Protein Data Bank File : 1g47 Title : CELL ADHESION 26-OCT-00 1G47 Number of Amino Acid Residues : 70 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 MET ALA ASN ALA LEU ALA SER ALA THR CYS 10 GLU ARG CYS LYS GLY GLY PHE ALA PRO ALA 20 GLU LYS ILE VAL ASN SER ASN GLY GLU LEU 30 TYR HIS GLU GLN CYS PHE VAL CYS ALA GLN 40 CYS PHE GLN GLN PHE PRO GLU GLY LEU PHE 50 TYR GLU PHE GLU GLY ARG LYS TYR CYS GLU 60 HIS ASP PHE GLN MET LEU PHE ALA PRO CYS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 MET 0.0 159.6 -179.9 -75.0 -179.3 168.6 2 ALA 59.1 -160.2 180.0 3 ASN -76.1 168.6 180.0 -64.2 -96.9 4 ALA -66.0 109.9 -179.9 5 LEU -78.3 138.8 -180.0 -49.9 177.3 6 ALA -75.6 -81.0 -179.9 7 SER -168.3 176.4 179.8 60.9 8 ALA -71.7 110.4 -179.8 9 THR -123.9 159.6 -179.0 57.8 10 CYS -64.8 166.6 -179.8 -164.3 11 GLU -86.6 -63.2 -179.2 171.1 62.5 88.7 12 ARG -82.9 23.4 179.7 47.7 -128.1 47.8 176.2 13 CYS -160.5 -25.2 179.8 107.3 14 LYS 57.7 41.7 179.3 -64.6 -77.6 171.5 -68.7 15 GLY -92.1 121.3 -179.5 16 GLY -58.0 101.7 179.9 17 PHE -113.4 -172.5 -179.8 39.7 -156.1 18 ALA -175.4 -55.4 -179.7 19 PRO -59.3 150.8 -179.9 -1.3 0.9 20 ALA -59.4 -15.3 179.7 21 GLU -81.0 -44.1 -179.9 176.0 -96.2 109.1 22 LYS -91.1 -31.5 -179.6 -55.3 -178.9 -173.7 177.4 23 ILE -92.0 129.7 179.1 -124.7 -56.7 24 VAL -144.4 122.6 -179.6 -159.0 25 ASN -111.7 145.4 179.9 164.2 90.1 26 SER -156.7 134.3 -178.9 86.3 27 ASN 72.0 -44.2 -179.5 115.5 64.2 28 GLY 155.9 -19.7 179.8 29 GLU -85.0 173.1 179.6 -100.4 149.4 93.6 30 LEU -113.9 138.2 -179.8 -62.3 -48.9 31 TYR -136.9 162.0 177.7 -38.3 66.4 32 HIS -94.6 178.2 178.6 -97.1 111.4 33 GLU -76.4 0.7 179.7 44.0 152.9 63.4 34 GLN -152.9 44.3 178.5 -158.2 -135.5 88.8 35 CYS -124.8 -23.7 -180.0 -80.5 36 PHE -42.6 108.1 -179.8 -77.1 73.1 37 VAL -114.8 172.7 179.1 -78.7 38 CYS -91.1 116.6 -179.8 -170.5 39 ALA -50.2 -14.0 -179.9 40 GLN -104.8 -68.3 -179.4 -56.2 176.2 68.9 41 CYS -82.0 -7.1 -179.8 74.3 42 PHE 58.8 21.6 179.5 -48.6 118.0 43 GLN -70.3 115.2 179.5 167.3 56.3 -102.6 44 GLN -72.3 173.1 -179.7 38.4 155.8 111.4 45 PHE -167.5 133.2 179.7 -131.1 -144.2 46 PRO -63.9 -150.8 -179.8 2.9 -2.2 47 GLU 70.6 -40.4 -179.9 -49.3 112.2 -121.4 48 GLY 84.4 21.6 179.9 49 LEU -177.7 133.5 178.7 -172.5 145.0 50 PHE -150.8 -130.9 179.1 55.7 10.6 51 TYR -93.3 57.5 -179.7 -115.0 -64.8 52 GLU -76.4 