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 CHITIN-BINDING 25-OCT-95 1MMC .
COMPND MOL_ID: 1; MOLECULE: ANTIMICROBIAL PEPTIDE 2; CHAIN: A; SYNONYM: AC-AM .
SOURCE MOL_ID: 1; ORGANISM_SCIENTIFIC: AMARANTHUS CAUDATUS; ORGANISM_COMMON: .
AUTHOR J.C.MARTINS,D.MAES,R.LORIS,H.A.M.PEPERMANS,L.WYNS,R.WILLEM, P.VERHEYDE .
30 1 3 3 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) .
2418.8 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) .
15 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 .
3 10.0 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 .
1 3.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-4), SAME NUMBER PER 100 RESIDUES .
1 3.3 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 .
3 10.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES .
3 10.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES .
2 6.7 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 .
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 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 V 0 0 89 0, 0.0 20,-0.4 0, 0.0 3,-0.1 0.000 360.0 360.0 360.0 178.9 -4.2 -0.2 -6.1 A A
2 2 A G - 0 0 59 1,-0.3 2,-0.3 18,-0.1 0, 0.0 0.960 360.0 -38.2 -65.2 -59.4 -5.2 3.4 -6.8 A A
3 3 A E - 0 0 119 17,-0.1 -1,-0.3 18,-0.0 17,-0.3 -0.910 69.8 -97.2-164.6 148.4 -4.6 4.8 -3.3 A A
4 4 A a - 0 0 3 15,-2.9 2,-2.2 -2,-0.3 5,-0.2 -0.060 44.6 -91.2 -64.1 172.0 -5.1 3.4 0.3 A A
5 5 A V S S- 0 0 110 3,-3.1 -1,-0.1 1,-0.2 10,-0.0 -0.549 97.2 -54.6 -84.2 69.9 -8.1 4.0 2.5 A A
6 6 A R S S- 0 0 187 -2,-2.2 -1,-0.2 1,-0.2 3,-0.1 0.897 119.9 -31.5 48.5 51.9 -6.2 6.9 4.0 A A
7 7 A G S S+ 0 0 49 1,-0.3 2,-0.3 12,-0.3 -1,-0.2 0.730 123.3 97.6 83.3 28.4 -3.2 4.6 4.8 A A
8 8 A R - 0 0 189 6,-0.1 -3,-3.1 13,-0.0 -1,-0.3 -0.981 46.0-177.0-135.3 140.5 -5.2 1.4 5.4 A A
9 9 A b - 0 0 32 4,-0.4 3,-0.4 -2,-0.3 6,-0.1 -0.894 28.5-104.7-127.5 164.4 -5.7 -1.5 3.0 A A
10 10 A P S > S+ 0 0 94 0, 0.0 3,-2.4 0, 0.0 -1,-0.0 -0.261 96.1 25.2 -82.8 173.0 -7.8 -4.7 3.3 A A
11 11 A S T 3 S- 0 0 98 1,-0.3 12,-0.0 -2,-0.1 0, 0.0 0.753 130.0 -70.4 37.8 41.9 -6.4 -8.3 3.8 A A
12 12 A G T 3 S+ 0 0 55 -3,-0.4 2,-0.3 1,-0.2 -1,-0.3 0.863 81.5 167.2 44.2 46.0 -3.3 -6.7 5.4 A A
13 13 A M < - 0 0 76 -3,-2.4 -4,-0.4 10,-0.1 2,-0.3 -0.687 39.3-112.5 -77.7 141.9 -2.1 -5.3 2.0 A A
14 14 A c E -A 22 0A 37 8,-0.7 8,-1.9 -2,-0.3 2,-0.6 -0.639 14.5-131.7 -83.7 134.6 0.7 -2.8 2.7 A A
15 15 A a E -A 21 0A 41 -2,-0.3 6,-0.3 6,-0.2 -6,-0.1 -0.756 34.0-129.9 -76.1 116.7 0.2 0.9 2.0 A A
16 16 A S > - 0 0 7 4,-2.6 3,-2.3 -2,-0.6 12,-0.2 -0.176 24.3-101.6 -55.1 164.8 3.4 1.8 -0.0 A A
17 17 A Q T 3 S+ 0 0 110 10,-1.1 -1,-0.1 12,-0.5 11,-0.1 0.730 127.9 60.3 -56.3 -20.9 5.5 4.8 0.9 A A
18 18 A F T 3 S- 0 0 122 9,-0.1 -1,-0.3 2,-0.1 3,-0.1 0.278 119.3-112.8 -91.3 2.4 3.6 6.3 -2.1 A A
19 19 A G S < S+ 0 0 33 -3,-2.3 -15,-2.9 1,-0.3 -12,-0.3 0.513 86.1 110.6 71.0 9.3 0.2 5.8 -0.4 A A
20 20 A Y - 0 0 122 -17,-0.3 -4,-2.6 -13,-0.1 2,-0.3 -0.322 59.4-135.6 -91.7-173.6 -0.8 3.1 -3.0 A A
21 21 A b E +A 15 0A 1 -20,-0.4 2,-0.2 -6,-0.3 -6,-0.2 -0.999 37.7 137.4-155.9 151.5 -1.1 -0.5 -1.8 A A
22 22 A G E -A 14 0A 9 -8,-1.9 2,-2.2 -2,-0.3 -8,-0.7 -0.796 57.0 -97.3 174.1 148.6 -0.4 -4.1 -2.5 A A
23 23 A K S S+ 0 0 136 -2,-0.2 -10,-0.1 -10,-0.2 -8,-0.1 -0.399 89.3 67.9 -82.8 66.4 0.8 -7.0 -0.3 A A
24 24 A G S >> S- 0 0 20 -2,-2.2 4,-2.4 -10,-0.2 3,-2.0 -0.970 92.6 -89.0-172.9 165.2 4.5 -6.9 -1.2 A A
25 25 A P H 3> S+ 0 0 102 0, 0.0 4,-1.8 0, 0.0 -1,-0.1 0.689 110.9 76.0 -49.3 -29.9 7.9 -5.2 -1.0 A A
26 26 A K H 34 S+ 0 0 177 2,-0.2 -3,-0.1 1,-0.1 0, 0.0 0.932 121.8 10.2 -48.2 -44.3 7.1 -3.3 -4.3 A A
27 27 A Y H <4 S+ 0 0 73 -3,-2.0 -10,-1.1 -5,-0.2 -9,-0.1 0.910 132.9 51.6 -92.8 -60.7 4.9 -1.2 -2.1 A A
28 28 A c H < S+ 0 0 63 -4,-2.4 -2,-0.2 -6,-0.4 -13,-0.1 0.629 86.9 100.2 -61.2 -27.1 5.8 -2.2 1.5 A A
29 29 A G < 0 0 19 -4,-1.8 -12,-0.5 -5,-0.3 -5,-0.0 -0.171 360.0 360.0 -58.8 159.2 9.6 -1.7 1.1 A A
30 30 A R 0 0 190 -14,-0.1 -1,-0.2 -13,-0.1 -2,-0.1 -0.398 360.0 360.0 63.7 360.0 11.3 1.4 2.4 A A