Protein Data Bank File : 1rax Title : RAS-BINDING DOMAIN 13-MAR-99 1RAX Number of Amino Acid Residues : 93 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLN GLN VAL GLY ASP CYS CYS ILE ILE ARG 10 VAL SER LEU ASP VAL ASP ASN GLY ASN MET 20 TYR LYS SER ILE LEU VAL THR SER GLN ASP 30 LYS ALA PRO ALA VAL ILE ARG LYS ALA MET 40 ASP LYS HIS ASN LEU GLU GLU GLU GLU PRO 50 GLU ASP TYR GLU LEU LEU GLN ILE LEU SER 60 ASP ASP ARG LYS LEU LYS ILE PRO GLU ASN 70 ALA ASN VAL PHE TYR ALA MET ASN SER THR 80 ALA ASN TYR ASP PHE VAL LEU LYS LYS ARG 90 THR PHE THR Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLN 0.0 124.2 178.6 -78.3 -86.1 -64.9 2 GLN 63.4 171.6 178.0 -54.3 -98.8 -113.9 3 VAL -75.1 134.2 -177.4 -177.1 4 GLY 58.1 -135.6 179.4 5 ASP 175.7 114.3 -178.0 -120.9 -38.2 6 CYS -150.7 158.7 -178.2 46.6 7 CYS -154.3 157.9 -179.5 70.1 8 ILE -101.5 126.6 179.7 -64.4 156.0 9 ILE -111.9 155.4 -179.2 54.4 155.4 10 ARG -104.8 129.6 -177.6 150.6 -173.7 -74.4 124.9 11 VAL -127.8 115.6 174.5 -143.7 12 SER -105.5 158.7 172.9 31.0 13 LEU -90.1 165.7 175.1 -95.9 46.5 14 ASP -69.5 69.0 -172.9 53.0 19.8 15 VAL -104.6 -82.2 -176.9 -139.3 16 ASP 168.3 -73.3 -178.9 -106.2 -60.0 17 ASN -95.8 175.1 176.5 -97.7 84.2 18 GLY -45.8 151.1 -172.1 19 ASN -153.4 -149.4 172.5 -146.7 63.9 20 MET -91.8 79.1 169.5 -74.8 -132.0 -111.3 21 TYR -65.3 117.0 -179.3 -113.2 -56.0 22 LYS -99.3 162.9 -178.1 -111.8 65.3 96.7 64.8 23 SER -134.9 142.4 -172.6 -178.4 24 ILE -152.0 158.5 -179.5 54.3 171.4 25 LEU -103.3 142.2 -175.1 -167.7 147.3 26 VAL -122.8 138.9 -175.7 94.5 27 THR -115.5 151.2 179.8 74.6 28 SER -24.3 -53.0 -175.5 55.4 29 GLN -80.4 -9.2 172.6 -141.0 132.8 -124.5 30 ASP -28.6 108.1 -175.8 44.4 18.0 31 LYS -95.8 154.7 169.7 -11.8 -172.7 -157.5 -48.3 32 ALA -45.0 -57.0 -178.0 33 PRO -66.2 -11.1 178.6 23.0 -28.1 34 ALA -84.7 -52.4 174.1 35 VAL -54.0 -33.8 179.2 160.1 36 ILE -74.2 -34.8 179.1 -72.1 140.2 37 ARG -60.6 -38.4 -179.1 179.0 -133.7 169.9 -118.4 38 LYS -71.2 -52.5 -177.5 -155.8 99.7 110.3 120.1 39 ALA -59.5 -33.9 -178.2 40 MET -73.8 -54.7 175.3 -80.7 -166.0 92.4 41 ASP -50.0 -32.5 178.2 -173.6 56.4 42 LYS -68.9 -45.2 -177.5 -114.3 140.2 -158.9 -99.7 43 HIS -85.3 -2.6 175.5 -89.7 107.8 44 ASN 60.0 46.1 -175.1 -53.3 76.7 45 LEU -118.1 46.6 178.7 -74.9 173.0 46 GLU -62.0 -16.8 174.4 -69.9 -90.0 60.1 47 GLU -40.6 -32.7 -180.0 64.3 -176.2 14.9 48 GLU -133.7 171.5 -177.5 -61.7 135.0 6.4 49 GLU -92.3 170.8 179.2 -88.4 122.5 -54.4 50 PRO -72.5 -36.7 179.4 23.1 -29.2 51 GLU -56.8 -24.1 -178.8 -65.4 -70.5 -5.8 52 ASP -93.4 27.8 -175.3 -148.3 -20.8 53 TYR -146.5 126.3 176.1 -89.4 -89.3 54 GLU -79.8 144.1 171.9 -66.9 -52.7 -71.3 55 LEU -103.4 120.9 -174.0 -164.3 56.3 56 LEU -124.2 137.0 176.4 -57.7 -52.4 57 GLN -106.9 137.3 -178.4 -155.8 -159.7 -13.4 58 ILE -102.0 129.0 -176.7 -62.4 131.8 59 LEU -106.7 -77.2 178.0 -54.2 -6.9 60 SER -91.5 179.1 177.7 -24.2 61 ASP -78.7 45.9 -173.7 45.9 55.8 62 ASP 168.6 -31.9 -177.0 -103.1 -4.3 63 ARG -90.4 113.4 179.0 -118.7 -85.0 -159.2 -167.4 64 LYS -117.2 160.5 -176.5 -97.5 -160.6 -66.4 -175.8 65 LEU -128.6 163.3 -177.3 -101.1 172.1 66 LYS -128.6 135.7 -177.8 -150.3 140.5 130.1 -112.8 67 ILE -110.7 127.4 176.8 -42.5 -157.7 68 PRO -72.1 168.5 -173.6 24.7 -28.2 69 GLU -56.9 -20.1 -174.9 -176.5 -170.9 -88.2 70 ASN -136.0 3.0 173.4 -135.2 128.9 71 ALA -59.6 111.7 171.1 72 ASN -43.5 100.1 -179.1 33.1 -141.0 73 VAL -44.9 -49.5 -179.8 169.3 74 PHE -49.1 -27.9 -178.5 -165.4 66.2 75 TYR -115.0 2.0 -176.0 -103.9 57.5 76 ALA -115.8 15.9 -174.1 77 MET -115.9 150.9 174.7 -46.3 154.7 -48.6 78 ASN -70.5 106.4 179.7 -179.9 -60.2 79 SER -63.3 -42.8 -179.1 -149.6 80 THR -58.8 -13.8 -179.3 70.4 81 ALA -103.4 -149.6 -178.0 82 ASN -117.8 158.1 -177.5 41.7 -139.3 83 TYR -83.1 54.8 -177.4 -58.5 -48.7 84 ASP -103.4 136.6 -169.0 -57.3 41.2 85 PHE -137.1 137.1 175.4 -74.7 70.0 86 VAL -113.5 139.1 175.7 162.7 87 LEU -107.2 107.3 -175.4 -166.0 63.3 88 LYS -113.3 148.8 178.7 -127.0 -150.6 86.8 -174.1 89 LYS -86.3 151.5 179.3 -159.4 171.8 136.8 -110.6 90 ARG -83.8 50.6 178.4 -134.0 -145.3 -62.1 -104.5 91 THR -64.5 167.2 177.6 -18.0 92 PHE -62.5 63.7 -170.8 41.5 31.3 93 THR -156.6 0.1 0.0 -58.3 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLN 69.071 1.483 -21.504 2 GLN 66.842 -1.548 -20.988 3 VAL 63.477 -1.330 -19.231 4 GLY 63.657 0.808 -16.088 5 ASP 67.108 0.577 -14.520 6 CYS 68.475 -1.597 -11.718 7 CYS 71.725 -3.242 -10.557 8 ILE 73.077 -5.589 -7.902 9 ILE 75.393 -4.143 -5.257 10 ARG 77.555 -5.888 -2.671 11 VAL 77.129 -4.812 1.015 12 SER 79.590 -5.628 3.837 13 LEU 79.403 -4.429 7.387 14 ASP 81.786 -2.108 9.246 15 VAL 83.917 -4.968 10.503 16 ASP 87.472 -4.985 9.165 17 ASN 88.349 -8.207 7.341 18 GLY 86.236 -10.331 4.970 19 ASN 82.839 -11.306 6.324 20 MET 79.299 -12.144 5.279 21 TYR 79.231 -9.953 2.220 22 LYS 75.549 -9.704 1.258 23 SER 74.091 -8.795 -2.139 24 ILE 70.971 -6.796 -3.032 25 LEU 69.299 -5.088 -6.011 26 VAL 68.943 -1.302 -6.339 27 THR 66.445 0.571 -8.559 28 SER 66.784 4.178 -9.974 29 GLN 64.969 5.798 -6.959 30 ASP 66.979 3.618 -4.529 31 LYS 67.533 5.738 -1.516 32 ALA 70.393 5.394 0.927 33 PRO 67.942 4.427 3.788 34 ALA 66.305 1.937 1.392 35 VAL 69.464 0.068 0.467 36 ILE 70.147 -0.016 4.195 37 ARG 66.724 -1.473 4.956 38 LYS 67.557 -4.400 2.696 39 ALA 71.172 -4.798 3.808 40 MET 70.089 -4.583 7.466 41 ASP 67.234 -7.088 7.295 42 LYS 69.856 -9.318 5.686 43 HIS 72.364 -8.902 8.482 44 ASN 69.679 -9.331 11.175 45 LEU 70.659 -6.040 12.862 46 GLU 67.240 -4.793 13.853 47 GLU 68.920 -3.630 17.085 48 GLU 69.182 -0.265 15.301 49 GLU 67.438 1.672 12.541 50 PRO 68.531 2.338 8.931 51 GLU 68.866 6.037 9.600 52 ASP 71.673 5.183 12.014 53 TYR 73.825 3.724 9.230 54 GLU 76.017 5.321 6.540 55 LEU 76.151 4.036 3.003 56 LEU 79.715 3.978 1.725 57 GLN 80.944 2.893 -1.670 58 ILE 84.396 1.353 -2.014 59 LEU 86.389 2.342 -5.048 60 SER 90.107 1.818 -4.557 61 ASP 91.785 -0.287 -1.851 62 ASP 91.537 2.726 0.520 63 ARG 89.359 5.235 -1.330 64 LYS 85.779 5.156 -0.102 65 LEU 82.759 7.308 -0.943 66 LYS 79.645 8.389 0.929 67 ILE 76.036 8.332 -0.224 68 PRO 73.452 10.838 1.155 69 GLU 69.981 9.797 2.315 70 ASN 68.340 10.254 -1.122 71 ALA 71.131 10.072 -3.634 72 ASN 69.784 7.666 -6.196 73 VAL 72.274 4.857 -5.516 74 PHE 72.102 3.864 -9.221 75 TYR 73.372 7.421 -9.974 76 ALA 75.408 8.252 -6.794 77 MET 78.093 5.604 -7.066 78 ASN 81.512 5.682 -8.709 79 SER 80.825 3.900 -11.991 80 THR 84.559 3.698 -12.800 81 ALA 84.903 1.499 -9.700 82 ASN 83.024 -1.550 -8.458 83 TYR 79.577 -1.838 -6.843 84 ASP 81.013 -2.490 -3.360 85 PHE 79.146 -0.921 -0.444 86 VAL 79.853 -0.705 3.312 87 LEU 77.167 -0.342 5.913 88 LYS 78.611 1.672 8.762 89 LYS 76.936 2.778 11.970 90 ARG 76.680 6.484 12.786 91 THR 78.797 5.928 15.877 92 PHE 80.656 8.833 17.584 93 THR 83.287 8.975 14.840 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C S S S S S/S S S S 10 S S S S/S S S S/S S S S/S 20 S S S S S S S S C C 30 H H H H H H H H H H 40 H H H H C C C C T T 50 T T/S S S S S S S S S/T 60 T T T/S S S S S S S C 70 C T T T T C C T T T 80 T C S S S S S S S S/S 90 S