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 DE NOVO PROTEIN 03-AUG-17 5WOV .
COMPND MOL_ID: 1; MOLECULE: TWO INHIBITOR PEPTIDE TOPOLOGIES 2; CHAIN: A; ENG .
SOURCE MOL_ID: 1; SYNTHETIC: YES; ORGANISM_SCIENTIFIC: MOMORDICA COCHINCHINEN .
AUTHOR C.I.SCHROEDER,S.KWON .
34 1 3 3 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) .
2508.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) .
17 50.0 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 .
4 11.8 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 .
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 .
1 2.9 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 8.8 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES .
5 14.7 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES .
2 5.9 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+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 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 60 0, 0.0 2,-0.3 0, 0.0 31,-0.2 0.000 360.0 360.0 360.0 87.3 -5.0 7.4 -6.5 A A
2 2 A G - 0 0 32 30,-0.9 2,-0.6 2,-0.1 19,-0.1 -0.930 360.0 -84.4-172.1 156.3 -6.5 3.9 -6.4 A A
3 3 A V + 0 0 128 -2,-0.3 17,-2.6 17,-0.0 18,-0.4 -0.622 59.6 148.4 -78.1 116.8 -9.2 2.0 -4.5 A A
4 4 A a - 0 0 22 -2,-0.6 15,-0.1 15,-0.2 3,-0.1 -0.990 46.5-146.2-146.1 138.9 -7.9 0.7 -1.2 A A
5 5 A P S S+ 0 0 102 0, 0.0 2,-0.7 0, 0.0 -1,-0.2 0.968 103.7 45.4 -64.8 -54.3 -9.5 0.1 2.1 A A
6 6 A K S S- 0 0 121 1,-0.2 3,-0.2 -3,-0.1 26,-0.1 -0.814 71.3-179.2 -88.8 113.7 -6.3 1.1 3.8 A A
7 7 A I S S+ 0 0 108 -2,-0.7 2,-0.4 1,-0.3 -1,-0.2 0.565 75.8 42.4 -93.6 -7.3 -5.2 4.2 2.1 A A
8 8 A L S S+ 0 0 109 24,-0.1 2,-0.4 -3,-0.1 -1,-0.3 -0.866 75.9 140.0-142.8 97.5 -2.1 4.5 4.1 A A
9 9 A Q - 0 0 30 -2,-0.4 20,-3.2 20,-0.3 2,-0.3 -0.989 43.9-131.3-140.3 144.3 -0.3 1.3 4.8 A A
10 10 A R B -A 28 0A 186 -2,-0.4 2,-0.4 18,-0.3 18,-0.3 -0.674 33.9-131.8 -87.9 155.2 3.3 0.4 4.9 A A
11 11 A b - 0 0 21 16,-2.6 3,-0.1 -2,-0.3 4,-0.0 -0.864 33.2-177.5-124.2 144.8 4.3 -2.6 2.9 A A
12 12 A R S S- 0 0 195 1,-0.6 2,-0.3 -2,-0.4 -1,-0.2 0.799 88.6 -17.9 -89.5 -47.4 6.2 -5.8 3.4 A A
13 13 A R S >> S- 0 0 172 1,-0.1 3,-1.6 14,-0.0 -1,-0.6 -0.919 76.4 -93.8-151.5 170.9 5.6 -6.8 -0.2 A A
