Protein Data Bank File : 1ycqa Title : COMPLEX (ONCOGENE PROTEIN/PEPTIDE) 30-SEP-96 1YCQ Number of Amino Acid Residues : 88 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLU LYS LEU VAL GLN PRO THR PRO LEU LEU 10 LEU SER LEU LEU LYS SER ALA GLY ALA GLN 20 LYS GLU THR PHE THR MET LYS GLU VAL ILE 30 TYR HIS LEU GLY GLN TYR ILE MET ALA LYS 40 GLN LEU TYR ASP GLU LYS GLN GLN HIS ILE 50 VAL HIS CYS SER ASN ASP PRO LEU GLY GLU 60 LEU PHE GLY VAL GLN GLU PHE SER VAL LYS 70 GLU PRO ARG ARG LEU TYR ALA MET ILE SER 80 ARG ASN LEU VAL SER ALA ASN VAL Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLU 0.0 177.8 -179.8 -60.8 106.4 52.8 2 LYS -65.6 151.3 179.2 -67.3 -152.4 -70.9 -176.9 3 LEU -98.7 145.4 -179.3 -65.6 -168.7 4 VAL -125.3 148.2 180.0 -48.5 5 GLN -114.9 105.9 179.3 -178.2 -167.1 149.5 6 PRO -67.0 155.2 178.4 23.0 -39.9 7 THR -69.5 167.1 -179.8 50.5 8 PRO -51.4 -42.4 -179.2 -33.9 43.5 9 LEU -66.0 -50.9 178.2 179.4 56.3 10 LEU -60.2 -38.1 178.7 -177.4 44.5 11 LEU -61.4 -44.5 -178.5 -140.6 -153.0 12 SER -64.0 -30.1 179.4 79.9 13 LEU -72.9 -46.9 179.3 -55.8 -168.2 14 LEU -58.5 -46.5 179.6 -56.5 -175.5 15 LYS -58.1 -42.7 179.9 -68.1 -89.8 -168.8 58.6 16 SER -69.5 -17.4 178.7 81.9 17 ALA -93.4 11.5 178.0 18 GLY 100.9 -2.6 179.1 19 ALA -65.5 146.8 179.3 20 GLN -117.6 -8.0 -178.2 -82.2 -173.0 79.2 21 LYS -96.8 -173.0 179.1 -40.6 -168.6 -66.7 164.9 22 GLU -129.2 -10.1 179.1 -129.0 81.8 8.4 23 THR -133.8 134.5 -176.5 -66.0 24 PHE -143.1 173.7 175.0 -46.3 76.1 25 THR -94.9 167.3 179.2 57.9 26 MET -60.7 -32.8 178.7 -91.0 -68.4 -29.0 27 LYS -64.6 -33.3 179.1 -71.5 -164.7 177.1 -172.6 28 GLU -75.2 -39.2 177.4 -63.8 -179.5 -68.3 29 VAL -59.7 -48.0 -179.8 -177.1 30 ILE -64.2 -41.6 178.7 -71.1 -62.1 31 TYR -61.1 -49.8 -178.8 171.5 73.6 32 HIS -64.8 -34.4 179.1 -70.7 -58.2 33 LEU -66.4 -38.6 178.4 -157.9 56.3 34 GLY -64.4 -35.6 179.2 35 GLN -67.5 -38.5 178.6 -69.2 -57.0 -58.2 36 TYR -63.6 -46.7 -178.8 176.3 79.1 37 ILE -65.0 -37.0 178.8 -63.1 161.2 38 MET -66.6 -51.9 -179.3 -163.2 110.6 -120.1 39 ALA -61.8 -38.0 179.5 40 LYS -86.1 -13.3 180.0 -72.8 -102.8 -153.2 156.5 41 GLN 58.0 51.7 -179.7 -72.8 -71.3 106.4 42 LEU -84.9 -16.4 179.4 -59.1 174.2 43 TYR -75.6 157.4 -178.9 62.4 88.0 44 ASP -76.8 131.4 179.0 -168.3 -87.6 45 GLU -50.2 -46.2 -178.2 45.9 169.9 -21.9 46 LYS -91.4 -54.1 179.4 -38.8 -71.7 173.6 49.1 47 GLN -101.8 88.3 -176.8 -77.3 -82.6 -96.9 48 GLN -70.2 3.9 178.1 -59.2 -157.2 -3.2 49 HIS -94.7 -9.9 -179.8 54.2 96.6 50 ILE -96.2 126.5 179.7 -68.7 159.0 51 VAL -110.8 123.7 179.1 176.2 52 HIS -99.5 117.2 -179.4 -65.5 115.3 53 CYS -125.8 25.3 -178.5 36.1 54 SER -56.1 -33.8 -179.2 -35.1 55 ASN -122.6 37.0 -177.5 -61.1 -44.5 56 ASP -135.2 151.6 -179.8 -177.7 87.8 57 PRO -56.2 -26.7 179.0 -27.9 41.4 58 LEU -59.7 -31.5 178.5 -175.2 64.5 59 GLY -72.6 -33.9 178.8 60 GLU -71.4 -40.3 -179.8 -62.8 -57.4 -52.3 61 LEU -64.5 -53.8 -178.9 179.0 74.3 62 PHE -78.4 -31.2 -178.7 -75.5 -10.7 63 GLY 79.6 32.9 -179.9 64 VAL -133.7 167.2 -179.7 -59.9 65 GLN -92.1 -26.0 -179.1 -55.1 173.6 153.3 66 GLU -168.8 172.1 178.3 55.2 174.6 78.3 67 PHE -159.9 164.7 -179.7 68.0 85.0 68 SER -110.6 133.3 179.1 179.4 69 VAL -72.1 -7.4 178.6 -28.7 70 LYS -86.0 9.3 177.4 -89.7 175.9 173.4 175.4 71 GLU -128.0 70.6 -179.3 -67.7 170.5 -20.0 72 PRO -50.9 -40.5 -179.0 -27.3 42.2 73 ARG -60.7 -49.8 -179.5 -163.3 -134.1 49.4 139.8 74 ARG -63.4 -36.8 -180.0 178.9 174.2 178.9 50.9 75 LEU -61.0 -52.3 179.6 177.5 67.4 76 TYR -58.3 -32.7 179.8 -65.5 -57.2 77 ALA -68.8 -37.5 179.7 78 MET -68.1 -37.5 178.1 -58.1 -169.0 -73.9 79 ILE -68.0 -47.8 -179.6 -75.4 168.1 80 SER -57.5 -44.2 178.1 -63.9 81 ARG -69.2 3.6 178.9 43.6 -171.4 174.7 63.1 82 ASN -120.5 26.6 177.2 -84.6 -76.4 83 LEU -117.8 117.9 179.2 -58.5 171.1 84 VAL -67.0 -24.1 177.6 18.1 85 SER -150.8 120.6 -179.9 45.0 86 ALA -89.1 11.9 179.9 87 ASN -158.5 102.1 178.6 -159.8 -12.0 88 VAL -105.4 130.6 0.0 -174.7 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLU 57.209 4.072 24.729 2 LYS 53.506 4.739 25.413 3 LEU 52.023 8.004 24.267 4 VAL 50.309 10.368 26.678 5 GLN 47.928 13.175 25.944 6 PRO 48.408 16.236 28.198 7 THR 45.443 18.437 29.268 8 PRO 45.025 21.818 27.492 9 LEU 47.043 23.727 30.147 10 LEU 49.954 21.320 30.285 11 LEU 49.865 21.315 26.462 12 SER 50.170 25.111 26.291 13 LEU 53.250 25.111 28.520 14 LEU 55.021 22.415 26.504 15 LYS 54.138 24.243 23.252 16 SER 55.546 27.495 24.595 17 ALA 58.709 25.571 25.439 18 GLY 59.034 24.593 21.778 19 ALA 