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 27-FEB-10 2KUS .
COMPND MOL_ID: 1; MOLECULE: SM-AMP-1.1A; CHAIN: A .
SOURCE MOL_ID: 1; ORGANISM_SCIENTIFIC: STELLARIA MEDIA; ORGANISM_TAXID: 13274 .
AUTHOR T.N.BOZIN,E.V.BOCHAROV,V.A.SOBOL,A.A.VASSILEVSKI,A.A.ARSENIEV .
35 1 3 3 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) .
2683.6 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) .
16 45.7 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 .
7 20.0 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 .
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-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 2.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES .
5 14.3 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 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 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 .
2 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 ANTIPARALLEL BRIDGES PER LADDER .
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 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 S 0 0 79 0, 0.0 6,-0.1 0, 0.0 11,-0.1 0.000 360.0 360.0 360.0 133.4 2.1 0.0 -1.2 A A
2 2 A G > - 0 0 11 4,-0.6 3,-1.7 1,-0.1 9,-0.0 0.046 360.0 -98.8 -53.4 170.7 5.7 -1.1 -1.5 A A
3 3 A P T 3 S+ 0 0 129 0, 0.0 -1,-0.1 0, 0.0 0, 0.0 0.617 123.5 54.5 -75.0 -12.6 8.5 1.5 -1.1 A A
4 4 A N T 3 S- 0 0 120 2,-0.0 22,-0.1 0, 0.0 -2,-0.1 0.404 125.8 -97.9 -97.5 -0.2 8.9 1.8 -4.8 A A
5 5 A G < + 0 0 10 -3,-1.7 21,-2.5 1,-0.2 2,-0.2 0.770 58.4 177.9 88.5 28.7 5.2 2.6 -5.4 A A
6 6 A Q B -A 25 0A 37 19,-0.2 -4,-0.6 14,-0.1 2,-0.3 -0.475 6.5-168.2 -68.8 129.9 4.2 -0.9 -6.3 A A
7 7 A a + 0 0 14 17,-2.3 6,-0.2 -2,-0.2 7,-0.1 -0.924 35.2 49.9-122.6 146.9 0.4 -1.2 -6.9 A A
8 8 A G B >> S+B 12 0B 30 4,-2.8 4,-2.3 -2,-0.3 3,-2.1 -0.879 89.3 10.5 125.6-158.7 -1.8 -4.2 -7.3 A A
9 9 A P T 34 S+ 0 0 145 0, 0.0 -2,-0.0 0, 0.0 4,-0.0 -0.283 131.6 4.5 -75.0 84.7 -2.7 -7.5 -5.7 A A
10 10 A G T 34 S+ 0 0 75 -2,-1.9 -3,-0.0 0, 0.0 0, 0.0 0.236 127.2 56.4 135.1 -10.9 -1.0 -7.4 -2.3 A A
11 11 A W T <4 S- 0 0 145 -3,-2.1 2,-0.2 1,-0.2 -4,-0.1 0.667 95.5-129.8-114.9 -33.1 0.5 -3.9 -2.1 A A
12 12 A G B < -B 8 0B 37 -4,-2.3 -4,-2.8 -11,-0.1 -1,-0.2 -0.665 29.9 -56.0 113.0-169.8 -2.5 -1.7 -2.7 A A
