Protein Data Bank File : 1qb3c Title : CELL CYCLE 30-APR-99 1QB3 Number of Amino Acid Residues : 109 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 HIS ALA PHE GLN GLY ARG LYS LEU THR ASP 10 GLN GLU ARG ALA ARG VAL LEU GLU PHE GLN 20 ASP SER ILE HIS TYR SER PRO ARG TYR SER 30 ASP ASP ASN TYR GLU TYR ARG HIS VAL MET 40 LEU PRO LYS ALA MET LEU LYS VAL ILE PRO 50 SER ASP TYR PHE ASN SER GLU VAL GLY THR 60 LEU ARG ILE LEU THR GLU ASP GLU TRP ARG 70 GLY LEU GLY ILE THR GLN SER LEU GLY TRP 80 GLU HIS TYR GLU CYS HIS ALA PRO GLU PRO 90 HIS ILE LEU LEU PHE LYS ARG PRO LEU ASN 100 TYR GLU ALA GLU LEU ARG ALA ALA THR Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 HIS 0.0 -30.4 -179.3 0.0 0.0 2 ALA 64.8 62.5 179.9 3 PHE -11.4 126.9 179.4 -158.2 83.9 4 GLN -112.6 106.5 -179.3 174.0 -177.6 -71.1 5 GLY 132.6 -156.7 179.6 6 ARG -105.0 87.3 -178.5 -155.9 -124.4 87.3 -162.5 7 LYS -50.7 145.1 179.1 -171.8 -179.5 169.5 170.8 8 LEU -79.7 150.1 178.9 -65.3 174.3 9 THR -76.6 159.4 -179.2 65.8 10 ASP -49.3 -37.0 178.3 -66.9 -43.2 11 GLN -72.4 -51.6 -178.2 -93.4 144.4 157.7 12 GLU -48.6 -50.7 -178.9 -69.3 174.8 -40.8 13 ARG -55.1 -57.3 -177.2 169.9 73.5 172.2 -176.1 14 ALA -59.5 -17.4 178.4 15 ARG -91.1 -44.3 -179.1 -113.6 -117.3 77.6 175.0 16 VAL -60.2 -41.7 -180.0 179.0 17 LEU -52.3 -10.6 179.4 -83.1 -176.7 18 GLU -61.0 -43.2 -178.7 179.1 -177.8 -44.7 19 PHE -83.3 -10.5 -177.6 -57.5 -83.0 20 GLN -38.0 -63.3 -179.0 176.5 156.6 64.2 21 ASP -57.5 1.7 -177.0 -65.0 -25.2 22 SER -126.0 7.3 175.1 -38.1 23 ILE -75.4 134.6 -177.4 -60.8 -155.7 24 HIS -114.1 138.2 -178.3 -176.5 -100.2 25 TYR -112.3 124.4 179.3 -52.4 97.3 26 SER -72.9 169.8 179.6 68.7 27 PRO -80.5 159.5 -179.4 -20.1 41.6 28 ARG -80.5 159.7 178.6 -58.9 173.8 -70.6 157.7 29 TYR -153.0 162.4 -177.9 50.2 92.2 30 SER -153.0 177.5 177.3 50.0 31 ASP -138.9 -167.0 -180.0 55.3 -2.2 32 ASP -75.9 47.2 178.6 -81.4 42.7 33 ASN 179.2 -27.3 -178.4 -156.0 -41.5 34 TYR -137.1 168.9 177.5 -94.4 -74.8 35 GLU -122.0 133.3 -176.5 -151.0 -174.8 -175.2 36 TYR -127.4 154.4 176.7 -59.9 -74.7 37 ARG -171.1 169.0 177.3 86.7 118.5 52.6 96.8 38 HIS -141.2 149.6 178.4 59.1 -86.2 39 VAL -108.7 125.2 -179.5 -172.5 40 MET -103.3 111.3 -178.9 177.1 179.9 -115.0 