57.049 21.334 21.549 20 GLN 55.283 20.805 18.215 21 LYS 53.138 17.741 18.877 22 GLU 49.973 17.070 20.829 23 THR 51.038 13.565 21.885 24 PHE 54.433 12.746 23.452 25 THR 56.210 10.061 25.450 26 MET 56.817 10.814 29.157 27 LYS 60.457 11.560 28.342 28 GLU 59.407 14.315 25.922 29 VAL 56.988 15.750 28.477 30 ILE 59.835 15.807 31.048 31 TYR 62.276 17.261 28.527 32 HIS 59.903 20.040 27.498 33 LEU 58.987 20.860 31.096 34 GLY 62.662 21.408 32.019 35 GLN 62.950 23.804 29.068 36 TYR 59.875 25.732 30.260 37 ILE 61.339 26.044 33.757 38 MET 64.684 27.021 32.264 39 ALA 63.270 29.641 29.891 40 LYS 61.094 31.220 32.574 41 GLN 63.888 30.903 35.186 42 LEU 61.522 29.529 37.849 43 TYR 64.255 27.588 39.666 44 ASP 66.077 29.001 42.671 45 GLU 69.330 30.889 42.118 46 LYS 71.035 29.266 45.145 47 GLN 69.182 25.991 45.739 48 GLN 68.647 25.045 42.112 49 HIS 66.564 21.963 42.893 50 ILE 63.708 24.193 44.131 51 VAL 61.276 25.498 41.506 52 HIS 59.097 28.450 42.499 53 CYS 55.824 28.601 40.570 54 SER 53.590 30.741 42.785 55 ASN 52.850 33.339 40.087 56 ASP 53.242 31.181 36.989 57 PRO 50.731 28.904 35.172 58 LEU 52.860 25.931 36.284 59 GLY 51.652 26.718 39.800 60 GLU 48.054 26.702 38.611 61 LEU 48.669 23.440 36.821 62 PHE 50.379 21.631 39.693 63 GLY 48.560 23.545 42.397 64 VAL 51.697 24.201 44.504 65 GLN 53.864 27.246 45.314 66 GLU 57.016 25.299 44.657 67 PHE 58.558 21.857 44.441 68 SER 61.942 20.115 44.541 69 VAL 63.306 18.236 41.565 70 LYS 64.800 16.090 44.323 71 GLU 61.359 14.590 45.026 72 PRO 60.706 12.608 41.781 73 ARG 57.643 10.827 43.138 74 ARG 55.538 13.931 43.883 75 LEU 56.518 15.414 40.508 76 TYR 55.352 12.426 38.492 77 ALA 52.047 12.446 40.365 78 MET 51.402 16.063 39.470 79 ILE 52.131 15.322 35.770 80 SER 49.979 12.159 35.789 81 ARG 46.848 13.824 37.117 82 ASN 47.306 16.067 34.071 83 LEU 47.246 13.510 31.238 84 VAL 43.785 12.949 29.753 85 SER 45.225 9.649 28.520 86 ALA 48.399 7.915 29.693 87 ASN 48.029 5.627 26.717 88 VAL 47.117 7.193 23.386 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S S S/H H H H 10 H H H H H H H H/S S S 20 S S S S S/H H H H H H 30 H H H H H H H H H H 40 H C C T T T T C S S 50 S S S S C H H H H H 60 H H H C C S S S S C 70 H H H H H H H H H H 80 H H H C C