Protein Data Bank File : 1kjs Title : CELL ADHESION 09-JAN-97 1KJS Number of Amino Acid Residues : 74 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 MET LEU GLN LYS LYS ILE GLU GLU ILE ALA 10 ALA LYS TYR LYS HIS SER VAL VAL LYS LYS 20 CYS CYS TYR ASP GLY ALA CYS VAL ASN ASN 30 ASP GLU THR CYS GLU GLN ARG ALA ALA ARG 40 ILE SER LEU GLY PRO ARG CYS ILE LYS ALA 50 PHE THR GLU CYS CYS VAL VAL ALA SER GLN 60 LEU ARG ALA ASN ILE SER HIS LYS ASP MET 70 GLN LEU GLY ARG Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 MET 0.0 69.6 178.7 -84.1 66.1 122.2 2 LEU -71.6 4.2 -179.2 -166.1 75.3 3 GLN 175.5 61.9 -179.0 69.6 -144.0 138.3 4 LYS -96.1 -54.7 -179.6 -131.4 -80.3 91.3 70.3 5 LYS -76.1 -15.1 -178.6 100.3 172.8 -59.6 -150.6 6 ILE -97.8 -33.7 178.5 -45.8 -78.0 7 GLU -75.2 -22.9 179.6 74.5 86.4 51.3 8 GLU -78.0 -45.9 179.8 73.9 178.5 33.8 9 ILE -70.8 -28.4 179.0 -158.2 -59.5 10 ALA -70.1 -50.6 -179.7 11 ALA -65.0 -31.0 -179.5 12 LYS -86.9 43.6 178.9 66.2 106.4 105.8 -135.8 13 TYR -107.4 144.9 179.6 -89.9 -47.7 14 LYS -83.6 40.5 -179.2 70.5 -162.6 -57.2 -62.7 15 HIS -173.9 106.4 -179.6 -116.6 94.0 16 SER -39.9 -43.6 -178.8 -58.0 17 VAL -61.5 -41.0 180.0 -170.6 18 VAL -51.5 -22.0 179.7 -170.0 19 LYS -60.7 -53.8 179.8 -143.7 -163.0 -74.0 -152.4 20 LYS -60.5 -45.5 -179.7 167.1 114.9 53.0 121.9 21 CYS -50.9 -49.7 179.3 -71.3 22 CYS -69.9 -25.2 179.3 159.9 23 TYR -58.8 -55.7 179.2 -115.8 -68.0 24 ASP -63.5 -46.5 179.3 -40.4 -53.6 25 GLY -40.9 -56.8 178.7 26 ALA -61.5 -38.5 180.0 27 CYS -86.7 15.5 -179.2 -50.5 28 VAL -28.3 147.2 -179.9 43.6 29 ASN -47.4 -56.7 -179.6 -117.8 93.0 30 ASN -167.9 -62.1 -178.8 174.4 95.8 31 ASP -107.5 -165.2 -179.5 -133.0 42.9 32 GLU -36.7 -76.0 -179.3 -95.2 -70.3 18.3 33 THR -44.2 85.4 179.4 150.7 34 CYS -81.0 -83.8 177.8 -8.4 35 GLU -61.4 -23.6 177.4 -129.6 -71.6 -23.7 36 GLN -60.9 -46.9 177.1 -93.5 -129.1 -131.0 37 ARG -58.5 -35.2 178.3 -97.4 -89.8 -141.3 -151.5 38 ALA -48.8 -70.3 179.3 39 ALA 177.9 -40.0 179.8 40 ARG 178.5 114.7 -179.4 -110.3 -173.1 113.1 -127.8 41 ILE -53.3 92.4 179.4 -171.9 61.6 42 SER -136.0 50.9 178.5 86.8 43 LEU -119.2 -5.2 179.4 -65.3 137.7 44 GLY 149.3 169.7 179.7 45 PRO -79.8 -58.4 179.4 24.2 -23.1 46 ARG -49.4 -24.6 179.5 79.5 -72.6 -66.4 -119.5 47 CYS -66.5 -57.7 -178.4 -129.6 48 ILE -36.0 -62.7 -178.4 -86.6 63.6 49 LYS -82.2 -22.0 179.8 -94.0 -119.0 144.9 -176.0 50 ALA -72.2 -62.2 179.2 51 PHE -63.9 -47.4 -178.6 94.6 74.6 52 THR -54.2 -45.4 -179.7 -68.8 53 GLU -62.7 -59.1 -179.5 172.9 47.5 -69.2 54 CYS -56.5 -28.3 -179.4 -90.3 55 CYS -80.7 -27.4 179.3 145.7 56 VAL -79.4 -48.3 178.0 -178.4 57 VAL -62.4 -42.8 177.0 -59.3 58 ALA -63.1 -28.3 179.9 59 SER -63.6 -41.7 -179.8 -155.6 60 GLN -77.8 -27.3 179.9 -120.0 156.9 107.7 61 LEU -71.2 -34.1 179.9 -73.1 -166.1 62 ARG -100.1 -10.2 -179.9 69.2 164.9 88.0 -125.5 63 ALA -100.5 54.5 180.0 64 ASN 179.9 -32.3 -179.7 -175.5 -22.3 65 ILE -113.1 -166.8 -179.8 -31.3 -56.1 66 SER -172.7 30.7 -179.8 -125.5 67 HIS -145.4 -145.2 180.0 -140.2 -137.9 68 LYS -37.1 -51.3 179.4 -88.4 -179.1 176.7 -150.2 69 ASP -61.3 -58.7 180.0 -127.2 -76.9 70 MET -70.1 -72.2 -179.8 -165.4 -76.6 -136.8 71 GLN -39.3 -36.2 180.0 -169.0 143.8 -148.5 72 LEU -111.3 -77.7 179.6 -111.5 57.8 73 GLY -40.6 -28.1 179.9 74 ARG 60.1 -147.0 0.0 -56.3 -129.6 161.3 160.5 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 MET 55.855 -9.320 -8.467 2 LEU 53.562 -6.626 -7.043 3 GLN 55.749 -6.934 -3.917 4 LYS 58.642 -9.427 -4.154 5 LYS 61.740 -7.456 -3.137 6 ILE 59.537 -5.407 -0.806 7 GLU 57.519 -8.235 0.771 8 GLU 60.851 -9.968 1.395 9 ILE 62.508 -6.985 3.105 10 ALA 59.221 -6.389 4.935 11 ALA 58.987 -9.948 6.250 12 LYS 62.693 -9.866 7.153 13 TYR 62.104 -7.079 9.687 14 LYS 62.866 -7.445 13.406 15 HIS 59.416 -6.037 14.221 16 SER 56.002 -7.232 12.968 17 VAL 54.915 -3.542 12.729 18 VAL 57.865 -2.665 10.456 19 LYS 56.011 -4.937 8.021 20 LYS 53.178 -2.418 7.505 21 CYS 55.669 0.483 7.418 22 CYS 57.475 -1.141 4.482 23 TYR 54.046 -2.016 3.088 24 ASP 53.211 1.651 2.504 25 GLY 56.843 2.396 1.586 26 ALA 56.411 0.121 -1.451 27 CYS 52.895 1.574 -1.961 28 VAL 54.403 5.079 -1.486 29 ASN 52.026 7.855 -2.603 30 ASN 54.012 8.477 -5.810 31 ASP 57.439 10.156 -5.537 32 GLU 60.118 10.418 -2.814 33 THR 57.857 11.918 -0.093 34 CYS 56.066 8.613 0.597 35 GLU 54.692 8.887 4.123 36 GLN 55.551 12.542 3.565 37 ARG 52.844 12.546 0.904 38 ALA 50.797 10.856 3.642 39 ALA 50.890 13.904 5.921 40 ARG 53.754 13.410 8.377 41 ILE 55.685 10.225 9.191 42 SER 54.131 9.800 12.588 43 LEU 53.398 6.133 12.875 44 GLY 56.678 5.087 14.533 45 PRO 60.509 5.179 14.232 46 ARG 61.131 1.819 12.525 47 CYS 58.575 3.222 10.058 48 ILE 60.591 6.237 8.966 49 LYS 63.439 4.067 7.567 50 ALA 61.289 0.958 7.048 51 PHE 58.687 2.570 4.851 52 THR 61.109 5.190 3.520 53 GLU 63.494 2.386 2.510 54 CYS 60.873 0.099 0.927 55 CYS 59.496 3.210 -0.761 56 VAL 62.937 4.188 -2.085 57 VAL 63.845 0.756 -3.387 58 ALA 60.273 0.621 -4.573 59 SER 61.085 4.078 -5.919 60 GLN 63.760 2.625 -8.213 61 LEU 61.556 -0.340 -9.056 