166.3 -180.0 89.8 84.0 33.9 53 PHE -154.9 176.5 -179.1 -106.8 -81.5 54 GLU -69.3 116.9 178.9 -169.8 -163.2 82.7 55 GLY 70.2 -3.6 -179.7 56 ARG -149.0 135.6 179.8 -33.3 172.1 -125.5 -45.9 57 LYS -125.5 153.0 -179.9 79.8 -81.4 -168.4 -173.9 58 TYR -147.5 148.2 177.8 -50.3 103.5 59 CYS -90.2 173.6 -180.0 47.7 60 GLU -66.8 6.5 -179.8 -168.1 52.1 78.3 61 HIS -81.3 -75.7 -179.4 137.0 -115.5 62 ASP -56.6 -35.2 -178.3 -114.1 -60.9 63 PHE -74.6 -33.7 178.6 -98.6 58.6 64 GLN -68.8 -25.4 178.6 70.5 110.8 94.9 65 MET -67.8 -41.0 178.2 -65.0 -64.6 160.5 66 LEU -67.9 -21.4 -180.0 -36.7 -175.6 67 PHE 66.3 86.2 -179.8 -138.2 99.2 68 ALA -126.5 83.4 179.9 69 PRO -62.1 106.8 -179.8 1.0 -0.4 70 CYS 60.3 23.5 0.0 -41.4 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 MET 9.720 -21.767 3.465 2 ALA 7.000 -19.848 5.369 3 ASN 3.380 -20.503 4.301 4 ALA 2.530 -21.778 0.792 5 LEU 3.061 -18.700 -1.421 6 ALA 0.657 -18.411 -4.385 7 SER 2.483 -16.367 -7.063 8 ALA 3.624 -12.838 -8.009 9 THR 0.389 -10.792 -8.100 10 CYS -0.296 -7.023 -8.280 11 GLU -0.834 -4.954 -5.117 12 ARG -3.964 -2.872 -5.882 13 CYS -5.340 -5.685 -8.089 14 LYS -3.540 -8.967 -7.226 15 GLY -3.291 -9.816 -10.943 16 GLY -0.850 -12.687 -11.576 17 PHE 1.753 -10.858 -13.702 18 ALA 5.405 -11.589 -14.613 19 PRO 6.596 -9.906 -17.850 20 ALA 8.189 -6.440 -17.455 21 GLU 5.067 -5.160 -19.265 22 LYS 2.566 -6.524 -16.723 23 ILE 5.001 -6.691 -13.778 24 VAL 6.198 -3.331 -12.392 25 ASN 7.934 -2.854 -9.023 26 SER 8.444 0.460 -7.208 27 ASN 9.444 1.258 -3.585 28 GLY 9.167 -2.501 -2.969 29 GLU 5.530 -3.254 -3.889 30 LEU 4.376 -4.663 -7.258 31 TYR 2.099 -2.742 -9.671 32 HIS 0.720 -3.246 -13.202 33 GLU 1.192 -0.785 -16.059 34 GLN -2.323 0.439 -15.163 35 CYS -2.915 -0.273 -11.449 36 PHE -0.929 2.590 -9.889 37 VAL -3.665 4.219 -7.727 38 CYS -3.701 7.132 -5.257 39 ALA -3.354 5.819 -1.676 40 GLN -5.896 8.599 -0.938 41 CYS -8.363 8.989 -3.860 42 PHE -7.420 5.493 -5.127 43 GLN -7.362 7.077 -8.608 44 GLN -5.659 4.502 -10.859 45 PHE -3.403 5.663 -13.704 46 PRO -1.756 4.102 -16.784 47 GLU 1.945 4.714 -17.646 48 GLY 2.800 2.202 -14.888 49 LEU 4.462 4.897 -12.731 50 PHE 3.475 8.198 -11.068 51 TYR 4.069 9.735 -7.604 52 GLU 4.434 6.329 -5.899 53 PHE 6.370 5.952 -2.600 54 GLU 7.564 3.397 -0.001 55 GLY 4.495 1.690 1.523 56 ARG 2.433 4.542 0.016 57 LYS 1.664 5.509 -3.597 58 TYR 0.031 