13 13 A G - 0 0 53 -6,-0.2 2,-0.2 -2,-0.2 13,-0.1 -0.132 56.2 -86.5 -97.3-164.1 -3.4 1.2 -5.0 A A
14 14 A b - 0 0 38 4,-0.2 -1,-0.1 1,-0.2 6,-0.1 -0.647 44.5 -92.2-105.5 163.9 -1.8 4.6 -5.6 A A
15 15 A R > - 0 0 174 -2,-0.2 3,-1.1 4,-0.1 -1,-0.2 -0.104 46.5 -94.4 -66.5 169.7 -2.3 7.9 -3.9 A A
16 16 A G T 3 S+ 0 0 87 1,-0.3 -1,-0.1 3,-0.0 -2,-0.1 0.920 130.0 37.9 -52.0 -49.7 -4.8 10.5 -5.0 A A
17 17 A G T 3 S+ 0 0 62 11,-0.0 -1,-0.3 2,-0.0 2,-0.3 0.482 113.9 74.6 -81.8 -2.0 -2.3 12.3 -7.1 A A
18 18 A L < - 0 0 46 -3,-1.1 2,-0.3 10,-0.1 10,-0.2 -0.735 61.6-166.2-110.0 159.7 -0.7 9.0 -8.1 A A
19 19 A c E -C 27 0C 31 8,-1.8 8,-1.9 -2,-0.3 2,-0.5 -0.991 31.4 -98.7-145.1 150.8 -1.9 6.3 -10.5 A A
20 20 A a E -C 26 0C 54 -2,-0.3 6,-0.2 6,-0.2 15,-0.1 -0.566 42.4-148.4 -72.6 118.7 -1.0 2.7 -11.3 A A
21 21 A S > - 0 0 12 4,-1.7 3,-1.8 -2,-0.5 11,-0.1 -0.221 30.7 -98.5 -80.3 174.1 1.3 2.6 -14.4 A A
22 22 A Q T 3 S+ 0 0 145 1,-0.3 -1,-0.1 2,-0.1 10,-0.1 0.610 126.6 54.2 -68.6 -10.8 1.5 -0.1 -17.0 A A
23 23 A Y T 3 S- 0 0 168 2,-0.3 -1,-0.3 0, 0.0 3,-0.1 0.252 122.1-105.8-105.3 9.5 4.5 -1.4 -15.1 A A
24 24 A G S < S+ 0 0 24 -3,-1.8 -17,-2.3 1,-0.3 2,-0.5 0.645 82.2 128.8 75.6 14.0 2.7 -1.6 -11.8 A A
25 25 A Y B -A 6 0A 132 -19,-0.2 -4,-1.7 -11,-0.0 -1,-0.3 -0.891 61.4-120.0-107.8 131.3 4.5 1.5 -10.6 A A
26 26 A b E +C 20 0C 24 -21,-2.5 2,-0.3 -2,-0.5 -6,-0.2 -0.391 48.3 145.3 -67.1 140.4 2.7 4.5 -9.1 A A
27 27 A G E -C 19 0C 10 -8,-1.9 -8,-1.8 -12,-0.1 2,-0.2 -0.987 40.3-111.5-167.9 166.7 3.2 7.7 -10.9 A A
28 28 A S + 0 0 81 -2,-0.3 3,-0.2 -10,-0.2 -10,-0.1 -0.553 62.7 62.7-103.7 170.2 1.7 11.0 -12.0 A A
29 29 A G S >> S- 0 0 36 -12,-0.2 4,-2.2 -2,-0.2 3,-0.9 -0.245 90.3 -78.0 103.3 166.2 0.7 12.4 -15.4 A A
30 30 A P H 3> S+ 0 0 101 0, 0.0 4,-1.2 0, 0.0 -1,-0.1 0.687 126.6 64.1 -74.9 -19.6 -1.8 11.3 -18.2 A A
31 31 A K H 34 S+ 0 0 173 1,-0.2 -2,-0.1 -3,-0.2 -3,-0.0 0.546 115.2 30.5 -79.2 -7.3 0.6 8.6 -19.2 A A
32 32 A Y H <4 S+ 0 0 91 -3,-0.9 3,-0.3 -11,-0.1 -1,-0.2 0.630 128.4 37.2-119.3 -31.8 0.1 7.0 -15.8 A A
33 33 A c H < S+ 0 0 56 -4,-2.2 2,-1.3 1,-0.2 -2,-0.1 0.835 111.7 58.1 -90.3 -39.2 -3.4 8.0 -14.9 A A
34 34 A A < 0 0 77 -4,-1.2 -1,-0.2 -5,-0.3 -13,-0.0 -0.420 360.0 360.0 -90.5 59.8 -4.9 7.7 -18.4 A A
35 35 A H 0 0 178 -2,-1.3 -1,-0.2 -3,-0.3 -2,-0.1 0.745 360.0 360.0 -72.3 360.0 -4.0 4.0 -18.9 A A