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 18-JUN-13 2M9O .
COMPND MOL_ID: 1; MOLECULE: KALATA-B7; CHAIN: A; FRAGMENT: UNP RESIDUES 76-10 .
SOURCE MOL_ID: 1; ORGANISM_SCIENTIFIC: OLDENLANDIA AFFINIS; ORGANISM_TAXID: 6 .
AUTHOR N.DALY,A.ELLIOTT,D.CRAIK .
29 1 3 3 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) .
2180.9 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) .
13 44.8 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 .
9 31.0 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 .
0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-4), SAME NUMBER PER 100 RESIDUES .
1 3.4 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 .
1 3.4 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES .
2 6.9 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 .
2 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 ANTIPARALLEL BRIDGES PER LADDER .
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 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 55 0, 0.0 28,-0.3 0, 0.0 18,-0.1 0.000 360.0 360.0 360.0 17.9 3.4 7.9 4.6 A A
2 2 A L B -A 28 0A 90 26,-2.3 26,-2.9 0, 0.0 2,-1.8 -0.977 360.0-146.5-135.5 121.7 4.9 6.8 1.3 A A
3 3 A P + 0 0 75 0, 0.0 3,-0.4 0, 0.0 24,-0.2 -0.207 62.8 121.3 -78.3 47.5 3.1 4.8 -1.4 A A
4 4 A V + 0 0 98 -2,-1.8 23,-0.1 24,-0.3 15,-0.0 -0.144 36.7 99.4-104.0 37.8 6.3 3.0 -2.3 A A
5 5 A a S S- 0 0 19 21,-0.8 -1,-0.2 2,-0.2 22,-0.1 0.796 78.9-137.7 -89.6 -33.3 5.0 -0.5 -1.7 A A
6 6 A G + 0 0 79 -3,-0.4 2,-0.3 20,-0.3 -2,-0.1 0.783 64.4 109.4 79.2 29.3 4.3 -1.2 -5.4 A A
7 7 A E - 0 0 54 19,-0.3 19,-1.2 -4,-0.0 2,-0.4 -0.955 62.7-129.0-135.3 154.6 0.9 -2.9 -4.7 A A
8 8 A T B -B 25 0A 88 -2,-0.3 17,-0.4 17,-0.2 3,-0.2 -0.802 8.0-163.1-103.1 143.5 -2.7 -2.0 -5.2 A A
9 9 A b + 0 0 2 15,-0.6 16,-0.3 -2,-0.4 14,-0.2 -0.157 53.8 117.5-118.4 40.7 -5.3 -2.2 -2.4 A A
10 10 A T S S+ 0 0 95 14,-0.5 -1,-0.1 1,-0.2 15,-0.1 0.812 83.1 49.1 -73.3 -27.4 -8.5 -2.2 -4.4 A A
11 11 A L S S- 0 0 109 -3,-0.2 -1,-0.2 2,-0.2 -2,-0.1 0.660 123.0-108.9 -81.9 -19.8 -9.1 -5.6 -3.0 A A
12 12 A G S S+ 0 0 49 1,-0.3 2,-0.3 12,-0.0 -3,-0.1 0.872 81.6 100.2 91.0 44.4 -8.4 -4.3 0.5 A A
13 13 A T - 0 0 67 -5,-0.2 2,-0.3 7,-0.1 -1,-0.3 -0.986 45.4-166.5-156.9 152.9 -5.1 -6.0 1.2 A A
14 14 A c - 0 0 32 -2,-0.3 7,-0.1 5,-0.1 5,-0.1 -0.981 8.6-170.5-146.0 127.5 -1.4 -5.3 1.2 A A
15 15 A Y + 0 0 186 -2,-0.3 -1,-0.1 2,-0.1 -8,-0.0 0.644 61.7 99.2 -91.1 -19.4 1.5 -7.8 1.3 A A
16 16 A T S > S- 0 0 45 1,-0.1 3,-0.8 2,-0.1 2,-0.3 -0.266 82.8 -99.9 -69.5 155.6 4.2 -5.2 1.8 A A
17 17 A Q T 3 S- 0 0 180 1,-0.2 3,-0.1 -12,-0.1 -1,-0.1 -0.613 99.9 -0.0 -81.9 133.8 5.6 -4.4 5.2 A A
18 18 A G T 3 S+ 0 0 57 -2,-0.3 11,-1.0 1,-0.3 2,-0.4 0.578 97.5 141.2 67.6 9.7 4.3 -1.3 7.1 A A
19 19 A a E < -C 28 0A 18 -3,-0.8 2,-0.4 9,-0.2 9,-0.3 -0.684 38.1-154.9 -88.4 134.3 2.1 -0.6 4.2 A A
20 20 A T E -C 27 0A 73 7,-2.7 7,-2.6 -2,-0.4 2,-0.3 -0.873 29.5 -98.4-111.1 142.5 -1.4 0.6 4.8 A A
21 21 A b E +C 26 0A 73 -2,-0.4 5,-0.2 5,-0.2 2,-0.2 -0.415 47.5 165.8 -61.4 117.5 -4.4 0.2 2.5 A A
22 22 A S E > -C 25 0A 28 3,-3.1 3,-2.9 -2,-0.3 -13,-0.2 -0.647 47.9 -95.2-136.2 72.3 -4.8 3.5 0.6 A A
23 23 A W T 3 S+ 0 0 190 1,-0.4 -13,-0.1 -14,-0.2 3,-0.1 0.036 108.6 12.9 -35.7 129.1 -7.2 2.7 -2.2 A A
24 24 A P T 3 S+ 0 0 68 0, 0.0 -15,-0.6 0, 0.0 -14,-0.5 -0.891 136.2 20.1 -97.5 29.0 -6.2 2.0 -4.8 A A
25 25 A I E < S-BC 8 22A 66 -3,-2.9 -3,-3.1 -17,-0.4 2,-0.4 -0.620 74.3 -99.3-132.9-166.6 -2.7 1.4 -3.5 A A
26 26 A c E - C 0 21A 1 -19,-1.2 -21,-0.8 -5,-0.2 2,-0.5 -0.969 26.9-162.5-124.3 136.6 -0.6 0.7 -0.4 A A
27 27 A K E - C 0 20A 68 -7,-2.6 -7,-2.7 -2,-0.4 2,-0.4 -0.975 1.1-161.4-126.2 123.3 1.3 3.3 1.6 A A
28 28 A R E AC 2 19A 110 -26,-2.9 -26,-2.3 -2,-0.5 -24,-0.3 -0.865 360.0 360.0-104.6 133.7 4.1 2.6 4.1 A A
29 29 A N 0 0 107 -11,-1.0 -1,-0.2 -2,-0.4 -10,-0.1 0.805 360.0 360.0 42.2 360.0 5.2 5.2 6.7 A A