Protein Data Bank File : 1cdb Title : T LYMPHOCYTE ADHESION GLYCOPROTEIN 15-SEP-93 1CDB Number of Amino Acid Residues : 105 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 LYS GLU ILE THR ASN ALA LEU GLU THR TRP 10 GLY ALA LEU GLY GLN ASP ILE ASN LEU ASP 20 ILE PRO SER PHE GLN MET SER ASP ASP ILE 30 ASP ASP ILE LYS TRP GLU LYS THR SER ASP 40 LYS LYS LYS ILE ALA GLN PHE ARG LYS GLU 50 LYS GLU THR PHE LYS GLU LYS ASP THR TYR 60 LYS LEU PHE LYS ASN GLY THR LEU LYS ILE 70 LYS HIS LEU LYS THR ASP ASP GLN ASP ILE 80 TYR LYS VAL SER ILE TYR ASP THR LYS GLY 90 LYS ASN VAL LEU GLU LYS ILE PHE ASP LEU 100 LYS ILE GLN GLU ARG Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 LYS 0.0 130.9 174.8 70.0 -177.5 -178.1 75.4 2 GLU -75.5 117.8 -167.4 63.2 -177.8 84.8 3 ILE -92.1 122.9 -176.3 -48.4 171.3 4 THR -76.6 169.5 168.4 -31.2 5 ASN -106.2 57.8 -167.8 -173.2 -113.4 6 ALA -123.8 151.9 172.0 7 LEU -103.1 122.7 167.0 -56.9 -178.6 8 GLU -75.8 116.4 -156.8 -69.7 -70.3 89.3 9 THR -131.0 104.6 -151.6 -70.6 10 TRP -104.6 149.7 172.4 -73.7 103.0 11 GLY -172.0 126.6 173.1 12 ALA -68.4 163.9 -172.6 13 LEU -55.9 130.5 177.0 -84.0 71.2 14 GLY 78.4 64.9 178.7 15 GLN -153.4 163.4 176.6 75.5 -173.6 67.1 16 ASP -92.4 127.7 170.1 -174.2 85.2 17 ILE -136.5 147.3 172.1 -84.3 135.9 18 ASN -101.6 145.6 168.2 -69.7 36.9 19 LEU -104.3 110.3 -158.3 -84.9 173.2 20 ASP -138.7 123.4 -174.0 56.3 -89.2 21 ILE -85.3 158.5 175.8 70.5 -73.2 22 PRO -64.9 170.1 -176.6 26.3 -36.1 23 SER -82.8 39.9 176.3 -59.6 24 PHE -53.6 141.7 -176.0 -170.8 76.8 25 GLN -64.2 143.5 179.5 65.6 179.7 98.3 26 MET -123.6 129.1 178.3 61.3 -175.3 179.7 27 SER -90.2 -72.5 -173.1 -63.6 28 ASP -156.3 104.2 168.7 -58.7 -72.9 29 ASP 95.0 107.1 172.7 -64.6 75.9 30 ILE -144.2 129.7 -171.8 37.5 64.2 31 ASP -136.5 -57.3 -167.8 -156.6 -66.9 32 ASP -87.3 137.8 174.3 -177.4 -49.1 33 ILE -133.5 111.2 -177.9 -64.3 88.2 34 LYS -109.5 137.2 171.9 169.3 177.5 -72.5 78.6 35 TRP -125.8 112.5 -171.9 -72.5 92.5 36 GLU -122.7 174.4 -176.5 61.6 176.9 -75.8 37 LYS -95.2 152.3 172.8 -61.7 -176.9 -172.3 -72.8 38 THR -86.2 -55.4 -179.2 63.4 39 SER -61.7 -43.1 172.1 -170.5 40 ASP -83.0 -31.6 -166.8 -61.8 85.2 41 LYS 64.9 69.7 -160.2 -159.9 -172.8 -65.1 -175.5 42 LYS -149.7 114.3 177.0 -168.5 -177.1 -178.0 -176.1 43 LYS -71.4 88.0 -179.4 48.4 -173.0 172.0 -73.1 44 ILE -72.3 -47.1 162.8 -170.3 161.4 45 ALA -136.3 153.4 -178.7 46 GLN -160.4 148.4 -173.7 61.7 93.3 -10.2 47 PHE -121.3 144.3 164.7 -94.2 68.4 48 ARG -148.5 -117.5 -158.4 -168.4 -178.2 174.1 -169.9 49 LYS -137.2 62.6 -166.2 -166.9 -179.9 73.3 -83.5 50 GLU 50.6 37.9 -177.8 -54.8 -68.3 -89.7 51 LYS -155.8 108.8 -169.2 50.2 -173.8 -67.1 