S/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S e E E E E E 10 E E E e S S S 20 E E E E E E e T t 30 h H H H H H H H H H 40 H H H h t T T t t 50 T e E E E E E E e S 60 S S e E E E E t T T 70 t h H H H H h t T T 80 t e E E E E E E e 90 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLN 0.0 0.0 92.4 2 GLN 5.6 3.8 88.1 3 VAL 0.0 0.0 87.9 4 GLY 0.0 0.0 79.9 5 ASP 64.5 58.4 62.3 6 CYS 50.7 51.1 60.7 7 CYS 78.7 79.3 38.7 8 ILE 48.2 33.6 72.9 9 ILE 143.3 99.9 28.2 10 ARG 90.9 43.5 71.1 11 VAL 118.8 100.0 34.4 12 SER 73.4 87.8 51.4 13 LEU 129.3 87.5 47.6 14 ASP 67.0 60.7 52.1 15 VAL 61.2 51.5 77.3 16 ASP 2.0 1.8 87.7 17 ASN 0.0 0.0 87.9 18 GLY 0.0 0.0 75.2 19 ASN 67.2 55.6 61.9 20 MET 20.3 12.8 80.9 21 TYR 115.5 63.8 67.5 22 LYS 132.5 76.4 56.6 23 SER 36.2 43.3 62.4 24 ILE 135.6 94.5 40.4 25 LEU 79.2 53.6 55.8 26 VAL 116.2 97.8 31.7 27 THR 35.6 33.3 70.2 28 SER 24.2 28.9 69.4 29 GLN 13.5 9.1 91.0 30 ASP 102.7 92.9 43.2 31 LYS 86.5 49.9 68.5 32 ALA 68.3 94.0 43.5 33 PRO 101.7 81.7 48.6 34 ALA 40.2 55.4 60.7 35 VAL 113.1 95.2 29.6 36 ILE 139.9 97.5 39.2 37 ARG 55.1 26.4 74.7 38 LYS 85.1 49.1 68.8 39 ALA 72.6 100.0 35.7 40 MET 149.1 93.5 46.0 41 ASP 35.7 32.3 82.9 42 LYS 100.5 57.9 67.5 43 HIS 138.3 92.1 52.8 44 ASN 18.6 15.4 86.2 45 LEU 109.3 74.0 59.6 46 GLU 14.4 10.4 85.6 47 GLU 49.1 35.4 75.1 48 GLU 102.6 74.1 64.5 49 GLU 20.9 15.1 68.6 50 PRO 84.4 67.8 45.3 51 GLU 50.6 36.5 68.5 52 ASP 59.3 53.6 61.6 53 TYR 173.1 95.7 48.1 54 GLU 105.0 75.8 54.7 55 LEU 147.8 100.0 29.9 56 LEU 134.9 91.2 43.9 57 GLN 148.5 100.0 38.8 58 ILE 107.0 74.6 59.9 59 LEU 137.9 93.3 53.6 60 SER 27.9 33.3 71.2 61 ASP 0.0 0.0 82.7 62 ASP 0.0 0.0 87.9 63 ARG 40.6 19.4 81.0 64 LYS 92.7 53.4 57.3 65 LEU 77.2 52.2 70.4 66 LYS 53.0 30.6 72.7 67 ILE 143.0 99.7 39.3 68 PRO 40.2 32.3 74.5 69 GLU 43.4 31.3 73.9 70 ASN 34.4 28.4 75.3 71 ALA 55.5 76.5 50.7 72 ASN 60.0 49.6 71.7 73 VAL 118.8 100.0 30.4 74 PHE 127.8 76.6 53.4 75 TYR 34.6 19.1 82.6 76 ALA 55.5 76.4 58.4 77 MET 152.4 95.6 42.9 78 ASN 75.2 62.2 58.9 79 SER 14.1 16.8 80.8 80 THR 5.3 4.9 86.1 81 ALA 59.3 81.6 67.0 82 ASN 54.3 44.9 74.5 83 TYR 92.0 50.9 65.8 84 ASP 91.0 82.3 60.1 85 PHE 166.8 100.0 30.7 86 VAL 103.4 87.1 53.6 87 LEU 147.8 100.0 30.6 88 LYS 108.8 62.8 58.9 89 LYS 111.2 64.2 67.9 90 ARG 74.1 35.5 84.8 91 THR 64.0 59.9 63.8 92 PHE 1.5 0.9 84.4 93 THR 27.6 25.8 82.4