8.655 -5.056 59 CYS -1.028 9.892 -8.494 60 GLU -0.139 13.366 -9.803 61 HIS -3.522 14.369 -8.300 62 ASP -3.032 14.601 -4.503 63 PHE 0.645 15.290 -5.173 64 GLN 0.085 18.136 -7.691 65 MET -1.993 19.775 -4.941 66 LEU 1.061 19.652 -2.658 67 PHE 2.858 21.145 -5.674 68 ALA 6.088 19.118 -6.041 69 PRO 7.937 20.231 -9.191 70 CYS 10.187 17.231 -9.996 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C S S S S S/S S S S/T 10 T T T C S S S S S/T T 20 T T/S S S S/T T T T/S S S 30 S S/T T T T/S S S S/T T T 40 T S S S S S S S S S 50 S C T T T T/S S S S S 60 H H H H H H H/S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S B 10 S S S B t T 20 T T t E E E T T E E 30 E t T T T t t T T 40 T t g G G G g S 50 E E E T T E E E h H 60 H H H H H H h Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 MET 0.0 0.0 95.9 2 ALA 13.1 18.0 78.4 3 ASN 0.0 0.0 83.3 4 ALA 0.0 0.0 87.3 5 LEU 23.8 16.1 86.0 6 ALA 1.0 1.3 86.5 7 SER 20.6 24.7 72.6 8 ALA 21.5 29.6 70.3 9 THR 76.4 71.5 62.7 10 CYS 99.2 100.0 41.1 11 GLU 80.9 58.3 76.3 12 ARG 186.1 89.1 43.1 13 CYS 59.1 59.6 55.5 14 LYS 67.9 39.2 78.0 15 GLY 12.9 37.0 62.7 16 GLY 15.4 44.4 72.2 17 PHE 165.4 99.2 44.0 18 ALA 15.9 21.8 63.3 19 PRO 57.8 46.4 63.6 20 ALA 1.0 1.4 83.7 21 GLU 50.0 36.1 68.1 22 LYS 73.7 42.5 70.7 23 ILE 105.6 73.6 49.7 24 VAL 84.5 71.2 65.5 25 ASN 56.2 46.5 63.8 26 SER 69.6 83.2 54.3 27 ASN 99.0 81.9 69.0 28 GLY 6.5 18.5 85.9 29 GLU 96.1 69.3 68.6 30 LEU 86.9 58.8 57.9 31 TYR 180.3 99.6 50.7 32 HIS 120.3 80.1 40.5 33 GLU 60.9 43.9 64.5 34 GLN 59.8 40.2 76.1 35 CYS 81.7 82.3 48.4 36 PHE 166.6 99.9 41.9 37 VAL 99.0 83.3 51.3 38 CYS 99.2 100.0 46.9 39 ALA 54.1 74.5 54.0 40 GLN 71.7 48.3 63.1 41 CYS 60.1 60.6 53.8 42 PHE 42.0 25.2 79.7 43 GLN 60.9 41.0 61.2 44 GLN 64.6 43.5 74.6 45 PHE 85.8 51.4 63.9 46 PRO 57.0 45.8 67.8 47 GLU 56.4 40.7 67.7 48 GLY 32.9 94.6 54.4 49 LEU 38.7 26.2 70.7 50 PHE 152.9 91.6 46.4 51 TYR 136.2 75.2 58.8 52 GLU 117.9 85.1 50.7 53 PHE 64.2 38.5 67.4 54 GLU 24.3 17.5 83.2 55 GLY 10.3 29.7 81.4 56 ARG 78.2 37.5 75.4 57 LYS 139.5 80.4 49.0 58 TYR 149.9 82.8 40.2 59 CYS 97.0 97.8 39.5 60 GLU 57.3 41.3 57.9 61 HIS 79.3 52.8 53.5 62 ASP 86.8 78.6 55.1 63 PHE 141.9 85.1 38.6 64 GLN 68.5 46.1 65.5 65 MET 56.7 35.6 79.4 66 LEU 55.6 37.6 70.1 67 PHE 22.3 13.4 82.9 68 ALA 42.4 58.5 62.5 69 PRO 34.5 27.7 71.9 70 CYS 0.0 0.0 82.0