==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=27-NOV-2009 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER TRANSMEMBRANE PROTEIN 20-JAN-00 1DXZ . COMPND 2 MOLECULE: ACETYLCHOLINE RECEPTOR PROTEIN, ALPHA CHAIN; . SOURCE 2 SYNTHETIC: THE C-TERMINAL CARBOXYL GROUP OF THR267 IS . AUTHOR V.S.PASHKOV,I.V.MASLENNIKOV,L.D.TCHIKIN,R.G.EFREMOV, . 32 1 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 3075.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 23 71.9 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 . 0 0.0 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 . 0 0.0 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 . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 1 3.1 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 22 68.8 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 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 1 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 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 1 236 A P 0 0 172 0, 0.0 2,-0.4 0, 0.0 6,-0.1 0.000 360.0 360.0 360.0 83.5 -4.6 22.1 -5.0 2 237 A T + 0 0 90 1,-0.1 3,-0.1 4,-0.1 0, 0.0 -0.962 360.0 175.2-131.0 114.7 -1.3 20.4 -4.2 3 238 A D S S- 0 0 141 -2,-0.4 -1,-0.1 1,-0.1 2,-0.0 0.915 83.6 -12.6 -82.6 -47.5 0.5 21.1 -1.0 4 239 A S S S- 0 0 93 0, 0.0 -1,-0.1 0, 0.0 5,-0.1 -0.434 116.3 -59.7-159.3 70.6 3.4 18.7 -1.4 5 240 A G S > S+ 0 0 29 3,-0.1 4,-2.7 -3,-0.1 5,-0.1 0.897 83.0 150.3 50.4 46.9 3.0 16.2 -4.2 6 241 A E H > S+ 0 0 102 2,-0.2 4,-2.3 1,-0.2 5,-0.2 0.953 73.0 41.5 -72.8 -52.9 -0.2 14.9 -2.5 7 242 A K H > S+ 0 0 155 2,-0.2 4,-2.5 1,-0.2 -1,-0.2 0.878 117.2 52.2 -59.2 -39.0 -1.9 13.9 -5.8 8 243 A M H > S+ 0 0 118 2,-0.2 4,-2.1 1,-0.2 -2,-0.2 0.944 109.6 46.0 -61.8 -51.2 1.4 12.5 -6.9 9 244 A T H X S+ 0 0 82 -4,-2.7 4,-2.9 1,-0.2 -1,-0.2 0.832 113.0 51.7 -63.3 -33.7 2.0 10.5 -3.8 10 245 A L H X S+ 0 0 113 -4,-2.3 4,-1.9 2,-0.2 5,-0.3 0.912 106.5 53.5 -65.4 -44.5 -1.6 9.2 -4.1 11 246 A S H X S+ 0 0 45 -4,-2.5 4,-2.7 1,-0.2 5,-0.3 0.877 114.6 41.6 -58.4 -40.1 -0.9 8.3 -7.7 12 247 A I H X S+ 0 0 81 -4,-2.1 4,-2.9 2,-0.2 5,-0.5 0.927 110.0 56.6 -70.9 -47.4 2.1 6.2 -6.5 13 248 A S H X S+ 0 0 74 -4,-2.9 4,-0.5 1,-0.2 -2,-0.2 0.798 120.0 32.4 -56.2 -30.5 0.3 4.8 -3.5 14 249 A V H X S+ 0 0 80 -4,-1.9 4,-2.3 2,-0.1 -2,-0.2 0.922 121.9 42.7 -91.1 -56.2 -2.4 3.5 -5.8 15 250 A L H X S+ 0 0 92 -4,-2.7 4,-2.5 -5,-0.3 -3,-0.2 0.816 113.6 54.2 -66.6 -32.0 -0.6 2.6 -9.1 16 251 A L H X S+ 0 0 104 -4,-2.9 4,-2.3 -5,-0.3 -1,-0.2 0.916 112.0 42.8 -68.5 -44.8 2.3 1.1 -7.2 17 252 A S H X S+ 0 0 67 -4,-0.5 4,-2.3 -5,-0.5 -2,-0.2 0.806 114.7 52.6 -68.4 -30.7 0.1 -1.2 -5.3 18 253 A L H X S+ 0 0 91 -4,-2.3 4,-2.2 2,-0.2 -2,-0.2 0.871 110.4 47.0 -70.0 -38.7 -1.8 -1.8 -8.5 19 254 A T H X S+ 0 0 88 -4,-2.5 4,-2.3 2,-0.2 -2,-0.2 0.861 113.3 48.0 -72.2 -37.5 1.5 -2.7 -10.3 20 255 A V H X S+ 0 0 82 -4,-2.3 4,-2.8 2,-0.2 -2,-0.2 0.912 113.6 47.6 -66.4 -44.4 2.5 -5.0 -7.4 21 256 A F H X S+ 0 0 124 -4,-2.3 4,-2.1 2,-0.2 -2,-0.2 0.851 110.9 51.7 -64.4 -36.3 -0.9 -6.6 -7.5 22 257 A L H X S+ 0 0 86 -4,-2.2 4,-2.2 2,-0.2 -2,-0.2 0.895 109.2 50.9 -64.7 -41.6 -0.6 -6.9 -11.2 23 258 A L H X S+ 0 0 94 -4,-2.3 4,-1.9 2,-0.2 -2,-0.2 0.943 108.8 50.6 -57.6 -50.3 2.8 -8.6 -10.6 24 259 A V H X S+ 0 0 70 -4,-2.8 4,-1.9 1,-0.2 -1,-0.2 0.878 109.7 51.6 -55.6 -40.2 1.2 -10.9 -8.2 25 260 A I H X S+ 0 0 64 -4,-2.1 4,-2.6 1,-0.2 -1,-0.2 0.895 108.6 49.8 -64.1 -41.7 -1.5 -11.7 -10.8 26 261 A V H < S+ 0 0 81 -4,-2.2 -1,-0.2 1,-0.2 -2,-0.2 0.778 111.4 51.0 -69.0 -27.0 1.2 -12.4 -13.4 27 262 A E H < S+ 0 0 126 -4,-1.9 -1,-0.2 -5,-0.2 -2,-0.2 0.851 117.1 37.5 -75.6 -36.9 2.9 -14.7 -10.9 28 263 A L H >X S+ 0 0 104 -4,-1.9 3,-2.2 -5,-0.2 4,-1.9 0.777 102.2 72.7 -87.5 -29.7 -0.2 -16.7 -10.1 29 264 A I T 3< S+ 0 0 108 -4,-2.6 3,-0.5 1,-0.3 -1,-0.2 0.915 98.3 46.7 -54.1 -51.8 -1.7 -16.7 -13.6 30 265 A P T 34 S+ 0 0 105 0, 0.0 -1,-0.3 0, 0.0 -2,-0.1 0.355 111.6 56.5 -75.0 7.5 0.9 -19.2 -14.9 31 266 A S T <4 0 0 80 -3,-2.2 -2,-0.2 1,-0.1 -3,-0.1 0.722 360.0 360.0-105.4 -35.2 0.2 -21.2 -11.8 32 267 A T < 0 0 134 -4,-1.9 -1,-0.1 -3,-0.5 -4,-0.0 -0.575 360.0 360.0 -77.7 360.0 -3.6 -21.6 -12.2