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 ANTIMICROBIAL PROTEIN 07-SEP-11 2LJ7 .
COMPND MOL_ID: 1; MOLECULE: DEFENSIN LC-DEF; CHAIN: A; ENGINEERED: YES .
SOURCE MOL_ID: 1; ORGANISM_SCIENTIFIC: LENS CULINARIS SUBSP. CULINARIS; ORGAN .
AUTHOR Z.SHENKAREV,K.MINEEV,A.GIZATULLINA .
47 1 5 5 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) .
3753.3 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) .
22 46.8 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 23.4 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 .
1 2.1 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 .
1 2.1 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES .
3 6.4 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES .
5 10.6 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 1 0 0 0 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 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 0 200 0, 0.0 46,-1.6 0, 0.0 2,-0.3 0.000 360.0 360.0 360.0 160.9 -21.4 4.9 8.8 A A
2 2 A T E -A 46 0A 65 44,-0.3 2,-0.3 2,-0.0 44,-0.3 -0.993 360.0-155.0-145.4 150.0 -22.8 6.0 5.4 A A
3 3 A a E -A 45 0A 58 42,-2.9 42,-2.4 -2,-0.3 2,-0.4 -0.855 12.0-134.1-124.2 159.9 -23.4 9.3 3.5 A A
4 4 A E E +A 44 0A 80 -2,-0.3 2,-0.3 40,-0.2 40,-0.2 -0.952 26.7 168.6-118.4 132.3 -25.8 10.3 0.7 A A
5 5 A N E -A 43 0A 51 38,-1.9 38,-3.1 -2,-0.4 2,-0.1 -0.979 40.3 -93.8-140.8 152.4 -24.7 12.4 -2.3 A A
6 6 A L E -A 42 0A 83 -2,-0.3 36,-0.3 36,-0.2 34,-0.0 -0.415 47.5-113.5 -66.4 135.4 -26.3 13.4 -5.6 A A
7 7 A S - 0 0 19 34,-3.2 -1,-0.1 -2,-0.1 34,-0.1 0.069 25.0-107.9 -58.8 177.0 -25.3 11.1 -8.5 A A
8 8 A D S S- 0 0 97 1,-0.1 -1,-0.1 0, 0.0 -2,-0.1 0.977 94.1 -26.3 -73.9 -59.7 -23.2 12.3 -11.4 A A
9 9 A S S S+ 0 0 79 2,-0.1 2,-0.7 31,-0.0 -1,-0.1 -0.241 77.8 162.9-155.8 55.3 -25.8 12.4 -14.1 A A
10 10 A F + 0 0 13 31,-0.1 2,-0.2 10,-0.0 31,-0.2 -0.715 15.6 158.5 -84.9 116.0 -28.6 10.0 -13.3 A A
11 11 A K + 0 0 137 -2,-0.7 -2,-0.1 29,-0.1 29,-0.1 -0.693 22.5 60.2-127.0-179.8 -31.8 10.8 -15.4 A A
12 12 A G S S- 0 0 42 -2,-0.2 2,-0.1 27,-0.0 27,-0.0 0.014 89.1 -45.4 85.0 164.6 -34.9 9.0 -16.5 A A
13 13 A P - 0 0 124 0, 0.0 2,-0.1 0, 0.0 -2,-0.1 -0.390 58.2-127.1 -69.8 143.9 -37.8 7.4 -14.6 A A
14 14 A b - 0 0 59 22,-0.1 -2,-0.0 -2,-0.1 20,-0.0 -0.473 17.6-135.6 -89.1 162.4 -36.9 5.1 -11.7 A A
15 15 A I > - 0 0 78 -2,-0.1 3,-0.7 1,-0.1 4,-0.3 -0.819 20.4-119.3-118.5 158.5 -38.1 1.5 -11.2 A A
16 16 A P T 3 S+ 0 0 145 0, 0.0 -1,-0.1 0, 0.0 -2,-0.0 0.575 113.7 59.1 -69.8 -8.8 -39.5 -0.5 -8.2 A A
17 17 A D T 3 S- 0 0 144 0, 0.0 -3,-0.0 0, 0.0 0, 0.0 0.745 121.2 -96.0 -90.5 -28.3 -36.6 -2.9 -8.6 A A
18 18 A G < + 0 0 17 -3,-0.7 4,-0.4 3,-0.1 16,-0.1 0.527 47.7 172.4 110.4 104.3 -33.9 -0.2 -8.2 A A
19 19 A N S > S+ 0 0 51 -4,-0.3 4,-0.8 2,-0.1 15,-0.1 0.595 80.2 60.1-111.0 -20.8 -32.1 1.6 -11.0 A A
