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 22-OCT-13 2MFS .
COMPND MOL_ID: 1; MOLECULE: EP-AMP1; CHAIN: A; ENGINEERED: YES .
SOURCE MOL_ID: 1; SYNTHETIC: YES; ORGANISM_SCIENTIFIC: SYNTHETIC; ORGANISM_TA .
AUTHOR K.ROSENGREN,U.GORANSSON,S.GUNASEKERA,T.L.ABOYE .
35 1 3 3 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) .
2672.7 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) .
19 54.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES .
2 5.7 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES .
8 22.9 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES .
1 2.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-5), SAME NUMBER PER 100 RESIDUES .
1 2.9 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 .
3 8.6 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES .
2 5.7 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES .
3 8.6 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 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 RESIDUES PER ALPHA HELIX .
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 0 PARALLEL BRIDGES PER LADDER .
1 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 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 a 0 0 120 0, 0.0 15,-0.3 0, 0.0 2,-0.2 0.000 360.0 360.0 360.0 152.9 -8.8 -2.2 -2.2 A A
2 2 A V B -a 16 0A 24 13,-2.5 15,-2.7 4,-0.1 2,-0.2 -0.629 360.0-124.4-106.8 167.4 -5.7 -2.3 -4.3 A A
3 3 A L > - 0 0 78 -2,-0.2 3,-1.8 13,-0.2 30,-0.5 -0.466 43.1 -60.7-107.4 176.0 -3.4 -5.1 -5.2 A A
4 4 A I T 3 S+ 0 0 87 1,-0.3 30,-0.2 -2,-0.2 -1,-0.2 -0.273 121.7 18.7 -61.1 135.0 0.4 -5.8 -4.9 A A
5 5 A G T 3 S+ 0 0 63 28,-2.8 2,-0.3 1,-0.4 -1,-0.3 0.240 100.9 110.6 87.6 -13.3 2.6 -3.4 -6.8 A A
6 6 A Q S < S- 0 0 92 -3,-1.8 27,-2.1 27,-0.2 -1,-0.4 -0.657 76.7-104.7 -90.4 151.2 -0.2 -0.9 -6.9 A A
7 7 A R B +B 32 0B 175 -2,-0.3 25,-0.3 25,-0.2 2,-0.2 -0.522 44.2 170.6 -85.9 146.2 0.2 2.2 -4.8 A A
8 8 A b - 0 0 3 23,-1.7 2,-0.3 -2,-0.2 18,-0.2 -0.732 26.9-141.7-139.1 176.9 -1.7 2.7 -1.7 A A
9 9 A D > - 0 0 21 5,-3.1 4,-1.5 -2,-0.2 22,-0.1 -0.851 11.0-148.9-152.1 117.3 -1.9 5.0 1.3 A A
10 10 A N T 4 S+ 0 0 63 -2,-0.3 -1,-0.1 20,-0.3 5,-0.0 0.813 94.1 30.2 -57.1 -39.0 -2.6 3.6 4.7 A A
11 11 A D T 4 S+ 0 0 157 2,-0.1 -1,-0.2 3,-0.1 4,-0.1 0.910 131.3 26.9 -91.9 -47.6 -4.4 6.6 6.1 A A
12 12 A R T 4 S- 0 0 202 1,-0.2 -2,-0.2 2,-0.1 3,-0.1 0.807 111.8-108.8 -89.5 -29.9 -6.1 8.2 3.2 A A
