Protein Data Bank File : 1tul Title : TELOKIN-LIKE PROTEIN 17-AUG-96 1TUL Number of Amino Acid Residues : 102 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLY THR PRO ASP ILE ILE VAL ASN ALA GLN 10 ILE ASN SER GLU ASP GLU ASN VAL LEU ASP 20 PHE ILE ILE GLU ASP GLU TYR TYR LEU LYS 30 LYS ARG GLY VAL GLY ALA HIS ILE ILE LYS 40 VAL ALA SER SER PRO GLN LEU ARG LEU LEU 50 TYR LYS ASN ALA TYR SER THR VAL SER CYS 60 GLY ASN TYR GLY VAL LEU CYS ASN LEU VAL 70 GLN ASN GLY GLU TYR ASP LEU ASN ALA ILE 80 MET PHE ASN CYS ALA GLU ILE LYS LEU ASN 90 LYS GLY GLN MET LEU PHE GLN THR LYS ILE 100 TRP ARG Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLY 0.0 97.0 -179.0 2 THR -57.4 144.3 178.4 89.4 3 PRO -71.6 150.1 177.5 0.6 4.5 4 ASP -67.6 150.5 175.4 -63.3 -15.7 5 ILE -91.5 130.4 -177.2 -67.1 139.5 6 ILE -105.4 128.1 178.0 -64.4 155.1 7 VAL -129.8 162.1 178.2 -62.3 8 ASN -131.6 132.9 -179.5 -67.6 -72.2 9 ALA -84.7 136.1 177.8 10 GLN -138.3 150.5 177.0 -64.7 -175.8 179.3 11 ILE -75.2 131.3 -179.7 -45.3 -129.6 12 ASN -61.6 142.3 -179.1 -169.5 -88.9 13 SER -65.0 -38.0 -177.3 -81.9 14 GLU -86.3 -41.6 -177.2 -108.3 85.0 -69.3 15 ASP -126.6 116.4 -178.7 -168.0 -15.1 16 GLU -65.5 -11.6 179.6 38.4 162.9 8.8 17 ASN -102.1 18.5 177.6 -68.7 -47.3 18 VAL -126.4 129.4 175.8 174.0 19 LEU -107.9 128.5 176.6 -69.1 172.6 20 ASP -93.1 141.4 178.3 -63.8 -18.7 21 PHE -118.3 103.2 -175.1 -69.8 84.8 22 ILE -94.0 137.2 179.8 -79.3 65.4 23 ILE -67.9 124.3 -176.9 -67.9 140.7 24 GLU -76.9 -42.2 -179.8 -167.5 -180.0 -80.3 25 ASP -135.8 153.3 178.0 -54.7 -59.2 26 GLU -56.7 137.3 -179.0 169.8 175.6 -47.7 27 TYR -142.8 109.4 -178.0 -163.8 -84.0 28 TYR -121.2 125.7 180.0 -92.8 57.4 29 LEU -146.6 107.9 178.6 177.6 68.8 30 LYS -82.9 99.0 -177.7 156.7 -160.0 -54.1 162.3 31 LYS -110.8 170.6 -179.4 148.9 171.2 -99.2 165.5 32 ARG -127.5 114.9 179.0 24.5 108.8 -175.9 -106.5 33 GLY 95.2 176.8 179.6 34 VAL -77.2 115.9 -179.7 172.2 35 GLY -115.1 159.8 179.6 36 ALA -111.2 129.4 -178.7 37 HIS -129.9 128.0 -178.7 -52.8 -99.8 38 ILE -74.0 132.2 178.5 -71.3 -178.8 39 ILE -106.9 129.5 178.1 -69.7 154.8 40 LYS -96.6 106.8 -178.8 -176.3 -156.9 -142.3 104.7 41 VAL -95.4 117.1 178.9 -176.6 42 ALA -63.4 137.7 179.8 43 SER -65.7 135.0 176.5 -45.5 44 SER -152.8 148.6 -178.3 72.2 45 PRO -55.5 -37.4 179.9 11.7 -12.9 46 GLN -52.1 -26.2 -175.7 -63.2 84.2 -85.9 47 LEU -65.2 -20.0 -176.6 -64.8 -179.9 48 ARG -55.8 -28.9 -178.8 -148.5 172.3 93.6 90.8 49 LEU -57.7 -29.0 -177.7 -79.7 91.4 50 LEU -74.1 -15.3 -177.7 -68.4 -177.3 51 TYR -99.5 -0.4 -179.1 -70.6 