Protein Data Bank File : 1ip9 Title : SIGNALING PROTEIN 26-APR-01 1IP9 Number of Amino Acid Residues : 85 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLY ALA MET GLY SER SER THR SER GLY LEU 10 LYS THR THR LYS ILE LYS PHE TYR TYR LYS 20 ASP ASP ILE PHE ALA LEU MET LEU LYS GLY 30 ASP THR THR TYR LYS GLU LEU ARG SER LYS 40 ILE ALA PRO ARG ILE ASP THR ASP ASN PHE 50 LYS LEU GLN THR LYS LEU PHE ASP GLY SER 60 GLY GLU GLU ILE LYS THR ASP SER GLN VAL 70 SER ASN ILE ILE GLN ALA LYS LEU LYS ILE 80 SER VAL HIS ASP ILE Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLY 0.0 81.2 179.9 2 ALA -110.7 179.8 -179.7 3 MET -153.8 147.9 -179.7 57.8 108.7 101.7 4 GLY -88.5 -31.1 -179.9 5 SER -56.8 179.5 -179.9 -75.8 6 SER -174.3 145.7 -180.0 126.5 7 THR -68.2 122.4 -179.9 49.6 8 SER -98.4 114.0 179.8 151.6 9 GLY -126.6 168.4 -179.9 10 LEU -125.6 -171.2 -179.9 -105.5 92.5 11 LYS -108.1 121.4 179.8 -104.1 -135.1 -159.8 140.3 12 THR -50.1 124.4 179.8 11.8 13 THR -88.3 133.6 -179.5 -72.5 14 LYS -87.2 113.8 -180.0 -132.1 -124.6 -99.0 -178.2 15 ILE -122.2 119.6 -179.5 -32.0 -153.4 16 LYS -95.3 115.5 179.1 -85.5 -84.4 -143.9 76.1 17 PHE -80.6 166.5 -178.9 -75.3 60.3 18 TYR -134.6 70.9 179.1 -79.2 -114.2 19 TYR -71.8 115.7 -179.7 -175.3 -125.7 20 LYS 53.3 -137.6 179.8 -39.8 -140.4 66.6 172.2 21 ASP -85.8 -8.1 179.9 -66.4 -163.5 22 ASP -90.3 164.0 -179.5 -83.5 5.0 23 ILE -148.7 151.2 178.0 -83.3 132.0 24 PHE -139.4 -172.5 -179.0 31.9 -71.4 25 ALA -138.0 166.4 179.9 26 LEU -146.3 136.7 179.0 -134.5 87.3 27 MET -106.9 105.8 -178.6 -53.3 -110.7 52.4 28 LEU -93.9 121.0 179.4 -54.9 -40.5 29 LYS -85.5 6.9 -179.7 -160.4 140.8 -154.2 70.6 30 GLY 100.8 -22.5 180.0 31 ASP -88.2 -13.4 -179.8 53.9 -160.6 32 THR -54.0 -179.9 179.5 -10.1 33 THR -157.4 -173.9 178.8 111.3 34 TYR -83.7 -35.9 178.8 171.1 81.9 35 LYS -77.3 -22.8 177.7 -72.4 -176.3 -74.8 -138.9 36 GLU -69.6 -51.8 178.2 -122.4 82.5 -28.1 37 LEU -56.7 -34.4 179.9 171.7 80.3 38 ARG -52.2 -44.6 -179.9 -121.7 -168.6 64.9 -171.8 39 SER -81.9 -23.5 -180.0 -165.9 40 LYS -80.7 -11.8 -179.7 -55.0 -178.3 -135.0 -116.1 41 ILE -108.3 -41.9 -178.8 -70.8 174.2 42 ALA -42.1 -50.7 -179.1 43 PRO -70.7 -29.5 178.9 21.5 -23.6 44 ARG -85.2 -1.1 179.9 -61.0 -113.6 152.4 76.5 45 ILE -105.5 -33.2 -176.5 -52.2 -130.3 46 ASP 93.9 5.7 179.9 -48.6 138.6 47 THR -138.8 178.7 179.6 166.5 48 ASP -112.1 -6.5 179.9 87.7 137.0 49 ASN -130.2 123.5 179.5 -107.9 -129.6 50 PHE -151.9 171.4 179.9 27.8 -79.8 51 LYS -122.6 118.4 -179.7 -8.4 168.9 67.5 178.7 52 LEU -93.7 142.1 178.9 -45.0 -30.1 53 GLN -140.4 173.4 178.9 -42.1 118.3 127.1 54 THR -85.5 82.8 -179.1 26.6 55 LYS -29.2 100.7 178.6 -151.4 -75.7 -151.8 -88.5 56 LEU -96.2 -161.0 179.3 -66.0 174.4 57 PHE -85.7 -29.6 180.0 103.1 85.3 58 ASP -73.2 -35.7 -179.8 72.4 -89.8 59 GLY 159.8 -45.9 -179.9 60 SER -158.5 154.7 179.7 32.5 61 GLY -115.4 -127.6 179.8 62 GLU -70.1 109.5 -179.4 -77.1 -70.7 148.6 63 GLU -54.7 96.9 179.0 165.1 177.0 75.3 64 ILE -43.8 123.9 180.0 -48.9 109.1 65 LYS -147.3 16.8 179.9 -89.1 -104.1 -164.2 126.5 66 THR -152.2 146.4 -180.0 41.4 67 ASP -47.0 -23.0 -179.8 -44.3 -19.9 68 SER -79.7 -44.3 179.8 105.3 69 GLN -60.1 -35.1 179.7 -46.4 -105.6 58.3 70 VAL -73.7 -48.5 179.4 -168.7 71 SER -64.5 -13.5 178.7 -48.1 72 ASN -85.5 -47.1 176.5 -154.6 79.6 73 ILE -64.7 -17.2 179.7 -86.3 99.9 74 ILE -81.8 -46.3 -179.2 -84.7 -166.4 75 GLN -77.2 -17.6 -178.9 -106.0 126.3 70.6 76 ALA -115.5 0.6 -179.4 77 LYS 44.3 78.8 -179.3 -173.6 131.7 54.0 162.5 78 LEU -104.1 136.8 178.0 -94.7 -82.8 79 LYS -68.3 126.2 -177.7 -76.0 -172.6 -115.2 -61.6 80 ILE -96.3 154.3 178.5 -48.4 -114.7 81 SER -118.3 144.2 -178.2 168.2 82 VAL -124.7 130.5 178.7 -156.6 83 HIS -116.4 165.5 179.5 -63.7 -94.7 84 ASP -97.7 133.0 -179.2 -6.7 130.3 85 ILE -143.5 19.7 0.0 39.1 130.1 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLY 4.243 11.867 38.600 2 ALA 2.847 12.730 35.186 3 MET 2.883 10.808 31.875 4 GLY 2.816 11.626 28.135 5 SER 0.974 8.459 27.040 6 SER -2.852 8.509 27.092 7 THR -5.803 6.126 26.631 8 SER -6.856 6.291 22.962 9 GLY -10.586 5.608 22.509 10 LEU -13.129 6.338 19.753 11 LYS -16.878 7.041 19.522 12 THR -19.192 4.029 19.115 13 THR -20.696 4.390 15.622 14 LYS -24.450 3.689 15.393 15 ILE -25.123 1.302 12.498 16 LYS -28.651 -0.028 11.903 17 PHE -28.667 -3.381 10.084 18 TYR -31.726 -4.412 8.053 19 TYR -32.331 -8.169 8.266 20 LYS -35.426 -8.817 6.138 21 ASP -38.163 -6.369 7.214 22 ASP -36.719 -6.272 10.758 23 ILE -33.796 -4.028 11.787 24 PHE -31.308 -3.710 14.662 25 ALA -28.297 -1.517 15.531 26 LEU -24.613 -1.895 16.488 27 MET -22.187 0.396 18.350 28 LEU -18.641 -0.090 17.013 29 LYS -15.886 1.340 19.234 30 GLY -13.419 0.823 16.354 31 ASP -12.233 -2.541 17.720 32 THR -15.195 -4.366 16.139 33 THR -14.603 -6.501 13.039 34 TYR -16.533 -8.362 10.342 35 LYS -16.328 -11.682 12.204 36 GLU -17.226 -9.776 15.362 37 LEU -20.379 -8.472 13.719 38 ARG -20.927 -12.062 12.569 39 SER -21.668 -13.110 16.173 40 LYS -23.442 -9.807 16.937 41 ILE -25.856 -10.457 14.039 42 ALA -26.250 -14.266 14.051 43 PRO -28.316 -14.131 17.270 44 ARG -30.281 -11.112 16.017 45 ILE -30.979 -13.055 12.787 46 ASP -32.078 -16.441 14.193 47 THR -29.443 -18.134 11.986 48 ASP -25.640 -18.471 11.866 49 ASN -25.164 -17.504 8.200 50 PHE -26.340 -14.214 6.651 51 LYS -25.015 -11.536 4.260 52 LEU -24.439 -7.949 5.460 53 GLN -24.294 -5.026 2.977 54 THR -24.264 -1.199 3.116 55 LYS -28.073 -0.734 3.181 56 LEU -28.496 1.633 0.210 57 PHE -31.782 2.987 -1.192 58 ASP -32.138 0.142 -3.717 59 GLY -31.700 -2.521 -1.011 60 SER -27.975 -3.163 -0.414 61 GLY -24.564 -1.782 -1.441 62 GLU -21.082 -3.311 -1.013 63 GLU -21.776 -6.575 0.855 64 ILE -19.568 -5.981 3.929 65 LYS -17.260 -9.023 3.984 66 THR -14.005 -7.762 5.541 67 ASP -12.927 -6.061 8.788 