==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=2-JAN-2010 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER MEMBRANE PROTEIN, SIGNALING PROTEIN 18-SEP-09 2KOE . COMPND 2 MOLECULE: HUMAN CANNABINOID RECEPTOR 1 - HELIX 7/8 PEPTIDE; . SOURCE 2 SYNTHETIC: YES; . AUTHOR L.DESHMUKH,O.VINOGRADOVA,A.MAKRIYANNIS,E.TIBURU, . 40 1 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 3716.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 32 80.0 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 . 2 5.0 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 . 1 2.5 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 . 3 7.5 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 4 10.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 18 45.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 6 15.0 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 1 0 0 0 0 0 0 1 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 . 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 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 0 155 0, 0.0 4,-1.7 0, 0.0 3,-1.5 0.000 360.0 360.0 360.0 59.3 19.7 8.6 -6.3 2 2 A V H 3> + 0 0 127 1,-0.3 4,-3.6 2,-0.2 5,-0.3 0.861 360.0 65.2 -51.5 -30.4 19.0 7.9 -2.6 3 3 A F H 3> S+ 0 0 159 1,-0.2 4,-3.0 2,-0.2 -1,-0.3 0.927 98.4 51.8 -60.6 -38.1 17.9 4.5 -3.9 4 4 A A H <> S+ 0 0 42 -3,-1.5 4,-3.5 2,-0.2 5,-0.3 0.943 112.6 46.9 -63.5 -39.7 21.5 3.9 -5.0 5 5 A F H X S+ 0 0 132 -4,-1.7 4,-3.8 2,-0.2 5,-0.3 0.997 113.3 45.6 -62.7 -62.3 22.5 4.9 -1.4 6 6 A A H X S+ 0 0 49 -4,-3.6 4,-3.3 2,-0.2 5,-0.2 0.890 118.5 46.5 -48.9 -39.6 19.8 2.7 0.2 7 7 A S H X S+ 0 0 46 -4,-3.0 4,-3.2 -5,-0.3 6,-0.3 0.994 114.3 43.2 -68.7 -60.8 20.9 -0.1 -2.2 8 8 A M H X>S+ 0 0 90 -4,-3.5 5,-1.4 -5,-0.2 4,-1.1 0.919 119.2 48.2 -50.5 -42.0 24.7 0.3 -1.7 9 9 A L H X>S+ 0 0 44 -4,-3.8 5,-2.1 -5,-0.3 4,-1.5 0.997 111.2 46.4 -63.6 -61.1 23.9 0.6 2.0 10 10 A C H <5S+ 0 0 91 -4,-3.3 -1,-0.2 -5,-0.3 -2,-0.2 0.865 130.6 28.1 -49.1 -34.7 21.6 -2.4 2.2 11 11 A L H X>S+ 0 0 117 -4,-3.2 4,-3.0 -5,-0.2 5,-0.6 0.885 129.9 31.5 -91.8 -81.4 24.3 -4.2 0.2 12 12 A L H X5S+ 0 0 55 -4,-1.1 4,-0.6 -5,-0.2 -3,-0.2 0.821 131.2 40.3 -50.3 -31.7 27.8 -2.8 0.8 13 13 A N H <S+ 0 0 3 -3,-0.2 5,-2.3 -2,-0.1 2,-0.5 0.175 74.5 