Protein Data Bank File : 1awo Title : KINASE 03-OCT-97 1AWO Number of Amino Acid Residues : 57 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 SER LEU PHE VAL ALA LEU TYR ASP PHE VAL 10 ALA SER GLY ASP ASN THR LEU SER ILE THR 20 LYS GLY GLU LYS LEU ARG VAL LEU GLY TYR 30 ASN HIS ASN GLY GLU TRP CYS GLU ALA GLN 40 THR LYS ASN GLY GLN GLY TRP VAL PRO SER 50 ASN TYR ILE THR PRO VAL SER Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 SER 0.0 180.0 180.0 -180.0 2 LEU -98.5 150.2 -180.0 -56.6 -50.9 3 PHE -115.9 153.7 180.0 -29.6 81.6 4 VAL -118.3 162.5 180.0 -91.3 5 ALA -69.0 132.2 180.0 6 LEU -113.1 -79.3 180.0 159.5 73.9 7 TYR -79.9 163.9 -180.0 -79.6 -47.4 8 ASP -87.6 176.7 -180.0 82.0 -52.4 9 PHE -136.5 167.3 180.0 -154.6 -81.0 10 VAL -127.2 143.2 180.0 177.8 11 ALA -53.5 158.6 180.0 12 SER -149.1 -58.0 180.0 164.0 13 GLY -164.4 -155.3 180.0 14 ASP -93.6 60.1 180.0 -149.4 50.2 15 ASN -163.5 -43.4 -180.0 -46.1 -76.3 16 THR -69.6 173.9 180.0 -121.5 17 LEU -134.0 117.5 -180.0 -146.7 171.3 18 SER -93.6 111.9 180.0 -67.2 19 ILE -130.6 -177.7 -180.0 2.4 72.8 20 THR -106.6 170.1 -180.0 -40.0 21 LYS -72.6 161.6 180.0 46.3 -100.2 -132.7 150.5 22 GLY 37.7 30.1 180.0 23 GLU -83.2 160.6 -180.0 -157.5 129.6 83.4 24 LYS -81.0 84.4 -180.0 173.7 -109.5 -140.7 72.7 25 LEU -140.5 113.8 -180.0 161.7 166.3 26 ARG -118.1 146.3 -180.0 164.0 -179.3 150.9 -85.7 27 VAL -70.6 134.8 180.0 177.8 28 LEU -107.3 -40.3 -180.0 -109.8 -169.9 29 GLY -138.1 166.8 -180.0 30 TYR -120.3 174.9 180.0 -35.9 -55.2 31 ASN -92.6 21.9 -180.0 85.9 100.8 32 HIS 69.3 36.7 180.0 -140.8 -171.9 33 ASN -177.0 -175.4 -180.0 -132.2 -39.0 34 GLY -106.3 54.7 180.0 35 GLU -120.3 -66.9 180.0 -72.2 92.5 89.6 36 TRP -135.3 156.3 -180.0 -76.3 60.6 37 CYS -136.0 141.0 180.0 -41.0 38 GLU -81.2 134.9 180.0 -158.7 -119.9 -89.0 39 ALA -134.3 163.1 -180.0 40 GLN -115.9 161.7 -180.0 -42.9 165.0 -34.0 41 THR -135.5 146.0 -180.0 41.1 42 LYS -56.6 -21.9 -180.0 -124.1 146.4 78.1 155.8 43 ASN -86.8 -40.1 180.0 166.0 69.1 44 GLY -171.6 -131.3 180.0 45 GLN -148.7 178.7 180.0 -100.2 153.4 10.8 46 GLY 158.1 -177.5 -180.0 47 TRP -88.5 155.3 -180.0 -91.0 92.0 48 VAL -147.4 123.5 180.0 -34.0 49 PRO -75.0 145.5 -180.0 18.7 -14.1 50 SER -68.9 -19.2 -180.0 25.8 51 ASN -75.4 -11.3 -180.0 -126.9 103.7 52 TYR -105.6 -10.1 180.0 -88.6 54.5 53 ILE -127.8 143.2 -179.9 -57.9 128.3 54 THR -123.3 160.1 180.0 141.5 55 PRO -75.0 168.8 -180.0 18.7 -14.0 56 VAL -83.6 4.7 180.0 178.2 57 SER -148.8 -100.0 0.0 -167.1 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 SER 2.073 0.000 -1.245 2 LEU 5.801 0.000 -1.899 3 PHE 8.049 3.015 -1.472 4 VAL 11.109 4.147 -3.391 5 ALA 14.199 6.088 -2.388 6 LEU 13.665 9.830 -2.568 7 TYR 16.169 11.863 -0.587 8 ASP 19.803 10.936 -0.080 9 PHE 21.489 9.876 3.139 10 VAL 24.754 10.368 4.989 11 ALA 26.959 7.822 6.717 12 SER 26.646 7.536 10.478 