S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 B E E h H H H 10 H H H H H H h T t 20 S B h H H H H H 30 H H H H H H H H H H 40 h t B S S t T e E 50 E E e T T h H H H H 60 H H h t e E E E e T 70 h H H H H H H H H H 80 h e E E E S Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLU 34.2 24.7 79.4 2 LYS 49.9 28.8 83.9 3 LEU 84.7 57.3 65.2 4 VAL 113.6 95.7 40.0 5 GLN 80.9 54.5 64.8 6 PRO 124.5 100.0 39.3 7 THR 72.4 67.7 56.9 8 PRO 16.0 12.8 76.2 9 LEU 83.3 56.4 61.3 10 LEU 147.8 100.0 31.0 11 LEU 123.0 83.2 53.7 12 SER 30.8 36.8 67.1 13 LEU 138.9 94.0 43.6 14 LEU 147.8 100.0 30.5 15 LYS 109.2 63.0 70.2 16 SER 27.7 33.1 74.7 17 ALA 66.6 91.7 62.3 18 GLY 0.6 1.7 85.2 19 ALA 71.2 98.1 50.8 20 GLN 5.5 3.7 86.0 21 LYS 85.6 49.4 72.8 22 GLU 49.9 36.0 68.9 23 THR 77.7 72.7 44.9 24 PHE 166.5 99.8 39.6 25 THR 84.2 78.8 61.8 26 MET 102.4 64.2 45.7 27 LYS 21.4 12.3 86.1 28 GLU 85.3 61.5 62.6 29 VAL 118.8 100.0 25.5 30 ILE 88.4 61.6 53.9 31 TYR 55.0 30.4 78.5 32 HIS 122.8 81.8 44.4 33 LEU 143.2 96.9 27.7 34 GLY 5.1 14.7 74.6 35 GLN 79.2 53.3 66.8 36 TYR 175.3 96.9 40.8 37 ILE 122.0 85.0 36.3 38 MET 61.6 38.6 79.9 39 ALA 14.2 19.6 78.9 40 LYS 88.7 51.1 66.4 41 GLN 51.1 34.4 79.9 42 LEU 124.5 84.2 51.8 43 TYR 146.0 80.7 60.8 44 ASP 80.8 73.1 55.7 45 GLU 29.7 21.5 78.0 46 LYS 37.1 21.4 85.2 47 GLN 48.3 32.5 69.5 48 GLN 55.8 37.6 76.8 49 HIS 111.9 74.5 57.5 50 ILE 104.5 72.8 63.3 51 VAL 117.2 98.7 32.4 52 HIS 80.4 53.5 71.8 53 CYS 98.7 99.5 43.6 54 SER 39.0 46.6 73.1 55 ASN 0.0 0.0 85.8 56 ASP 102.7 93.0 46.3 57 PRO 73.2 58.8 62.7 58 LEU 147.8 100.0 21.8 59 GLY 32.8 94.3 69.9 60 GLU 25.1 18.1 79.6 61 LEU 143.5 97.1 40.7 62 PHE 166.8 100.0 33.3 63 GLY 6.2 17.8 82.1 64 VAL 97.8 82.3 60.7 65 GLN 20.5 13.8 78.5 66 GLU 73.7 53.2 61.1 67 PHE 151.3 90.7 33.3 68 SER 67.9 81.2 55.6 69 VAL 51.4 43.3 60.8 70 LYS 39.4 22.7 75.7 71 GLU 40.8 29.4 73.4 72 PRO 50.8 40.8 71.5 73 ARG 23.7 11.3 80.2 74 ARG 113.7 54.4 69.1 75 LEU 124.2 84.0 37.9 76 TYR 79.9 44.1 59.5 77 ALA 31.0 42.7 77.3 78 MET 159.1 99.8 43.7 79 ILE 143.2 99.8 25.2 80 SER 32.3 38.6 68.0 81 ARG 103.1 49.3 79.3 82 ASN 102.8 85.1 58.3 83 LEU 142.1 96.1 43.9 84 VAL 49.1 41.4 73.5 85 SER 55.2 66.0 70.3 86 ALA 23.3 32.1 63.7 87 ASN 42.0 34.8 75.7 88 VAL 78.3 65.9 74.7