41 LEU -86.7 144.9 178.7 -55.0 177.8 42 PRO -69.3 123.5 -177.4 31.2 -45.1 43 LYS -37.9 -48.9 177.0 -54.1 -164.7 170.2 160.4 44 ALA -38.7 -48.2 -179.6 45 MET -54.7 -31.3 178.7 175.2 176.7 -175.9 46 LEU -57.4 -42.5 -179.4 -98.5 175.1 47 LYS -61.7 -22.1 177.1 -61.6 -172.3 -167.9 62.2 48 VAL -106.8 19.0 178.0 -42.0 49 ILE -98.6 130.9 179.7 -74.6 172.9 50 PRO -44.7 151.5 -179.2 -36.9 40.3 51 SER -77.8 -18.8 179.4 65.2 52 ASP -76.6 -4.0 179.9 55.3 -57.4 53 TYR -93.8 9.8 -178.2 -89.2 49.1 54 PHE -120.3 153.4 178.9 -78.3 -92.8 55 ASN -94.0 99.8 -178.9 -163.7 -75.0 56 SER -52.3 -29.9 -179.7 59.7 57 GLU -75.6 -20.8 -176.0 -57.8 20.3 -105.3 58 VAL -122.0 -33.9 -177.5 -159.1 59 GLY 94.9 3.9 179.0 60 THR -101.5 178.2 179.9 36.8 61 LEU -81.7 139.2 178.0 -69.4 168.1 62 ARG -71.4 173.0 179.5 57.6 164.6 175.4 100.6 63 ILE -62.4 139.8 179.6 -65.0 -63.2 64 LEU -113.6 135.4 176.4 -66.0 -173.3 65 THR -71.8 166.1 -179.5 79.0 66 GLU -63.6 -44.8 178.6 172.0 167.5 11.8 67 ASP -52.4 -43.7 179.4 -69.0 -42.9 68 GLU -59.2 -62.7 -177.4 -72.8 178.4 -9.4 69 TRP -61.8 -21.9 177.7 60.7 -112.0 70 ARG -72.8 -35.8 -179.5 -68.2 -91.6 175.7 -168.5 71 GLY -57.5 -40.4 179.4 72 LEU -69.5 -2.9 -178.4 -60.7 176.0 73 GLY 91.9 1.9 176.6 74 ILE -74.9 131.4 -179.4 -60.0 170.6 75 THR -138.5 128.2 179.4 73.9 76 GLN -153.6 168.4 -179.6 28.1 -178.6 23.7 77 SER -59.1 177.4 -176.2 61.2 78 LEU -70.5 160.3 176.9 -75.2 161.4 79 GLY 71.9 12.6 179.0 80 TRP -83.1 131.3 179.2 -79.9 113.4 81 GLU -109.3 130.8 179.9 -70.3 -179.4 51.0 82 HIS -86.4 121.5 178.0 167.1 47.1 83 TYR -123.0 154.6 -176.1 59.9 -61.7 84 GLU -71.1 -46.9 -178.5 -79.1 162.5 -48.9 85 CYS -147.3 164.2 -175.3 -167.0 86 HIS -124.3 73.0 178.4 -162.3 -51.6 87 ALA -38.7 145.4 -179.6 88 PRO -81.7 179.9 179.3 41.5 -44.8 89 GLU -66.0 148.4 -179.6 -31.4 -150.9 -39.0 90 PRO -45.6 -30.5 -178.7 27.7 -43.4 91 HIS -80.7 -7.4 179.7 57.6 114.9 92 ILE -105.6 108.5 177.8 -59.5 176.0 93 LEU -95.5 141.0 178.3 -66.1 56.4 94 LEU -101.5 137.6 179.0 -60.7 -168.7 95 PHE -134.0 151.9 178.4 -69.7 -84.6 96 LYS -149.3 153.7 173.9 66.7 -176.4 166.3 50.8 97 ARG -141.0 140.4 179.6 43.2 142.2 87.6 116.5 98 PRO -63.9 129.7 -179.5 24.7 -42.1 99 LEU -47.3 -20.7 178.1 -75.5 160.9 100 ASN -111.8 42.6 179.9 