62 ARG 58.871 2.049 -10.290 63 ALA 61.267 4.821 -11.446 64 ASN 62.653 2.987 -14.501 65 ILE 60.175 0.324 -15.677 66 SER 56.412 0.300 -16.361 67 HIS 55.298 -3.344 -16.670 68 LYS 55.571 -6.600 -14.670 69 ASP 58.513 -4.997 -12.855 70 MET 56.796 -1.602 -12.452 71 GLN 53.080 -2.532 -12.558 72 LEU 54.070 -5.281 -10.077 73 GLY 57.663 -5.043 -8.795 74 ARG 56.782 -1.338 -8.464 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C H H H H H H H H 10 H H H C C H H H H 3 20 3/H H H H H H H H C C 30 C C H H H H H H H C 40 C C C H H H H H 3/H H 50 H H H H H H H H H H 60 H H H H H C T T T T/T 70 T T T/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 t T T h H H H H H H 10 H h t S h H H H H H 20 H H H H H H h t S S 30 S S h H H H H H h t 40 S h H H H H H H 50 H H H H H H H H H H 60 H H h S h H H H 70 H h T t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 MET 34.6 21.7 71.5 2 LEU 81.1 54.9 72.2 3 GLN 75.5 50.8 62.9 4 LYS 70.1 40.4 72.1 5 LYS 90.0 51.9 58.0 6 ILE 140.1 97.6 38.2 7 GLU 75.2 54.2 60.3 8 GLU 58.8 42.4 67.4 9 ILE 110.6 77.0 43.0 10 ALA 68.9 95.0 44.6 11 ALA 28.2 38.8 78.2 12 LYS 37.6 21.7 77.3 13 TYR 149.3 82.5 53.0 14 LYS 6.2 3.6 86.9 15 HIS 60.1 40.0 74.0 16 SER 2.1 2.5 77.6 17 VAL 40.5 34.1 69.1 18 VAL 112.5 94.7 35.3 19 LYS 74.6 43.0 66.2 20 LYS 35.0 20.2 78.9 21 CYS 96.4 97.2 43.1 22 CYS 99.0 99.8 43.6 23 TYR 80.3 44.4 68.0 24 ASP 53.3 48.3 55.1 25 GLY 34.8 100.0 44.3 26 ALA 66.9 92.1 44.2 27 CYS 48.1 48.5 72.0 28 VAL 114.7 96.5 64.6 29 ASN 52.9 43.7 73.4 30 ASN 39.6 32.8 82.0 31 ASP 24.8 22.4 81.0 32 GLU 37.3 26.9 70.2 33 THR 57.3 53.6 61.7 34 CYS 95.2 96.0 48.5 35 GLU 120.9 87.2 38.8 36 GLN 31.6 21.3 78.1 37 ARG 85.9 41.1 79.5 38 ALA 41.2 56.8 76.0 39 ALA 5.4 7.5 84.5 40 ARG 22.2 10.6 86.9 41 ILE 106.8 74.5 46.3 42 SER 21.2 25.4 79.2 43 LEU 54.0 36.5 75.8 44 GLY 21.1 60.6 61.2 45 PRO 31.2 25.0 74.5 46 ARG 130.6 62.5 47.9 47 CYS 96.9 97.7 33.4 48 ILE 77.5 54.0 58.9 49 LYS 16.8 9.7 80.4 50 ALA 68.8 94.7 50.5 51 PHE 158.3 94.9 40.4 52 THR 64.7 60.5 43.8 53 GLU 73.3 52.9 62.9 54 CYS 99.2 100.0 41.0 55 CYS 98.9 99.7 45.0 56 VAL 72.0 60.6 68.8 57 VAL 85.8 72.2 57.1 58 ALA 72.6 100.0 51.0 59 SER 60.5 72.4 58.6 60 GLN 25.4 17.1 78.5 61 LEU 114.2 77.3 60.5 62 ARG 166.8 79.9 59.1 63 ALA 22.0 30.4 75.6 64 ASN 23.1 19.1 80.7 65 ILE 78.9 55.0 73.3 66 SER 22.0 26.3 65.6 67 HIS 23.6 15.7 79.4 68 LYS 10.3 5.9 81.5 69 ASP 43.6 39.4 60.0 70 MET 91.6 57.5 68.4 71 GLN 39.8 26.8 71.0 72 LEU 86.9 58.8 60.5 73 GLY 28.7 82.6 54.8 74 ARG 134.7 64.5 61.2