==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=7-DEC-2009 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER VIRAL PROTEIN 01-APR-98 1MFS . COMPND 2 MOLECULE: HIV-1 NUCLEOCAPSID PROTEIN; . SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS; . AUTHOR M.F.SUMMERS,B.G.TURNER,R.N.DE GUZMAN,B.M.LEE,N.TJANDRA . 55 1 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 5736.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 24 43.6 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 . 2 3.6 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 2 3.6 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 . 2 3.6 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 . 10 18.2 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 5 9.1 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 2 3.6 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 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 . 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 M 0 0 203 0, 0.0 3,-0.1 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 168.1 2.1 0.0 -1.2 2 2 A Q - 0 0 145 1,-0.1 2,-1.1 2,-0.0 3,-0.5 -0.162 360.0 -92.6 -61.3 158.4 1.1 -1.0 -4.8 3 3 A K S S+ 0 0 205 1,-0.2 -1,-0.1 3,-0.0 3,-0.1 -0.657 106.1 59.3 -78.8 101.5 -0.2 -4.5 -5.5 4 4 A G S S+ 0 0 56 -2,-1.1 2,-0.4 1,-0.4 -1,-0.2 -0.090 87.6 58.7 179.1 -63.2 2.9 -6.3 -6.5 5 5 A N + 0 0 70 -3,-0.5 -1,-0.4 1,-0.2 3,-0.1 -0.779 46.6 138.7 -95.1 134.6 5.7 -6.4 -3.8 6 6 A F + 0 0 160 -2,-0.4 2,-1.0 -3,-0.1 -1,-0.2 0.509 65.4 54.7-138.1 -45.1 4.9 -7.8 -0.4 7 7 A R S S- 0 0 164 2,-0.1 2,-2.0 1,-0.1 -1,-0.0 -0.663 118.0 -88.1-100.8 76.1 7.9 -9.9 0.7 8 8 A N - 0 0 148 -2,-1.0 3,-0.1 1,-0.2 -1,-0.1 -0.372 69.4 -87.2 60.4 -84.4 10.7 -7.4 0.4 9 9 A Q S S+ 0 0 111 -2,-2.0 -1,-0.2 1,-0.6 -2,-0.1 -0.075 99.6 72.6-178.2 -64.4 11.4 -8.2 -3.2 10 10 A R S S+ 0 0 177 13,-0.1 -1,-0.6 17,-0.0 13,-0.2 -0.036 72.0 59.4 -65.3 174.4 13.9 -11.0 -3.7 11 11 A K S S+ 0 0 115 11,-0.3 11,-0.2 1,-0.2 -4,-0.1 0.030 87.3 30.9 86.3 162.3 13.0 -14.6 -3.1 12 12 A T S S+ 0 0 70 9,-0.1 10,-0.6 1,-0.0 -1,-0.2 0.071 89.1 69.0 46.9-164.1 