Protein Data Bank File : 1a1x Title : PROTO-ONCOGENE 18-DEC-97 1A1X Number of Amino Acid Residues : 106 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ALA GLY GLU ASP VAL GLY ALA PRO PRO ASP 10 HIS LEU TRP VAL HIS GLN GLU GLY ILE TYR 20 ARG ASP GLU TYR GLN ARG THR TRP VAL ALA 30 VAL VAL GLU GLU GLU THR SER PHE LEU ARG 40 ALA ARG VAL GLN GLN ILE GLN VAL PRO LEU 50 GLY ASP ALA ALA ARG PRO SER HIS LEU LEU 60 THR SER GLN LEU PRO LEU MET TRP GLN LEU 70 TYR PRO GLU GLU ARG TYR MET ASP ASN ASN 80 SER ARG LEU TRP GLN ILE GLN HIS HIS LEU 90 MET VAL ARG GLY VAL GLN GLU LEU LEU LEU 100 LYS LEU LEU PRO ASP ASP Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ALA 0.0 96.9 -178.2 2 GLY 92.1 9.5 -179.8 3 GLU -112.3 166.4 177.7 -68.7 -72.0 -56.6 4 ASP -127.1 36.9 -178.7 -76.6 -77.9 5 VAL -80.5 -22.6 179.3 68.1 6 GLY 85.5 -162.4 -178.5 7 ALA -79.9 144.5 179.4 8 PRO -75.7 161.7 179.7 30.7 -43.4 9 PRO -63.3 139.6 178.5 27.3 -41.7 10 ASP -61.5 -34.4 178.0 168.2 64.4 11 HIS -158.1 156.6 179.4 62.2 -110.1 12 LEU -134.1 118.8 -179.9 -68.1 158.8 13 TRP -109.8 129.2 179.5 -69.1 106.9 14 VAL -65.0 145.6 177.5 70.6 15 HIS -117.2 -53.7 178.4 -173.8 77.0 16 GLN -134.7 159.0 -179.6 -171.3 -180.0 71.9 17 GLU -49.0 119.6 179.4 -128.0 -83.2 84.6 18 GLY 84.4 -8.3 179.3 19 ILE -118.0 119.8 -178.3 -57.3 177.9 20 TYR -114.8 167.5 177.3 -66.2 75.2 21 ARG -135.1 136.9 -179.6 -76.2 -162.9 -62.2 -154.2 22 ASP -95.1 -172.4 -179.7 59.9 23.5 23 GLU -60.7 -16.2 179.8 61.4 -95.9 32.8 24 TYR -100.9 6.6 -178.9 -58.3 -46.9 25 GLN 72.3 12.0 178.4 -68.4 170.6 -102.5 26 ARG -80.8 143.6 -179.9 -65.4 179.9 -53.4 175.6 27 THR -90.8 145.1 179.1 53.7 28 TRP -129.2 135.4 179.2 -72.0 75.5 29 VAL -103.2 125.4 -179.5 175.0 30 ALA -110.7 131.4 178.4 31 VAL -122.5 147.5 179.4 -61.9 32 VAL -92.5 133.8 176.7 176.6 33 GLU -129.9 88.3 -177.1 -56.3 -169.2 -38.3 34 GLU -82.4 126.2 177.8 -168.2 179.9 -27.2 35 GLU -93.5 -176.8 179.9 -58.1 -61.1 -40.4 36 THR -70.7 -46.2 -177.4 -63.1 37 SER -96.4 -11.7 -179.4 -46.2 38 PHE -157.1 179.1 -178.8 54.9 -87.6 39 LEU -123.6 139.3 178.1 -174.6 135.4 40 ARG -124.1 151.3 177.4 -74.6 -156.0 -167.8 98.2 41 ALA -126.8 128.2 178.6 42 ARG -104.9 118.9 -176.6 -171.2 152.2 56.9 84.7 43 VAL -118.7 123.7 -179.5 -159.1 44 GLN -119.9 138.5 179.8 -65.9 -175.8 -8.9 45 GLN -82.0 94.1 179.5 -153.4 -76.8 -83.7 46 ILE -128.9 134.4 178.9 -61.4 174.8 47 GLN -72.1 112.8 179.7 -176.7 174.1 -62.9 48 VAL -126.8 159.6 180.0 -66.7 49 PRO -69.9 154.1 178.6 32.2 -43.5 50 LEU -122.2 129.3 178.2 -71.0 176.3 51 GLY -110.3 -137.2 179.1 52 ASP -73.9 148.7 177.0 -57.5 -19.1 53 ALA -73.4 139.0 -179.8 54 ALA -72.3 152.7 178.3 55 ARG -76.2 139.1 179.8 -56.9 -59.3 -174.7 -178.4 56 PRO -53.0 -29.7 179.4 -32.7 43.9 57 SER -57.9 -36.1 178.7 53.9 58 HIS -78.2 -30.4 -178.3 -84.0 120.1 59 LEU -81.0 -14.7 -179.2 -52.9 169.5 60 LEU -58.6 -31.7 -178.1 -65.1 175.4 61 THR -88.9 -12.5 -179.0 59.2 62 SER -60.2 150.9 178.1 179.8 63 GLN -79.6 -22.8 179.2 -65.5 -178.2 -80.3 64 LEU -93.3 151.7 -179.5 -91.0 11.1 65 PRO -81.9 167.8 178.4 37.5 -42.1 66 LEU -72.6 -29.1 -179.4 -63.8 179.1 67 MET -159.5 153.4 177.8 63.5 133.6 -93.0 68 TRP -127.4 136.6 179.6 -88.6 -61.1 69 GLN -127.3 127.0 179.9 -177.5 179.1 91.8 70 LEU -55.1 127.9 -177.5 -164.8 50.6 71 TYR -122.1 152.7 -180.0 -161.9 71.0 72 PRO -54.9 149.7 179.4 -31.0 42.9 73 GLU 76.9 37.6 179.4 -51.9 -60.3 -57.2 74 GLU 45.0 68.8 178.2 -70.7 -45.6 -88.6 75 ARG -160.6 165.1 -179.5 49.6 -152.8 -171.3 159.0 76 TYR -118.0 143.5 176.2 -75.9 -89.8 77 MET -107.6 127.8 179.7 179.7 178.4 -90.4 78 ASP -89.0 -173.2 -179.5 62.8 24.6 79 ASN -69.6 -16.0 178.4 51.1 -73.1 80 ASN -98.0 8.1 -178.8 -61.9 141.1 81 SER 75.7 9.0 179.3 -78.1 82 ARG -81.7 151.5 -179.6 -58.7 172.5 -175.7 142.6 83 LEU -104.3 139.5 179.7 -93.5 44.7 84 TRP -122.4 119.4 -179.4 -64.5 69.0 85 GLN -78.2 132.1 176.8 -178.0 67.1 57.9 86 ILE -82.8 106.4 -179.8 -66.7 171.0 87 GLN -80.4 -32.6 174.4 -58.2 -161.2 -78.4 88 HIS -160.7 148.8 -179.9 82.6 42.5 89 HIS -138.7 101.0 -178.1 179.1 -160.1 90 LEU -145.1 173.3 179.0 27.2 79.7 91 MET -97.4 119.4 179.6 -157.0 66.6 42.4 92 VAL -122.7 116.6 -178.9 179.0 93 ARG 55.2 33.8 178.9 -81.1 61.4 -175.8 -129.5 94 GLY 87.4 -1.6 -179.8 95 VAL -112.4 134.0 178.9 177.1 96 GLN -70.4 132.4 -177.8 -168.1 175.3 163.1 97 GLU -133.7 134.7 177.2 172.2 -177.4 -73.1 98 LEU -112.1 136.3 176.4 -77.0 170.6 99 LEU -117.7 107.3 -178.1 -176.1 64.9 100 LEU -103.7 142.3 179.5 -54.6 178.6 101 LYS -125.9 121.3 179.4 -175.7 -179.7 -179.8 174.6 102 LEU -72.1 118.1 -179.4 176.7 57.5 103 LEU -90.9 155.1 179.8 -60.1 174.7 104 PRO -66.6 143.2 -179.3 27.7 -40.9 105 ASP -66.8 128.2 179.5 -172.3 -78.8 106 ASP -117.7 60.5 0.0 -170.2 9.5 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ALA 9.560 25.910 36.169 2 GLY 6.682 23.653 37.152 3 GLU 5.178 26.594 39.057 4 ASP 2.109 28.817 38.696 5 VAL 3.794 31.769 40.475 6 GLY 3.627 34.047 37.445 7 ALA 5.935 36.896 36.465 8 PRO 8.609 38.392 38.759 9 PRO 8.460 42.095 39.656 10 ASP 9.603 44.511 36.940 11 HIS 11.475 46.421 39.641 12 LEU 12.301 46.599 43.336 13 TRP 13.135 49.902 45.014 14 VAL 14.671 49.900 48.495 15 HIS 12.779 51.667 51.289 16 GLN 14.740 50.621 54.333 17 GLU 17.742 48.280 54.469 18 GLY 16.446 44.910 53.306 19 ILE 12.892 46.071 52.553 20 TYR 11.950 46.777 48.958 21 ARG 8.795 47.780 47.097 22 ASP 7.751 46.703 43.588 23 GLU 5.680 48.429 