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 PLANT PROTEIN 17-JAN-06 2FQA .
COMPND MOL_ID: 1; MOLECULE: VIOLACIN 1; CHAIN: A; FRAGMENT: RESIDUES 1-27; SY .
SOURCE MOL_ID: 1; ORGANISM_SCIENTIFIC: VIOLA ODORATA; ORGANISM_TAXID: 97441 .
AUTHOR D.C.IRELAND,D.J.CRAIK,N.L.DALY .
27 1 3 3 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) .
2177.4 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) .
16 59.3 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 .
8 29.6 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 .
2 7.4 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 .
5 18.5 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES .
2 7.4 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+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 .
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 .
1 2 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 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 S 0 0 80 0, 0.0 18,-0.2 0, 0.0 17,-0.1 0.000 360.0 360.0 360.0 158.4 -5.3 8.6 -0.3 A A
2 2 A A - 0 0 41 16,-1.6 3,-0.4 15,-0.2 4,-0.2 0.082 360.0 -83.9 -77.0-166.8 -2.6 10.4 -2.3 A A
3 3 A I S S+ 0 0 165 1,-0.2 2,-1.6 2,-0.1 -1,-0.1 0.844 118.5 73.4 -69.9 -36.3 -2.0 10.3 -6.0 A A
4 4 A S S S+ 0 0 62 13,-0.2 -1,-0.2 2,-0.0 12,-0.2 -0.096 95.7 56.9 -74.2 41.3 0.0 7.2 -5.8 A A
5 5 A a + 0 0 13 -2,-1.6 -2,-0.1 -3,-0.4 22,-0.1 -0.001 42.9 117.4-132.0-120.0 -3.1 5.1 -5.1 A A
6 6 A G S S+ 0 0 87 20,-0.2 2,-0.3 -4,-0.2 21,-0.1 0.759 80.7 57.6 51.2 30.8 -6.2 4.7 -7.2 A A
7 7 A E S S- 0 0 102 19,-0.3 19,-1.5 -3,-0.1 -1,-0.2 -0.961 92.2 -69.8-166.6-178.6 -5.6 1.0 -7.7 A A
8 8 A T B -A 25 0A 85 -2,-0.3 17,-0.3 17,-0.2 2,-0.3 -0.323 39.7-153.1 -78.9 165.5 -5.0 -2.4 -6.1 A A
9 9 A b - 0 0 1 15,-1.6 2,-0.4 13,-0.1 16,-0.2 -0.781 4.2-161.3-152.2 105.2 -1.8 -3.1 -4.3 A A
10 10 A F - 0 0 137 -2,-0.3 2,-1.0 14,-0.2 3,-0.2 -0.704 67.8 -26.7 -88.3 132.7 -0.2 -6.5 -3.8 A A
11 11 A K S S- 0 0 163 -2,-0.4 12,-0.7 1,-0.2 -2,-0.0 -0.557 125.4 -29.0 70.8 -98.2 2.3 -7.0 -1.0 A A
12 12 A F S S+ 0 0 120 -2,-1.0 -1,-0.2 10,-0.1 -2,-0.1 -0.394 84.5 131.2-151.6 64.0 3.9 -3.6 -0.4 A A
13 13 A K + 0 0 90 -3,-0.2 2,-0.5 1,-0.1 -2,-0.1 0.860 63.7 65.8 -86.0 -39.3 3.8 -1.6 -3.6 A A
14 14 A c + 0 0 2 1,-0.1 7,-1.8 11,-0.1 13,-0.1 -0.744 44.9 142.9 -89.4 127.1 2.3 1.6 -2.1 A A
15 15 A Y E +C 20 0B 171 -2,-0.5 5,-0.2 5,-0.2 -1,-0.1 -0.012 33.3 125.0-150.0 28.1 4.5 3.4 0.4 A A
16 16 A T E > S-C 19 0B 46 3,-1.2 3,-2.0 -12,-0.2 -14,-0.2 -0.669 78.3 -78.0 -92.1 145.5 3.7 7.0 -0.4 A A
17 17 A P T 3 S+ 0 0 108 0, 0.0 -15,-0.2 0, 0.0 -13,-0.2 -0.212 120.8 1.5 -47.8 120.4 2.4 9.4 2.3 A A
18 18 A R T 3 S+ 0 0 153 -17,-0.1 -16,-1.6 9,-0.1 2,-0.1 0.827 115.4 95.6 64.9 36.1 -1.3 8.6 2.8 A A
19 19 A a E < +C 16 0B 1 -3,-2.0 -3,-1.2 8,-0.4 2,-0.4 -0.559 54.7 176.1-151.9 71.4 -1.1 5.8 0.3 A A
20 20 A S E -C 15 0B 54 7,-1.2 7,-3.3 -5,-0.2 2,-1.7 -0.690 33.9-126.8 -89.7 136.9 -0.4 2.5 2.2 A A
21 21 A b E +B 26 0A 12 -7,-1.8 2,-1.5 -2,-0.4 5,-0.2 -0.604 31.6 177.1 -82.0 86.3 -0.2 -0.8 0.5 A A
22 22 A S E > -B 25 0A 82 3,-2.3 3,-2.7 -2,-1.7 -13,-0.1 -0.668 51.3 -88.5 -92.8 77.7 -2.8 -2.7 2.5 A A
23 23 A Y T 3 S+ 0 0 157 -2,-1.5 -13,-0.2 -12,-0.7 -2,-0.0 0.056 112.7 9.9 -32.2 120.8 -2.6 -6.0 0.6 A A
24 24 A P T 3 S+ 0 0 62 0, 0.0 -15,-1.6 0, 0.0 -1,-0.4 -0.753 127.6 55.7-105.1 43.7 -4.3 -6.2 -1.7 A A
25 25 A V E < -AB 8 22A 64 -3,-2.7 -3,-2.3 -17,-0.3 2,-0.6 -0.987 65.4-134.0-134.1 141.4 -5.5 -2.5 -1.7 A A
26 26 A c E B 0 21A 1 -19,-1.5 -19,-0.3 -2,-0.4 -5,-0.2 -0.796 360.0 360.0 -92.3 121.5 -3.7 0.8 -1.9 A A
27 27 A K 0 0 119 -7,-3.3 -7,-1.2 -2,-0.6 -8,-0.4 -0.815 360.0 360.0-152.4 360.0 -5.0 3.3 0.6 A A