14 14 A D G >4 S+ 0 0 84 -2,-0.3 3,-1.7 1,-0.3 -1,-0.1 0.885 121.4 57.3 -61.3 -41.2 3.1 -5.8 -2.9 A A
15 15 A S G 34 S+ 0 0 81 1,-0.3 -1,-0.3 7,-0.1 6,-0.0 0.599 96.6 65.2 -67.2 -12.6 0.7 -8.6 -2.0 A A
16 16 A D G <4 S+ 0 0 53 -3,-1.6 -1,-0.3 2,-0.1 -2,-0.2 0.702 85.1 88.6 -82.9 -18.3 0.5 -7.2 1.5 A A
17 17 A c S << S- 0 0 12 -3,-1.7 2,-0.1 -4,-0.5 6,-0.1 -0.618 78.3-132.7 -81.9 134.0 -1.1 -4.1 0.1 A A
18 18 A P > - 0 0 31 0, 0.0 3,-1.6 0, 0.0 14,-0.1 -0.444 62.6 -6.8 -85.0 160.6 -4.9 -4.2 -0.2 A A
19 19 A G T 3 S- 0 0 64 1,-0.3 -15,-0.2 -2,-0.1 -2,-0.1 -0.285 129.8 -22.5 60.5-134.5 -7.0 -3.2 -3.2 A A
20 20 A A T 3 S+ 0 0 53 -17,-2.6 -1,-0.3 2,-0.1 11,-0.2 0.465 101.7 128.5 -88.1 -4.2 -5.1 -1.6 -6.0 A A
21 21 A a < - 0 0 4 -3,-1.6 2,-0.3 -18,-0.4 -4,-0.1 -0.281 40.8-164.8 -57.7 131.1 -2.4 -0.5 -3.7 A A
22 22 A I - 0 0 65 -6,-0.1 8,-1.7 6,-0.0 2,-0.4 -0.828 24.8-107.3-114.9 157.1 1.1 -1.5 -4.8 A A
23 23 A b B -B 29 0B 40 -2,-0.3 6,-0.2 6,-0.2 2,-0.2 -0.704 36.1-158.4 -87.5 129.1 4.2 -1.5 -2.7 A A
24 24 A R > - 0 0 143 4,-2.7 3,-1.9 -2,-0.4 -13,-0.1 -0.648 31.0-104.3-103.4 170.8 6.6 1.3 -3.5 A A
25 25 A G T 3 S+ 0 0 90 1,-0.3 -1,-0.1 -2,-0.2 -2,-0.0 0.709 117.6 63.2 -68.6 -21.9 10.3 1.5 -2.9 A A
26 26 A N T 3 S- 0 0 115 2,-0.2 -1,-0.3 1,-0.0 3,-0.1 0.591 121.3-106.1 -77.7 -11.7 9.8 3.9 0.1 A A
27 27 A G S < S+ 0 0 24 -3,-1.9 -16,-2.6 1,-0.4 2,-0.3 0.636 81.5 117.7 96.1 15.6 8.0 1.0 1.8 A A
28 28 A Y B S-A 10 0A 96 -18,-0.3 -4,-2.7 -4,-0.1 2,-1.4 -0.842 76.0-111.8-113.8 152.9 4.5 2.4 1.4 A A
29 29 A c B > +B 23 0B 1 -20,-3.2 4,-0.9 -2,-0.3 -20,-0.3 -0.719 48.2 177.2 -77.9 95.0 1.4 1.1 -0.4 A A
30 30 A G H >> + 0 0 14 -8,-1.7 4,-2.6 -2,-1.4 3,-0.5 0.956 58.0 61.7 -74.9 -56.5 1.6 3.9 -2.9 A A
31 31 A S H 34 S+ 0 0 32 -9,-0.4 -1,-0.2 1,-0.3 -10,-0.2 0.782 106.8 47.3 -47.6 -39.0 -1.2 3.4 -5.5 A A
32 32 A G H 34 S+ 0 0 3 2,-0.2 -30,-0.9 1,-0.2 -1,-0.3 0.927 116.2 42.9 -71.2 -42.1 -4.0 3.8 -2.9 A A
33 33 A S H << 0 0 71 -4,-0.9 -2,-0.2 -3,-0.5 -1,-0.2 0.795 360.0 360.0 -70.6 -29.5 -2.6 6.8 -1.3 A A
34 34 A D < 0 0 146 -4,-2.6 -2,-0.2 -5,-0.1 -3,-0.2 0.940 360.0 360.0 -80.7 360.0 -1.8 8.2 -4.8 A A