40.904 24 TYR 2.488 47.528 42.843 25 GLN 3.694 49.077 46.126 26 ARG 3.953 45.605 47.650 27 THR 6.791 45.039 50.098 28 TRP 9.507 42.404 49.701 29 VAL 11.948 41.421 52.452 30 ALA 15.483 40.632 51.293 31 VAL 18.021 38.593 53.236 32 VAL 21.646 37.861 52.398 33 GLU 22.835 34.252 52.161 34 GLU 26.538 34.495 51.446 35 GLU 28.492 31.541 50.059 36 THR 32.303 31.288 49.966 37 SER 32.705 32.346 46.353 38 PHE 29.545 34.404 45.860 39 LEU 26.498 36.110 47.272 40 ARG 22.810 35.248 47.058 41 ALA 19.769 37.244 48.148 42 ARG 16.542 35.481 49.087 43 VAL 13.641 37.875 48.581 44 GLN 10.119 37.152 49.799 45 GLN 6.898 39.081 49.222 46 ILE 5.734 39.664 52.776 47 GLN 3.612 42.583 53.999 48 VAL 5.709 44.526 56.522 49 PRO 5.277 47.980 58.078 50 LEU 6.928 50.937 56.414 51 GLY 8.381 53.797 58.394 52 ASP 10.709 56.493 57.094 53 ALA 12.722 55.826 53.934 54 ALA 16.360 55.370 54.910 55 ARG 18.942 57.998 53.903 56 PRO 21.203 56.906 51.007 57 SER 24.202 57.625 53.274 58 HIS 23.228 54.605 55.405 59 LEU 22.568 52.455 52.349 60 LEU 25.981 53.029 50.699 61 THR 27.560 50.286 52.807 62 SER 24.844 47.642 52.321 63 GLN 25.515 44.375 50.460 64 LEU 22.130 44.737 48.707 65 PRO 21.435 47.390 46.018 66 LEU 19.244 50.487 45.992 67 MET 17.273 48.972 43.126 68 TRP 16.792 45.946 40.886 69 GLN 15.301 46.222 37.396 70 LEU 14.100 43.156 35.471 71 TYR 16.596 42.389 32.699 72 PRO 16.377 39.890 29.742 73 GLU 17.267 36.230 30.374 74 GLU 15.662 36.051 33.826 75 ARG 17.950 38.278 35.813 76 TYR 18.013 41.716 37.409 77 MET 20.323 44.633 36.799 78 ASP 20.959 46.760 39.892 79 ASN 21.905 50.434 40.246 80 ASN 25.628 49.607 39.870 81 SER 25.002 47.789 36.536 82 ARG 25.653 44.383 38.109 83 LEU 23.558 41.366 37.100 84 TRP 21.722 39.051 39.471 85 GLN 20.610 35.667 38.151 86 ILE 17.126 34.520 39.155 87 GLN 17.951 30.974 40.311 88 HIS 14.376 30.269 41.348 89 HIS 10.985 31.956 41.612 90 LEU 8.483 29.908 43.549 91 MET 5.782 29.789 46.182 92 VAL 7.194 28.536 49.487 93 ARG 4.801 27.950 52.377 94 GLY 2.376 30.317 50.646 95 VAL 4.881 33.147 50.136 96 GLN 6.322 34.187 46.770 97 GLU 10.110 33.859 46.782 98 LEU 12.947 34.997 44.515 99 LEU 16.406 33.497 44.861 100 LEU 18.950 35.881 43.312 101 LYS 22.630 35.284 42.677 102 LEU 25.077 38.140 42.119 103 LEU 27.095 37.332 39.008 104 PRO 30.660 38.558 38.297 105 ASP 30.739 41.746 36.238 106 ASP 31.352 40.962 32.577 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C C C C S S S S C 10 S S S S S S/T T T T/S S 20 S S/T T T T/S S S S S S 30 S S S S S/T T T T/S S S 40 S S S S S S S/S S S S 50 S S/S S S S/H H H H H H 60 C C S S S S S S S S 70 S/T T T T/S S S S S/T T T 80 T/S S S S S S S/S S S S 90 S/T T T T/S S S S S S S 100 S S S