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 21-MAR-12 2LR3 .
COMPND MOL_ID: 1; MOLECULE: DEFENSIN; CHAIN: A; FRAGMENT: UNP RESIDUES 30-76; .
SOURCE MOL_ID: 1; ORGANISM_SCIENTIFIC: MEDICAGO TRUNCATULA; ORGANISM_COMMON: .
AUTHOR G.W.BUCHKO,T.J.SMITH,D.M.SHAH .
47 1 4 4 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) .
3758.1 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) .
32 68.1 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 .
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 .
9 19.1 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 .
10 21.3 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 R 0 0 229 0, 0.0 46,-1.0 0, 0.0 2,-0.7 0.000 360.0 360.0 360.0 137.0 6.1 -1.7 0.4 A A
2 2 A T E -A 46 0A 127 44,-0.2 2,-0.4 42,-0.1 44,-0.2 -0.610 360.0-172.5 -67.1 112.1 4.0 -4.1 -1.6 A A
3 3 A a E -A 45 0A 21 42,-2.9 42,-2.9 -2,-0.7 2,-0.3 -0.932 11.2-161.5-118.2 132.0 6.0 -4.1 -4.9 A A
4 4 A E E +A 44 0A 128 -2,-0.4 2,-0.2 40,-0.2 40,-0.2 -0.865 13.9 168.5-114.8 149.2 5.0 -5.7 -8.1 A A
5 5 A S E -A 43 0A 41 38,-2.4 38,-1.4 -2,-0.3 2,-0.3 -0.809 31.5 -97.1-144.6-177.3 7.1 -6.6 -11.1 A A
6 6 A Q E -A 42 0A 73 36,-0.3 2,-0.7 -2,-0.2 36,-0.2 -0.837 18.7-142.3-114.6 147.8 7.1 -8.6 -14.4 A A
7 7 A S + 0 0 7 34,-2.5 34,-0.3 -2,-0.3 17,-0.0 -0.878 30.9 158.2-114.2 99.7 8.3 -12.1 -15.1 A A
8 8 A H S S+ 0 0 185 -2,-0.7 4,-0.1 1,-0.1 -1,-0.1 0.310 70.4 74.3 -95.8 3.8 9.9 -12.4 -18.5 A A
9 9 A K S S+ 0 0 117 2,-0.1 -1,-0.1 -3,-0.1 -2,-0.1 0.834 74.8 90.2 -83.9 -37.8 11.7 -15.4 -17.3 A A
10 10 A F S S- 0 0 32 1,-0.1 2,-0.8 31,-0.1 31,-0.1 -0.333 91.2-106.8 -62.4 141.7 8.7 -17.6 -17.4 A A
11 11 A K S S- 0 0 186 -2,-0.0 4,-0.2 2,-0.0 -1,-0.1 -0.620 70.9 -42.6 -82.1 105.7 8.2 -19.4 -20.8 A A
12 12 A G S S- 0 0 43 -2,-0.8 -2,-0.1 -4,-0.1 2,-0.0 -0.506 104.6 -11.4 85.5-147.7 5.4 -17.9 -22.8 A A
13 13 A P S S- 0 0 61 0, 0.0 2,-1.5 0, 0.0 26,-0.2 -0.176 93.8 -66.4 -80.0-179.0 2.0 -16.9 -21.3 A A
14 14 A b + 0 0 0 24,-1.7 24,-0.2 1,-0.2 3,-0.2 -0.552 49.8 176.1 -75.6 90.2 0.6 -17.7 -17.9 A A
15 15 A A S S- 0 0 45 -2,-1.5 2,-0.3 1,-0.3 -1,-0.2 0.953 76.1 -18.5 -54.2 -50.6 0.2 -21.5 -18.1 A A
16 16 A S > - 0 0 48 -3,-0.2 4,-2.5 1,-0.1 3,-0.3 -0.946 56.9-129.4-159.9 140.1 -0.8 -21.4 -14.4 A A
17 17 A D H > S+ 0 0 24 -2,-0.3 4,-2.9 1,-0.2 5,-0.2 0.932 112.1 50.5 -53.4 -50.8 -0.4 -18.9 -11.6 A A
18 18 A H H > S+ 0 0 152 1,-0.2 4,-2.7 2,-0.2 -1,-0.2 0.812 110.5 51.8 -59.6 -32.1 1.0 -21.5 -9.2 A A
19 19 A N H > S+ 0 0 83 -3,-0.3 4,-2.6 2,-0.2 -2,-0.2 0.960 113.1 40.8 -71.7 -51.8 3.5 -22.5 -11.9 A A
20 20 A c H X S+ 0 0 1 -4,-2.5 4,-3.0 1,-0.2 -2,-0.2 0.857 116.7 53.2 -64.6 -32.9 4.8 -19.1 -12.6 A A
21 21 A A H X S+ 0 0 10 -4,-2.9 4,-2.1 -5,-0.3 -2,-0.2 0.952 107.9 48.7 -63.7 -51.1 4.8 -18.5 -8.9 A A