79.3 52 LYS -103.7 -20.2 -176.6 -74.9 -1.6 -163.0 156.7 53 ASN -153.8 165.7 175.5 -55.1 94.8 54 ALA -63.4 163.4 -179.9 55 TYR -157.2 162.8 177.6 72.9 -87.4 56 SER -127.1 135.2 178.1 -61.3 57 THR -84.5 131.3 180.0 -59.0 58 VAL -112.2 126.6 178.3 -176.8 59 SER -90.4 138.5 -178.5 176.4 60 CYS -97.8 15.9 179.9 -55.1 61 GLY -171.3 -153.9 -177.0 62 ASN -89.8 62.8 -178.9 -159.4 -151.0 63 TYR -165.1 169.1 179.1 46.9 77.5 64 GLY -120.5 151.6 -179.8 65 VAL -127.9 132.9 176.9 173.1 66 LEU -105.5 117.3 178.4 163.6 69.4 67 CYS -111.2 144.2 176.9 -59.1 68 ASN -137.0 143.8 174.6 -92.5 -177.7 69 LEU -74.6 168.4 178.3 -59.0 179.3 70 VAL -113.9 142.9 -176.5 -36.4 71 GLN -55.3 -50.8 -178.0 -157.0 -174.4 -160.5 72 ASN -83.0 109.3 175.4 -135.9 -154.3 73 GLY 75.9 154.5 -176.1 74 GLU -99.7 17.3 -178.0 -40.7 -147.2 -37.0 75 TYR -123.4 21.8 178.7 -48.8 -60.9 76 ASP -134.0 167.5 178.7 -75.3 -71.8 77 LEU -156.0 142.5 175.3 -168.8 74.0 78 ASN -101.4 142.1 179.0 -81.4 -0.7 79 ALA -155.7 140.8 178.5 80 ILE -129.2 135.0 178.3 -54.1 -175.9 81 MET -104.8 134.6 176.1 167.5 -177.7 83.2 82 PHE -113.6 101.8 -177.8 -54.9 88.0 83 ASN -80.3 140.4 178.8 67.7 -75.5 84 CYS -97.0 -42.4 -179.8 -60.3 85 ALA -113.4 -159.5 176.7 86 GLU -78.6 147.8 -177.6 59.9 166.1 -24.4 87 ILE -88.6 110.5 177.7 -40.9 178.3 88 LYS -129.4 78.9 -179.1 128.4 -164.3 -174.6 175.4 89 LEU -102.6 121.1 178.3 -45.4 161.4 90 ASN -89.0 151.4 178.4 -55.5 93.8 91 LYS -58.7 137.8 178.0 165.1 164.0 -174.3 81.1 92 GLY 81.6 -4.2 177.6 93 GLN -74.9 149.4 176.9 -177.2 160.9 -33.6 94 MET -86.3 124.0 -178.3 -167.3 165.9 -52.7 95 LEU -87.3 -48.1 179.8 -171.2 64.2 96 PHE -161.8 170.9 178.4 72.8 -89.7 97 GLN -135.5 156.7 174.1 -43.5 174.0 -68.9 98 THR -125.1 124.3 178.4 57.8 99 LYS -101.2 121.3 -176.0 158.8 109.1 -99.3 -22.0 100 ILE -95.2 127.2 -179.3 -65.0 124.0 101 TRP -95.2 100.0 -179.9 -49.2 99.9 102 ARG -77.2 -21.3 0.0 -80.2 -179.5 130.9 136.7 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLY 44.855 49.411 2.852 2 THR 42.609 52.234 1.657 3 PRO 43.235 55.708 2.860 4 ASP 40.761 57.207 5.335 5 ILE 38.029 59.619 4.286 6 ILE 38.418 62.948 6.070 7 VAL 35.550 65.063 7.260 8 ASN 35.012 68.208 9.252 9 ALA 31.975 68.965 11.313 10 GLN 30.068 72.211 10.837 11 ILE 26.900 73.540 12.235 12 ASN 24.122 73.344 9.764 13 SER 23.068 76.681 8.431 14 GLU 19.295 76.095 8.766 15 ASP 19.073 74.010 11.879 16 GLU 21.334 74.574 14.820 17 ASN 20.612 70.993 15.942 18 VAL 22.163 69.490 12.874 19 LEU 25.843 68.912 12.290 20 ASP 27.048 68.691 8.760 21 PHE 30.107 66.550 7.978 22 ILE 32.058 67.910 