13 13 A G S < S+ 0 0 30 -4,-1.5 -1,-0.2 1,-0.4 2,-0.2 -0.216 81.8 120.1 102.6 160.3 -6.6 5.3 0.9 A A
14 14 A P - 0 0 66 0, 0.0 -5,-3.1 0, 0.0 -1,-0.4 0.562 54.5-168.9 -79.7 167.5 -6.5 3.3 -1.2 A A
15 15 A R - 0 0 167 -7,-0.2 -13,-2.5 -2,-0.2 3,-0.1 -0.868 24.6 -95.7-122.0 156.2 -5.5 0.3 0.9 A A
16 16 A c B -a 2 0A 21 -2,-0.3 -13,-0.2 -15,-0.3 2,-0.1 -0.274 43.5 -98.2 -70.2 149.3 -4.4 -3.2 -0.1 A A
17 17 A a >> - 0 0 24 -15,-2.7 3,-2.8 1,-0.1 4,-1.1 -0.469 37.3-112.6 -68.4 143.7 -6.8 -6.1 -0.3 A A
18 18 A S T 34 S+ 0 0 139 1,-0.3 -1,-0.1 2,-0.2 -2,-0.1 0.695 117.8 40.5 -54.3 -26.5 -6.7 -8.3 2.8 A A
19 19 A G T 34 S+ 0 0 75 1,-0.0 -1,-0.3 3,-0.0 3,-0.1 0.172 108.3 67.7-108.1 16.5 -5.1 -11.2 0.9 A A
20 20 A Q T <4 S- 0 0 60 -3,-2.8 2,-0.3 1,-0.3 -2,-0.2 0.887 101.3 -71.8 -97.7 -68.1 -2.8 -9.0 -1.2 A A
21 21 A G < - 0 0 25 -4,-1.1 2,-0.4 14,-0.1 -1,-0.3 -0.967 48.0 -69.9-175.8-179.2 -0.1 -7.4 0.9 A A
22 22 A N E -C 34 0B 106 12,-2.7 12,-2.5 -2,-0.3 2,-1.2 -0.751 45.5-118.6 -93.3 139.6 0.7 -4.9 3.5 A A
23 23 A b E -C 33 0B 6 -2,-0.4 10,-0.3 10,-0.2 -13,-0.1 -0.699 32.9-165.7 -79.5 98.1 0.6 -1.3 2.4 A A
24 24 A V E -C 32 0B 63 8,-2.9 8,-2.6 -2,-1.2 -16,-0.2 -0.808 21.6-121.4 -89.6 120.1 4.2 -0.3 3.0 A A
25 25 A P E -C 31 0B 87 0, 0.0 6,-0.4 0, 0.0 -16,-0.1 -0.330 23.7-155.2 -67.2 141.7 4.4 3.5 2.9 A A
26 26 A L E > -C 30 0B 60 4,-0.8 4,-1.1 -18,-0.2 -18,-0.0 -0.913 25.7-112.3-119.4 144.2 6.6 5.2 0.4 A A
27 27 A P T 4 S- 0 0 129 0, 0.0 -1,-0.1 0, 0.0 0, 0.0 0.848 105.6 -7.0 -40.3 -57.3 8.3 8.6 0.7 A A
28 28 A F T 4 S+ 0 0 182 1,-0.1 3,-0.0 -3,-0.0 -2,-0.0 0.648 128.4 65.9-119.2 -24.2 6.3 10.4 -2.1 A A
29 29 A L T 4 S- 0 0 82 1,-0.1 2,-1.8 -4,-0.0 -21,-0.1 0.440 98.5-129.4 -79.9 0.5 4.3 7.6 -3.7 A A
30 30 A G E < - C 0 26B 15 -4,-1.1 -4,-0.8 -23,-0.1 2,-0.3 -0.388 61.6 -46.3 87.6 -59.2 2.4 7.2 -0.5 A A
31 31 A G E - C 0 25B 0 -2,-1.8 -23,-1.7 -6,-0.4 2,-0.3 -0.945 49.5-131.8 171.6 170.8 2.8 3.5 -0.2 A A
32 32 A V E -BC 7 24B 34 -8,-2.6 -8,-2.9 -25,-0.3 2,-0.6 -0.994 25.5-111.9-147.3 146.1 2.6 0.3 -2.1 A A
33 33 A c E + C 0 23B 2 -27,-2.1 -28,-2.8 -30,-0.5 2,-0.3 -0.704 49.8 157.4 -80.1 118.4 1.1 -3.0 -1.5 A A
34 34 A A E C 0 22B 37 -12,-2.5 -12,-2.7 -2,-0.6 -18,-0.0 -0.969 360.0 360.0-143.9 153.7 3.8 -5.6 -1.0 A A
35 35 A V 0 0 178 -2,-0.3 -1,-0.2 -14,-0.3 -13,-0.1 0.942 360.0 360.0 -87.6 360.0 4.2 -9.0 0.7 A A