Protein Data Bank File : 1g9oa Title : SIGNALING PROTEIN 26-NOV-00 1G9O Number of Amino Acid Residues : 91 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ARG MET LEU PRO ARG LEU CYS CYS LEU GLU 10 LYS GLY PRO ASN GLY TYR GLY PHE HIS LEU 20 HIS GLY GLU LYS GLY LYS LEU GLY GLN TYR 30 ILE ARG LEU VAL GLU PRO GLY SER PRO ALA 40 GLU LYS ALA GLY LEU LEU ALA GLY ASP ARG 50 LEU VAL GLU VAL ASN GLY GLU ASN VAL GLU 60 LYS GLU THR HIS GLN GLN VAL VAL SER ARG 70 ILE ARG ALA ALA LEU ASN ALA VAL ARG LEU 80 LEU VAL VAL ASP PRO GLU THR ASP GLU GLN 90 LEU Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ARG 0.0 -133.3 179.4 0.0 0.0 0.0 0.0 2 MET -131.0 156.2 -178.1 -66.1 -174.2 78.9 3 LEU -67.2 152.4 178.2 -58.0 169.9 4 PRO -64.8 154.2 -175.6 -30.9 41.7 5 ARG -130.3 139.8 179.3 -179.5 166.7 67.7 81.3 6 LEU -96.6 127.8 178.4 -168.5 64.3 7 CYS -116.1 123.2 -178.8 -67.7 8 CYS -108.8 107.3 -177.3 -59.5 9 LEU -97.9 138.2 176.9 -68.1 64.4 10 GLU -103.8 119.5 -177.5 -179.0 -172.5 -27.5 11 LYS -59.2 136.2 -177.6 -161.3 177.9 -179.0 -177.0 12 GLY -106.4 -173.6 -179.3 13 PRO -49.5 -34.6 179.8 25.4 -40.3 14 ASN -118.1 14.0 179.8 -67.9 164.3 15 GLY 116.8 -156.1 179.5 16 TYR -88.5 -27.2 175.9 -68.7 -63.9 17 GLY 80.4 34.0 174.8 18 PHE -138.6 171.6 -177.6 65.4 -80.2 19 HIS -131.8 143.6 -179.6 -57.1 -84.1 20 LEU -117.3 151.8 175.3 -67.4 173.7 21 HIS -162.9 164.9 179.2 70.8 161.3 22 GLY -85.3 179.1 178.6 23 GLU -130.3 152.0 -179.2 -82.5 -160.9 -2.6 24 LYS -59.5 124.2 179.8 179.6 170.1 -63.7 -57.9 25 GLY 79.6 1.2 -178.7 26 LYS -117.1 158.0 -178.8 -56.9 173.4 180.0 -55.2 27 LEU -86.2 -37.1 -176.5 -65.3 -177.6 28 GLY -90.7 -169.6 -179.4 29 GLN -102.6 142.9 -178.8 -68.5 -66.5 -62.0 30 TYR -128.1 155.9 179.3 -61.9 68.4 31 ILE -78.7 115.4 -179.7 -59.0 -169.0 32 ARG -78.0 -37.2 -177.4 -178.6 -172.4 -177.3 -179.4 33 LEU -163.9 140.8 176.3 171.0 70.1 34 VAL -110.2 124.6 -179.2 172.5 35 GLU -76.7 133.1 179.5 -54.5 -150.1 -21.6 36 PRO -56.3 138.5 179.5 -32.8 42.5 37 GLY 78.2 -1.3 -177.3 38 SER -77.7 163.7 178.2 68.3 39 PRO -60.7 -31.8 178.5 -35.9 42.5 40 ALA -62.1 -44.5 178.9 41 GLU -65.3 -42.9 -179.3 -178.8 -177.6 -82.4 42 LYS -61.9 -28.6 179.9 -61.1 -55.9 177.0 -177.7 43 ALA -89.6 0.0 178.2 44 GLY 87.8 15.4 178.8 45 LEU -71.9 147.2 179.0 -74.4 179.0 46 LEU -129.7 