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 26-AUG-10 2L2R .
COMPND MOL_ID: 1; MOLECULE: ANTIMICROBIAL PEPTIDE ECAMP1; CHAIN: A .
SOURCE MOL_ID: 1; ORGANISM_SCIENTIFIC: ECHINOCHLOA CRUS-GALLI; ORGANISM_COMMO .
AUTHOR S.B.NOLDE,N.A.BARINOV,T.A.BALASHOVA,A.S.ARSENIEV,A.A.VASSILEVSKI, E.A. .
37 1 2 2 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) .
3846.5 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) .
19 51.4 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 .
0 0.0 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 .
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 .
0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES .
5 13.5 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES .
14 37.8 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 1 1 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 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 ANTIPARALLEL BRIDGES PER LADDER .
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 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 G 0 0 115 0, 0.0 0, 0.0 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 -49.2 15.7 8.7 -34.7 A A
2 2 A S - 0 0 133 2,-0.0 0, 0.0 0, 0.0 0, 0.0 0.826 360.0 -83.5 61.9 32.6 16.9 8.6 -31.1 A A
3 3 A G - 0 0 61 3,-0.0 2,-0.2 0, 0.0 3,-0.0 0.176 59.0 -75.1 59.8 173.8 18.8 5.4 -31.9 A A
4 4 A R S S+ 0 0 215 1,-0.1 -2,-0.0 5,-0.0 0, 0.0 -0.544 89.7 68.6-102.1 168.7 17.2 1.9 -31.8 A A
5 5 A G + 0 0 77 1,-0.2 2,-0.3 -2,-0.2 -1,-0.1 0.937 60.6 134.7 86.5 77.2 16.1 -0.3 -28.9 A A
6 6 A S > - 0 0 59 1,-0.1 4,-2.1 -3,-0.0 -1,-0.2 -0.989 62.1-124.5-155.4 145.5 13.2 1.3 -27.0 A A
7 7 A a H > S+ 0 0 35 -2,-0.3 4,-2.7 1,-0.2 5,-0.2 0.786 110.5 60.1 -59.3 -27.7 9.9 0.2 -25.6 A A
8 8 A R H > S+ 0 0 174 2,-0.2 4,-2.6 1,-0.2 -1,-0.2 0.993 108.0 38.3 -64.2 -64.3 8.2 2.8 -27.7 A A
9 9 A S H > S+ 0 0 45 1,-0.2 4,-2.1 2,-0.2 5,-0.2 0.844 119.1 52.3 -56.2 -34.7 9.3 1.6 -31.2 A A
10 10 A Q H X S+ 0 0 98 -4,-2.1 4,-1.8 2,-0.2 -1,-0.2 0.932 112.8 41.7 -68.0 -47.5 8.8 -2.0 -29.9 A A
11 11 A b H X S+ 0 0 2 -4,-2.7 4,-1.2 2,-0.2 -2,-0.2 0.778 112.9 56.9 -71.2 -26.5 5.2 -1.3 -28.7 A A
12 12 A M H < S+ 0 0 92 -4,-2.6 -2,-0.2 2,-0.2 -1,-0.2 0.935 110.0 41.5 -69.0 -48.6 4.5 0.8 -31.8 A A
13 13 A R H >< S+ 0 0 154 -4,-2.1 3,-1.0 1,-0.2 -2,-0.2 0.853 113.8 53.9 -68.2 -35.7 5.4 -2.1 -34.2 A A
14 14 A R H 3< S+ 0 0 179 -4,-1.8 -1,-0.2 1,-0.3 3,-0.2 0.791 116.6 38.9 -69.3 -27.1 3.6 -4.6 -32.0 A A
15 15 A H T 3< S+ 0 0 31 -4,-1.2 3,-0.3 1,-0.1 -1,-0.3 -0.327 70.3 136.5-118.5 49.2 0.5 -2.4 -32.2 A A
16 16 A E S < S+ 0 0 157 -3,-1.0 -1,-0.1 1,-0.2 -2,-0.1 0.770 77.4 51.2 -65.2 -26.5 0.6 -1.2 -35.8 A A
17 17 A D S S+ 0 0 141 1,-0.2 -1,-0.2 -3,-0.2 -2,-0.1 0.759 127.9 20.2 -81.7 -25.7 -3.1 -1.9 -36.0 A A
18 18 A E > + 0 0 93 -3,-0.3 3,-1.6 -6,-0.2 -1,-0.2 -0.565 62.8 163.3-145.6 75.6 -3.8 0.2 -32.9 A A
19 19 A P G > S+ 0 0 74 0, 0.0 3,-0.7 0, 0.0 4,-0.3 0.563 70.3 78.6 -69.5 -7.6 -1.0 2.6 -32.0 A A
20 20 A W G 3 S+ 0 0 224 1,-0.2 3,-0.2 2,-0.1 4,-0.1 0.643 94.8 46.7 -75.9 -14.8 -3.5 4.4 -29.8 A A
21 21 A R G X> S+ 0 0 92 -3,-1.6 4,-1.1 -6,-0.2 3,-0.6 0.388 82.1 98.4-105.6 0.5 -2.9 1.7 -27.2 A A
22 22 A V H X> S+ 0 0 12 -3,-0.7 4,-3.1 1,-0.2 3,-0.6 0.867 74.6 64.7 -54.3 -39.5 0.9 1.8 -27.5 A A
23 23 A Q H 3> S+ 0 0 140 -4,-0.3 4,-3.2 1,-0.3 -1,-0.2 0.917 98.2 52.8 -50.9 -48.2 1.0 4.0 -24.4 A A
24 24 A E H <> S+ 0 0 122 -3,-0.6 4,-1.3 1,-0.2 -1,-0.3 0.851 113.4 44.9 -57.7 -35.7 -0.4 1.2 -22.2 A A
25 25 A b H + 0 0 149 1,-0.1 4,-1.6 3,-0.1 -1,-0.2 0.962 70.0 156.2 53.0 59.0 9.7 -2.3 -13.8 A A
33 33 A R T 4 + 0 0 193 1,-0.2 -1,-0.1 2,-0.2 -2,-0.1 0.627 60.5 71.8 -87.1 -16.3 12.8 -2.6 -16.0 A A
34 34 A G T 4 S- 0 0 82 1,-0.1 -1,-0.2 0, 0.0 -2,-0.1 0.803 134.2 -48.7 -69.8 -29.2 14.8 -4.3 -13.2 A A
35 35 A G T 4 S+ 0 0 72 -3,-0.2 -2,-0.2 2,-0.1 -1,-0.1 0.321 74.2 176.8 159.4 48.1 12.8 -7.5 -13.5 A A
36 36 A G < 0 0 35 -4,-1.6 -4,-0.0 -5,-0.1 -8,-0.0 -0.074 360.0 360.0 -63.6 168.6 9.0 -6.9 -13.5 A A
37 37 A D 0 0 195 0, 0.0 -1,-0.1 0, 0.0 -2,-0.1 -0.029 360.0 360.0 -81.3 360.0 6.5 -9.7 -14.0 A A