Protein Data Bank File : 1tle Title : GLYCOPROTEIN 26-JAN-96 1TLE Number of Amino Acid Residues : 58 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ARG PRO CYS GLN CYS ASN ASP ASN ILE ASP 10 PRO ASN ALA VAL GLY ASN CYS ASN ARG LEU 20 THR GLY GLU CYS LEU LYS CYS ILE TYR ASN 30 THR ALA GLY PHE TYR CYS ASP ARG CYS LYS 40 GLU GLY PHE PHE GLY ASN PRO LEU ALA PRO 50 ASN PRO ALA ASP LYS CYS LYS ALA Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ARG 0.0 98.3 -179.9 -145.9 68.9 90.8 -94.9 2 PRO -78.1 -41.5 179.7 22.4 -20.6 3 CYS -106.1 133.9 -179.6 42.9 4 GLN -65.0 136.0 179.9 -76.7 -94.1 -35.9 5 CYS 178.9 157.2 179.9 -167.8 6 ASN -54.1 170.4 -179.3 -86.6 50.0 7 ASP -82.7 67.4 179.4 -169.3 80.7 8 ASN -142.8 62.7 -179.7 -27.9 81.2 9 ILE -154.1 152.4 179.9 57.8 113.6 10 ASP -107.8 129.2 -179.6 -91.2 -23.1 11 PRO -75.9 -6.6 -179.4 22.3 -22.7 12 ASN -78.5 -69.3 -179.9 -79.6 112.5 13 ALA -59.7 169.2 -180.0 14 VAL -119.0 152.8 -179.7 166.6 15 GLY 97.4 -11.6 -179.4 16 ASN -52.5 -15.3 -179.9 -81.2 -156.5 17 CYS -122.4 150.0 179.7 -126.1 18 ASN -84.3 122.1 -178.7 -39.4 10.4 19 ARG -79.3 -6.9 -179.3 -159.1 86.6 144.6 -99.8 20 LEU -108.2 -45.1 -179.7 67.8 162.4 21 THR -91.7 -15.5 -179.4 27.2 22 GLY 66.0 61.0 -179.3 23 GLU -156.6 152.5 -179.7 76.0 174.6 85.6 24 CYS -51.9 119.0 179.6 -77.7 25 LEU -84.6 -31.4 -179.6 -135.9 -153.7 26 LYS -143.9 84.7 179.7 -41.7 169.1 -155.3 -88.7 27 CYS -53.4 155.7 -178.7 -44.8 28 ILE -86.4 -66.6 -177.1 17.5 159.2 29 TYR -64.6 77.7 177.8 -56.3 -37.9 30 ASN 26.0 48.9 179.9 -41.7 140.7 31 THR -121.9 150.9 -179.5 55.0 32 ALA -139.3 171.5 180.0 33 GLY 119.7 158.6 -179.6 34 PHE -54.3 -29.6 -179.6 -171.5 -81.2 35 TYR -122.0 32.0 -179.9 -80.1 -69.4 36 CYS 49.7 27.2 -179.8 -64.8 37 ASP -94.8 20.4 -180.0 -111.3 49.1 38 ARG -130.7 -174.6 -179.7 -142.4 124.1 -48.9 150.7 39 CYS -120.1 135.4 -178.8 -65.4 40 LYS -55.8 147.1 -179.6 67.4 127.2 98.7 -69.3 41 GLU -60.2 123.6 -178.9 171.4 72.0 49.6 42 GLY 122.4 -33.4 177.4 43 PHE -122.5 129.8 179.7 -48.0 -37.1 44 PHE -118.5 178.9 -179.9 -31.4 -76.6 45 GLY 127.2 -143.8 180.0 46 ASN -116.0 110.1 -179.5 -79.8 -17.2 47 PRO -78.4 -9.8 -179.8 22.6 -20.8 48 LEU -109.8 37.9 179.6 -72.1 121.2 49 ALA -93.2 153.2 179.1 50 PRO -75.0 -29.7 179.1 22.1 -22.6 51 ASN -101.3 138.6 179.5 -48.4 -99.4 52 PRO -75.8 -19.4 179.6 22.0 -21.6 53 ALA -74.8 -18.1 179.9 54 ASP -113.4 17.8 -179.9 -76.9 33.9 55 LYS -71.8 -130.7 179.6 -161.1 67.0 45.9 54.2 56 CYS -101.1 102.9 -179.7 -44.8 57 LYS -109.2 168.3 179.9 -95.7 -85.0 -159.6 171.7 58 ALA -64.5 140.2 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ARG 13.758 65.127 88.085 2 PRO 14.922 63.382 84.897 3 CYS 12.455 60.470 85.118 4 GLN 8.768 61.133 85.893 5 CYS 7.741 59.615 89.249 6 ASN 6.118 60.503 92.600 7 ASP 8.241 62.574 95.022 8 ASN 9.980 59.599 96.719 9 ILE 13.567 59.355 95.419 10 ASP 17.005 60.713 96.359 11 PRO 19.079 62.578 93.734 12 ASN 22.269 61.649 95.608 13 ALA 22.531 57.863 