85.6 52 GLU 52.5 84.8 -180.0 -65.2 -179.5 89.1 53 THR -121.2 102.5 172.6 -58.8 54 PHE -88.3 126.7 -169.1 -52.2 -24.1 55 LYS -147.8 -28.8 168.8 51.2 78.6 76.7 -78.7 56 GLU 57.6 -145.1 -179.5 68.7 174.5 73.2 57 LYS -88.1 167.2 179.5 74.7 -161.8 78.5 176.8 58 ASP -58.8 -30.1 171.2 -52.3 -73.4 59 THR -56.6 -22.8 167.1 73.2 60 TYR -149.9 99.8 -171.6 -119.5 -79.6 61 LYS -147.6 122.2 -162.8 -175.9 -92.9 -76.6 78.4 62 LEU -96.2 124.1 -179.2 -12.6 -168.7 63 PHE -65.7 151.8 -172.0 -165.4 75.1 64 LYS -72.3 -49.7 173.9 -62.7 178.3 -68.6 -70.8 65 ASN -52.9 -44.3 170.9 -62.9 44.3 66 GLY 149.1 78.6 -177.2 67 THR -158.5 179.7 168.5 -90.5 68 LEU -139.0 150.8 172.0 -171.6 146.8 69 LYS -130.4 114.8 171.1 -61.6 -162.4 93.4 -67.6 70 ILE -92.5 103.6 -174.7 -47.3 176.2 71 LYS -107.0 103.5 -170.5 -65.2 -175.1 -179.0 176.1 72 HIS 76.1 105.6 171.1 -53.3 95.7 73 LEU -106.5 -171.9 179.3 70.2 81.3 74 LYS 178.3 -176.1 170.0 -89.3 166.6 68.8 177.7 75 THR -63.0 -42.0 173.1 -49.4 76 ASP -77.5 -23.5 167.7 -164.5 84.2 77 ASP -67.0 -22.5 -171.1 -73.2 83.5 78 GLN -100.7 172.4 173.5 61.3 64.9 -79.5 79 ASP -159.5 172.5 162.8 -145.9 74.4 80 ILE -80.0 140.2 -178.6 -58.5 73.7 81 TYR -123.9 163.0 158.3 -78.5 -85.6 82 LYS -139.0 127.7 169.1 176.1 177.5 179.6 175.9 83 VAL -79.1 144.8 163.0 73.2 84 SER -140.4 133.5 -173.9 -48.6 85 ILE -117.3 132.6 -176.1 -65.7 175.7 86 TYR -129.1 154.0 -171.9 -48.0 82.3 87 ASP -80.1 -175.2 160.8 -62.9 -56.8 88 THR -57.2 -39.1 165.0 87.9 89 LYS -71.1 -33.4 -175.4 -63.4 -170.3 -177.4 -178.0 90 GLY 97.6 70.0 -178.9 91 LYS -137.3 127.6 -162.5 -69.4 -61.1 -68.3 81.3 92 ASN -76.3 114.8 -174.1 2.8 98.2 93 VAL -104.0 -86.4 -172.4 -88.4 94 LEU -94.4 118.2 179.9 -157.6 -68.6 95 GLU -131.5 132.6 -168.9 -69.1 -176.3 -71.7 96 LYS -163.9 144.0 -174.0 -174.4 -173.6 175.5 79.2 97 ILE -92.8 152.6 -170.0 -44.7 174.9 98 PHE -151.8 168.8 -177.5 -82.4 -90.1 99 ASP -156.6 106.8 162.5 -72.7 79.7 100 LEU -74.6 116.6 -180.0 -160.6 -56.2 101 LYS -119.3 158.6 -175.7 -72.2 -91.2 68.7 65.1 102 ILE -108.8 129.4 176.6 -57.4 -64.6 103 GLN -64.1 143.7 178.3 -78.4 -81.3 -44.7 104 GLU -135.6 88.8 -169.6 47.4 -177.7 61.7 105 ARG -140.2 -77.3 0.0 -166.3 -178.6 74.8 -175.1 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 LYS 18.503 -2.561 -19.595 2 GLU 16.220 0.437 -18.654 3 ILE 16.635 0.806 -14.816 4 THR 13.365 1.432 -12.821 5 ASN 12.674 3.575 -9.666 6 ALA 11.310 0.487 -7.852 7 LEU 11.713 -1.548 -4.600 8 GLU 12.049 -5.354 -4.947 9 THR 9.706 -6.348 -2.104 10 TRP 9.930 -10.071 -1.230 11 GLY 7.793 -12.988 0.145 12 ALA 7.617 -16.851 -0.233 13 LEU 4.207 -18.654 -0.953 14 GLY 1.503 -18.154 1.795 15 GLN 2.458 -15.062 3.959 16 ASP 1.469 -11.532 5.249 