75.3-173.6 -49.9 30.5 -2.8 7.3 18 18 A P T 5S+ 0 0 102 0, 0.0 -4,-0.1 0, 0.0 -5,-0.1 0.223 101.7 55.9 -65.1 22.0 29.1 -3.4 10.8 19 19 A I T 5S- 0 0 114 -2,-0.5 -3,-0.0 0, 0.0 0, 0.0 0.681 131.6 -36.9-117.3 -66.2 32.4 -5.3 11.2 20 20 A I T 5S+ 0 0 125 2,-0.0 3,-0.2 3,-0.0 6,-0.1 0.589 130.4 52.8-128.3 -66.2 35.4 -3.0 10.5 21 21 A Y T > + 0 0 65 1,-0.2 2,-3.6 4,-0.1 5,-0.6 0.840 68.8 174.8 -50.3 -31.9 34.8 -0.6 7.6 22 22 A A B < -A 25 0A 53 -5,-2.3 -1,-0.2 1,-0.2 3,-0.1 -0.225 68.9 -66.9 58.7 -68.6 31.6 0.6 9.4 23 23 A L T >5S+ 0 0 90 -2,-3.6 4,-0.8 1,-0.6 3,-0.2 0.032 115.7 92.4 174.5 -31.3 31.1 3.3 6.7 24 24 A R T 45S+ 0 0 202 1,-0.2 2,-1.9 -3,-0.2 -1,-0.6 -0.370 103.7 10.5 -69.4 154.5 34.0 5.7 7.3 25 25 A S B >>5S+A 22 0A 63 1,-0.2 4,-3.3 -3,-0.1 3,-1.3 0.218 99.8 107.8 57.9 -21.7 37.0 4.8 5.1 26 26 A K H 3>X + 0 0 6 -2,-1.9 4,-1.9 -5,-0.6 5,-0.6 0.946 68.9 66.6 -45.6 -48.3 34.5 2.4 3.3 27 27 A D H 3X5S+ 0 0 116 -4,-0.8 4,-0.9 1,-0.3 -1,-0.3 0.882 112.3 30.7 -39.3 -48.1 34.8 4.9 0.5 28 28 A L H <>5S+ 0 0 111 -3,-1.3 4,-3.9 3,-0.2 5,-0.3 0.897 111.0 69.1 -80.9 -42.8 38.4 3.9 0.1 29 29 A R H X5S+ 0 0 77 -4,-3.3 4,-1.8 2,-0.2 -2,-0.2 0.922 113.8 24.8 -40.8 -66.0 37.9 0.3 1.2 30 30 A H H <5S+ 0 0 59 -4,-1.9 5,-0.2 2,-0.2 -1,-0.2 0.968 120.4 56.6 -73.2 -47.4 35.9 -0.8 -1.8 31 31 A A H >XXS+ 0 0 20 -4,-0.9 3,-3.0 -5,-0.6 4,-1.4 0.958 105.7 54.3 -47.0 -47.7 37.3 1.8 -4.2 32 32 A F H ><5S+ 0 0 109 -4,-3.9 3,-0.9 1,-0.3 -1,-0.3 0.960 112.3 41.7 -48.2 -52.9 40.6 0.3 -3.2 33 33 A R T 3<5S+ 0 0 169 -4,-1.8 -1,-0.3 -5,-0.3 -2,-0.2 0.086 133.3 26.7 -79.1 24.1 39.1 -3.1 -4.3 34 34 A S T <45S+ 0 0 82 -3,-3.0 -2,-0.3 -5,-0.1 -1,-0.2 0.266 138.0 11.3-166.3 10.3 37.6 -1.2 -7.3 35 35 A M T <<5S+ 0 0 148 -4,-1.4 -3,-0.3 -3,-0.9 -4,-0.1 0.302 76.5 117.9-161.3 -55.6 39.8 1.8 -8.1 36 36 A F < - 0 0 99 -5,-1.1 -1,-0.2 -8,-0.2 -8,-0.0 -0.184 35.6-172.8 -45.3 119.2 43.2 2.1 -6.3 37 37 A P - 0 0 101 0, 0.0 -1,-0.2 0, 0.0 -5,-0.0 0.746 20.9-146.6 -83.6 -27.2 45.8 2.0 -9.1 38 38 A S + 0 0 79 2,-0.1 -2,-0.1 1,-0.1 -6,-0.0 0.809 52.0 139.7 63.5 26.5 48.7 1.8 -6.7 39 39 A A 0 0 84 1,-0.1 -1,-0.1 0, 0.0 -3,-0.0 0.962 360.0 360.0 -66.2 -49.2 50.7 3.9 -9.2 40 40 A E 0 0 241 0, 0.0 -2,-0.1 0, 0.0 -1,-0.1 -0.772 360.0 360.0-124.3 360.0 52.4 5.9 -6.5