148.1 176.3 -60.9 175.7 47 ALA -61.3 140.7 -179.0 48 GLY 96.0 -14.5 178.7 49 ASP -60.6 139.3 177.3 -81.8 -12.6 50 ARG -98.0 130.7 179.5 178.0 170.9 75.0 79.5 51 LEU -85.6 122.2 179.0 -95.0 63.5 52 VAL -100.5 -46.1 178.6 -175.0 53 GLU -138.2 150.5 174.6 -65.0 -179.6 -2.2 54 VAL -126.2 118.0 -177.9 173.0 55 ASN 48.6 46.4 176.5 -75.9 157.4 56 GLY 79.2 -0.1 -179.8 57 GLU -104.2 131.3 -179.7 -61.5 -62.1 -68.4 58 ASN -68.2 128.8 -178.8 -171.1 103.7 59 VAL -121.7 16.2 -178.4 -66.4 60 GLU -60.3 -26.3 -179.3 -67.3 179.6 -65.4 61 LYS -115.3 6.4 -179.4 -59.4 -167.6 -67.7 -173.9 62 GLU -83.8 161.3 -179.9 -66.4 -163.0 -24.6 63 THR -79.2 164.3 177.5 67.5 64 HIS -52.2 -50.3 -178.7 176.3 77.2 65 GLN -61.5 -39.4 -179.4 -173.5 60.0 -99.0 66 GLN -63.3 -42.9 -179.0 -70.8 170.9 -26.1 67 VAL -69.2 -44.6 179.2 -180.0 68 VAL -58.0 -43.6 179.7 166.5 69 SER -64.5 -33.7 178.7 -69.3 70 ARG -64.7 -33.3 -179.5 -71.9 -179.8 -179.5 -78.1 71 ILE -79.9 -44.9 -178.8 -67.1 157.5 72 ARG -62.3 -34.6 179.5 -175.9 166.3 -78.2 137.7 73 ALA -78.8 -3.7 177.1 74 ALA -91.6 96.1 -174.2 75 LEU -75.8 -17.6 -177.4 -52.2 -170.2 76 ASN -121.5 -40.5 -179.1 -63.4 107.7 77 ALA -153.7 151.3 177.7 78 VAL -140.6 136.1 -180.0 67.8 79 ARG -103.5 120.0 -179.5 -54.7 -175.0 -49.8 -76.6 80 LEU -115.2 119.9 176.7 -55.1 173.0 81 LEU -93.8 120.7 -176.6 -175.8 71.7 82 VAL -128.9 162.5 174.6 -55.7 83 VAL -119.1 122.1 -178.2 175.0 84 ASP -70.0 151.6 179.9 -68.6 -56.3 85 PRO -66.9 144.8 177.5 29.9 -41.4 86 GLU -134.6 160.0 179.8 -61.4 -58.5 -13.7 87 THR -175.1 154.5 176.9 -178.3 88 ASP -109.1 8.6 -179.9 -81.9 -33.3 89 GLU -92.5 109.4 179.0 -163.6 163.7 68.7 90 GLN -108.3 115.5 179.3 179.0 -169.9 45.6 91 LEU -109.8 152.5 0.0 -75.8 178.3 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ARG 4.809 36.535 13.041 2 MET 5.602 33.177 14.550 3 LEU 7.646 31.859 17.439 4 PRO 11.176 30.484 17.093 5 ARG 11.117 26.680 16.818 6 LEU 13.543 24.020 18.058 7 CYS 14.624 21.282 15.634 8 CYS 16.565 18.363 17.108 9 LEU 18.600 16.485 14.505 10 GLU 20.222 13.053 14.889 11 LYS 23.283 12.816 12.629 12 GLY 22.867 10.255 9.867 13 PRO 24.989 8.102 7.510 14 ASN 26.073 11.084 5.422 15 GLY 25.637 13.881 7.945 16 TYR 22.753 16.210 8.776 17 GLY 21.803 16.915 5.193 18 PHE 21.214 20.629 4.902 19 HIS 22.987 23.680 3.500 20 LEU 