Protein Data Bank File : 1gotg Title : COMPLEX (GTP-BINDING/TRANSDUCER) 07-AUG-96 1GOT Number of Amino Acid Residues : 58 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 LEU THR GLU LYS ASP LYS LEU LYS MET GLU 10 VAL ASP GLN LEU LYS LYS GLU VAL THR LEU 20 GLU ARG MET LEU VAL SER LYS CYS CYS GLU 30 GLU PHE ARG ASP TYR VAL GLU GLU ARG SER 40 GLY GLU ASP PRO LEU VAL LYS GLY ILE PRO 50 GLU ASP LYS ASN PRO PHE LYS GLU Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 LEU 0.0 175.1 179.6 0.0 0.0 2 THR 45.0 -98.6 180.0 0.0 3 GLU -45.0 -52.8 -179.9 -58.2 176.7 -47.7 4 LYS -68.1 -43.4 -178.8 -70.6 66.3 -172.8 163.9 5 ASP -72.2 -28.8 176.1 -85.2 73.9 6 LYS -70.6 -48.6 179.6 143.0 76.5 -128.5 -50.0 7 LEU -62.2 -43.9 178.6 -171.0 41.3 8 LYS -57.7 -31.4 179.3 -75.6 175.3 -173.9 175.3 9 MET -83.5 -27.7 177.2 -65.7 -167.4 -74.0 10 GLU -62.2 -60.8 178.4 173.0 174.7 -30.4 11 VAL -55.9 -30.8 179.8 174.5 12 ASP -69.8 -28.8 178.3 -140.9 44.3 13 GLN -80.9 -39.8 178.9 176.8 61.3 30.2 14 LEU -58.2 -50.7 178.5 -70.9 172.2 15 LYS -47.4 -40.6 -180.0 -75.3 -175.7 170.1 71.5 16 LYS -70.9 -45.7 -179.2 -178.5 -157.1 179.1 -61.8 17 GLU -67.5 -33.7 179.9 -72.3 171.4 -3.2 18 VAL -62.5 -20.5 179.8 87.7 19 THR -93.1 15.3 179.3 58.9 20 LEU -67.2 127.9 179.8 -109.9 166.5 21 GLU -89.6 91.3 -178.4 -55.0 159.1 -0.6 22 ARG -76.5 143.7 178.3 -74.0 78.3 168.1 -161.3 23 MET -93.7 161.0 179.9 -173.4 -162.1 -91.5 24 LEU -71.8 133.7 -179.4 -74.3 170.3 25 VAL -51.0 -52.2 179.9 175.6 26 SER -52.7 -44.9 178.3 45.0 27 LYS -63.3 -46.0 179.5 -72.7 173.0 -171.2 168.7 28 CYS -60.2 -54.5 178.8 -66.7 29 CYS -53.9 -52.5 -178.9 -73.5 30 GLU -56.0 -41.6 178.3 -70.5 177.7 22.3 31 GLU -69.5 -33.2 178.1 -64.3 -171.6 57.6 32 PHE -64.5 -57.0 179.9 -174.9 75.5 33 ARG -52.8 -49.2 179.8 173.6 169.4 59.1 51.4 34 ASP -59.4 -37.8 180.0 -63.9 -22.4 35 TYR -60.5 -51.7 -179.0 179.3 85.9 36 VAL -62.2 -52.1 -179.5 -175.8 37 GLU -55.8 -34.0 178.0 -73.7 -52.6 -74.9 38 GLU -66.8 -26.2 -178.8 -79.4 -174.2 34.9 39 ARG -125.6 -3.6 179.3 63.3 -88.8 -65.3 164.4 40 SER -60.6 -24.9 179.8 59.6 41 GLY -66.5 -17.3 180.0 42 GLU -116.1 13.0 179.7 52.2 -153.3 -44.0 43 ASP -82.9 111.9 -179.8 -168.5 -40.1 44 PRO -54.2 -30.4 180.0 -31.4 44.1 45 LEU -84.2 -13.0 178.6 -57.7 -175.8 46 VAL -94.9 -45.7 -178.0 167.9 47 LYS -89.3 -25.5 -176.1 -49.9 -84.7 72.2 178.9 48 GLY 94.8 170.7 -179.4 49 ILE -127.9 130.0 179.3 -55.5 159.4 50 PRO -58.6 130.4 -178.4 -33.1 43.3 51 GLU -43.0 -40.0 -178.5 -90.7 -65.8 -69.8 52 ASP -67.6 -20.0 179.3 -61.9 -43.8 53 LYS -102.8 2.9 -177.2 -59.0 176.4 69.2 173.2 54 ASN -91.2 115.5 179.7 -160.3 166.3 55 PRO -71.2 -17.8 180.0 32.2 -43.1 56 PHE -97.5 25.9 176.6 -64.8 -73.5 57 LYS -84.1 158.0 179.7 54.4 -176.7 169.9 -65.2 58 GLU -66.5 132.4 0.0 -60.3 -73.7 -58.6 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 LEU 22.009 7.185 21.203 2 THR 23.977 10.451 21.589 3 GLU 26.046 9.723 24.722 4 LYS 26.424 6.074 23.724 5 ASP 26.802 6.859 20.036 6 LYS 29.343 9.630 20.543 7 LEU 31.184 7.161 22.810 8 LYS 30.689 4.215 20.424 9 MET 32.413 