66.1 -56.4 101 TYR -67.4 -24.8 178.3 76.8 -82.7 102 GLU -51.9 -53.9 -179.3 -60.9 -71.1 67.4 103 ALA -60.4 -68.4 -179.1 104 GLU -37.9 -33.5 -178.1 -68.7 166.1 35.4 105 LEU -83.1 -23.6 178.6 -171.4 28.6 106 ARG -76.0 -47.9 178.5 -147.3 129.9 46.3 -164.2 107 ALA -47.5 -41.8 -179.8 108 ALA -85.2 58.0 176.8 109 THR 174.8 50.2 0.0 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 HIS 31.141 -36.454 144.806 2 ALA 31.939 -33.093 146.419 3 PHE 29.936 -31.001 143.937 4 GLN 31.936 -29.484 141.114 5 GLY 30.532 -26.136 139.926 6 ARG 28.034 -23.689 141.413 7 LYS 25.495 -25.872 143.192 8 LEU 21.943 -24.547 143.038 9 THR 20.261 -23.332 146.229 10 ASP 17.401 -25.290 147.648 11 GLN 14.948 -22.860 146.089 12 GLU 16.704 -22.759 142.763 13 ARG 16.632 -26.509 142.745 14 ALA 13.003 -26.913 143.735 15 ARG 11.942 -24.603 140.998 16 VAL 13.921 -25.948 138.054 17 LEU 12.837 -29.423 138.895 18 GLU 9.405 -28.302 137.733 19 PHE 10.441 -28.894 134.105 20 GLN 12.354 -32.141 134.553 21 ASP 9.680 -34.470 133.151 22 SER 9.493 -32.337 129.971 23 ILE 13.199 -32.175 129.115 24 HIS 13.758 -33.976 125.791 25 TYR 16.641 -36.160 124.662 26 SER 17.545 -36.652 121.040 27 PRO 18.671 -40.013 119.768 28 ARG 22.438 -40.576 119.719 29 TYR 24.478 -40.359 116.555 30 SER 28.216 -40.672 115.968 31 ASP 31.237 -40.404 113.725 32 ASP 34.679 -42.049 113.572 33 ASN 35.554 -40.827 117.046 34 TYR 32.555 -39.649 119.067 35 GLU 28.998 -40.262 120.147 36 TYR 26.562 -37.335 120.002 37 ARG 23.149 -36.108 121.201 38 HIS 21.337 -33.058 122.464 39 VAL 18.952 -32.180 125.214 40 MET 16.112 -29.746 124.404 41 LEU 14.770 -27.875 127.462 42 PRO 11.260 -26.457 127.442 43 LYS 11.946 -22.681 127.062 44 ALA 9.930 -21.720 130.163 45 MET 12.659 -23.571 132.068 46 LEU 15.234 -21.190 130.686 47 LYS 13.539 -18.426 132.714 48 VAL 14.088 -20.309 135.973 49 ILE 17.801 -21.227 135.437 50 PRO 20.187 -19.009 137.508 51 SER 21.786 -16.245 135.526 52 ASP 25.297 -17.284 136.477 53 TYR 24.573 -20.428 134.409 54 PHE 24.517 -18.162 131.386 55 ASN 26.964 -16.666 128.943 56 SER 26.083 -12.967 129.207 57 GLU 27.645 -12.187 125.758 58 VAL 25.456 -14.678 123.912 59 GLY 22.377 -15.553 125.969 60 THR 23.125 -19.274 125.830 61 LEU 24.284 -21.496 128.679 62 ARG 27.940 -21.361 129.741 63 ILE 29.714 -24.717 129.852 64 LEU 28.254 -26.837 132.587 65 THR 30.160 -29.348 134.706 66 GLU 28.268 -32.640 134.993 67 ASP 27.214 -31.996 138.593 68 GLU 25.775 -28.741 137.322 69 TRP 23.747 -30.090 134.431 70 ARG 22.660 -33.031 136.601 71 GLY 21.581 -30.329 139.008 72 LEU 19.154 -28.846 136.486 73 GLY 17.393 -32.207 136.405 74 ILE 18.920 -33.214 133.055 75 THR 19.647 -36.897 133.415 76 GLN 21.528 -39.334 131.276 77 SER 24.029 -42.202 131.497 78 LEU 27.667 -41.821 132.224 79 GLY 30.489 -40.097 130.503 80 TRP 28.464 -37.469 128.727 81 GLU 30.307 -34.139 128.194 82 HIS 28.458 -30.779 127.686 83 TYR 30.062 -28.684 124.916 84 GLU 29.107 -25.231 123.575 85 CYS 29.067 -25.579 119.869 86 HIS 29.631 -28.040 117.057 87 ALA 31.657 -26.535 114.220 88 PRO 30.788 -28.162 110.853 89 GLU 32.886 -30.258 108.424 90 PRO 35.802 -28.452 106.738 91 HIS 34.203 -27.976 103.316 92 ILE 31.411 -25.960 104.870 93 LEU 32.355 -22.385 105.747 94 LEU 30.162 -20.121 107.960 95 PHE 29.533 -16.386 107.353 96 LYS 27.589 -13.621 109.069 97 ARG 26.931 -9.948 108.715 98 PRO 25.457 -7.621 111.300 99 LEU 21.854 -6.731 110.445 100 ASN 22.826 -3.065 110.311 101 TYR 25.802 -3.387 107.877 102 GLU 24.175 -0.673 105.732 103 ALA 25.075 1.792 108.457 104 GLU 28.563 0.803 109.616 105 LEU 29.275 1.195 105.867 106 ARG 27.479 4.499 105.574 107 ALA 29.711 5.800 108.422 108 ALA 32.483 4.770 106.127 109 THR 31.707 7.184 103.247 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C S S S S/S S S S S/H H 10 H H H H H H H H T T 20 T T/S S S S S S S S S 30 S S C S S S S S S S 40 S S/H H H H H 3 3 3 T 50 T T T C T T T T S S 60 S S S C H H H H H H 70 H H H/S S S S S C S S 80 S S S S/S S S S S S C 90 S S S S S S S S S H 100 H H H H H H H H H Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S h H 10 H H H H H H h G g G 20 G G g E E e E E 30 e S S e E E e E E 40 h H H H H h G g g 50 G G G B t T T T t S 60 B h H H H H H 70 H h T t t T T t 80 S t T 90 T t t T h 100 H H H H H H H h t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 HIS 83.2 55.4 92.9 2 ALA 0.0 0.0 89.1 3 PHE 121.6 72.9 61.5 4 GLN 29.7 20.0 79.6 5 GLY 21.5 61.7 59.3 6 ARG 131.5 63.0 66.4 7 LYS 43.2 24.9 75.5 8 LEU 144.0 97.4 44.1 9 THR 37.0 34.6 80.1 