Protein Data Bank File : 1egwb Title : TRANSCRIPTION/DNA 17-FEB-00 1EGW Number of Amino Acid Residues : 72 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLY ARG LYS LYS ILE GLN ILE THR ARG ILE 10 MET ASP GLU ARG ASN ARG GLN VAL THR PHE 20 THR LYS ARG LYS PHE GLY LEU MET LYS LYS 30 ALA TYR GLU LEU SER VAL LEU CYS ASP CYS 40 GLU ILE ALA LEU ILE ILE PHE ASN SER SER 50 ASN LYS LEU PHE GLN TYR ALA SER THR ASP 60 MET ASP LYS VAL LEU LEU LYS TYR THR GLU 70 TYR ASN Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLY 0.0 178.8 -178.2 2 ARG -60.8 -32.8 177.8 -66.6 -49.3 -175.7 95.0 3 LYS -140.7 149.4 178.2 0.0 0.0 0.0 0.0 4 LYS -72.7 145.7 177.9 171.3 177.3 177.1 175.6 5 ILE -119.8 155.4 178.2 63.9 168.9 6 GLN -89.5 151.8 178.6 -64.7 -54.4 -51.1 7 ILE -90.6 90.3 176.7 -57.1 -56.7 8 THR -154.1 161.4 -175.9 -175.8 9 ARG -53.7 127.6 177.8 -174.5 -178.0 -173.2 -78.7 10 ILE -75.3 123.7 -175.8 -66.5 161.5 11 MET -83.2 -21.4 179.6 -55.3 -65.0 -69.9 12 ASP -86.3 123.1 -177.8 175.8 61.5 13 GLU -57.1 -45.3 -177.9 -170.9 -170.5 73.5 14 ARG -64.4 -47.7 177.4 -73.9 -174.2 -172.5 -75.9 15 ASN -67.3 -33.4 -179.3 177.1 42.8 16 ARG -62.7 -40.9 -178.3 -172.0 166.0 62.2 -112.2 17 GLN -71.2 -41.0 177.9 179.1 47.0 50.0 18 VAL -63.2 -46.0 178.8 170.3 19 THR -61.4 -40.0 179.6 -63.3 20 PHE -60.0 -49.5 -177.5 175.9 78.2 21 THR -60.3 -46.9 -178.5 -60.8 22 LYS -66.4 -51.3 -178.6 -66.2 174.0 160.9 -169.1 23 ARG -68.4 -28.9 177.6 -77.6 179.9 170.6 -104.8 24 LYS -67.5 -39.7 178.3 170.2 173.3 65.5 75.0 25 PHE -62.0 -46.5 -177.8 178.5 91.4 26 GLY -62.3 -39.7 -178.4 27 LEU -68.7 -40.3 178.8 178.4 68.6 28 MET -68.4 -34.4 179.1 -73.9 -172.0 170.5 29 LYS -64.3 -45.5 178.4 -173.0 163.1 169.2 -70.6 30 LYS -66.0 -33.5 178.3 -75.0 -173.3 171.8 -59.3 31 ALA -67.8 -45.0 176.2 32 TYR -57.1 -47.3 -178.3 162.2 71.8 33 GLU -63.8 -40.7 179.1 -68.1 -178.8 -16.6 34 LEU -63.4 -41.1 -179.1 -178.1 59.9 35 SER -60.2 -40.0 -177.9 82.1 36 VAL -79.2 -50.8 179.7 176.8 37 LEU -58.0 -42.4 -173.8 -68.2 164.8 38 CYS -108.6 11.3 176.8 -57.0 39 ASP 51.1 60.6 179.5 -164.0 -5.9 40 CYS -131.8 151.3 -179.3 61.6 41 GLU -91.2 127.9 -175.9 -61.1 174.4 176.2 42 ILE -135.1 140.2 173.1 -60.9 178.1 43 ALA -126.5 138.2 178.8 44 LEU -134.9 122.3 -179.2 172.3 62.4 45 ILE -122.1 127.7 -177.7 -72.7 159.4 46 ILE -131.2 127.6 175.2 -57.9 165.7 47 PHE -112.4 125.6 179.6 -73.0 96.4 48 ASN -78.8 -178.4 -178.3 63.4 16.0 49 SER -65.4 -30.5 178.6 63.4 50 SER -81.3 2.4 178.7 -57.9 51 ASN 75.9 17.7 178.8 -138.9 66.7 52 LYS -82.7 146.7 -178.4 -176.6 179.9 179.2 -167.2 53 LEU -93.6 134.1 175.6 169.3 71.4 54 PHE -132.1 144.2 -177.2 -60.3 86.9 55 GLN -151.1 158.9 177.3 58.7 -174.2 -68.2 56 TYR -145.5 138.2 174.2 160.6 75.1 57 ALA -146.6 142.8 -178.0 58 SER -76.4 -11.9 178.7 54.8 59 THR -145.7 -160.0 178.5 72.0 60 ASP -68.3 131.6 179.8 0.0 0.0 61 MET -55.9 -49.3 -178.6 176.3 68.3 78.7 62 ASP -55.6 -32.8 179.4 0.0 0.0 63 LYS -66.9 -49.8 -179.8 0.0 0.0 0.0 0.0 64 VAL -59.0 -42.1 179.9 -174.3 65 LEU -66.3 -33.0 178.5 -63.1 177.3 66 LEU -63.2 -46.6 178.5 0.0 0.0 67 LYS -59.1 -42.2 -179.1 -101.9 -152.1 -177.0 -163.5 68 TYR -58.9 -61.3 -178.6 -177.3 69.5 69 THR -54.7 -43.0 180.0 41.4 70 GLU -66.3 -46.1 179.6 0.0 0.0 0.0 71 TYR -51.0 -40.1 -178.3 -175.8 102.2 72 ASN -75.5 -107.8 0.0 -66.6 -60.9 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLY -8.123 -4.962 8.110 2 ARG -10.546 -6.720 10.475 3 LYS -12.983 -7.141 7.593 4 LYS -12.578 -6.670 3.865 5 ILE -14.229 -3.527 2.578 6 GLN -15.715 -2.635 -0.736 7 ILE -14.297 0.359 -2.495 8 THR -17.180 2.800 -2.516 9 ARG -17.844 6.044 -0.695 10 ILE -17.912 5.817 3.093 11 MET -21.210 7.562 4.003 12 ASP -20.424 8.388 7.684 13 GLU -18.338 11.553 8.118 14 ARG -16.367 10.350 11.125 15 ASN -15.274 7.003 9.653 16 ARG -14.681 8.741 6.323 17 GLN -12.329 11.211 8.026 18 VAL -10.464 8.606 10.053 19 THR -9.978 6.557 6.868 20 PHE -8.852 9.616 4.952 21 THR -6.190 10.494 7.508 22 LYS -4.816 6.943 7.682 23 ARG -4.896 6.211 3.937 24 LYS -3.525 9.640 2.949 25 PHE -0.541 8.941 5.197 26 GLY -0.158 5.502 3.574 27 LEU -0.436 6.876 0.087 28 MET 2.203 9.616 0.700 29 LYS 4.494 6.979 2.271 30 LYS 4.263 4.823 -0.863 31 ALA 4.827 7.853 -3.123 32 TYR 7.881 8.812 -1.141 33 GLU 9.232 5.236 -1.318 34 LEU 8.666 4.966 -5.051 35 SER 10.491 8.262 -5.569 36 VAL 13.530 7.017 -3.647 37 LEU 13.693 3.380 -4.707 38 CYS 13.204 4.131 -8.378 39 ASP 14.712 7.590 -8.687 40 CYS 11.580 9.249 -9.971 41 GLU 9.994 12.681 -9.634 42 ILE 6.514 12.641 -8.190 43 ALA 3.817 15.081 -7.388 44 LEU 0.645 14.219 -5.478 45 ILE -2.213 16.673 -4.941 46 ILE -5.227 15.752 -2.827 47 PHE -8.377 17.742 -2.057 48 ASN -10.561 16.183 0.630 49 SER -14.376 16.285 0.599 50 SER -14.384 19.433 2.736 51 ASN -12.130 20.754 -0.043 52 LYS -8.878 21.197 1.913 53 LEU -5.564 20.763 0.063 54 PHE -2.876 18.225 0.964 55 GLN 0.198 17.641 -1.129 56 TYR 3.460 15.753 -1.504 57 ALA 6.262 16.284 -3.997 58 SER 9.662 14.602 -4.190 