17 ILE 3.280 -8.386 3.818 18 ASN 2.321 -4.622 3.971 19 LEU 2.752 -2.051 1.070 20 ASP 3.936 1.013 3.031 21 ILE 5.228 4.455 1.845 22 PRO 8.094 6.687 3.451 23 SER 7.640 9.386 6.172 24 PHE 7.392 12.342 3.649 25 GLN 6.322 15.810 5.032 26 MET 2.624 16.993 5.103 27 SER 1.491 20.708 5.100 28 ASP -2.413 20.932 5.060 29 ASP -4.773 18.148 3.707 30 ILE -3.800 14.518 2.695 31 ASP -6.486 11.725 2.120 32 ASP -6.206 9.212 -0.855 33 ILE -3.696 6.279 -1.078 34 LYS -3.913 4.291 -4.403 35 TRP -2.078 1.035 -5.323 36 GLU -2.360 0.353 -9.116 37 LYS -0.548 -1.909 -11.775 38 THR 2.579 -1.073 -13.975 39 SER 2.151 -3.574 -16.969 40 ASP -1.698 -2.989 -17.367 41 LYS -1.884 0.680 -15.934 42 LYS -4.889 -0.337 -13.739 43 LYS -6.267 0.881 -10.330 44 ILE -6.889 -2.548 -8.624 45 ALA -7.586 -0.998 -5.127 46 GLN -7.696 2.712 -4.031 47 PHE -8.809 4.759 -0.962 48 ARG -10.332 8.237 -0.362 49 LYS -13.200 9.693 1.840 50 GLU -16.427 7.522 1.509 51 LYS -16.457 8.388 -2.308 52 GLU -15.182 5.810 -4.825 53 THR -13.361 3.260 -2.516 54 PHE -12.096 0.116 -4.373 55 LYS -11.023 -2.457 -1.668 56 GLU -12.032 -6.121 -2.653 57 LYS -11.024 -9.189 -0.428 58 ASP -8.506 -9.360 2.554 59 THR -5.665 -10.843 0.333 60 TYR -5.227 -7.287 -1.228 61 LYS -6.902 -4.550 0.948 62 LEU -5.503 -0.993 1.456 63 PHE -5.435 0.668 4.999 64 LYS -7.159 4.091 5.560 65 ASN -4.341 6.227 7.245 66 GLY -1.974 5.197 4.375 67 THR -0.843 1.514 4.173 68 LEU -1.730 -1.858 2.524 69 LYS -2.256 -5.407 3.981 70 ILE -1.705 -8.512 1.745 71 LYS -3.249 -11.190 4.129 72 HIS -2.247 -14.696 2.782 73 LEU -0.242 -14.644 -0.516 74 LYS 0.981 -17.198 -3.113 75 THR 2.225 -16.692 -6.773 76 ASP -1.400 -15.981 -8.019 77 ASP -2.186 -13.618 -4.995 78 GLN 0.687 -11.120 -6.019 79 ASP 1.556 -8.425 -8.690 80 ILE 3.939 -5.529 -9.697 81 TYR 2.701 -2.106 -8.215 82 LYS 3.031 1.711 -8.446 83 VAL 1.709 3.960 -5.575 84 SER 0.077 7.386 -6.222 85 ILE -1.079 9.642 -3.300 86 TYR -3.710 12.450 -3.741 87 ASP -4.988 15.134 -1.237 88 THR -8.495 15.904 0.295 89 LYS -8.929 18.101 -2.897 90 GLY -7.218 15.413 -5.195 91 LYS -3.713 16.711 -6.209 92 ASN -0.881 14.205 -6.997 93 VAL 1.860 14.449 -4.253 94 LEU 3.963 11.246 -3.596 95 GLU 4.359 8.825 -6.622 96 LYS 6.859 5.837 -6.605 97 ILE 7.280 2.359 -8.311 98 PHE 7.141 -1.053 -6.371 99 ASP 7.130 -4.936 -6.952 100 LEU 5.627 -7.860 -4.825 101 LYS 7.999 -10.774 -5.862 102 ILE 8.171 -14.520 -4.796 103 GLN 11.314 -16.130 -3.177 104 GLU 13.083 -19.110 -4.900 105 ARG 15.413 -20.596 -2.241 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 S S/S S S S/S 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/T T T T 40 S S S S S/S S S S/T T T 50 T/S S S S S S S/T T T T/S 60 S S S/T T T T S S S S 70 