.6 2,-0.3 -0.992 29.9-128.8-134.0 129.1 -4.7 1.6 8.8 A A
45 45 A N E A 2 0A 114 -2,-0.4 -43,-0.2 -43,-0.2 -2,-0.0 -0.555 360.0 360.0 -75.7 133.4 -6.4 1.0 12.2 A A
46 46 A a 0 0 123 -45,-0.8 -2,-0.0 -2,-0.3 0, 0.0 -0.992 360.0 360.0-152.0 360.0 -10.1 1.9 12.5 A A