Protein Data Bank File : 1hfi Title : GLYCOPROTEIN 23-FEB-93 1HFI Number of Amino Acid Residues : 62 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLU LYS ILE PRO CYS SER GLN PRO PRO GLN 10 ILE GLU HIS GLY THR ILE ASN SER SER ARG 20 SER SER GLN GLU SER TYR ALA HIS GLY THR 30 LYS LEU SER TYR THR CYS GLU GLY GLY PHE 40 ARG ILE SER GLU GLU ASN GLU THR THR CYS 50 TYR MET GLY LYS TRP SER SER PRO PRO GLN 60 CYS GLU Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLU 0.0 104.6 179.9 61.3 -58.7 -67.4 2 LYS -81.2 145.3 -179.8 -69.2 78.0 -178.0 64.3 3 ILE -109.0 153.5 175.8 46.8 176.0 4 PRO -72.3 163.6 -179.5 35.1 -43.5 5 CYS -107.8 165.9 179.6 -10.0 6 SER -112.9 -172.6 179.8 -172.8 7 GLN -33.5 132.6 -178.2 -59.8 -63.3 -15.4 8 PRO -64.1 160.0 -179.4 30.3 -42.9 9 PRO -63.0 177.1 179.8 29.3 -41.6 10 GLN -125.2 144.2 -179.8 -59.0 95.6 -55.6 11 ILE -132.9 100.1 179.9 46.7 169.1 12 GLU -6.0 116.7 179.6 -50.1 179.1 -67.6 13 HIS 86.0 -45.2 -179.5 -56.0 -81.2 14 GLY -104.3 165.8 -179.6 15 THR -141.3 178.8 179.9 57.8 16 ILE -75.8 158.2 180.0 -162.9 78.8 17 ASN -126.0 58.5 -179.7 58.3 -172.1 18 SER -93.9 -45.8 -180.0 -176.9 19 SER 140.2 50.5 -180.0 60.3 20 ARG 36.5 -75.0 -179.8 -56.2 176.0 60.3 59.9 21 SER -125.6 101.6 179.8 179.8 22 SER -121.9 -58.1 179.6 179.3 23 GLN -123.0 -178.8 179.8 -68.2 -177.9 -179.2 24 GLU -114.5 -41.8 179.8 -63.2 -179.5 -66.2 25 SER -117.3 158.5 179.8 175.2 26 TYR -128.3 173.8 -180.0 -55.4 77.7 27 ALA -101.4 171.8 179.9 28 HIS -74.6 134.0 -180.0 51.7 -76.6 29 GLY 113.7 -39.0 -179.6 30 THR -33.2 134.7 179.8 -60.0 31 LYS -128.6 107.9 -179.9 -47.4 90.6 70.6 -178.0 32 LEU -105.1 157.6 179.9 -58.0 177.5 33 SER -106.1 174.1 -179.6 -60.1 34 TYR -123.6 164.7 179.5 -109.7 -71.8 35 THR -147.4 146.0 179.9 -64.2 36 CYS -116.9 163.3 179.9 -55.6 37 GLU -50.1 169.3 -179.7 -40.1 -166.6 -58.3 38 GLY -74.8 82.5 179.9 39 GLY 136.4 19.6 179.5 40 PHE -118.9 150.5 179.8 -73.0 59.5 41 ARG -108.8 145.7 180.0 -52.6 -58.2 -62.4 147.5 42 ILE -108.6 151.7 179.6 -172.2 92.1 43 SER -67.9 167.4 -179.9 -56.5 44 GLU -34.3 147.7 -179.8 -61.1 -179.9 1.1 45 GLU 32.6 99.1 -180.0 -56.5 179.3 3.1 46 ASN -82.4 74.9 179.8 48.6 46.2 47 GLU -147.5 152.0 179.5 -160.1 -177.5 65.3 48 THR -134.2 140.1 -179.8 179.7 49 THR -123.6 157.9 179.6 -64.0 50 CYS -111.4 137.8 179.9 171.0 51 TYR -133.4 138.9 -179.6 158.2 72.0 52 MET 21.3 74.9 -180.0 -61.1 -71.8 -86.3 53 GLY 41.6 31.8 179.7 54 LYS -136.3 154.6 179.8 -176.0 -172.0 -175.9 65.0 55 TRP -105.0 175.8 -179.6 -67.0 89.0 56 SER -108.9 144.1 179.8 -172.8 57 SER -24.0 87.3 -168.7 -61.0 58 PRO -63.0 155.6 177.4 30.5 -43.9 59 PRO -67.5 173.3 179.8 30.9 -41.2 60 GLN -129.6 161.9 -179.8 -170.4 -176.2 -61.6 61 CYS -104.4 128.7 179.7 -55.3 62 GLU -120.8 -125.1 0.0 -35.0 -55.0 -57.3 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLU 65.648 54.437 -25.525 2 LYS 68.231 53.339 -28.104 3 ILE 68.427 55.494 -31.198 4 PRO 68.993 54.507 -34.832 5 CYS 72.254 55.363 -36.563 6 SER 72.647 57.196 -39.892 7 GLN 74.954 56.488 -42.889 8 PRO 78.082 54.598 -41.579 9 PRO 81.403 56.555 -41.304 10 GLN 83.997 56.732 -44.126 11 ILE 87.666 55.582 -44.056 12 GLU 90.159 56.923 -46.700 13 HIS 90.376 54.647 -49.820 14 GLY 