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 2M2Q .
COMPND MOL_ID: 1; MOLECULE: INHIBITOR CYSTINE KNOT PEPTIDE MCH-1; 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 .
32 1 3 3 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) .
2211.6 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) .
16 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 .
8 25.0 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES .
1 3.1 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-5), SAME NUMBER PER 100 RESIDUES .
1 3.1 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-4), SAME NUMBER PER 100 RESIDUES .
1 3.1 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-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 3.1 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES .
3 9.4 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 .
0 0 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 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 0 112 0, 0.0 4,-0.0 0, 0.0 15,-0.0 0.000 360.0 360.0 360.0 38.7 10.5 -3.4 -0.2 A A
2 2 A a > + 0 0 20 2,-0.1 3,-2.2 15,-0.1 29,-0.3 0.856 360.0 95.7 -80.6 -38.8 7.1 -2.3 1.0 A A
3 3 A A T 3 S+ 0 0 75 1,-0.3 29,-0.2 27,-0.1 3,-0.1 -0.298 88.9 24.6 -57.0 130.3 7.7 1.4 0.6 A A
4 4 A G T 3 S+ 0 0 65 27,-2.2 -1,-0.3 1,-0.3 28,-0.1 0.184 88.9 138.8 99.5 -16.5 6.3 2.7 -2.7 A A
5 5 A K < - 0 0 88 -3,-2.2 26,-3.1 26,-0.3 -1,-0.3 -0.328 57.2-115.0 -63.6 142.7 3.8 -0.2 -3.0 A A
6 6 A S E +A 30 0A 102 24,-0.2 2,-0.3 -3,-0.1 24,-0.3 -0.558 49.8 151.3 -78.5 140.0 0.3 0.7 -4.3 A A
7 7 A b E -A 29 0A 3 22,-2.4 22,-3.3 -2,-0.2 2,-0.3 -0.924 29.7-143.3-156.4 179.2 -2.5 0.2 -1.8 A A
8 8 A N E > -A 28 0A 33 5,-1.1 3,-1.9 20,-0.3 5,-0.5 -0.987 30.2-118.5-155.6 146.8 -5.9 1.4 -0.6 A A
9 9 A I T 3 S+ 0 0 95 18,-2.9 19,-0.1 -2,-0.3 18,-0.0 0.636 98.3 91.4 -59.1 -14.4 -7.8 1.9 2.6 A A
10 10 A L T 3 S- 0 0 127 17,-0.3 -1,-0.3 1,-0.1 18,-0.1 0.767 95.2-130.6 -53.3 -28.1 -10.2 -0.7 1.3 A A
11 11 A G S < S+ 0 0 49 -3,-1.9 -1,-0.1 2,-0.1 -2,-0.1 0.232 87.0 100.1 93.6 -14.4 -8.1 -3.3 3.0 A A
12 12 A S S S+ 0 0 78 1,-0.3 -3,-0.1 2,-0.1 -5,-0.0 0.835 93.2 30.0 -70.0 -35.5 -7.9 -5.4 -0.1 A A
13 13 A D S S+ 0 0 84 -5,-0.5 -5,-1.1 8,-0.0 -1,-0.3 -0.579 84.9 146.3-125.3 65.9 -4.5 -4.1 -0.9 A A
14 14 A P - 0 0 78 0, 0.0 2,-0.3 0, 0.0 17,-0.1 0.478 45.0 -86.7 -76.0-137.8 -2.8 -3.3 2.5 A A
15 15 A c - 0 0 29 4,-0.3 3,-0.1 6,-0.1 6,-0.1 -0.910 39.5 -78.9-138.8 166.8 0.9 -3.7 3.2 A A
16 16 A D S > S- 0 0 72 -2,-0.3 3,-1.8 1,-0.2 -1,-0.1 -0.186 70.9 -71.4 -60.2 153.9 3.6 -6.1 4.3 A A
17 17 A A T 3 S+ 0 0 110 1,-0.3 -1,-0.2 3,-0.0 3,-0.1 -0.242 124.9 19.8 -51.8 125.2 3.9 -6.9 8.1 A A
18 18 A G T 3 S+ 0 0 83 1,-0.4 -1,-0.3 -3,-0.1 2,-0.2 -0.207 110.4 86.2 106.0 -40.4 5.3 -3.8 9.8 A A
19 19 A a < - 0 0 37 -3,-1.8 -1,-0.4 12,-0.0 2,-0.4 -0.531 66.0-147.2 -90.1 158.6 4.5 -1.4 7.0 A A
20 20 A F - 0 0 124 12,-2.3 12,-2.3 -2,-0.2 2,-0.6 -0.960 20.3-108.1-132.5 149.4 1.1 0.4 6.7 A A
21 21 A b E -B 31 0A 26 -2,-0.4 10,-0.2 10,-0.2 -6,-0.1 -0.627 34.5-159.9 -75.6 113.5 -1.0 1.6 3.8 A A
22 22 A L E -B 30 0A 81 8,-2.5 8,-2.8 -2,-0.6 -15,-0.1 -0.863 18.7-121.5-100.4 122.2 -0.9 5.3 3.7 A A
23 23 A P E +B 29 0A 66 0, 0.0 6,-0.3 0, 0.0 5,-0.1 -0.389 28.3 178.0 -64.4 131.7 -3.7 7.1 1.9 A A
24 24 A V S S- 0 0 111 4,-2.9 5,-0.2 -2,-0.1 2,-0.1 0.553 73.0 -6.6-106.2 -17.2 -2.7 9.3 -1.0 A A
25 25 A G S S- 0 0 51 3,-2.2 -17,-0.0 0, 0.0 4,-0.0 -0.327 113.9 -38.7-143.8-133.3 -6.2 10.3 -2.0 A A
26 26 A I S S- 0 0 174 -2,-0.1 3,-0.1 3,-0.0 -18,-0.0 0.838 129.0 -24.7 -76.5 -35.3 -9.8 9.4 -1.1 A A
27 27 A V S S+ 0 0 46 -20,-0.1 -18,-2.9 1,-0.1 -17,-0.3 0.423 118.3 90.1-147.4 -32.9 -9.1 5.7 -0.7 A A
28 28 A A E +A 8 0A 46 -20,-0.2 -4,-2.9 -5,-0.1 -3,-2.2 -0.390 49.9 140.1 -73.4 152.4 -6.0 5.0 -2.8 A A
29 29 A G E -AB 7 23A 6 -22,-3.3 -22,-2.4 -6,-0.3 2,-0.3 -0.851 40.6 -99.2-164.2-160.2 -2.6 5.2 -1.2 A A
30 30 A V E -AB 6 22A 58 -8,-2.8 -8,-2.5 -24,-0.3 -24,-0.2 -0.988 34.9 -99.2-144.5 150.5 0.9 3.7 -1.0 A A
31 31 A c E B 0 21A 3 -26,-3.1 -27,-2.2 -2,-0.3 -26,-0.3 -0.498 360.0 360.0 -71.8 133.1 2.8 1.5 1.4 A A
32 32 A V 0 0 78 -12,-2.3 -12,-2.3 -2,-0.2 -29,-0.0 -0.865 360.0 360.0-136.9 360.0 5.1 3.3 3.9 A A