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 UNKNOWN FUNCTION 01-JAN-13 2M2R .
COMPND MOL_ID: 1; MOLECULE: INHIBITOR CYSTINE KNOT PEPTIDE MCH-2; CHAIN: A .
SOURCE MOL_ID: 1; ORGANISM_SCIENTIFIC: MOMORDICA CHARANTIA; ORGANISM_TAXID: 3 .
AUTHOR W.HE,L.CHAN,R.J.CLARK,J.TANG,G.ZENG,O.L.FRANCO,C.CANTACESSI, D.J.CRAIK .
33 1 3 3 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) .
2448.7 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) .
13 39.4 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 .
7 21.2 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 .
4 12.1 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES .
2 6.1 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 .
0 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 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 G 0 0 104 0, 0.0 32,-0.1 0, 0.0 31,-0.0 0.000 360.0 360.0 360.0 49.3 11.8 1.6 -0.4 A A
2 2 A a + 0 0 31 17,-0.1 2,-1.6 13,-0.1 13,-0.4 -0.166 360.0 146.9-113.5 35.4 10.3 -1.8 -1.1 A A
3 3 A A + 0 0 58 30,-0.2 11,-0.1 1,-0.2 30,-0.1 -0.574 17.2 173.4 -76.6 87.6 8.2 -0.6 -4.0 A A
4 4 A G S S- 0 0 71 -2,-1.6 -1,-0.2 9,-0.2 3,-0.1 0.904 70.9 -65.4 -62.1 -42.4 8.3 -3.7 -6.2 A A
5 5 A K S S- 0 0 190 -3,-0.2 2,-0.3 1,-0.1 -2,-0.1 0.082 100.6 -20.1-174.2 -50.8 5.8 -2.2 -8.6 A A
6 6 A A - 0 0 60 7,-0.2 2,-0.3 25,-0.1 25,-0.3 -0.960 48.5-156.1-169.9 158.6 2.4 -1.7 -7.0 A A
7 7 A b E -A 30 0A 2 23,-2.7 23,-0.9 -2,-0.3 2,-0.4 -0.949 10.1-145.6-150.8 127.3 0.4 -2.9 -4.0 A A
8 8 A N E -A 29 0A 84 -2,-0.3 2,-2.3 21,-0.2 3,-0.4 -0.764 23.4-126.6 -94.0 136.0 -3.4 -2.9 -3.4 A A
9 9 A L S S+ 0 0 90 19,-3.5 20,-0.1 -2,-0.4 -1,-0.1 -0.169 91.4 93.5 -74.3 47.1 -4.6 -2.3 0.1 A A
10 10 A L S S- 0 0 126 -2,-2.3 2,-0.3 18,-0.1 -1,-0.2 -0.034 105.3 -32.3-126.1 25.4 -6.6 -5.6 -0.1 A A
11 11 A G S S- 0 0 50 -3,-0.4 2,-0.3 9,-0.0 9,-0.2 -0.916 85.5 -64.1 162.4-131.4 -4.0 -7.8 1.4 A A
12 12 A L + 0 0 147 -2,-0.3 7,-0.1 7,-0.1 -3,-0.0 -0.977 42.4 150.0-158.4 142.3 -0.2 -7.8 1.5 A A
13 13 A T + 0 0 98 -2,-0.3 2,-0.3 2,-0.1 -9,-0.2 -0.074 48.8 103.4-166.9 44.1 2.6 -8.1 -1.0 A A
14 14 A c S S- 0 0 29 4,-0.1 3,-0.1 -11,-0.1 6,-0.1 -0.939 76.2 -85.4-133.5 154.9 5.5 -6.1 0.3 A A
15 15 A D > - 0 0 105 -13,-0.4 3,-1.9 -2,-0.3 -2,-0.1 -0.162 64.0 -78.8 -56.6 150.2 8.8 -6.9 2.1 A A
16 16 A A T 3 S+ 0 0 109 1,-0.3 -1,-0.2 3,-0.0 3,-0.1 -0.309 121.2 20.2 -55.5 124.0 8.6 -7.3 5.9 A A
17 17 A G T 3 S+ 0 0 81 1,-0.2 2,-1.0 -3,-0.1 -1,-0.3 -0.111 98.9 101.5 106.8 -34.6 8.5 -3.9 7.5 A A
18 18 A a < - 0 0 19 -3,-1.9 -1,-0.2 -16,-0.0 2,-0.1 -0.744 65.5-149.6 -88.5 103.3 7.4 -2.1 4.4 A A
19 19 A F - 0 0 138 -2,-1.0 14,-1.6 1,-0.1 2,-0.5 -0.438 22.6-105.6 -73.7 146.1 3.6 -1.5 4.8 A A
20 20 A b E -B 32 0A 21 12,-0.2 12,-0.2 -9,-0.2 -1,-0.1 -0.598 39.6-161.0 -73.6 118.2 1.4 -1.4 1.8 A A
21 21 A R E -B 31 0A 109 10,-1.3 10,-2.7 -2,-0.5 -14,-0.2 -0.902 10.5-131.9-108.2 130.9 0.4 2.2 1.2 A A
22 22 A P E -B 30 0A 33 0, 0.0 8,-0.3 0, 0.0 6,-0.1 -0.256 26.5-110.4 -71.5 161.8 -2.6 3.3 -0.9 A A
23 23 A D S S- 0 0 104 6,-3.2 2,-0.2 1,-0.1 7,-0.1 0.969 77.5 -60.0 -58.7 -54.8 -2.2 6.0 -3.5 A A
24 24 A G S > S- 0 0 37 5,-0.3 3,-1.0 3,-0.1 2,-0.4 -0.658 87.8 -12.9-160.2-143.6 -4.2 8.5 -1.6 A A
25 25 A V T 3 S+ 0 0 143 1,-0.2 3,-0.1 -2,-0.2 -2,-0.0 -0.618 125.1 3.6 -81.0 131.3 -7.6 9.2 -0.1 A A
26 26 A G T 3 S+ 0 0 91 -2,-0.4 2,-0.4 1,-0.2 -1,-0.2 0.779 102.5 122.4 67.3 29.0 -10.4 6.9 -1.1 A A
27 27 A I < - 0 0 69 -3,-1.0 -1,-0.2 1,-0.1 -3,-0.1 -0.983 43.6-172.1-127.0 132.8 -8.1 4.7 -3.2 A A
28 28 A V + 0 0 87 -2,-0.4 -19,-3.5 -6,-0.1 2,-0.2 0.772 69.6 78.2 -89.3 -31.6 -7.5 1.0 -2.7 A A
29 29 A A E +A 8 0A 39 -21,-0.2 -6,-3.2 -20,-0.1 -5,-0.3 -0.515 58.5 124.2 -79.8 147.4 -4.6 0.8 -5.1 A A
30 30 A G E -AB 7 22A 13 -23,-0.9 -23,-2.7 -8,-0.3 2,-0.3 -0.791 48.2 -91.6-167.4-148.7 -1.2 2.0 -4.1 A A
31 31 A V E - B 0 21A 48 -10,-2.7 -10,-1.3 -25,-0.3 -28,-0.1 -0.994 36.9 -94.8-153.1 149.5 2.5 0.9 -3.7 A A
32 32 A c E B 0 20A 4 -2,-0.3 -12,-0.2 -12,-0.2 -13,-0.1 -0.397 360.0 360.0 -64.9 137.7 4.8 -0.5 -1.1 A A
33 33 A V 0 0 59 -14,-1.6 -30,-0.2 -31,-0.1 -1,-0.1 0.616 360.0 360.0 -72.5 360.0 6.7 2.1 0.9 A A