S/S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 e 10 E E E E E E T e E E 20 E E e T t e E E E E 30 E E E E e S S e E E 40 E E E E e 50 S h H H H H h 60 T t S S e E E E E 70 E T T e E E E E e T 80 t e E E E E E E E E 90 E E T T E E E E E E 100 E E e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ALA 0.0 0.0 94.0 2 GLY 0.0 0.0 84.7 3 GLU 92.0 66.4 70.0 4 ASP 0.0 0.0 89.8 5 VAL 109.8 92.4 57.7 6 GLY 0.0 0.0 81.5 7 ALA 9.3 12.8 73.8 8 PRO 112.6 90.4 51.2 9 PRO 120.9 97.1 52.9 10 ASP 42.3 38.3 69.2 11 HIS 102.4 68.2 63.1 12 LEU 147.8 100.0 28.7 13 TRP 70.6 34.4 70.6 14 VAL 104.1 87.7 49.4 15 HIS 133.9 89.1 55.9 16 GLN 66.9 45.0 63.6 17 GLU 58.2 42.0 62.9 18 GLY 24.9 71.5 62.9 19 ILE 116.3 81.1 54.7 20 TYR 180.1 99.5 41.1 21 ARG 123.2 59.0 59.6 22 ASP 110.5 100.0 53.2 23 GLU 99.6 71.9 57.7 24 TYR 52.2 28.8 80.9 25 GLN 13.3 8.9 87.1 26 ARG 121.3 58.1 70.5 27 THR 99.7 93.3 49.6 28 TRP 205.0 100.0 42.9 29 VAL 79.3 66.7 53.3 30 ALA 72.6 100.0 36.2 31 VAL 55.1 46.4 70.1 32 VAL 93.5 78.7 51.4 33 GLU 79.1 57.0 68.1 34 GLU 57.9 41.8 77.1 35 GLU 73.4 53.0 72.3 36 THR 0.0 0.0 89.6 37 SER 14.1 16.9 71.3 38 PHE 109.8 65.8 65.2 39 LEU 128.7 87.1 43.6 40 ARG 150.4 72.0 56.7 41 ALA 72.6 100.0 38.4 42 ARG 129.3 61.9 67.8 43 VAL 118.8 100.0 32.6 44 GLN 115.2 77.5 53.6 45 GLN 117.2 78.9 55.8 46 ILE 74.2 51.7 67.6 47 GLN 0.0 0.0 89.6 48 VAL 92.4 77.8 42.9 49 PRO 7.9 6.4 79.6 50 LEU 113.5 76.8 58.1 51 GLY 0.5 1.5 84.2 52 ASP 0.0 0.0 90.1 53 ALA 25.9 35.6 78.7 54 ALA 50.8 70.0 63.1 55 ARG 32.1 15.3 85.9 56 PRO 38.6 31.0 67.4 57 SER 20.8 24.9 68.0 58 HIS 22.3 14.9 82.4 59 LEU 138.8 93.9 43.2 60 LEU 29.1 19.7 79.6 61 THR 6.8 6.3 89.0 62 SER 71.1 85.1 73.8 63 GLN 61.8 41.6 69.3 64 LEU 141.2 95.5 45.5 65 PRO 114.7 92.2 56.7 66 LEU 82.0 55.5 55.6 67 MET 132.8 83.3 50.4 68 TRP 205.0 100.0 22.1 69 GLN 50.5 34.0 69.1 70 LEU 109.8 74.3 61.5 71 TYR 106.9 59.1 57.9 72 PRO 34.3 27.6 69.6 73 GLU 21.6 15.6 80.4 74 GLU 49.3 35.6 65.9 75 ARG 147.0 70.4 51.8 76 TYR 181.0 100.0 32.8 77 MET 105.6 66.3 62.2 78 ASP 109.5 99.1 47.5 79 ASN 86.8 71.8 57.3 80 ASN 58.4 48.3 84.4 81 SER 24.4 29.2 75.5 82 ARG 97.2 46.5 73.8 83 LEU 112.5 76.1 51.8 84 TRP 202.0 98.5 40.7 85 GLN 94.5 63.6 59.9 86 ILE 136.5 95.1 44.3 87 GLN 100.3 67.5 59.5 88 HIS 93.5 62.2 56.6 89 HIS 133.5 88.9 47.9 90 LEU 100.5 68.0 58.9 91 MET 93.0 58.3 68.5 92 VAL 81.0 68.2 69.2 93 ARG 6.8 3.2 85.8 94 GLY 3.8 11.0 69.9 95 VAL 78.0 65.7 68.4 96 GLN 124.2 83.6 51.7 97 GLU 130.4 94.1 51.6 98 LEU 147.8 100.0 30.3 99 LEU 120.7 81.7 56.7 100 LEU 147.8 100.0 32.3 101 LYS 126.0 72.7 53.7 102 LEU 108.8 73.6 54.8 103 LEU 104.5 70.7 58.2 104 PRO 13.9 11.1 81.6 105 ASP 33.7 30.5 81.7 106 ASP 0.0 0.0 94.2