22 22 A S H X S+ 0 0 58 -4,-2.7 4,-2.0 2,-0.2 -2,-0.2 0.937 115.2 45.4 -55.3 -50.1 6.8 -21.7 -8.2 A A
23 23 A V H >X S+ 0 0 40 -4,-2.6 4,-2.3 1,-0.2 3,-0.5 0.964 113.7 47.9 -55.1 -55.7 9.3 -20.6 -10.8 A A
24 24 A d H 3X S+ 0 0 0 -4,-3.0 4,-1.5 1,-0.3 -1,-0.2 0.764 116.5 45.9 -60.2 -25.6 9.5 -17.0 -9.5 A A
25 25 A Q H 3< S+ 0 0 111 -4,-2.1 -1,-0.3 2,-0.2 -2,-0.2 0.711 109.0 53.7 -90.0 -25.1 9.9 -18.4 -6.0 A A
26 26 A T H << S+ 0 0 110 -4,-2.0 -2,-0.2 -3,-0.5 -3,-0.2 0.811 119.5 34.2 -78.9 -31.0 12.5 -21.0 -7.0 A A
27 27 A E H < S- 0 0 66 -4,-2.3 2,-0.2 -5,-0.2 -2,-0.2 0.878 134.3 -8.1 -87.1 -43.1 14.7 -18.4 -8.6 A A
28 28 A R S < S- 0 0 121 -4,-1.5 2,-0.9 -5,-0.3 -1,-0.2 -0.786 77.0 -88.8-143.5 180.0 13.9 -15.4 -6.2 A A
29 29 A F S S+ 0 0 185 -2,-0.2 2,-0.2 -3,-0.1 -4,-0.2 -0.802 77.3 110.2-102.2 92.0 11.6 -14.3 -3.3 A A
30 30 A S - 0 0 6 -2,-0.9 2,-0.3 -6,-0.2 15,-0.2 -0.787 64.4-125.9-165.6 114.8 8.6 -12.8 -5.0 A A
31 31 A G E -B 44 0A 30 13,-1.9 13,-2.9 -2,-0.2 2,-0.3 -0.495 33.9-153.0 -69.9 126.1 5.1 -14.3 -5.1 A A
32 32 A G E +B 43 0A 4 -2,-0.3 -11,-0.3 11,-0.3 2,-0.3 -0.765 25.7 149.4-114.3 145.0 3.9 -14.6 -8.7 A A
33 33 A R E -B 42 0A 164 9,-2.6 9,-3.0 -2,-0.3 2,-0.4 -0.887 40.0 -97.5-151.6-179.6 0.5 -14.6 -10.4 A A
34 34 A b E -B 41 0A 10 7,-0.3 2,-0.7 -2,-0.3 7,-0.2 -0.865 36.9-102.6-114.5 143.0 -1.1 -13.5 -13.7 A A
35 35 A R S > S- 0 0 187 5,-2.9 2,-2.1 -2,-0.4 4,-0.6 -0.489 99.2 -35.9 -60.0 106.0 -2.9 -10.4 -14.6 A A
36 36 A G T 4 S- 0 0 62 -2,-0.7 2,-0.2 3,-0.1 -2,-0.2 -0.543 122.2 -47.5 72.7 -80.2 -6.5 -11.7 -14.5 A A
37 37 A F T 4 S+ 0 0 114 -2,-2.1 2,-0.8 -4,-0.1 -2,-0.1 -0.769 115.2 1.5 176.9 137.0 -5.5 -15.1 -15.9 A A
38 38 A R T 4 S+ 0 0 128 -24,-0.2 -24,-1.7 -2,-0.2 3,-0.1 0.059 104.0 94.4 73.0 -27.4 -3.4 -16.6 -18.8 A A
39 39 A R S < S- 0 0 189 -2,-0.8 2,-0.3 -4,-0.6 -1,-0.1 0.981 94.7 -27.6 -66.5 -69.3 -2.4 -13.0 -19.9 A A
40 40 A R - 0 0 110 -5,-0.3 -5,-2.9 -27,-0.1 2,-0.5 -0.983 57.6-119.5-158.4 139.6 0.9 -12.1 -18.3 A A
41 41 A c E - B 0 34A 3 -34,-0.3 -34,-2.5 -2,-0.3 2,-0.4 -0.694 26.6-177.0 -94.2 126.3 2.8 -13.0 -15.1 A A
42 42 A F E -AB 6 33A 82 -9,-3.0 -9,-2.6 -2,-0.5 2,-0.4 -0.916 13.8-145.2-117.8 145.3 3.7 -10.5 -12.4 A A
43 43 A d E -AB 5 32A 2 -38,-1.4 -38,-2.4 -2,-0.4 2,-0.4 -0.905 8.3-149.7-114.7 140.4 5.7 -11.1 -9.3 A A
44 44 A T E +AB 4 31A 68 -13,-2.9 -13,-1.9 -2,-0.4 2,-0.3 -0.908 30.0 139.3-115.7 137.2 5.2 -9.4 -5.9 A A
45 45 A T E -A 3 0A 44 -42,-2.9 -42,-2.9 -2,-0.4 2,-0.9 -0.861 56.1 -76.5-158.4-179.6 7.8 -8.7 -3.3 A A
46 46 A H E A 2 0A 151 -2,-0.3 -44,-0.2 -44,-0.2 -2,-0.0 -0.832 360.0 360.0-101.2 100.2 9.0 -6.0 -0.9 A A
47 47 A a 0 0 98 -46,-1.0 -43,-0.1 -2,-0.9 -2,-0.0 -0.825 360.0 360.0 -91.9 360.0 10.8 -3.2 -2.7 A A