95.155 14 VAL 22.317 56.480 91.593 15 GLY 19.938 53.832 90.185 16 ASN 16.949 55.298 92.101 17 CYS 15.175 55.281 88.705 18 ASN 14.674 52.407 86.213 19 ARG 16.495 53.215 82.947 20 LEU 14.372 50.666 81.036 21 THR 10.785 50.981 82.371 22 GLY 11.133 54.671 83.363 23 GLU 9.735 54.280 86.907 24 CYS 11.075 54.668 90.480 25 LEU 13.275 51.547 90.942 26 LYS 13.846 52.145 94.679 27 CYS 11.527 54.711 96.379 28 ILE 13.172 56.299 99.461 29 TYR 10.528 56.677 102.224 30 ASN 9.764 52.929 102.698 31 THR 7.383 53.154 99.733 32 ALA 6.905 50.753 96.807 33 GLY 4.820 50.474 93.621 34 PHE 5.232 51.606 89.996 35 TYR 4.738 55.195 91.270 36 CYS 6.038 54.826 94.846 37 ASP 2.335 55.064 95.761 38 ARG 2.579 52.017 98.042 39 CYS 4.369 50.954 101.233 40 LYS 7.256 48.415 101.283 41 GLU 6.177 44.973 102.556 42 GLY 6.660 44.991 106.343 43 PHE 5.546 48.563 106.809 44 PHE 1.991 49.685 106.161 45 GLY 0.214 53.042 106.553 46 ASN 0.127 56.020 104.181 47 PRO 3.128 56.301 101.840 48 LEU 1.778 59.604 100.464 49 ALA 1.761 61.538 103.763 50 PRO 3.388 64.948 104.194 51 ASN 4.873 63.828 107.521 52 PRO 7.312 60.893 107.662 53 ALA 6.032 59.972 111.157 54 ASP 2.670 59.075 109.578 55 LYS 4.116 57.404 106.461 56 CYS 4.140 53.556 106.305 57 LYS 4.956 52.190 109.784 58 ALA 4.693 48.640 111.183 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C S S S S S S S S S 10 C S S S S C C T T T 20 T C C C C C T T T T/S 30 S S S/T T T T S S S S/T 40 T T T/S S S S S S S S 50 T T T T S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S 10 S S S S S B t T T 20 T t S B S S S S e 30 E E t T T t E E e 40 T T t E E e T T t S 50 g G G G e E E Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ARG 105.9 50.7 75.0 2 PRO 21.5 17.3 76.4 3 CYS 74.5 75.1 49.2 4 GLN 0.0 0.0 88.3 5 CYS 96.6 97.4 51.0 6 ASN 78.7 65.1 63.2 7 ASP 16.1 14.5 87.3 8 ASN 109.7 90.7 52.9 9 ILE 131.0 91.3 47.7 10 ASP 54.2 49.1 58.7 11 PRO 31.7 25.5 83.9 12 ASN 3.6 3.0 81.4 13 ALA 15.7 21.7 81.4 14 VAL 0.0 0.0 88.6 15 GLY 8.4 24.1 70.5 16 ASN 102.4 84.7 54.5 17 CYS 77.1 77.7 55.1 18 ASN 111.2 91.9 55.3 19 ARG 0.0 0.0 92.1 20 LEU 23.4 15.8 79.3 21 THR 46.9 43.8 67.9 22 GLY 8.3 24.0 74.2 23 GLU 111.9 80.7 56.6 24 CYS 99.2 100.0 45.8 25 LEU 74.6 50.4 75.9 26 LYS 61.6 35.5 77.8 27 CYS 96.0 96.8 57.6 28 ILE 108.3 75.5 67.7 29 TYR 71.2 39.4 72.3 30 ASN 55.5 45.9 67.2 31 THR 106.9 100.0 47.5 32 ALA 32.8 45.1 63.4 33 GLY 19.3 55.5 72.1 34 PHE 80.9 48.5 73.4 35 TYR 69.1 38.2 67.9 36 CYS 99.2 100.0 50.8 37 ASP 68.2 61.7 65.9 38 ARG 64.8 31.0 74.9 39 CYS 88.6 89.3 50.7 40 LYS 97.6 56.3 63.8 41 GLU 5.7 4.1 82.2 42 GLY 7.7 22.0 60.5 43 PHE 96.1 57.6 59.2 44 PHE 52.7 31.6 80.1 45 GLY 4.7 13.5 71.7 46 ASN 22.4 18.6 72.1 47 PRO 111.0 89.2 49.6 48 LEU 71.2 48.2 79.3 49 ALA 63.5 87.5 53.9 50 PRO 22.5 18.0 84.0 51 ASN 42.4 35.0 61.7 52 PRO 33.7 27.1 78.4 53 ALA 7.3 10.1 77.6 54 ASP 20.6 18.7 77.3 55 LYS 157.4 90.8 55.0 56 CYS 99.2 100.0 46.6 57 LYS 27.2 15.7 88.6 58 ALA 17.6 24.3 73.3