59 THR 11.128 17.992 -5.107 60 ASP 9.609 21.478 -5.317 61 MET 5.979 21.066 -6.446 62 ASP 6.093 24.002 -8.836 63 LYS 9.071 22.370 -10.568 64 VAL 7.299 19.059 -11.154 65 LEU 4.216 20.849 -12.465 66 LEU 6.501 22.916 -14.723 67 LYS 7.877 19.645 -16.106 68 TYR 4.326 18.396 -16.545 69 THR 3.013 21.375 -18.488 70 GLU 6.139 21.591 -20.665 71 TYR 6.166 17.850 -21.367 72 ASN 2.625 18.295 -22.681 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C S S S S S S S S S 10 S S/H H H H H H H H H 20 H H H H H H H H H H 30 H H H H H H H H H/S S 40 S S S S S S S S/T T T 50 T/S S S S S S S S C H 60 H H H H H H H H H H 70 H H Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S 10 h H H H H H H H H 20 H H H H H H H H H H 30 H H H H H H H h T t 40 e E E E E E e T T 50 t e E E E E E e S h 60 H H H H H H H H H H 70 H h Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLY 0.0 0.0 94.6 2 ARG 0.0 0.0 92.3 3 LYS 108.9 62.8 85.3 4 LYS 15.9 9.2 90.7 5 ILE 56.3 39.2 77.5 6 GLN 26.8 18.0 75.1 7 ILE 24.3 16.9 83.2 8 THR 15.5 14.5 81.0 9 ARG 79.3 38.0 74.8 10 ILE 100.8 70.3 63.6 11 MET 28.8 18.1 86.4 12 ASP 29.1 26.4 74.3 13 GLU 25.3 18.3 82.3 14 ARG 13.9 6.7 89.3 15 ASN 44.7 37.0 68.6 16 ARG 156.9 75.1 66.3 17 GLN 59.9 40.3 74.4 18 VAL 37.8 31.9 73.1 19 THR 77.9 72.9 56.5 20 PHE 125.1 75.0 51.0 21 THR 35.7 33.4 76.4 22 LYS 34.3 19.8 75.3 23 ARG 65.1 31.2 70.0 24 LYS 134.1 77.3 39.8 25 PHE 31.9 19.1 75.6 26 GLY 7.2 20.5 67.2 27 LEU 58.0 39.3 64.7 28 MET 120.4 75.5 54.8 29 LYS 63.9 36.8 71.7 30 LYS 24.7 14.2 86.3 31 ALA 59.5 82.0 46.0 32 TYR 62.7 34.6 67.4 33 GLU 80.7 58.2 59.6 34 LEU 56.4 38.2 61.8 35 SER 77.6 92.8 55.6 36 VAL 39.4 33.1 77.0 37 LEU 31.0 21.0 74.0 38 CYS 36.3 36.6 66.5 39 ASP 0.0 0.0 91.3 40 CYS 60.1 60.6 59.9 41 GLU 73.8 53.2 62.5 42 ILE 112.6 78.5 48.8 43 ALA 64.1 88.3 39.4 44 LEU 112.7 76.3 43.7 45 ILE 87.2 60.8 46.1 46 ILE 114.9 80.1 40.8 47 PHE 73.5 44.1 69.2 48 ASN 99.6 82.4 50.9 49 SER 26.1 31.2 85.5 50 SER 8.6 10.3 87.2 51 ASN 18.7 15.5 82.5 52 LYS 42.6 24.6 78.6 53 LEU 87.3 59.0 58.4 54 PHE 126.8 76.0 54.0 55 GLN 74.9 50.4 53.7 56 TYR 144.5 79.8 46.6 57 ALA 67.9 93.5 50.3 58 SER 71.0 84.9 60.8 59 THR 46.3 43.3 70.0 60 ASP 48.3 43.7 78.7 61 MET 133.5 83.7 49.5 62 ASP 39.9 36.1 74.4 63 LYS 124.8 72.0 71.8 64 VAL 99.5 83.8 61.0 65 LEU 76.1 51.5 55.0 66 LEU 92.9 62.8 82.5 67 LYS 46.0 26.5 83.3 68 TYR 41.8 23.1 77.7 69 THR 24.4 22.8 76.0 70 GLU 73.8 53.3 85.9 71 TYR 8.4 4.6 89.0 72 ASN 59.5 49.2 60.7