10.3 -16.7 -4.7 13 13 A V S S- 0 0 78 8,-0.1 9,-1.7 -3,-0.1 2,-0.3 0.138 82.4-103.6 48.2-174.4 9.3 -15.9 -8.3 14 14 A K B -A 21 0A 90 7,-0.3 2,-0.7 8,-0.2 11,-0.4 -0.995 16.1-118.6-147.9 143.5 11.8 -16.7 -11.0 15 15 A C > - 0 0 0 5,-2.2 4,-1.5 -2,-0.3 5,-0.2 -0.751 18.9-169.8 -86.2 114.7 14.1 -14.6 -13.1 16 16 A F T 4 S+ 0 0 159 -2,-0.7 -1,-0.1 1,-0.2 8,-0.1 0.253 83.9 60.9 -86.2 11.7 13.2 -14.9 -16.8 17 17 A N T 4 S+ 0 0 30 3,-0.1 -1,-0.2 14,-0.0 7,-0.0 0.785 126.7 7.2-102.6 -43.1 16.3 -13.1 -17.7 18 18 A C T 4 S- 0 0 71 2,-0.1 -2,-0.2 -3,-0.0 3,-0.1 0.723 98.1-120.3-107.4 -38.3 18.9 -15.5 -16.3 19 19 A G < + 0 0 45 -4,-1.5 2,-0.6 1,-0.3 -3,-0.2 0.670 61.4 143.1 101.1 25.2 16.6 -18.3 -15.3 20 20 A K > - 0 0 144 -5,-0.2 -5,-2.2 3,-0.0 3,-0.9 -0.881 48.6-130.1-102.4 122.4 17.4 -18.3 -11.6 21 21 A E B 3 S+A 14 0A 177 -2,-0.6 -7,-0.3 -7,-0.2 -8,-0.1 -0.526 86.6 49.1 -72.5 131.3 14.5 -19.0 -9.2 22 22 A G T 3 S+ 0 0 14 -9,-1.7 -11,-0.3 -10,-0.6 2,-0.2 -0.240 104.9 47.7 136.3 -45.0 14.2 -16.4 -6.4 23 23 A H S < S- 0 0 45 -3,-0.9 -1,-0.5 -13,-0.2 2,-0.2 -0.648 74.6-121.2-118.8 176.1 14.4 -13.1 -8.3 24 24 A I > - 0 0 59 -2,-0.2 3,-1.0 -9,-0.2 -9,-0.3 -0.689 29.0-106.9-115.1 169.1 12.7 -11.6 -11.3 25 25 A A G > S+ 0 0 41 -11,-0.4 3,-1.7 1,-0.3 5,-0.1 0.854 123.4 56.4 -62.0 -35.8 14.1 -10.2 -14.6 26 26 A K G 3 S+ 0 0 193 1,-0.3 -1,-0.3 3,-0.0 -11,-0.1 0.698 112.0 43.3 -68.3 -19.3 13.2 -6.8 -13.3 27 27 A N G < S+ 0 0 40 -3,-1.0 2,-0.7 -18,-0.1 -1,-0.3 0.129 84.1 130.1-110.0 15.8 15.4 -7.6 -10.3 28 28 A C < - 0 0 19 -3,-1.7 -3,-0.1 1,-0.2 -12,-0.0 -0.640 42.2-165.9 -76.2 113.4 18.1 -9.1 -12.5 29 29 A R S S+ 0 0 233 -2,-0.7 -1,-0.2 1,-0.2 -4,-0.1 0.416 80.2 68.1 -78.7 1.7 21.4 -7.6 -11.5 30 30 A A S S+ 0 0 61 -5,-0.1 -1,-0.2 2,-0.0 -2,-0.0 -0.777 72.4 179.5-125.8 85.1 22.8 -9.0 -14.7 31 31 A P + 0 0 86 0, 0.0 2,-0.3 0, 0.0 -2,-0.0 -0.071 2.8 170.4 -75.0-179.8 21.2 -7.2 -17.7 32 32 A R - 0 0 133 11,-0.1 11,-0.0 0, 0.0 -2,-0.0 -0.945 49.2 -4.1 179.6 165.2 22.0 -7.8 -21.3 33 33 A K + 0 0 133 -2,-0.3 3,-0.1 1,-0.2 0, 0.0 -0.128 61.6 142.7 40.5-104.3 20.9 -7.0 -24.9 34 34 A K + 