==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=4-OCT-2013 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER MEMBRANE PROTEIN 20-SEP-13 2ME2 . COMPND 2 MOLECULE: ENVELOPE GLYCOPROTEIN GP160; . SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; . AUTHOR Z.J.SUN,G.WAGNER,E.L.REINHERZ,M.KIM,L.SONG,J.CHOI,Y.CHENG, . 27 1 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 3232.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 19 70.4 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 . 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 . 2 7.4 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 8 29.6 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 9 33.3 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 1 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 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 1 657 A E 0 0 196 0, 0.0 2,-0.1 0, 0.0 8,-0.0 0.000 360.0 360.0 360.0 -41.7 17.8 -26.2 -7.1 2 658 A K + 0 0 162 7,-0.0 2,-0.1 6,-0.0 5,-0.0 -0.494 360.0 156.6-132.6 66.9 21.4 -25.2 -6.6 3 659 A D - 0 0 101 -2,-0.1 6,-0.2 1,-0.1 7,-0.1 -0.338 52.8-114.3 -85.0 172.2 23.7 -27.8 -8.2 4 660 A L S S+ 0 0 140 1,-0.2 -1,-0.1 -2,-0.1 6,-0.1 0.795 114.5 54.1 -77.7 -26.2 27.3 -27.1 -9.4 5 661 A L S S+ 0 0 154 1,-0.1 2,-1.5 2,-0.1 -1,-0.2 0.951 87.8 81.1 -71.7 -49.0 26.3 -27.7 -13.0 6 662 A A > - 0 0 37 1,-0.2 3,-1.6 2,-0.1 4,-0.4 -0.367 59.8-177.3 -60.2 90.4 23.5 -25.2 -13.0 7 663 A L G >> S+ 0 0 103 -2,-1.5 4,-1.3 1,-0.3 3,-0.6 0.662 70.3 83.6 -69.9 -10.1 25.7 -22.1 -13.5 8 664 A D G 34 S+ 0 0 125 1,-0.3 4,-0.3 2,-0.2 -1,-0.3 0.820 96.3 44.7 -61.9 -23.5 22.5 -20.0 -13.3 9 665 A S G <> S+ 0 0 43 -3,-1.6 4,-0.6 -6,-0.2 3,-0.4 0.639 99.8 69.7 -92.9 -15.5 23.1 -20.3 -9.5 10 666 A W H X> S+ 0 0 74 -3,-0.6 4,-3.5 -4,-0.4 3,-1.0 0.850 82.2 73.9 -70.5 -32.0 26.9 -19.6 -9.8 11 667 A K H 3X S+ 0 0 136 -4,-1.3 4,-1.9 1,-0.3 -1,-0.2 0.904 94.2 52.2 -49.1 -41.6 26.1 -15.9 -10.7 12 668 A N H 3> S+ 0 0 134 -3,-0.4 4,-0.6 -4,-0.3 -1,-0.3 0.860 114.2 43.9 -64.7 -30.6 25.2 -15.3 -7.1 13 669 A L H XX S+ 0 0 48 -3,-1.0 4,-1.1 -4,-0.6 3,-0.5 0.861 107.3 57.9 -81.9 -35.7 28.6 -16.9 -6.2 14 670 A W H 3< S+ 0 0 133 -4,-3.5 3,-0.3 1,-0.3 -2,-0.2 0.874 103.3 55.0 -63.1 -31.2 30.5 -14.9 -9.0 15 671 A S H 3< S+ 0 0 102 -4,-1.9 -1,-0.3 -5,-0.3 -2,-0.2 0.822 100.0 61.4 -69.4 -28.3 29.2 -11.7 -7.3 16 672 A W H << S+ 0 0 199 -4,-0.6 2,-1.5 -3,-0.5 -1,-0.2 0.845 90.6 72.9 -67.1 -31.9 30.8 -13.0 -4.1 17 673 A F < + 0 0 102 -4,-1.1 3,-0.5 -3,-0.3 2,-0.4 -0.633 58.7 172.4 -86.2 87.5 34.2 -12.9 -5.7 18 674 A S >> + 0 0 74 -2,-1.5 3,-1.3 1,-0.2 4,-1.0 -0.094 32.1 129.2 -87.7 39.4 34.9 -9.2 -5.9 19 675 A I H >> + 0 0 87 -2,-0.4 4,-2.8 1,-0.3 3,-1.1 0.942 63.0 65.5 -59.9 -46.7 38.5 -9.8 -7.1 20 676 A T H 34 S+ 0 0 88 -3,-0.5 4,-0.5 1,-0.3 -1,-0.3 0.785 101.3 54.8 -49.0 -19.9 38.1 -7.4 -10.1 21 677 A N H <4 S+ 0 0 119 -3,-1.3 4,-0.3 2,-0.2 3,-0.3 0.877 108.8 44.3 -80.6 -38.8 37.7 -4.9 -7.2 22 678 A W H X< S+ 0 0 139 -3,-1.1 3,-0.9 -4,-1.0 4,-0.4 0.806 108.6 58.5 -75.7 -27.8 41.0 -5.8 -5.7 23 679 A L G >X S+ 0 0 62 -4,-2.8 4,-3.0 1,-0.2 3,-0.9 0.727 89.2 74.0 -74.1 -18.9 42.7 -5.9 -9.1 24 680 A W G 34 S+ 0 0 187 -4,-0.5 -1,-0.2 -5,-0.4 -2,-0.2 0.796 89.6 59.5 -65.4 -23.8 41.7 -2.2 -9.6 25 681 A Y G <4 S+ 0 0 207 -3,-0.9 -1,-0.3 -4,-0.3 -2,-0.2 0.761 122.7 21.9 -75.8 -23.0 44.5 -1.3 -7.1 26 682 A I T <4 0 0 96 -3,-0.9 -2,-0.2 -4,-0.4 -1,-0.2 0.533 360.0 360.0-119.1 -12.2 47.1 -2.9 -9.4 27 683 A K < 0 0 184 -4,-3.0 -3,-0.2 -5,-0.1 -2,-0.1 0.913 360.0 360.0 -78.0 360.0 45.4 -2.9 -12.8