20 20 A d H > S+ 0 0 1 13,-0.3 4,-1.8 -5,-0.2 14,-0.3 0.746 104.4 52.4 -79.0 -25.0 -30.2 4.1 -8.9 A A
21 21 A N H > S+ 0 0 42 12,-0.5 4,-2.5 2,-0.2 5,-0.3 0.987 107.8 45.1 -73.5 -65.0 -28.4 1.4 -7.1 A A
22 22 A K H > S+ 0 0 102 -4,-0.4 4,-1.5 1,-0.2 -1,-0.2 0.813 114.5 55.8 -48.9 -32.3 -27.0 -0.7 -10.0 A A
23 23 A H H >X S+ 0 0 52 -4,-0.8 4,-2.1 2,-0.2 3,-1.0 0.999 114.6 32.2 -64.7 -68.8 -25.9 2.6 -11.5 A A
24 24 A e H 3< S+ 0 0 1 -4,-1.8 6,-2.9 1,-0.3 -2,-0.2 0.679 121.4 55.8 -63.5 -16.3 -23.8 4.1 -8.6 A A
25 25 A K H 3< S+ 0 0 102 -4,-2.5 -1,-0.3 4,-0.3 -2,-0.2 0.734 113.1 38.2 -87.0 -25.6 -22.9 0.5 -7.9 A A
26 26 A E H << S+ 0 0 139 -4,-1.5 -2,-0.2 -3,-1.0 -3,-0.2 0.628 131.8 27.7 -97.4 -18.6 -21.6 -0.2 -11.4 A A
27 27 A K S < S+ 0 0 124 -4,-2.1 -3,-0.2 -5,-0.1 -2,-0.1 0.815 138.3 18.3-104.4 -71.4 -20.0 3.2 -11.8 A A
28 28 A E S S- 0 0 110 -5,-0.3 -3,-0.2 1,-0.0 -4,-0.1 0.454 94.8-133.6 -82.5 -0.8 -19.0 4.7 -8.4 A A
29 29 A H + 0 0 146 -6,-0.3 -4,-0.3 -7,-0.1 -5,-0.1 0.894 50.2 159.2 48.1 46.0 -19.2 1.2 -7.0 A A
30 30 A L - 0 0 21 -6,-2.9 15,-0.2 -9,-0.2 3,-0.1 -0.122 55.2 -99.1 -86.2-173.0 -21.1 2.6 -4.0 A A
31 31 A L S S- 0 0 69 13,-2.0 2,-0.3 1,-0.3 14,-0.2 0.955 85.1 -45.6 -73.8 -53.0 -23.4 0.8 -1.6 A A
32 32 A S E -B 44 0A 29 12,-1.4 12,-2.7 -8,-0.1 2,-0.3 -0.940 51.3-138.1-165.1-177.3 -26.7 1.7 -3.2 A A
33 33 A G E -B 43 0A 9 10,-0.3 -12,-0.5 -2,-0.3 2,-0.3 -0.984 3.4-156.5-154.5 162.4 -28.8 4.5 -4.7 A A
34 34 A R E -B 42 0A 142 8,-2.9 8,-3.1 -2,-0.3 2,-0.2 -0.999 13.3-137.3-146.3 141.5 -32.3 6.0 -4.9 A A
35 35 A d E -B 41 0A 32 -2,-0.3 2,-0.3 6,-0.2 6,-0.2 -0.536 17.7-157.7 -94.8 162.9 -34.1 8.2 -7.4 A A
36 36 A R > - 0 0 173 4,-1.0 3,-0.8 -2,-0.2 -22,-0.1 -0.840 32.1-112.1-134.3 171.0 -36.4 11.2 -6.6 A A
37 37 A D T 3 S+ 0 0 160 -2,-0.3 4,-0.1 1,-0.2 -2,-0.0 0.580 109.1 73.8 -79.5 -10.3 -39.2 13.2 -8.3 A A
38 38 A D T 3 S- 0 0 74 2,-0.3 -1,-0.2 1,-0.0 3,-0.1 0.128 117.4-108.0 -88.9 20.7 -36.8 16.1 -8.6 A A
39 39 A F S < S+ 0 0 150 -3,-0.8 2,-0.4 1,-0.2 -2,-0.1 0.704 87.3 119.8 60.7 18.5 -35.0 14.3 -11.4 A A
40 40 A R - 0 0 136 -29,-0.1 -4,-1.0 -31,-0.0 2,-0.4 -0.916 50.2-155.2-118.1 142.9 -32.2 13.9 -8.9 A A
41 41 A c E - B 0 35A 3 -2,-0.4 -34,-3.2 -6,-0.2 2,-0.4 -0.932 4.2-151.5-119.1 140.7 -30.7 10.6 -7.6 A A
42 42 A W E -AB 6 34A 94 -8,-3.1 -8,-2.9 -2,-0.4 2,-0.4 -0.924 6.8-157.0-113.9 134.0 -28.9 10.0 -4.3 A A
43 43 A e E -AB 5 33A 0 -38,-3.1 -38,-1.9 -2,-0.4 2,-0.5 -0.900 10.2-139.1-112.0 137.2 -26.2 7.4 -3.8 A A
44 44 A T E +AB 4 32A 11 -12,-2.7 -13,-2.0 -2,-0.4 -12,-1.4 -0.809 29.6 166.2 -97.3 130.0 -25.3 5.9 -0.4 A A
45 45 A R E -A 3 0A 108 -42,-2.4 -42,-2.9 -2,-0.5 2,-0.2 -0.901 41.5 -84.3-137.4 165.6 -21.6 5.3 0.3 A A
46 46 A N E A 2 0A 104 -2,-0.3 -44,-0.3 -44,-0.3 0, 0.0 -0.503 360.0 360.0 -73.1 135.7 -19.4 4.5 3.3 A A
47 47 A a 0 0 76 -46,-1.6 -1,-0.1 -2,-0.2 -44,-0.0 -0.623 360.0 360.0-157.2 360.0 -18.3 7.5 5.4 A A