4.947 23 ILE 34.516 66.031 2.773 24 GLU 37.937 67.548 3.140 25 ASP 39.517 66.124 0.049 26 GLU 38.353 64.396 -3.136 27 TYR 37.998 60.651 -2.728 28 TYR 37.199 58.469 -5.590 29 LEU 37.116 54.860 -5.346 30 LYS 35.603 52.549 -7.876 31 LYS 34.968 49.503 -5.714 32 ARG 32.985 46.273 -6.092 33 GLY 30.512 45.180 -3.446 34 VAL 29.705 46.538 -0.052 35 GLY 32.899 47.878 1.493 36 ALA 33.737 49.403 4.810 37 HIS 35.681 52.661 4.885 38 ILE 37.036 54.311 7.869 39 ILE 36.047 57.888 8.201 40 LYS 38.358 60.280 9.944 41 VAL 36.468 62.944 11.891 42 ALA 38.522 65.912 12.901 43 SER 38.181 66.875 16.568 44 SER 36.155 70.013 17.002 45 PRO 34.386 71.735 19.808 46 GLN 30.977 71.505 17.924 47 LEU 31.098 67.741 18.489 48 ARG 30.259 68.208 22.087 49 LEU 26.642 68.462 21.128 50 LEU 26.591 64.725 20.340 51 TYR 27.409 63.907 23.878 52 LYS 24.472 65.872 25.326 53 ASN 21.455 64.299 23.551 54 ALA 20.219 61.472 21.405 55 TYR 20.826 61.803 17.668 56 SER 20.132 60.269 14.314 57 THR 22.652 59.748 11.526 58 VAL 21.561 61.004 8.104 59 SER 23.214 59.616 4.968 60 CYS 23.827 62.006 1.995 61 GLY 23.937 59.312 -0.574 62 ASN 24.002 55.677 -1.470 63 TYR 25.810 54.371 1.518 64 GLY 25.332 53.900 5.175 65 VAL 27.291 55.467 7.965 66 LEU 27.921 54.054 11.411 67 CYS 28.766 56.651 14.176 68 ASN 29.808 55.926 17.696 69 LEU 30.586 58.338 20.511 70 VAL 34.086 57.904 22.098 71 GLN 34.688 57.098 25.739 72 ASN 37.249 59.785 26.253 73 GLY 36.112 63.347 25.791 74 GLU 33.357 65.171 23.936 75 TYR 35.193 66.393 20.878 76 ASP 35.600 63.254 18.919 77 LEU 33.614 60.841 16.927 78 ASN 34.139 57.422 15.327 79 ALA 32.614 56.710 11.952 80 ILE 32.680 53.987 9.342 81 MET 31.189 54.225 5.901 82 PHE 29.510 51.261 4.118 83 ASN 29.390 51.976 0.452 84 CYS 26.758 50.547 -1.732 85 ALA 28.029 51.802 -5.090 86 GLU 31.330 53.174 -6.412 87 ILE 32.875 55.984 -4.338 88 LYS 32.892 59.388 -6.070 89 LEU 33.195 61.982 -3.274 90 ASN 34.037 65.510 -4.089 91 LYS 35.884 67.867 -1.904 92 GLY 33.514 70.034 0.036 93 GLN 30.740 67.525 -0.484 94 MET 28.514 66.675 2.483 95 LEU 28.998 63.083 3.535 96 PHE 26.574 62.875 6.304 97 GLN 24.732 64.712 9.064 98 THR 23.724 64.054 12.604 99 LYS 20.382 65.370 13.816 100 ILE 20.273 65.951 17.548 101 TRP 17.063 65.412 19.449 102 ARG 16.949 67.981 22.174 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 10 S T T T T C S S S S 20 S S S S S/S S S S S S/S 30 S S S/S S S S S S S S 40 S S S C C H H H 3 3 50 3 C S S S S S S S S 60 S S S S S S S S S S 70 S C C C S S S S S S 80 S S S S S/S S S S/S S S 90 S S S S S/S S S S S S 100 S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 