S S C T T T T C S S 80 S S S S S S S/T T T T/S 90 S S S S/S S S S S/S S S 100 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 E 10 e S S B 20 S 30 E E E E E S S S 40 S E E E S S 50 S S B t T T t 60 B t T T T t B B 70 S t T T T t e E 80 E E E E E E S S 90 e E E E E E E 100 E Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 LYS 9.4 5.4 86.8 2 GLU 0.0 0.0 90.4 3 ILE 24.8 17.3 90.3 4 THR 40.1 37.5 66.9 5 ASN 20.5 17.0 73.7 6 ALA 65.3 89.9 59.7 7 LEU 57.0 38.6 72.6 8 GLU 65.2 47.0 67.1 9 THR 79.3 74.2 52.2 10 TRP 104.9 51.1 74.3 11 GLY 32.6 93.6 54.6 12 ALA 28.8 39.6 71.0 13 LEU 65.1 44.0 65.3 14 GLY 14.7 42.4 67.6 15 GLN 75.0 50.5 65.9 16 ASP 57.5 52.0 76.1 17 ILE 114.1 79.5 54.9 18 ASN 77.9 64.4 60.9 19 LEU 146.0 98.8 31.9 20 ASP 37.4 33.8 75.3 21 ILE 120.7 84.1 41.5 22 PRO 56.5 45.3 61.7 23 SER 0.0 0.0 88.2 24 PHE 60.0 36.0 67.9 25 GLN 5.5 3.7 84.2 26 MET 40.5 25.4 74.7 27 SER 8.3 9.9 87.7 28 ASP 4.3 3.9 87.6 29 ASP 41.0 37.1 73.2 30 ILE 76.4 53.3 59.1 31 ASP 86.2 78.0 53.4 32 ASP 102.3 92.6 55.3 33 ILE 132.9 92.6 58.5 34 LYS 151.0 87.1 53.7 35 TRP 204.8 99.9 29.5 36 GLU 109.7 79.1 57.7 37 LYS 145.0 83.6 60.9 38 THR 71.1 66.5 55.8 39 SER 1.8 2.1 88.0 40 ASP 36.6 33.1 64.9 41 LYS 14.4 8.3 90.3 42 LYS 47.9 27.6 74.2 43 LYS 67.0 38.6 64.2 44 ILE 97.4 67.9 68.7 45 ALA 71.8 98.9 48.6 46 GLN 136.7 92.0 45.6 47 PHE 149.2 89.4 56.1 48 ARG 148.1 70.9 70.4 49 LYS 77.2 44.5 74.7 50 GLU 0.0 0.0 91.1 51 LYS 64.2 37.0 84.7 52 GLU 14.4 10.4 84.3 53 THR 80.0 74.9 61.2 54 PHE 85.3 51.1 71.2 55 LYS 83.8 48.3 63.0 56 GLU 74.5 53.8 64.6 57 LYS 32.6 18.8 85.8 58 ASP 28.6 25.9 71.8 59 THR 68.9 64.5 68.7 60 TYR 171.4 94.7 44.7 61 LYS 128.4 74.0 69.7 62 LEU 147.0 99.4 45.0 63 PHE 73.8 44.3 70.0 64 LYS 26.2 15.1 77.3 65 ASN 5.4 4.5 76.8 66 GLY 31.4 90.1 52.2 67 THR 77.3 72.3 58.0 68 LEU 147.8 100.0 35.7 69 LYS 113.9 65.7 68.3 70 ILE 143.5 100.0 41.1 71 LYS 97.3 56.1 72.5 72 HIS 10.6 7.1 82.2 73 LEU 147.8 100.0 39.5 74 LYS 56.0 32.3 70.0 75 THR 32.1 30.0 62.8 76 ASP 0.0 0.0 87.8 77 ASP 75.7 68.5 64.9 78 GLN 126.7 85.2 51.5 79 ASP 72.8 65.9 65.6 80 ILE 82.4 57.4 75.5 81 TYR 178.0 98.3 38.8 82 LYS 98.2 56.6 60.4 83 VAL 118.8 100.0 37.7 84 SER 80.9 96.7 56.7 85 ILE 127.8 89.1 39.1 86 TYR 135.4 74.8 65.6 87 ASP 88.8 80.4 53.2 88 THR 72.4 67.7 64.9 89 LYS 7.8 4.5 85.3 90 GLY 23.1 66.4 65.2 91 LYS 41.8 24.1 81.9 92 ASN 50.1 41.4 73.3 93 VAL 68.9 58.0 65.5 94 LEU 114.7 77.6 36.2 95 GLU 77.7 56.0 69.0 96 LYS 117.6 67.8 51.7 97 ILE 101.1 70.4 48.1 98 PHE 161.4 96.8 40.5 99 ASP 91.0 82.3 53.8 100 LEU 147.8 100.0 39.7 101 LYS 116.2 67.0 62.8 102 ILE 126.6 88.2 54.0 103 GLN 87.3 58.8 53.3 104 GLU 0.0 0.0 89.9 105 ARG 12.8 6.1 94.5