0 0 96 1,-0.2 2,-0.5 8,-0.0 9,-0.2 0.834 33.9 162.0 40.7 39.7 17.9 -4.9 -24.1 35 35 A G - 0 0 12 7,-0.2 7,-0.3 1,-0.1 -1,-0.2 -0.791 51.8-100.4 -94.9 129.5 19.0 -2.9 -27.1 36 36 A C > - 0 0 3 5,-2.7 4,-1.4 8,-1.2 9,-0.1 -0.243 31.9-167.2 -48.0 114.4 16.5 -0.6 -28.8 37 37 A W T 4 S+ 0 0 252 1,-0.2 -1,-0.2 2,-0.2 8,-0.1 0.190 84.0 60.0 -91.2 14.7 15.5 -2.6 -31.8 38 38 A K T 4 S+ 0 0 111 3,-0.1 -1,-0.2 16,-0.0 -2,-0.1 0.765 125.7 10.0-106.4 -44.1 13.9 0.5 -33.1 39 39 A C T 4 S- 0 0 54 2,-0.1 -2,-0.2 12,-0.0 3,-0.1 0.605 99.7-120.2-108.2 -23.2 16.8 2.8 -33.3 40 40 A G < + 0 0 47 -4,-1.4 2,-0.7 1,-0.3 -3,-0.1 0.209 59.1 151.8 99.8 -12.3 19.4 0.2 -32.7 41 41 A K - 0 0 137 1,-0.2 2,-2.7 -6,-0.1 -5,-2.7 -0.363 39.1-150.5 -56.1 101.1 20.7 1.9 -29.6 42 42 A E S S+ 0 0 172 -2,-0.7 -7,-0.2 -7,-0.3 -1,-0.2 -0.420 84.9 39.6 -76.4 66.9 21.9 -1.0 -27.6 43 43 A G S S+ 0 0 46 -2,-2.7 -1,-0.2 1,-0.7 2,-0.1 0.065 101.1 59.5-170.3 -60.6 21.2 0.6 -24.3 44 44 A H - 0 0 43 -8,-0.1 -8,-1.2 -3,-0.1 -1,-0.7 -0.384 66.7-144.6 -84.9 166.0 18.0 2.6 -24.2 45 45 A Q > - 0 0 72 -10,-0.1 3,-1.0 -2,-0.1 -9,-0.1 -0.620 33.8 -90.0-122.0-178.7 14.5 1.2 -24.8 46 46 A M G > S+ 0 0 97 1,-0.3 3,-1.4 2,-0.3 5,-0.1 0.868 127.0 56.6 -60.1 -38.9 11.3 2.3 -26.4 47 47 A K G 3 S+ 0 0 203 1,-0.3 -1,-0.3 3,-0.0 -3,-0.0 0.714 120.3 32.0 -65.3 -20.3 10.1 3.7 -23.0 48 48 A D G < S+ 0 0 116 -3,-1.0 2,-0.8 3,-0.0 -1,-0.3 0.102 91.9 120.0-121.1 16.7 13.3 5.7 -23.1 49 49 A C < - 0 0 18 -3,-1.4 -3,-0.1 1,-0.1 0, 0.0 -0.777 40.5-173.3 -89.1 109.2 13.4 6.1 -26.9 50 50 A T + 0 0 128 -2,-0.8 2,-0.3 2,-0.0 -1,-0.1 0.380 59.0 100.2 -81.1 3.8 13.3 9.8 -27.6 51 51 A E + 0 0 66 1,-0.2 -2,-0.1 -5,-0.1 4,-0.1 -0.678 40.8 169.3 -93.2 146.2 13.0 8.8 -31.3 52 52 A R S S+ 0 0 183 -2,-0.3 -1,-0.2 0, 0.0 -3,-0.0 0.713 80.3 5.2-116.8 -60.2 9.6 8.8 -33.1 53 53 A Q S S- 0 0 132 0, 0.0 2,-3.1 0, 0.0 -2,-0.0 -0.456 110.3 -85.5-128.9 58.6 10.3 8.4 -36.8 54 54 A A 0 0 86 1,-0.2 -16,-0.0 -16,-0.0 -15,-0.0 -0.355 360.0 360.0 74.3 -62.2 14.0 7.8 -37.0 55 55 A N 0 0 187 -2,-3.1 -1,-0.2 -4,-0.1 -4,-0.0 0.697 360.0 360.0 -42.5 360.0 14.6 11.6 -37.1