E E E E E E 10 E e S S t T e E E E 20 E E E e S E E E 30 S E E E E E E 40 E e g G G G G G G 50 G g t E E E E E E e 60 S e E E E E E E 70 S S S S E E E 80 E E E e S E E E t 90 T T e E E E E E E E 100 E Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLY 0.0 0.0 93.5 2 THR 56.4 52.8 68.4 3 PRO 26.0 20.9 81.2 4 ASP 65.8 59.6 64.7 5 ILE 142.1 99.0 29.6 6 ILE 93.2 65.0 67.6 7 VAL 118.8 100.0 34.8 8 ASN 72.3 59.8 62.0 9 ALA 72.6 100.0 44.9 10 GLN 54.4 36.6 70.1 11 ILE 77.1 53.7 60.6 12 ASN 98.4 81.4 66.5 13 SER 3.7 4.4 91.5 14 GLU 4.4 3.2 85.4 15 ASP 61.5 55.7 59.8 16 GLU 24.7 17.8 86.6 17 ASN 92.0 76.1 62.0 18 VAL 103.7 87.3 56.5 19 LEU 147.4 99.7 37.5 20 ASP 99.8 90.3 48.7 21 PHE 166.8 100.0 30.3 22 ILE 113.5 79.1 62.7 23 ILE 143.4 99.9 44.9 24 GLU 72.3 52.2 75.6 25 ASP 44.0 39.9 70.9 26 GLU 47.5 34.3 70.5 27 TYR 157.0 86.7 46.5 28 TYR 105.0 58.0 67.4 29 LEU 95.8 64.8 57.9 30 LYS 21.6 12.5 87.2 31 LYS 121.2 69.9 63.8 32 ARG 0.0 0.0 90.4 33 GLY 0.0 0.0 83.3 34 VAL 40.2 33.8 72.7 35 GLY 27.9 80.1 69.1 36 ALA 32.3 44.5 59.8 37 HIS 147.7 98.3 50.2 38 ILE 40.8 28.5 77.1 39 ILE 143.5 100.0 34.6 40 LYS 58.0 33.5 71.6 41 VAL 118.8 100.0 45.2 42 ALA 35.8 49.3 78.7 43 SER 37.7 45.1 78.0 44 SER 64.9 77.6 59.3 45 PRO 31.6 25.4 74.5 46 GLN 101.0 67.9 49.1 47 LEU 147.8 100.0 46.7 48 ARG 97.4 46.6 70.3 49 LEU 112.6 76.2 54.4 50 LEU 147.8 100.0 30.0 51 TYR 164.1 90.6 57.9 52 LYS 91.5 52.8 84.9 53 ASN 83.3 68.9 69.8 54 ALA 9.2 12.6 73.0 55 TYR 153.0 84.5 50.9 56 SER 36.7 43.9 69.0 57 THR 85.8 80.3 52.3 58 VAL 59.9 50.4 72.1 59 SER 62.7 74.9 63.0 60 CYS 72.4 73.0 65.7 61 GLY 10.8 31.1 72.4 62 ASN 31.0 25.7 65.7 63 TYR 163.4 90.3 50.3 64 GLY 6.5 18.6 65.1 65 VAL 118.8 100.0 33.7 66 LEU 61.0 41.3 69.4 67 CYS 98.7 99.5 43.3 68 ASN 43.7 36.1 73.6 69 LEU 90.2 61.0 56.6 70 VAL 91.5 77.0 73.1 71 GLN 0.0 0.0 88.8 72 ASN 0.0 0.0 86.2 73 GLY 3.7 10.7 75.3 74 GLU 92.7 66.9 53.3 75 TYR 75.5 41.7 65.7 76 ASP 61.0 55.2 66.2 77 LEU 147.8 100.0 31.2 78 ASN 32.5 26.9 73.4 79 ALA 72.1 99.4 38.6 80 ILE 83.6 58.3 53.2 81 MET 158.2 99.3 25.4 82 PHE 94.7 56.8 55.3 83 ASN 116.6 96.4 50.1 84 CYS 51.5 51.9 75.3 85 ALA 24.3 33.5 82.0 86 GLU 57.7 41.6 66.2 87 ILE 137.0 95.5 40.8 88 LYS 48.3 27.9 75.7 89 LEU 141.4 95.7 37.2 90 ASN 56.3 46.6 73.4 91 LYS 53.7 31.0 77.1 92 GLY 11.7 33.6 66.5 93 GLN 87.2 58.7 69.1 94 MET 102.1 64.0 62.6 95 LEU 147.8 100.0 24.2 96 PHE 166.8 100.0 21.6 97 GLN 113.5 76.4 46.1 98 THR 106.9 100.0 30.8 99 LYS 133.9 77.2 48.9 100 ILE 143.0 99.6 46.0 101 TRP 77.1 37.6 73.1 102 ARG 93.1 44.6 80.0