==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=6-DEC-2009 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER NEUROTOXIN(POTASSIUM CHANNEL INHIBITOR) 02-JUN-94 1KTX . COMPND 2 MOLECULE: KALIOTOXIN; . SOURCE 2 ORGANISM_SCIENTIFIC: ANDROCTONUS MAURETANICUS MAURETANICUS; . AUTHOR I.FERNANDEZ,R.ROMI,S.SZENDEFI,M.-F.MARTIN-EAUCLAIRE, . 37 1 3 3 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 2738.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 19 51.4 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 . 3 8.1 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 . 1 2.7 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 . 9 24.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 3 8.1 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 2 5.4 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 1 1 A G 0 0 116 0, 0.0 2,-0.1 0, 0.0 3,-0.1 0.000 360.0 360.0 360.0 96.5 -12.0 -2.1 -6.5 2 2 A V + 0 0 65 1,-0.1 27,-0.1 29,-0.0 28,-0.0 -0.491 360.0 89.3-124.0 54.9 -8.6 -1.6 -4.8 3 3 A E + 0 0 163 -2,-0.1 -1,-0.1 1,-0.0 24,-0.1 -0.479 33.7 137.3-144.8 71.0 -8.9 1.8 -3.2 4 4 A I + 0 0 104 1,-0.1 2,-0.3 -3,-0.1 24,-0.1 0.195 68.3 27.6-103.5 19.5 -10.3 1.5 0.4 5 5 A N - 0 0 50 22,-0.1 3,-0.1 -3,-0.0 -1,-0.1 -0.977 42.0-161.2-173.1 151.8 -7.9 4.0 2.1 6 6 A V S S+ 0 0 110 -2,-0.3 20,-0.1 20,-0.2 18,-0.0 -0.316 90.9 41.9-136.3 52.1 -5.7 7.1 1.9 7 7 A K + 0 0 165 1,-0.1 -1,-0.2 0, 0.0 2,-0.1 -0.117 69.6 115.1 166.5 79.7 -3.5 6.6 5.1 8 8 A a + 0 0 30 19,-0.1 2,-0.9 -3,-0.1 17,-0.2 -0.575 23.4 173.3-161.6 92.2 -2.2 3.0 5.9 9 9 A S + 0 0 84 -2,-0.1 2,-1.1 15,-0.1 15,-0.1 -0.584 22.7 147.2-100.6 67.7 1.6 2.4 5.9 10 10 A G > - 0 0 25 -2,-0.9 4,-2.1 1,-0.2 5,-0.3 -0.784 34.0-163.7-101.0 80.5 1.4 -1.2 7.2 11 11 A S H >>>S+ 0 0 24 -2,-1.1 2,-2.0 2,-0.2 3,-1.9 0.860 77.4 46.4 -40.2 -88.9 4.5 -2.2 5.2 12 12 A P H 345S+ 0 0 84 0, 0.0 -1,-0.2 0, 0.0 16,-0.0 -0.384 120.2 43.7 -64.9 88.3 4.3 -6.2 5.2 13 13 A Q H 345S+ 0 0 96 -2,-2.0 16,-0.3 20,-0.0 -2,-0.2 -0.259 135.4 15.1 168.1 -49.7 0.6 -6.0 4.4 14 14 A b H 4< + 0 0 15 -4,-2.0 2,-1.6 -7,-0.2 3,-0.7 -0.328 68.1 140.1-100.4 51.0 4.4 -4.0 -3.3 19 19 A K T < + 0 0 137 -3,-1.2 -1,-0.1 -2,-0.2 -3,-0.1 -0.287 57.6 82.7 -84.7 54.3 8.1 -4.8 -2.1 20 20 A D T 3 S- 0 0 144 -2,-1.6 -1,-0.2 2,-0.3 -2,-0.1 0.702 99.0 -3.2-126.6 -47.8 8.9 -2.8 -5.3 21 21 A A S < S- 0 0 80 -3,-0.7 2,-0.2 1,-0.4 15,-0.1 0.585 105.2 -26.8-121.7 -91.3 8.8 1.1 -4.7 22 22 A G - 0 0 15 13,-0.6 -1,-0.4 11,-0.1 -2,-0.3 -0.546 56.4-104.5-121.8-171.1 7.8 2.9 -1.4 23 23 A M S S+ 0 0 102 -2,-0.2 2,-0.3 1,-0.2 -8,-0.2 0.786 81.1 12.3 -92.7 -27.3 5.6 2.2 1.6 24 24 A R + 0 0 89 9,-0.1 12,-0.8 -15,-0.1 -1,-0.2 -0.974 38.1 122.8-159.2 166.6 2.4 4.3 0.9 25 25 A F E S+A 35 0A 124 -2,-0.3 2,-0.3 10,-0.2 10,-0.2 -0.113 94.1 7.8-178.9 -35.3 -0.1 6.5 -0.8 26 26 A G E S-A 34 0A 1 8,-0.5 8,-1.5 1,-0.3 -20,-0.2 -0.893 98.8 -21.3-167.4 137.2 -3.3 4.3 -0.3 27 27 A K - 0 0 44 -2,-0.3 6,-0.4 6,-0.2 2,-0.4 0.690 42.9-130.7 45.1 157.2 -4.6 1.0 1.5 28 28 A a S S+ 0 0 8 1,-0.4 4,-0.3 4,-0.2 -14,-0.3 -0.928 80.1 6.7-137.2 104.0 -2.8 -2.1 2.9 29 29 A M S S+ 0 0 78 2,-0.9 2,-1.1 -2,-0.4 -1,-0.4 0.576 127.1 36.4 85.3 124.8 -4.3 -5.5 1.8 30 30 A N S S+ 0 0 112 -3,-0.1 2,-0.6 -16,-0.1 -1,-0.1 -0.712 136.4 36.7 96.7 -67.0 -7.1 -5.6 -0.9 31 31 A R S S- 0 0 59 -2,-1.1 -2,-0.9 3,-0.0 2,-0.6 -0.960 88.8-154.2-106.4 119.2 -4.9 -2.8 -2.1 32 32 A K - 0 0 71 -2,-0.6 3,-0.2 -4,-0.3 -18,-0.2 -0.833 62.2 -61.0 -96.4 123.9 -1.3 -3.7 -1.3 33 33 A b - 0 0 0 -2,-0.6 2,-1.3 -6,-0.4 -1,-0.2 0.657 33.7-127.9 -32.4 155.7 -0.1 -0.2 -1.2 34 34 A H E -A 26 0A 59 -8,-1.5 2,-1.6 -7,-0.3 -8,-0.5 -0.828 42.7-153.5 -94.7 95.5 -0.2 2.5 -3.9 35 35 A c E +A 25 0A 29 -2,-1.3 -13,-0.6 -3,-0.2 -10,-0.2 -0.580 51.2 119.1 -92.1 80.4 3.4 2.9 -3.1 36 36 A T 0 0 88 -2,-1.6 -1,-0.1 -12,-0.8 -2,-0.1 -0.725 360.0 360.0-138.3 84.6 4.3 6.5 -4.1 37 37 A P 0 0 137 0, 0.0 -12,-0.1 0, 0.0 -2,-0.1 -0.668 360.0 360.0 -85.8 360.0 5.5 8.4 -0.9