13 GLY 27.754 4.159 11.780 14 ASP 27.347 0.418 11.379 15 ASN 23.572 0.577 11.165 16 THR 22.612 3.459 8.905 17 LEU 22.541 3.255 5.127 18 SER 24.285 5.786 2.918 19 ILE 22.582 6.043 -0.452 20 THR 21.930 8.633 -3.134 21 LYS 18.853 10.642 -4.044 22 GLY 16.253 9.285 -6.436 23 GLU 18.229 6.085 -6.005 24 LYS 16.816 2.613 -6.525 25 LEU 16.085 1.790 -2.904 26 ARG 12.807 0.280 -1.764 27 VAL 11.744 -0.775 1.712 28 LEU 11.663 -4.529 2.187 29 GLY 10.872 -4.735 5.883 30 TYR 9.817 -2.504 8.753 31 ASN 10.712 -2.064 12.405 32 HIS 7.281 -3.392 13.299 33 ASN 5.926 0.140 13.412 34 GLY 5.682 3.433 11.561 35 GLU 9.069 4.812 12.539 36 TRP 11.879 3.293 10.509 37 CYS 12.078 0.535 7.925 38 GLU 14.995 -1.645 6.894 39 ALA 16.102 -1.388 3.284 40 GLN 18.840 -2.859 1.125 41 THR 21.275 -1.331 -1.338 42 LYS 23.033 -2.646 -4.421 43 ASN 26.151 -1.588 -2.553 44 GLY 25.147 -3.165 0.738 45 GLN 22.473 -2.731 3.382 46 GLY 21.422 -0.573 6.309 47 TRP 18.541 1.245 7.957 48 VAL 16.431 3.783 6.104 49 PRO 14.001 6.326 7.569 50 SER 10.546 6.641 6.056 51 ASN 11.125 10.382 6.098 52 TYR 13.782 9.736 3.480 53 ILE 11.641 7.428 1.379 54 THR 8.225 8.010 -0.142 55 PRO 5.502 5.752 -1.558 56 VAL 4.834 5.230 -5.247 57 SER 1.516 6.949 -4.644 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S S S/S S S S 10 S S S C S S S S S S 20 S C S S S S S S/S S S 30 S C C C S S S S S S 40 S/T T T T S S S S S/T T 50 T T/S S S S S/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 e E E E e S 10 S S S B t 20 T T t S e E E E E 30 e S S S e E E E E E 40 e S S e E E E E E e 50 T e E E E e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 SER 31.4 37.5 69.8 2 LEU 63.9 43.3 71.6 3 PHE 108.8 65.2 53.3 4 VAL 50.6 42.6 65.0 5 ALA 71.5 98.5 53.2 6 LEU 72.8 49.2 61.4 7 TYR 49.4 27.3 72.5 8 ASP 59.2 53.6 64.2 9 PHE 149.0 89.3 49.4 10 VAL 10.4 8.7 82.4 11 ALA 12.3 16.9 76.3 12 SER 22.5 26.9 76.8 13 GLY 5.4 15.5 85.9 14 ASP 0.0 0.0 89.2 15 ASN 16.4 13.5 80.2 16 THR 91.1 85.2 58.4 17 LEU 142.9 96.7 53.4 18 SER 49.7 59.5 56.6 19 ILE 126.2 87.9 44.9 20 THR 39.7 37.1 66.6 21 LYS 43.3 25.0 76.9 22 GLY 1.6 4.6 81.4 23 GLU 76.6 55.3 66.5 24 LYS 27.8 16.0 80.7 25 LEU 146.2 98.9 34.8 26 ARG 119.7 57.3 58.0 27 VAL 115.9 97.6 33.4 28 LEU 75.4 51.0 85.3 29 GLY 8.2 23.6 65.1 30 TYR 80.9 44.7 68.1 31 ASN 84.3 69.8 60.5 32 HIS 0.0 0.0 88.0 33 ASN 35.3 29.2 87.7 34 GLY 0.0 0.0 83.2 35 GLU 56.4 40.7 78.8 36 TRP 101.0 49.2 58.1 37 CYS 86.0 86.7 46.8 38 GLU 70.8 51.1 62.4 39 ALA 72.6 100.0 45.4 40 GLN 80.2 53.9 64.1 41 THR 102.1 95.5 44.1 42 LYS 20.7 11.9 85.0 43 ASN 5.1 4.2 84.3 44 GLY 6.0 17.2 83.8 45 GLN 62.7 42.2 77.5 46 GLY 23.2 66.7 61.3 47 TRP 116.5 56.8 54.5 48 VAL 118.3 99.6 28.9 49 PRO 118.9 95.5 34.5 50 SER 39.0 46.7 70.5 51 ASN 0.2 0.2 81.1 52 TYR 101.9 56.3 56.1 53 ILE 139.3 97.1 39.6 54 THR 64.3 60.2 50.2 55 PRO 72.1 57.9 64.8 56 VAL 39.4 33.2 70.0 57 SER 7.9 9.5 84.8