==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=11-DEC-2009 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER TOXIN 19-NOV-03 1RJI . COMPND 2 MOLECULE: POTASSIUM CHANNEL TOXIN KX; . SOURCE 2 SYNTHETIC: YES; . AUTHOR Z.CAI,J.WU,Y.XU,C.-G.WANG,C.-W.CHI,Y.SHI . 31 1 3 3 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 2589.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 16 51.6 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 . 4 12.9 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 3.2 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 . 5 16.1 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 4 12.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 1 3.2 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 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 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 T 0 0 134 0, 0.0 2,-0.7 0, 0.0 4,-0.2 0.000 360.0 360.0 360.0 147.3 -8.7 1.2 -2.7 2 2 A P + 0 0 40 0, 0.0 25,-0.3 0, 0.0 14,-0.0 -0.138 360.0 97.2 -84.5 40.6 -5.3 2.6 -1.5 3 3 A Y S S+ 0 0 202 -2,-0.7 24,-0.2 23,-0.1 26,-0.0 0.921 95.1 20.0 -90.4 -60.6 -7.0 5.1 0.9 4 4 A P S S+ 0 0 98 0, 0.0 2,-0.9 0, 0.0 -1,-0.1 0.225 97.9 110.6 -94.7 13.1 -6.8 3.2 4.3 5 5 A V - 0 0 18 -4,-0.2 22,-1.3 22,-0.1 2,-0.2 -0.784 50.3-171.3 -94.6 103.3 -4.0 0.9 3.2 6 6 A N B +A 26 0A 106 -2,-0.9 20,-0.3 20,-0.3 2,-0.3 -0.496 13.6 149.1 -90.2 161.4 -0.9 1.8 5.2 7 7 A a - 0 0 9 18,-0.7 3,-0.1 -2,-0.2 18,-0.1 -0.980 41.8-146.4-175.4 172.6 2.7 0.5 4.6 8 8 A K S S+ 0 0 187 -2,-0.3 2,-0.2 1,-0.2 17,-0.2 0.662 86.9 26.4-118.8 -46.7 6.4 1.1 4.8 9 9 A T S > S- 0 0 77 16,-0.1 3,-0.5 12,-0.1 4,-0.5 -0.482 92.1 -94.2-110.5-178.4 7.7 -0.9 1.8 10 10 A D G > S+ 0 0 71 1,-0.2 3,-1.4 2,-0.2 10,-1.2 0.973 124.8 41.4 -62.3 -58.0 6.2 -2.1 -1.5 11 11 A R G > S+ 0 0 204 1,-0.3 3,-1.1 8,-0.2 -1,-0.2 0.447 96.6 82.9 -72.2 2.3 5.0 -5.5 -0.3 12 12 A D G < S+ 0 0 80 -3,-0.5 3,-0.4 1,-0.3 -1,-0.3 0.784 87.6 54.1 -75.7 -25.1 3.9 -3.9 3.0 13 13 A b G X> + 0 0 0 -3,-1.4 3,-2.8 -4,-0.5 4,-1.3 0.029 68.9 128.7 -94.2 25.1 0.6 -2.9 1.3 14 14 A V T <4 + 0 0 83 -3,-1.1 -1,-0.2 1,-0.3 -2,-0.1 0.796 61.9 70.9 -50.2 -30.6 0.0 -6.5 0.3 15 15 A M T 34 S+ 0 0 177 -3,-0.4 -1,-0.3 1,-0.2 -2,-0.1 0.799 103.0 42.9 -57.3 -29.0 -3.5 -6.1 1.8 16 16 A c T <4 S- 0 0 21 -3,-2.8 15,-0.5 1,-0.3 2,-0.3 0.907 130.2 -49.5 -83.4 -47.6 -4.2 -3.9 -1.2 17 17 A G < - 0 0 10 -4,-1.3 2,-1.3 13,-0.2 3,-0.3 -0.931 69.7 -57.7-168.1-169.5 -2.6 -6.0 -3.9 18 18 A L S S- 0 0 164 1,-0.3 -7,-0.1 -2,-0.3 -4,-0.1 -0.659 119.0 -3.9 -92.0 81.2 0.5 -8.0 -5.2 19 19 A G S S- 0 0 40 -2,-1.3 2,-0.4 -9,-0.2 -1,-0.3 0.818 78.8-170.5 99.1 82.2 3.2 -5.3 -5.1 20 20 A I - 0 0 0 -10,-1.2 -7,-0.4 -3,-0.3 2,-0.2 -0.899 25.8-118.9-109.2 133.2 1.9 -1.9 -4.1 21 21 A S - 0 0 58 -2,-0.4 7,-2.3 8,-0.4 2,-0.5 -0.480 31.9-138.8 -67.3 127.1 3.8 1.4 -4.3 22 22 A a B -B 27 0B 30 -2,-0.2 5,-0.2 5,-0.2 -12,-0.1 -0.812 21.1-174.0 -97.0 126.6 4.1 2.8 -0.8 23 23 A K - 0 0 107 3,-2.9 2,-3.7 -2,-0.5 3,-0.3 -0.005 61.9 -27.7 -94.6-158.3 3.7 6.6 -0.3 24 24 A N S S- 0 0 158 1,-0.3 -1,-0.1 3,-0.1 3,-0.1 -0.218 128.6 -43.9 -56.4 65.7 4.1 8.6 2.9 25 25 A G S S+ 0 0 36 -2,-3.7 -18,-0.7 1,-0.3 -1,-0.3 0.686 128.9 78.4 79.1 20.2 3.2 5.6 5.1 26 26 A Y B S-A 6 0A 123 -20,-0.3 -3,-2.9 -3,-0.3 2,-0.3 -0.807 84.4 -75.3-145.3-175.2 0.3 4.6 2.8 27 27 A b B -B 22 0B 2 -22,-1.3 -5,-0.2 -25,-0.3 -22,-0.1 -0.715 24.9-171.8 -92.4 138.9 -0.8 3.0 -0.4 28 28 A Q S S- 0 0 111 -7,-2.3 -1,-0.1 -2,-0.3 -6,-0.1 0.890 71.1 -35.8 -91.4 -51.8 -0.4 4.6 -3.8 29 29 A G + 0 0 45 -8,-0.4 -8,-0.4 -28,-0.1 -1,-0.1 -0.463 60.7 177.2 179.9 100.1 -2.4 2.3 -6.1 30 30 A c 0 0 32 1,-0.2 -13,-0.2 -10,-0.1 -9,-0.1 0.590 360.0 360.0 -79.0-128.8 -2.6 -1.5 -5.8 31 31 A T 0 0 166 -15,-0.5 -1,-0.2 -30,-0.0 -12,-0.0 -0.820 360.0 360.0 -99.8 360.0 -4.7 -3.7 -8.1