==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=29-DEC-2009 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER ION CHANNEL INHIBITOR 10-APR-06 2CK4 . COMPND 2 MOLECULE: POTASSIUM CHANNEL TOXIN ALPHA-KTX 3.7; . SOURCE 2 SYNTHETIC: YES; . AUTHOR S.ALPHONSE,S.MOUHAT,J.M.SABATIER,H.DARBON,C.BERNARD . 38 1 3 3 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 2937.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 27 71.1 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 21.1 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 . 1 2.6 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 . 7 18.4 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 4 10.5 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 6 15.8 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 1 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 1 1 A G 0 0 92 0, 0.0 2,-1.2 0, 0.0 35,-0.2 0.000 360.0 360.0 360.0 178.0 4.0 8.7 -0.1 2 2 A V E -A 35 0A 66 33,-1.6 33,-1.4 32,-0.0 2,-0.5 -0.712 360.0-178.2 -92.5 93.3 3.0 6.4 -2.9 3 3 A I E -A 34 0A 78 -2,-1.2 2,-0.4 31,-0.2 31,-0.2 -0.819 9.2-159.3 -94.5 124.1 -0.8 5.9 -2.4 4 4 A I E -A 33 0A 51 29,-2.2 29,-2.5 -2,-0.5 -2,-0.0 -0.844 20.3-133.7-103.4 142.5 -2.5 3.6 -4.9 5 5 A N + 0 0 135 -2,-0.4 2,-0.3 27,-0.2 -1,-0.1 0.112 62.0 132.1 -84.0 24.4 -6.2 3.8 -5.5 6 6 A V S S- 0 0 70 27,-0.1 2,-0.8 1,-0.1 27,-0.2 -0.576 70.8-104.4 -76.0 135.6 -6.5 -0.0 -5.2 7 7 A K - 0 0 112 -2,-0.3 2,-1.7 25,-0.1 3,-0.2 -0.509 31.5-149.6 -63.4 105.9 -9.3 -1.2 -2.9 8 8 A a + 0 0 3 23,-1.1 3,-0.1 -2,-0.8 23,-0.1 -0.588 29.3 166.2 -79.2 83.8 -7.5 -2.3 0.2 9 9 A K S S+ 0 0 160 -2,-1.7 2,-0.3 1,-0.3 -1,-0.2 0.767 84.7 4.7 -65.7 -18.5 -9.8 -5.1 1.4 10 10 A I S > S- 0 0 90 -3,-0.2 3,-0.6 1,-0.1 4,-0.5 -0.962 74.1-125.2-162.8 146.4 -6.7 -5.8 3.5 11 11 A S T >> S+ 0 0 43 -2,-0.3 4,-2.8 1,-0.2 3,-1.0 0.806 105.6 65.8 -71.0 -28.4 -3.4 -4.0 4.0 12 12 A R H 3> S+ 0 0 198 1,-0.3 4,-1.9 2,-0.2 -1,-0.2 0.811 95.1 57.8 -64.8 -29.0 -1.4 -7.2 3.1 13 13 A Q H <4 S+ 0 0 77 -3,-0.6 -1,-0.3 1,-0.2 -2,-0.2 0.723 114.2 39.1 -74.6 -20.1 -2.7 -7.1 -0.5 14 14 A b H <> S+ 0 0 1 -3,-1.0 4,-1.2 -4,-0.5 -2,-0.2 0.840 114.7 51.0 -92.3 -41.7 -1.3 -3.6 -0.9 15 15 A L H X S+ 0 0 43 -4,-2.8 4,-3.4 11,-0.4 5,-0.4 0.831 98.5 66.3 -69.2 -34.0 1.9 -4.1 1.0 16 16 A K H X S+ 0 0 150 -4,-1.9 4,-0.9 1,-0.2 -1,-0.2 0.957 112.0 31.4 -55.9 -56.9 3.0 -7.2 -0.8 17 17 A P H 4 S+ 0 0 65 0, 0.0 4,-0.5 0, 0.0 -1,-0.2 0.741 120.9 55.6 -72.9 -20.5 3.5 -5.5 -4.3 18 18 A c H >X>S+ 0 0 8 -4,-1.2 4,-2.8 2,-0.2 3,-1.2 0.958 107.6 43.5 -78.0 -50.6 4.5 -2.2 -2.5 19 19 A K H 3<5S+ 0 0 111 -4,-3.4 -1,-0.2 1,-0.3 -3,-0.1 0.759 112.7 56.8 -65.8 -21.3 7.4 -3.6 -0.4 20 20 A D T 3<5S+ 0 0 134 -4,-0.9 -1,-0.3 -5,-0.4 -2,-0.2 0.680 113.3 39.1 -80.8 -19.9 8.4 -5.4 -3.5 21 21 A A T <45S- 0 0 81 -3,-1.2 -2,-0.2 -4,-0.5 -1,-0.2 0.720 138.0 -74.3 -98.1 -30.2 8.6 -2.2 -5.4 22 22 A G T <5S+ 0 0 27 -4,-2.8 16,-2.0 1,-0.2 2,-0.4 0.575 87.6 125.4 134.8 45.8 10.1 -0.1 -2.6 23 23 A M < - 0 0 28 -5,-1.2 -1,-0.2 14,-0.4 13,-0.1 -0.921 34.8-169.8-131.0 106.6 7.5 0.7 0.0 24 24 A R S S+ 0 0 128 -2,-0.4 2,-0.3 12,-0.3 14,-0.1 0.765 78.0 44.4 -65.4 -27.3 8.4 -0.3 3.6 25 25 A F + 0 0 115 11,-2.8 11,-0.3 -7,-0.1 2,-0.1 -0.844 55.9 174.5-117.9 157.7 4.8 0.4 4.7 26 26 A G + 0 0 11 -2,-0.3 2,-0.4 9,-0.3 -11,-0.4 -0.556 13.8 167.0-162.3 88.6 1.5 -0.5 3.2 27 27 A K E -B 34 0A 129 7,-2.5 7,-3.0 -2,-0.1 2,-0.5 -0.902 36.4-121.4-116.9 134.8 -1.6 0.4 5.2 28 28 A a E +B 33 0A 37 -2,-0.4 2,-0.4 5,-0.2 5,-0.2 -0.605 38.9 173.2 -74.1 120.8 -5.2 0.4 4.1 29 29 A M E > -B 32 0A 72 3,-3.2 3,-2.3 -2,-0.5 -21,-0.1 -0.963 61.9 -25.8-138.7 116.7 -6.7 3.9 4.6 30 30 A N T 3 S- 0 0 155 -2,-0.4 3,-0.1 1,-0.3 -2,-0.1 0.588 125.9 -49.7 63.2 12.1 -10.1 5.2 3.5 31 31 A G T 3 S+ 0 0 14 1,-0.5 -23,-1.1 -23,-0.1 -1,-0.3 0.159 120.9 98.2 113.2 -17.0 -10.1 2.7 0.7 32 32 A K E < S- B 0 29A 97 -3,-2.3 -3,-3.2 -25,-0.2 2,-0.8 -0.697 76.4-115.5-103.7 156.3 -6.7 3.4 -0.7 33 33 A b E -AB 4 28A 0 -29,-2.5 -29,-2.2 -2,-0.3 2,-1.2 -0.814 24.1-154.7 -93.1 109.9 -3.4 1.6 -0.1 34 34 A H E -AB 3 27A 72 -7,-3.0 -7,-2.5 -2,-0.8 2,-0.7 -0.736 15.7-176.3 -87.7 95.7 -1.0 3.9 1.7 35 35 A c E -A 2 0A 0 -33,-1.4 -33,-1.6 -2,-1.2 -9,-0.3 -0.847 9.8-158.8-100.4 110.3 2.4 2.6 0.7 36 36 A T - 0 0 63 -2,-0.7 -11,-2.8 -11,-0.3 -12,-0.3 -0.767 32.6 -99.8 -90.0 129.6 5.2 4.4 2.4 37 37 A P 0 0 57 0, 0.0 -14,-0.4 0, 0.0 -1,-0.1 0.014 360.0 360.0 -54.4 149.6 8.6 4.0 0.6 38 38 A K 0 0 164 -16,-2.0 -15,-0.1 -20,-0.2 -16,-0.1 0.995 360.0 360.0 -68.1 360.0 11.2 1.5 1.8