10 ASP 0.0 0.0 85.0 11 GLN 3.7 2.5 86.5 12 GLU 94.3 68.0 56.0 13 ARG 112.6 53.9 62.1 14 ALA 16.8 23.2 73.5 15 ARG 93.9 45.0 71.8 16 VAL 118.8 100.0 41.4 17 LEU 106.8 72.2 70.0 18 GLU 49.2 35.5 79.2 19 PHE 144.8 86.8 50.3 20 GLN 91.2 61.4 61.9 21 ASP 0.0 0.0 86.8 22 SER 27.8 33.2 72.4 23 ILE 143.0 99.7 45.1 24 HIS 39.9 26.5 73.8 25 TYR 129.0 71.3 66.1 26 SER 78.3 93.7 50.7 27 PRO 14.0 11.3 84.4 28 ARG 81.4 39.0 76.8 29 TYR 72.8 40.2 76.3 30 SER 40.5 48.5 63.8 31 ASP 45.3 41.0 74.1 32 ASP 0.0 0.0 85.9 33 ASN 13.5 11.2 81.7 34 TYR 56.5 31.2 81.8 35 GLU 69.3 50.0 61.6 36 TYR 147.3 81.4 52.6 37 ARG 173.7 83.1 51.5 38 HIS 44.6 29.7 70.3 39 VAL 104.6 88.0 44.4 40 MET 25.8 16.2 82.3 41 LEU 133.5 90.3 30.9 42 PRO 86.0 69.1 55.0 43 LYS 11.1 6.4 86.6 44 ALA 29.7 40.9 64.5 45 MET 159.4 100.0 30.7 46 LEU 81.4 55.1 52.1 47 LYS 24.3 14.0 82.7 48 VAL 98.2 82.7 59.5 49 ILE 143.5 100.0 26.0 50 PRO 108.1 86.9 54.6 51 SER 1.8 2.1 81.6 52 ASP 52.4 47.4 68.7 53 TYR 180.4 99.7 39.7 54 PHE 131.1 78.6 57.1 55 ASN 78.5 64.9 68.3 56 SER 11.7 14.0 87.5 57 GLU 21.1 15.2 87.8 58 VAL 40.1 33.7 79.2 59 GLY 3.2 9.1 78.9 60 THR 28.0 26.2 69.6 61 LEU 119.4 80.8 40.9 62 ARG 145.7 69.8 69.9 63 ILE 75.2 52.4 72.3 64 LEU 145.2 98.3 39.7 65 THR 72.9 68.2 70.2 66 GLU 85.4 61.6 68.8 67 ASP 76.1 68.8 49.6 68 GLU 137.1 98.9 53.4 69 TRP 196.5 95.8 48.2 70 ARG 143.2 68.5 63.7 71 GLY 20.8 59.7 72.4 72 LEU 147.8 100.0 25.9 73 GLY 34.3 98.4 63.4 74 ILE 127.3 88.7 33.1 75 THR 44.4 41.5 76.1 76 GLN 119.8 80.6 48.3 77 SER 10.0 12.0 83.4 78 LEU 13.7 9.3 91.1 79 GLY 0.0 0.0 81.0 80 TRP 171.8 83.8 64.8 81 GLU 14.3 10.3 88.2 82 HIS 98.7 65.7 62.2 83 TYR 95.2 52.6 67.2 84 GLU 63.0 45.4 70.5 85 CYS 9.7 9.8 79.9 86 HIS 71.8 47.8 69.4 87 ALA 6.0 8.2 75.5 88 PRO 81.4 65.4 56.9 89 GLU 34.3 24.7 69.1 90 PRO 9.3 7.5 81.8 91 HIS 35.0 23.3 71.6 92 ILE 67.2 46.8 65.4 93 LEU 43.4 29.4 76.9 94 LEU 35.7 24.2 72.4 95 PHE 24.7 14.8 80.6 96 LYS 0.3 0.2 86.9 97 ARG 67.7 32.4 69.0 98 PRO 56.6 45.5 77.5 99 LEU 0.0 0.0 91.5 100 ASN 43.3 35.8 70.7 101 TYR 106.5 58.8 69.5 102 GLU 50.8 36.7 75.3 103 ALA 36.4 50.2 75.7 104 GLU 47.5 34.3 72.7 105 LEU 38.4 26.0 78.1 106 ARG 50.9 24.3 77.6 107 ALA 6.0 8.3 82.0 108 ALA 17.9 24.7 75.5 109 THR 41.9 39.2 81.7