6.392 17.823 10 GLU 35.069 7.462 20.330 11 VAL 36.070 3.819 20.930 12 ASP 35.686 3.359 17.183 13 GLN 38.383 5.994 16.526 14 LEU 40.730 4.626 19.201 15 LYS 40.640 1.131 17.661 16 LYS 41.897 2.704 14.426 17 GLU 44.540 4.808 16.180 18 VAL 45.703 1.870 18.276 19 THR 46.844 0.245 15.042 20 LEU 49.114 3.214 14.375 21 GLU 52.559 2.143 13.198 22 ARG 54.763 4.553 15.175 23 MET 58.303 5.601 14.223 24 LEU 61.203 6.033 16.702 25 VAL 61.462 9.461 18.386 26 SER 65.228 9.665 17.804 27 LYS 64.836 8.995 14.056 28 CYS 62.052 11.580 13.966 29 CYS 64.068 14.032 16.053 30 GLU 67.278 13.518 14.040 31 GLU 65.398 14.108 10.788 32 PHE 63.734 17.162 12.381 33 ARG 67.143 18.526 13.470 34 ASP 68.818 17.861 10.149 35 TYR 66.043 19.707 8.344 36 VAL 66.500 22.863 10.467 37 GLU 70.317 22.711 10.509 38 GLU 70.471 22.511 6.756 39 ARG 68.722 25.887 6.487 40 SER 68.899 27.912 9.708 41 GLY 72.044 29.502 8.324 42 GLU 69.952 31.327 5.737 43 ASP 66.991 32.142 7.959 44 PRO 66.565 35.975 8.066 45 LEU 64.956 35.775 11.495 46 VAL 67.860 33.683 12.879 47 LYS 70.715 35.593 11.254 48 GLY 69.257 39.073 10.904 49 ILE 69.155 40.884 7.565 50 PRO 71.765 43.216 6.082 51 GLU 69.981 46.575 5.908 52 ASP 70.434 46.826 2.127 53 LYS 68.551 43.550 1.541 54 ASN 65.784 44.390 4.013 55 PRO 62.547 45.385 2.252 56 PHE 61.223 46.747 5.569 57 LYS 63.928 49.333 6.005 58 GLU 62.811 52.958 6.081 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 H H H H H H H H H H 10 H H H H H H H H H H/S 20 S S S S/H H H H H H H 30 H H H H H H H H H H 40 C C H H H H H H C T 50 T T T C C S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 t h H H H H H H H H 10 H H H H H H H h T t 20 h H H H H H H 30 H H H H H H H H H h 40 T T h H H H H h g 50 G G G g T T t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 LEU 81.1 54.9 83.1 2 THR 36.9 34.5 72.4 3 GLU 17.8 12.8 80.6 4 LYS 57.1 33.0 78.6 5 ASP 54.4 49.3 66.2 6 LYS 50.3 29.0 74.0 7 LEU 56.6 38.3 74.0 8 LYS 49.8 28.7 77.2 9 MET 36.3 22.8 78.4 10 GLU 69.9 50.4 62.0 11 VAL 55.1 46.4 65.7 12 ASP 30.7 27.8 75.3 13 GLN 66.0 44.4 73.0 14 LEU 51.6 34.9 76.4 15 LYS 51.7 29.8 74.6 16 LYS 32.9 19.0 88.0 17 GLU 74.2 53.5 64.3 18 VAL 25.5 21.5 77.6 19 THR 21.7 20.3 81.7 20 LEU 55.7 37.7 76.8 21 GLU 0.0 0.0 90.3 22 ARG 79.8 38.2 77.2 23 MET 62.2 39.0 72.6 24 LEU 42.0 28.4 78.3 25 VAL 9.8 8.2 74.2 26 SER 24.0 28.7 67.9 27 LYS 60.6 34.9 69.8 28 CYS 47.0 47.4 62.1 29 CYS 33.9 34.1 63.7 30 GLU 50.5 36.5 75.2 31 GLU 39.3 28.4 72.6 32 PHE 20.3 12.2 77.7 33 ARG 81.3 38.9 69.5 34 ASP 49.3 44.6 75.5 35 TYR 48.9 27.0 80.0 36 VAL 54.1 45.5 61.8 37 GLU 44.8 32.4 77.2 38 GLU 35.0 25.2 84.0 39 ARG 115.8 55.4 68.2 40 SER 57.9 69.3 61.6 41 GLY 0.9 2.5 76.1 42 GLU 26.5 19.1 79.1 43 ASP 58.0 52.5 56.1 44 PRO 55.9 44.9 67.5 45 LEU 9.2 6.2 85.3 46 VAL 53.2 44.8 72.2 47 LYS 69.3 40.0 79.0 48 GLY 1.4 3.9 81.7 49 ILE 103.2 71.9 57.2 50 PRO 38.6 31.0 72.4 51 GLU 32.8 23.6 78.7 52 ASP 0.0 0.0 77.6 53 LYS 32.9 19.0 75.8 54 ASN 95.2 78.7 51.5 55 PRO 44.5 35.7 75.8 56 PHE 11.2 6.7 85.6 57 LYS 97.7 56.3 78.6 58 GLU 0.0 0.0 94.2