==== 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 2ME4 . 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) . 3547.0 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 . 4 14.8 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 7 25.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 8 29.6 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 3 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 . 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 0 212 0, 0.0 2,-0.5 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 82.3 43.2 16.8 -22.7 2 658 A K - 0 0 193 1,-0.0 2,-0.5 2,-0.0 0, 0.0 -0.432 360.0-163.4 -62.5 111.7 40.4 14.9 -20.9 3 659 A D - 0 0 88 -2,-0.5 3,-0.4 1,-0.1 6,-0.1 -0.855 18.6-161.0-102.5 128.8 42.3 12.2 -19.0 4 660 A L S S+ 0 0 156 -2,-0.5 -1,-0.1 1,-0.2 -2,-0.0 0.724 97.3 46.1 -78.2 -19.0 40.3 9.2 -17.7 5 661 A L S S+ 0 0 154 4,-0.0 2,-1.5 3,-0.0 -1,-0.2 0.441 76.1 126.2-100.8 -0.6 43.1 8.4 -15.2 6 662 A A >> - 0 0 23 -3,-0.4 3,-3.2 1,-0.2 4,-1.0 -0.361 45.9-163.8 -60.2 90.4 43.5 12.0 -14.1 7 663 A L H 3> S+ 0 0 124 -2,-1.5 4,-1.5 1,-0.3 -1,-0.2 0.795 83.4 75.2 -50.0 -25.7 43.0 11.3 -10.3 8 664 A D H 34 S+ 0 0 155 1,-0.2 -1,-0.3 2,-0.2 4,-0.1 0.804 103.2 38.3 -59.4 -24.5 42.5 15.1 -10.0 9 665 A K H X4 S+ 0 0 151 -3,-3.2 3,-0.8 1,-0.1 4,-0.4 0.643 105.6 66.2 -99.5 -17.5 39.0 14.4 -11.5 10 666 A W H >X S+ 0 0 103 -4,-1.0 4,-1.8 1,-0.2 3,-1.4 0.789 76.1 87.6 -74.0 -25.6 38.4 11.1 -9.7 11 667 A N T 3< S+ 0 0 121 -4,-1.5 4,-0.5 1,-0.3 -1,-0.2 0.819 86.7 54.4 -43.4 -32.9 38.3 12.9 -6.3 12 668 A S T X> S+ 0 0 86 -3,-0.8 3,-0.8 1,-0.2 4,-0.7 0.883 105.1 51.0 -73.7 -34.5 34.6 13.4 -6.9 13 669 A L H <> S+ 0 0 59 -3,-1.4 4,-2.0 -4,-0.4 3,-0.3 0.808 104.4 59.7 -71.4 -26.6 33.9 9.7 -7.4 14 670 A W H 3< S+ 0 0 138 -4,-1.8 -1,-0.2 1,-0.2 -2,-0.2 0.670 94.9 64.5 -75.6 -15.0 35.7 9.0 -4.1 15 671 A S H <4 S+ 0 0 99 -3,-0.8 -1,-0.2 -4,-0.5 -2,-0.2 0.831 120.3 17.2 -80.5 -28.7 33.2 11.1 -2.2 16 672 A W H < S+ 0 0 168 -4,-0.7 -2,-0.2 -3,-0.3 2,-0.1 0.697 124.6 55.3-112.3 -27.5 30.2 8.9 -2.9 17 673 A F S < S+ 0 0 121 -4,-2.0 2,-1.0 -5,-0.2 -1,-0.1 -0.168 72.0 139.5 -97.4 42.7 31.8 5.6 -4.0 18 674 A D + 0 0 68 1,-0.2 3,-0.3 -3,-0.2 4,-0.2 -0.725 18.9 167.7 -89.4 100.9 33.9 5.3 -0.9 19 675 A I >> + 0 0 80 -2,-1.0 3,-2.9 1,-0.2 4,-2.3 0.728 63.1 83.0 -85.6 -21.1 33.9 1.7 0.1 20 676 A T H 3> S+ 0 0 76 1,-0.3 4,-3.0 2,-0.2 5,-0.2 0.898 85.3 61.4 -49.7 -35.7 36.7 2.1 2.7 21 677 A K H 34 S+ 0 0 165 -3,-0.3 -1,-0.3 1,-0.2 4,-0.2 0.804 108.7 44.1 -60.9 -23.8 33.9 3.2 5.0 22 678 A W H X4 S+ 0 0 189 -3,-2.9 3,-0.6 -4,-0.2 4,-0.4 0.862 116.1 43.8 -85.2 -44.2 32.5 -0.3 4.4 23 679 A L H >X S+ 0 0 64 -4,-2.3 4,-1.1 1,-0.2 3,-0.8 0.744 96.9 75.1 -76.7 -22.4 35.8 -2.1 4.8 24 680 A W T 3< S+ 0 0 200 -4,-3.0 -1,-0.2 -5,-0.3 -2,-0.1 0.811 94.2 54.4 -61.0 -25.2 36.8 -0.1 7.9 25 681 A Y T <4 S+ 0 0 206 -3,-0.6 -1,-0.3 -4,-0.2 -2,-0.2 0.788 127.9 16.8 -79.0 -25.9 34.3 -2.2 9.8 26 682 A I T <4 0 0 129 -3,-0.8 -2,-0.2 -4,-0.4 -3,-0.1 0.774 360.0 360.0-108.3 -69.1 36.0 -5.5 8.6 27 683 A K < 0 0 219 -4,-1.1 -1,-0.1 -5,-0.1 0, 0.0 -0.369 360.0 360.0 -69.9 360.0 39.5 -4.8 7.3