87.876 52.088 -48.484 15 THR 84.126 52.229 -47.847 16 ILE 81.373 50.169 -46.200 17 ASN 80.182 46.972 -47.996 18 SER 76.463 46.880 -47.095 19 SER 75.050 47.676 -50.596 20 ARG 75.722 51.452 -50.750 21 SER 72.156 52.889 -50.730 22 SER 69.453 50.658 -49.277 23 GLN 68.415 52.676 -46.227 24 GLU 69.475 56.056 -44.809 25 SER 69.344 55.077 -41.147 26 TYR 70.045 51.732 -39.402 27 ALA 69.014 50.451 -35.936 28 HIS 71.005 50.087 -32.719 29 GLY 72.993 46.839 -32.597 30 THR 73.623 46.753 -36.376 31 LYS 77.037 45.308 -37.323 32 LEU 78.235 46.203 -40.849 33 SER 81.577 45.062 -42.332 34 TYR 84.145 47.110 -44.280 35 THR 86.051 46.736 -47.594 36 CYS 89.141 48.351 -49.185 37 GLU 90.182 48.822 -52.842 38 GLY 91.550 45.964 -54.980 39 GLY 95.068 45.741 -53.508 40 PHE 94.762 47.187 -49.961 41 ARG 94.970 45.249 -46.682 42 ILE 92.645 46.148 -43.781 43 SER 93.636 46.154 -40.109 44 GLU 92.284 43.364 -37.814 45 GLU 88.533 42.480 -38.007 46 ASN 86.902 44.555 -40.789 47 GLU 83.673 45.445 -38.951 48 THR 81.925 48.465 -37.423 49 THR 79.019 48.357 -34.941 50 CYS 76.402 50.890 -33.843 51 TYR 75.636 51.992 -30.287 52 MET 73.085 54.781 -29.497 53 GLY 72.882 56.088 -33.098 54 LYS 76.693 56.364 -33.392 55 TRP 79.155 53.863 -34.958 56 SER 82.456 52.515 -33.568 57 SER 86.049 53.446 -34.511 58 PRO 86.032 51.858 -38.030 59 PRO 89.105 49.876 -39.269 60 GLN 91.453 51.512 -41.795 61 CYS 93.018 50.394 -45.083 62 GLU 96.813 50.106 -45.386 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 S 10 S/T T T T/S S S S S C C 20 C 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 S S C S S S S S/T 50 T T T/S S S S S/S S S S 60 S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 E E e 10 B T T B E E e S S 20 S S e E E t T T e 30 E E E E E t T T t 40 B S S e E E E E 50 E T T E E e 60 B Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLU 0.0 0.0 85.7 2 LYS 65.3 37.6 68.7 3 ILE 58.5 40.8 67.4 4 PRO 50.3 40.4 73.1 5 CYS 98.7 99.5 50.0 6 SER 17.4 20.8 73.9 7 GLN 66.6 44.8 73.8 8 PRO 118.4 95.1 40.9 9 PRO 88.1 70.8 55.6 10 GLN 17.0 11.4 82.3 11 ILE 127.5 88.8 45.9 12 GLU 13.9 10.1 84.6 13 HIS 58.9 39.2 69.7 14 GLY 33.1 95.1 57.2 15 THR 28.9 27.0 77.0 16 ILE 125.4 87.4 42.7 17 ASN 74.5 61.6 70.2 18 SER 59.5 71.2 59.8 19 SER 18.9 22.6 74.6 20 ARG 21.7 10.4 84.8 21 SER 9.3 11.1 84.0 22 SER 28.8 34.5 83.0 23 GLN 48.1 32.4 76.6 24 GLU 5.2 3.8 83.6 25 SER 42.0 50.3 62.5 26 TYR 161.8 89.4 57.0 27 ALA 20.4 28.1 72.5 28 HIS 74.3 49.5 63.3 29 GLY 0.4 1.2 81.4 30 THR 75.2 70.3 48.0 31 LYS 54.7 31.5 79.0 32 LEU 124.5 84.2 42.8 33 SER 44.3 53.0 76.8 34 TYR 181.0 100.0 37.1 35 THR 39.2 36.7 74.6 36 CYS 95.8 96.5 42.3 37 GLU 59.0 42.5 65.7 38 GLY 0.0 0.0 83.3 39 GLY 0.0 0.0 77.5 40 PHE 112.9 67.7 64.3 41 ARG 20.0 9.6 89.7 42 ILE 117.6 82.0 54.0 43 SER 33.3 39.8 71.8 44 GLU 0.0 0.0 86.7 45 GLU 0.0 0.0 86.5 46 ASN 57.7 47.7 61.5 47 GLU 66.2 47.8 69.0 48 THR 104.4 97.7 41.3 49 THR 56.5 52.8 65.6 50 CYS 99.2 100.0 46.7 51 TYR 21.0 11.6 75.3 52 MET 101.1 63.4 62.7 53 GLY 34.3 98.5 52.7 54 LYS 26.6 15.3 84.5 55 TRP 192.1 93.7 44.3 56 SER 24.2 29.0 78.9 57 SER 0.0 0.0 80.4 58 PRO 98.3 78.9 49.7 59 PRO 108.3 87.0 51.5 60 GLN 60.1 40.5 77.4 61 CYS 99.2 100.0 43.4 62 GLU 55.8 40.3 83.3