Protein Data Bank File : 1cjga Title : TRANSCRIPTION/DNA 14-APR-99 1CJG Number of Amino Acid Residues : 62 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 MET LYS PRO VAL THR LEU TYR ASP VAL ALA 10 GLU TYR ALA GLY VAL SER TYR GLN THR VAL 20 SER ARG VAL VAL ASN GLN ALA SER HIS VAL 30 SER ALA LYS THR ARG GLU LYS VAL GLU ALA 40 ALA MET ALA GLU LEU ASN TYR ILE PRO ASN 50 ARG VAL ALA GLN GLN LEU ALA GLY LYS GLN 60 SER LEU Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 MET 0.0 -95.5 175.7 -61.3 174.1 -178.4 2 LYS -101.0 103.5 156.5 176.7 57.2 -178.9 171.0 3 PRO -58.6 152.5 -178.6 34.6 -37.1 4 VAL -128.9 166.5 -179.1 -175.2 5 THR -123.4 158.9 168.2 71.5 6 LEU -48.8 -32.7 177.5 76.5 -177.0 7 TYR -71.6 -40.7 -179.1 -62.6 -66.9 8 ASP -65.0 -42.9 173.6 -147.3 -74.5 9 VAL -63.4 -44.7 176.3 -166.6 10 ALA -60.1 -49.4 175.8 11 GLU -59.5 -42.4 175.7 -173.3 170.7 -60.8 12 TYR -64.8 -52.1 -177.4 -174.3 -86.4 13 ALA -72.6 -17.2 177.1 14 GLY 84.2 34.9 -174.7 15 VAL -125.0 -170.0 175.8 -59.9 16 SER -93.9 163.0 178.1 179.7 17 TYR -72.7 -24.9 172.6 51.8 -85.3 18 GLN -78.2 -24.8 172.7 -59.3 -169.8 -73.1 19 THR -65.6 -43.5 172.9 -53.4 20 VAL -59.2 -59.2 -177.5 173.7 21 SER -59.3 -21.4 168.8 66.5 22 ARG -59.4 -38.1 -174.6 176.3 -92.8 170.9 -91.1 23 VAL -81.9 -44.8 179.6 -172.2 24 VAL -65.0 -62.1 -174.7 -173.7 25 ASN -104.6 21.2 169.0 -54.5 -57.3 26 GLN 60.0 58.8 174.5 -53.5 172.8 39.4 27 ALA -90.4 -171.4 -173.4 28 SER -108.3 -64.9 -164.1 -56.6 29 HIS -84.7 74.9 170.6 -51.6 -41.7 30 VAL -126.3 -100.2 -179.0 177.9 31 SER 178.6 170.5 174.3 60.5 32 ALA -86.8 -27.0 179.6 33 LYS -58.5 -58.7 -178.8 -35.2 169.0 70.8 -77.9 34 THR -72.5 -29.3 177.4 -49.2 35 ARG -43.7 -54.5 177.2 -164.2 -174.6 80.3 68.1 36 GLU -65.2 -17.6 178.3 -59.4 179.5 3.7 37 LYS -81.6 -36.4 171.8 -62.3 -159.1 -65.7 -174.8 38 VAL -65.3 -41.0 -179.9 -171.0 39 GLU -57.2 -30.0 173.7 -64.9 -167.7 -55.1 40 ALA -69.9 -34.5 178.5 41 ALA -70.7 -42.8 168.7 42 MET -50.8 -35.1 -173.1 -57.6 -176.6 -159.9 43 ALA -77.6 -29.9 -179.1 44 GLU -78.8 -65.9 -173.7 -64.4 -68.5 -18.8 45 LEU -74.3 -21.6 -179.6 -35.7 143.6 46 ASN 74.0 71.2 179.4 -157.1 114.2 47 TYR -64.2 111.0 168.1 -172.5 33.0 48 ILE -108.8 106.5 156.7 -59.3 103.9 49 PRO -67.0 162.3 176.0 33.7 -25.9 50 ASN -90.6 125.1 176.6 -101.3 -73.3 51 ARG -70.1 -23.2 -179.5 -59.8 -147.7 -61.3 -163.8 52 VAL -72.2 -43.7 172.8 -164.3 53 ALA -60.3 -45.6 176.3 54 GLN -63.6 -26.2 176.9 -142.6 -72.6 -54.7 55 GLN -88.6 -46.9 -177.8 -79.6 174.8 89.0 56 LEU -63.6 -45.9 177.8 -152.4 57.7 57 ALA -82.6 -20.6 -175.7 58 GLY -64.5 45.2 177.2 59 LYS 53.9 138.9 177.2 -165.6 172.8 63.9 178.0 60 GLN -69.7 158.5 -177.0 -64.9 -171.0 -14.9 61 SER -83.4 136.5 -176.1 -170.0 62 LEU -94.2 121.1 0.0 -170.6 71.8 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 MET 50.551 14.049 16.870 2 LYS 51.708 14.220 20.479 3 PRO 52.546 17.707 21.616 4 VAL 55.134 18.181 24.346 5 THR 55.701 21.279 26.460 6 LEU 58.568 23.558 27.404 7 TYR 58.085 22.226 30.911 8 ASP 58.431 18.597 29.839 9 VAL 61.720 19.393 28.117 10 ALA 62.841 21.439 31.088 11 GLU 61.987 18.711 33.590 12 TYR 63.819 16.116 31.512 13 ALA 66.974 18.126 30.951 14 GLY 