68 SER -12.316 -3.064 6.499 69 GLN -15.830 -2.928 5.007 70 VAL -17.143 -2.955 8.584 71 SER -14.659 -0.362 9.878 72 ASN -15.763 1.581 6.781 73 ILE -19.460 1.344 7.596 74 ILE -18.109 2.314 11.038 75 GLN -16.254 5.480 9.969 76 ALA -19.122 6.362 7.650 77 LYS -21.987 4.989 9.769 78 LEU -23.680 3.069 6.953 79 LYS -27.089 1.445 7.404 80 ILE -26.413 -2.280 6.972 81 SER -28.744 -4.828 5.346 82 VAL -28.898 -8.496 6.387 83 HIS -29.967 -11.470 4.237 84 ASP -30.337 -15.157 5.129 85 ILE -27.782 -17.561 3.630 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 S 10 S S S S S S C T T T 20 T/S S S S/S S S S S/T T T 30 T C H H H H H H H H 40 H H 3 3 C S S S S/S S 50 S S S S C T T T T/S S 60 S S S S S S/H H H H H 70 H H H H H H H/S S S S 80 S S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S 10 E E E E E B T 20 T t E E E E E S 30 h H H H H H H H 40 H H H H H h t S e E 50 E E E E e S S S 60 S h H H H H 70 H H H H H h T t e E 80 E E E E e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLY 0.0 0.0 94.7 2 ALA 0.0 0.0 84.5 3 MET 38.3 24.1 79.1 4 GLY 0.0 0.0 83.6 5 SER 5.3 6.4 76.0 6 SER 19.3 23.1 79.8 7 THR 0.0 0.0 90.9 8 SER 8.4 10.1 86.1 9 GLY 5.1 14.5 76.7 10 LEU 51.6 34.9 79.3 11 LYS 0.0 0.0 90.9 12 THR 69.0 64.6 61.2 13 THR 89.3 83.5 54.4 14 LYS 66.6 38.4 62.8 15 ILE 142.0 98.9 39.3 16 LYS 93.4 53.8 59.9 17 PHE 165.3 99.1 23.9 18 TYR 139.4 77.0 46.9 19 TYR 159.5 88.1 45.3 20 LYS 56.8 32.7 82.5 21 ASP 0.0 0.0 88.0 22 ASP 9.4 8.5 81.1 23 ILE 104.0 72.5 56.0 24 PHE 144.4 86.6 43.3 25 ALA 50.0 68.9 50.7 26 LEU 134.3 90.9 36.3 27 MET 81.5 51.1 63.4 28 LEU 146.3 99.0 35.9 29 LYS 75.4 43.5 79.4 30 GLY 24.8 71.4 59.1 31 ASP 14.0 12.7 79.8 32 THR 103.2 96.6 47.5 33 THR 83.5 78.1 61.2 34 TYR 156.8 86.6 44.4 35 LYS 39.6 22.9 81.4 36 GLU 66.9 48.3 68.6 37 LEU 147.6 99.9 22.9 38 ARG 83.8 40.1 70.1 39 SER 9.7 11.6 77.9 40 LYS 101.7 58.6 50.3 41 ILE 143.5 100.0 20.9 42 ALA 52.7 72.6 53.1 43 PRO 55.9 44.9 74.2 44 ARG 79.4 38.0 71.6 45 ILE 143.5 100.0 38.0 46 ASP 5.8 5.2 86.4 47 THR 68.4 64.0 68.1 48 ASP 17.8 16.1 74.4 49 ASN 57.0 47.2 74.5 50 PHE 165.8 99.4 37.1 51 LYS 93.7 54.0 60.3 52 LEU 147.5 99.8 33.6 53 GLN 135.3 91.0 55.7 54 THR 92.5 86.5 39.6 55 LYS 119.7 69.0 57.0 56 LEU 70.6 47.8 75.7 57 PHE 0.0 0.0 84.5 58 ASP 46.8 42.3 65.1 59 GLY 9.8 28.0 86.1 60 SER 59.3 70.9 68.7 61 GLY 28.2 81.2 58.4 62 GLU 19.6 14.1 89.0 63 GLU 93.9 67.8 56.5 64 ILE 143.5 100.0 36.4 65 LYS 70.5 40.7 73.2 66 THR 36.2 33.8 71.8 67 ASP 41.3 37.4 67.3 68 SER 11.9 14.3 77.7 69 GLN 97.1 65.3 65.5 70 VAL 117.0 98.5 34.8 71 SER 51.3 61.4 68.2 72 ASN 29.1 24.1 75.7 73 ILE 140.1 97.7 33.3 74 ILE 139.4 97.2 48.6 75 GLN 38.3 25.8 74.1 76 ALA 32.3 44.5 70.0 77 LYS 68.2 39.3 69.7 78 LEU 99.8 67.5 54.7 79 LYS 62.0 35.8 74.1 80 ILE 143.3 99.9 29.0 81 SER 77.2 92.3 53.5 82 VAL 118.8 100.0 32.6 83 HIS 76.8 51.1 73.5 84 ASP 63.9 57.8 62.3 85 ILE 86.4 60.2 68.5