==== 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 VIRAL PROTEIN 08-JAN-00 1DSV . COMPND 2 MOLECULE: NUCLEIC ACID BINDING PROTEIN P14; . SOURCE 2 ORGANISM_SCIENTIFIC: MOUSE MAMMARY TUMOR VIRUS; . AUTHOR D.J.KLEIN,P.E.JOHNSON,E.S.ZOLLARS,R.N.DE GUZMAN,M.F.SUMMERS . 31 1 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 2993.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 15 48.4 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 . 5 16.1 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 . 1 3.2 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 12.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 3 9.7 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 3 9.7 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 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 ANTIPARALLEL 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 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 54 A P 0 0 152 0, 0.0 2,-1.5 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 159.7 2.1 0.0 -1.2 2 55 A P + 0 0 133 0, 0.0 2,-0.1 0, 0.0 11,-0.0 -0.573 360.0 133.5 -75.0 90.6 2.4 -2.6 -4.0 3 56 A G - 0 0 32 -2,-1.5 10,-2.0 11,-0.0 2,-0.8 -0.585 37.1-165.1-142.1 74.9 4.6 -5.2 -2.3 4 57 A L B -A 12 0A 77 8,-0.3 8,-0.3 -2,-0.1 10,-0.0 -0.494 37.3-112.7 -65.2 105.7 3.3 -8.7 -2.7 5 58 A C > - 0 0 0 6,-1.8 4,-1.6 -2,-0.8 6,-0.3 -0.180 30.4-165.5 -43.6 102.5 5.3 -10.6 -0.1 6 59 A P T 4 S+ 0 0 84 0, 0.0 -1,-0.2 0, 0.0 -2,-0.1 0.427 80.9 63.3 -74.9 1.6 7.3 -12.7 -2.5 7 60 A R T 4 S+ 0 0 137 16,-0.1 17,-2.0 17,-0.0 -2,-0.1 0.942 123.7 6.9 -87.1 -68.8 8.1 -14.8 0.5 8 61 A C T 4 S- 0 0 5 15,-0.3 18,-0.1 3,-0.1 17,-0.1 0.816 85.0-152.2 -83.7 -34.9 4.9 -16.3 1.7 9 62 A K < + 0 0 132 -4,-1.6 3,-0.1 2,-0.3 -5,-0.1 0.909 66.9 106.1 61.7 43.7 3.0 -14.9 -1.3 10 63 A K S S- 0 0 162 1,-0.4 2,-0.3 -5,-0.2 -1,-0.1 0.183 85.2 -1.3-133.3 9.6 -0.2 -14.8 0.8 11 64 A G S S- 0 0 20 -6,-0.3 -6,-1.8 2,-0.1 2,-0.6 -0.941 80.0 -83.4 175.2 168.1 -0.3 -11.0 1.2 12 65 A Y B S+A 4 0A 154 -8,-0.3 -8,-0.3 -2,-0.3 2,-0.3 -0.833 71.6 99.8 -96.7 118.8 1.4 -7.7 0.6 13 66 A H S S- 0 0 30 -10,-2.0 2,-0.2 -2,-0.6 5,-0.1 -0.947 70.8 -76.1 178.9 167.6 4.1 -6.8 3.0 14 67 A W > - 0 0 173 -2,-0.3 4,-1.0 1,-0.1 3,-0.3 -0.489 41.3-117.7 -79.6 151.0 7.9 -6.7 3.5 15 68 A K T >4 S+ 0 0 138 1,-0.3 3,-1.1 2,-0.3 -1,-0.1 0.927 121.2 44.2 -51.7 -50.6 9.7 -9.9 4.3 16 69 A S T 34 S+ 0 0 112 1,-0.3 -1,-0.3 3,-0.0 -2,-0.0 0.744 114.9 50.5 -66.3 -23.7 10.7 -8.5 7.7 17 70 A E T 34 S+ 0 0 131 -3,-0.3 2,-0.3 2,-0.0 -1,-0.3 0.512 80.5 123.9 -90.0 -7.9 7.1 -7.2 8.0 18 71 A C << + 0 0 18 -3,-1.1 -3,-0.1 -4,-1.0 -5,-0.0 -0.394 33.9 177.0 -58.1 115.0 5.8 -10.7 7.1 19 72 A K + 0 0 181 -2,-0.3 -1,-0.2 3,-0.0 -4,-0.1 0.226 40.0 121.5-104.4 10.0 3.6 -11.5 10.1 20 73 A S - 0 0 38 1,-0.1 3,-0.1 -9,-0.0 -9,-0.0 -0.242 64.6-135.3 -70.5 162.3 2.6 -14.8 8.5 21 74 A K S S+ 0 0 177 1,-0.2 8,-1.7 7,-0.1 2,-0.3 0.878 85.2 15.6 -84.7 -44.2 3.2 -18.1 10.2 22 75 A F E -B 28 0B 110 6,-0.3 2,-0.2 7,-0.0 -1,-0.2 -0.838 66.1-161.5-128.5 165.6 4.5 -19.9 7.1 23 76 A D E >> -B 27 0B 15 4,-2.5 4,-1.4 1,-0.4 3,-1.2 -0.719 48.6 -33.3-134.5-176.5 5.9 -19.0 3.7 24 77 A K G >4 S+ 0 0 152 -17,-2.0 3,-1.7 1,-0.3 -1,-0.4 0.074 130.3 25.7 -37.2 151.6 6.5 -20.6 0.3 25 78 A D G 34 S- 0 0 124 1,-0.3 -1,-0.3 -17,-0.1 -17,-0.1 0.628 131.1 -82.7 61.6 11.9 7.5 -24.2 0.5 26 79 A G G <4 S+ 0 0 49 -3,-1.2 -1,-0.3 1,-0.2 -2,-0.2 0.886 79.1 171.4 59.2 41.8 5.6 -24.1 3.8 27 80 A N E << -B 23 0B 64 -3,-1.7 -4,-2.5 -4,-1.4 2,-0.9 -0.551 42.8-101.8 -84.2 149.5 8.6 -22.7 5.5 28 81 A P E -B 22 0B 86 0, 0.0 -6,-0.3 0, 0.0 -1,-0.1 -0.611 42.2-112.3 -75.0 104.5 8.4 -21.4 9.1 29 82 A L - 0 0 34 -8,-1.7 -7,-0.0 -2,-0.9 -21,-0.0 -0.104 42.2-147.3 -39.2 99.7 8.2 -17.6 8.8 30 83 A P 0 0 93 0, 0.0 -1,-0.1 0, 0.0 -3,-0.0 -0.344 360.0 360.0 -75.0 157.5 11.6 -16.8 10.3 31 84 A P 0 0 180 0, 0.0 -2,-0.1 0, 0.0 -15,-0.0 0.388 360.0 360.0 -75.0 360.0 12.3 -13.7 12.3