23.589 27.178 4.845 21 HIS 24.145 30.572 3.291 22 GLY 23.652 34.208 4.153 23 GLU 20.854 36.375 2.802 24 LYS 20.797 39.697 0.991 25 GLY 20.658 42.575 3.459 26 LYS 20.890 40.263 6.474 27 LEU 23.520 39.359 9.084 28 GLY 22.858 35.689 9.791 29 GLN 22.721 32.273 8.198 30 TYR 19.676 30.717 6.526 31 ILE 18.856 27.239 5.280 32 ARG 19.477 27.179 1.543 33 LEU 18.238 23.625 0.946 34 VAL 17.164 20.591 2.969 35 GLU 18.115 17.275 1.365 36 PRO 15.259 14.775 0.992 37 GLY 15.395 11.921 3.505 38 SER 17.924 13.725 5.688 39 PRO 18.032 14.075 9.460 40 ALA 17.275 17.755 8.770 41 GLU 14.055 16.813 6.988 42 LYS 13.118 14.328 9.750 43 ALA 13.567 17.070 12.356 44 GLY 11.338 19.497 10.459 45 LEU 13.885 21.928 9.059 46 LEU 12.735 23.968 6.042 47 ALA 14.490 25.926 3.298 48 GLY 14.350 29.612 4.191 49 ASP 14.645 28.997 7.953 50 ARG 16.752 31.590 9.779 51 LEU 19.191 30.138 12.322 52 VAL 18.993 31.812 15.739 53 GLU 20.867 29.270 17.909 54 VAL 23.007 26.171 17.452 55 ASN 23.155 23.956 20.562 56 GLY 21.955 26.859 22.683 57 GLU 24.461 29.426 21.426 58 ASN 23.241 32.510 19.572 59 VAL 24.526 32.594 15.991 60 GLU 22.601 35.587 14.659 61 LYS 25.766 37.616 14.169 62 GLU 28.271 34.879 13.410 63 THR 29.924 34.169 10.080 64 HIS 29.105 31.316 7.738 65 GLN 32.242 29.438 8.813 66 GLN 31.565 29.921 12.504 67 VAL 28.040 28.553 12.214 68 VAL 29.109 25.667 9.980 69 SER 31.838 24.681 12.438 70 ARG 29.398 24.609 15.356 71 ILE 27.329 22.099 13.376 72 ARG 30.178 20.017 11.973 73 ALA 31.655 19.592 15.457 74 ALA 28.321 18.248 16.799 75 LEU 29.119 14.607 16.052 76 ASN 25.892 12.989 17.199 77 ALA 23.078 15.507 17.459 78 VAL 22.470 19.189 16.941 79 ARG 19.707 21.449 18.250 80 LEU 18.778 24.281 15.907 81 LEU 16.518 27.113 17.047 82 VAL 15.060 28.603 13.866 83 VAL 12.538 31.138 12.665 84 ASP 10.494 29.873 9.737 85 PRO 10.153 31.880 6.544 86 GLU 7.123 34.095 6.188 87 THR 5.900 36.156 3.251 88 ASP 2.753 37.740 1.853 89 GLU 3.870 36.942 -1.679 90 GLN 1.834 34.056 -3.141 91 LEU 2.965 32.859 -6.610 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S S S S S S 10 S T T T T S S S S/S S 20 S S S/T T T T S S S S 30 S S S S S S S H H H 40 H H H H/S S S S S/S S S 50 S S T T T T/S S S S S 60 C C H H H H H H H H 70 H H H H/T T T T/S S S S 80 S S S/S S S S S S/S S S 90 S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 