66.846 19.268 34.571 15 VAL 66.594 22.958 33.788 16 SER 64.153 25.849 33.812 17 TYR 61.534 26.525 31.147 18 GLN 63.259 29.784 30.330 19 THR 66.439 27.781 29.925 20 VAL 64.559 25.772 27.342 21 SER 63.022 28.656 25.422 22 ARG 66.433 30.217 24.946 23 VAL 67.466 27.244 22.860 24 VAL 64.146 26.766 21.125 25 ASN 63.061 30.329 20.439 26 GLN 66.473 31.988 20.383 27 ALA 66.886 34.036 23.527 28 SER 70.067 35.433 25.014 29 HIS 70.921 35.065 28.655 30 VAL 71.684 31.449 29.427 31 SER 75.036 29.919 28.416 32 ALA 76.526 27.626 25.792 33 LYS 77.069 24.955 28.435 34 THR 73.457 24.397 29.336 35 ARG 72.268 24.974 25.767 36 GLU 73.301 21.525 24.576 37 LYS 71.634 19.851 27.538 38 VAL 68.333 21.284 26.474 39 GLU 69.033 20.161 22.928 40 ALA 69.168 16.627 24.261 41 ALA 65.732 16.960 25.834 42 MET 64.054 18.063 22.622 43 ALA 65.515 15.007 20.965 44 GLU 64.116 12.401 23.330 45 LEU 60.546 13.382 24.019 46 ASN 60.254 15.076 20.635 47 TYR 59.356 18.649 21.516 48 ILE 56.648 20.102 19.347 49 PRO 55.717 23.416 20.815 50 ASN 52.348 25.020 20.194 51 ARG 52.322 27.823 17.651 52 VAL 49.124 29.042 19.290 53 ALA 50.784 29.536 22.668 54 GLN 53.658 31.245 20.929 55 GLN 51.219 33.597 19.249 56 LEU 48.856 34.386 22.117 57 ALA 51.569 35.017 24.658 58 GLY 54.029 36.351 22.079 59 LYS 53.554 39.939 23.219 60 GLN 51.107 42.573 22.054 61 SER 51.974 44.939 19.234 62 LEU 53.343 48.343 20.165 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S/H H H H H H 10 H H H H C H H H H H 20 H H H H H/S S S S S C 30 H H H H H 3 3 3/H H H 40 H H H H 3/S S S S C H 50 H H H H H H H H/S S S 60 S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 h H H H H H 10 H H H h t h H H H H 20 H H H H h T t S S S 30 h H H H H H H H H H 40 H H H H H h t h 50 H H H H H H h S 60 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 MET 0.0 0.0 93.9 2 LYS 16.4 9.4 80.8 3 PRO 61.4 49.3 75.0 4 VAL 105.9 89.2 51.9 5 THR 39.3 36.8 60.6 6 LEU 91.2 61.7 50.0 7 TYR 56.8 31.4 65.5 8 ASP 44.3 40.1 64.5 9 VAL 118.8 100.0 32.2 10 ALA 67.6 93.1 56.8 11 GLU 3.8 2.7 87.9 12 TYR 85.1 47.0 65.7 13 ALA 65.2 89.9 54.1 14 GLY 4.1 11.9 80.0 15 VAL 102.6 86.4 49.7 16 SER 33.0 39.4 65.9 17 TYR 82.4 45.5 61.4 18 GLN 21.1 14.2 83.5 19 THR 87.8 82.2 41.1 20 VAL 118.6 99.9 35.6 21 SER 50.2 60.1 64.5 22 ARG 150.8 72.2 59.8 23 VAL 115.3 97.0 50.8 24 VAL 100.9 84.9 49.7 25 ASN 63.4 52.5 63.3 26 GLN 14.2 9.6 92.2 27 ALA 23.6 32.4 77.8 28 SER 20.3 24.3 74.1 29 HIS 0.0 0.0 85.0 30 VAL 92.9 78.2 63.6 31 SER 46.9 56.1 66.8 32 ALA 6.0 8.3 76.5 33 LYS 10.7 6.2 86.8 34 THR 76.6 71.6 47.6 35 ARG 138.9 66.5 66.1 36 GLU 39.2 28.3 84.5 37 LYS 53.4 30.8 77.0 38 VAL 118.8 100.0 34.4 39 GLU 76.4 55.1 66.1 40 ALA 20.4 28.1 76.7 41 ALA 72.6 100.0 44.1 42 MET 118.2 74.2 49.7 43 ALA 17.6 24.2 80.6 44 GLU 53.8 38.8 74.3 45 LEU 99.5 67.3 57.6 46 ASN 28.4 23.5 77.6 47 TYR 169.2 93.5 35.9 48 ILE 65.9 45.9 75.1 49 PRO 73.9 59.4 67.4 50 ASN 48.1 39.8 66.0 51 ARG 10.4 5.0 86.9 52 VAL 15.3 12.9 81.7 53 ALA 15.3 21.1 73.5 54 GLN 49.4 33.2 76.2 55 GLN 33.5 22.5 81.1 56 LEU 8.6 5.8 87.1 57 ALA 6.0 8.2 87.4 58 GLY 16.4 47.1 79.7 59 LYS 3.2 1.8 92.2 60 GLN 0.0 0.0 89.8 61 SER 0.0 0.0 88.5 62 LEU 0.0 0.0 95.6