E E E E E E 10 e B T T B e E E E 20 E E e T T t S e E E 30 E E E E e T T h H H 40 H H h T t t T T t E 50 E E E E e T E E e T 60 T t h H H H H H H H 70 H H h t S e E E E E 80 E E E S 90 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ARG 172.9 82.8 81.6 2 MET 32.7 20.5 87.0 3 LEU 3.1 2.1 82.3 4 PRO 71.4 57.4 53.2 5 ARG 132.0 63.2 71.0 6 LEU 75.0 50.8 59.7 7 CYS 98.1 98.8 50.1 8 CYS 39.1 39.4 61.2 9 LEU 147.3 99.7 37.3 10 GLU 8.4 6.1 83.4 11 LYS 112.6 64.9 63.6 12 GLY 25.1 72.1 56.1 13 PRO 8.9 7.1 81.2 14 ASN 1.5 1.2 85.0 15 GLY 25.4 73.1 61.8 16 TYR 172.0 95.0 41.5 17 GLY 19.6 56.3 58.7 18 PHE 161.3 96.7 27.6 19 HIS 76.2 50.7 66.0 20 LEU 143.4 97.0 35.1 21 HIS 81.9 54.6 70.8 22 GLY 18.6 53.5 74.2 23 GLU 88.7 64.0 55.0 24 LYS 0.0 0.0 91.4 25 GLY 0.0 0.0 78.7 26 LYS 78.5 45.3 80.7 27 LEU 25.5 17.2 80.4 28 GLY 32.5 93.3 69.8 29 GLN 138.0 92.9 49.0 30 TYR 166.9 92.2 50.8 31 ILE 143.5 100.0 39.7 32 ARG 62.3 29.8 75.8 33 LEU 51.7 35.0 67.2 34 VAL 106.7 89.8 50.6 35 GLU 66.9 48.3 59.9 36 PRO 25.3 20.4 83.5 37 GLY 8.5 24.4 76.4 38 SER 74.5 89.1 53.0 39 PRO 100.6 80.8 55.1 40 ALA 72.6 100.0 39.9 41 GLU 72.6 52.4 71.6 42 LYS 42.3 24.4 83.5 43 ALA 60.7 83.6 63.8 44 GLY 7.6 21.9 83.1 45 LEU 147.8 100.0 28.2 46 LEU 51.1 34.6 77.4 47 ALA 32.6 45.0 70.9 48 GLY 16.8 48.4 68.2 49 ASP 110.5 100.0 47.3 50 ARG 136.5 65.4 59.4 51 LEU 147.8 100.0 30.4 52 VAL 102.1 85.9 54.5 53 GLU 88.2 63.7 58.8 54 VAL 118.2 99.5 36.9 55 ASN 84.5 69.9 66.1 56 GLY 14.8 42.5 79.7 57 GLU 49.5 35.7 85.8 58 ASN 63.9 52.8 67.9 59 VAL 118.6 99.8 49.0 60 GLU 84.1 60.7 74.0 61 LYS 30.2 17.4 79.6 62 GLU 104.1 75.1 68.1 63 THR 29.4 27.5 78.4 64 HIS 69.8 46.4 69.2 65 GLN 36.5 24.6 80.1 66 GLN 57.2 38.5 71.9 67 VAL 118.8 100.0 37.9 68 VAL 93.2 78.4 61.9 69 SER 33.7 40.3 75.7 70 ARG 125.8 60.2 68.3 71 ILE 128.2 89.3 31.7 72 ARG 46.8 22.4 81.8 73 ALA 14.3 19.7 78.8 74 ALA 59.1 81.4 72.7 75 LEU 38.6 26.1 87.0 76 ASN 5.8 4.8 80.2 77 ALA 25.4 35.0 75.5 78 VAL 118.8 100.0 36.8 79 ARG 101.0 48.4 64.1 80 LEU 147.8 100.0 26.9 81 LEU 108.4 73.4 53.4 82 VAL 118.8 100.0 45.9 83 VAL 85.4 71.9 66.4 84 ASP 84.2 76.2 61.5 85 PRO 72.1 57.9 72.8 86 GLU 62.3 45.0 66.6 87 THR 27.3 25.5 81.2 88 ASP 0.0 0.0 88.7 89 GLU 20.9 15.1 80.8 90 GLN 0.0 0.0 90.4 91 LEU 9.7 6.6 87.5