Protein Data Bank File : 2sivb Title : ENVELOPE GLYCOPROTEIN 17-JUN-98 2SIV Number of Amino Acid Residues : 34 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 TRP GLN GLU TRP GLU ARG LYS VAL ASP PHE 10 LEU GLU GLU ASN ILE THR ALA LEU LEU GLU 20 GLU ALA GLN ILE GLN GLN GLU LYS ASN MET 30 TYR GLU LEU GLN Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 TRP 0.0 -20.1 179.8 -78.4 97.1 2 GLN -72.2 -52.5 179.3 -101.1 -61.7 -93.6 3 GLU -73.2 -31.8 178.9 -168.0 65.3 -19.4 4 TRP -52.6 -61.0 180.0 175.1 83.3 5 GLU -52.4 -51.0 180.0 -161.6 -175.4 46.7 6 ARG -50.8 -35.1 -178.8 -106.3 172.9 -116.5 127.9 7 LYS -75.8 -46.2 -179.6 -83.6 148.4 121.3 -160.7 8 VAL -68.7 -23.6 179.7 -50.9 9 ASP -75.4 -32.4 179.7 -90.3 9.3 10 PHE -79.1 -38.7 179.5 168.8 84.9 11 LEU -64.0 -42.4 180.0 -69.1 -175.2 12 GLU -57.1 -50.9 179.7 160.7 62.4 -4.5 13 GLU -60.7 -43.3 178.6 -156.6 47.9 18.7 14 ASN -55.4 -63.5 -179.7 -165.2 -173.9 15 ILE -47.9 -44.1 179.5 -71.6 145.6 16 THR -61.4 -30.9 179.8 -71.6 17 ALA -69.7 -50.3 179.4 18 LEU -59.8 -43.0 -179.7 -67.9 163.8 19 LEU -61.5 -41.5 -179.9 -77.6 172.3 20 GLU -63.4 -53.0 -179.7 -107.0 140.5 41.7 21 GLU -64.2 -29.4 180.0 95.5 180.0 -1.4 22 ALA -67.9 -38.0 179.1 23 GLN -63.2 -33.3 179.3 177.9 67.1 -19.0 24 ILE -69.8 -56.5 179.5 -46.7 -83.9 25 GLN -62.9 -15.6 179.6 175.5 77.1 -21.0 26 GLN -80.7 -48.3 179.9 169.9 70.3 18.3 27 GLU -69.4 -25.3 178.5 -133.3 -44.2 -78.0 28 LYS -68.7 -41.1 -179.9 156.1 179.3 161.1 132.0 29 ASN -72.9 -23.1 179.2 -72.8 -6.6 30 MET -71.6 -55.1 -180.0 -114.2 -48.9 -83.5 31 TYR -72.7 -12.6 178.2 -84.5 0.5 32 GLU -75.3 -47.0 179.0 -131.9 146.8 73.1 33 LEU -54.6 -23.0 179.4 -46.9 146.5 34 GLN -83.5 115.7 0.0 -115.6 167.5 -109.6 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 TRP 41.534 -7.339 15.113 2 GLN 40.926 -11.036 15.648 3 GLU 37.520 -10.605 17.266 4 TRP 36.927 -7.542 15.108 5 GLU 36.989 -9.626 11.938 6 ARG 34.936 -12.421 13.485 7 LYS 32.289 -9.775 14.232 8 VAL 32.049 -8.017 10.885 9 ASP 31.885 -11.419 9.201 10 PHE 28.869 -12.429 11.303 11 LEU 27.167 -9.090 10.827 12 GLU 27.603 -9.372 7.067 13 GLU 25.937 -12.793 6.959 14 ASN 23.224 -11.573 9.337 15 ILE 22.353 -8.513 7.259 16 THR 22.216 -10.598 4.067 17 ALA 19.764 -12.846 5.898 18 LEU 17.542 -9.955 6.992 19 LEU 17.719 -8.447 3.511 20 GLU 16.705 -11.798 2.013 21 GLU 13.775 -12.357 4.335 22 ALA 12.795 -8.707 3.840 23 GLN 12.551 -9.295 0.093 24 ILE 10.186 -12.185 0.939 25 GLN 7.915 -10.287 3.328 26 GLN 7.935 -7.548 0.685 27 GLU 6.651 -9.673 -2.164 28 LYS 4.135 -11.212 0.222 29 ASN 2.721 -7.708 0.885 30 MET 2.784 -6.948 -2.850 31 TYR 0.584 -9.865 -3.881 32 GLU -1.553 -9.306 -0.757 33 LEU -2.980 -5.853 -1.640 34 GLN -3.956 -7.902 -4.714 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 H H H H H H H H H H 10 H H H H H H H H H H 20 H H H H H H H H H H 30 H H H H Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 h H H H H H H H H H 10 H H H H H H H H H H 20 H H H H H H H H H H 30 H H H h Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 TRP 21.8 10.6 80.7 2 GLN 28.0 18.8 91.5 3 GLU 48.1 34.7 72.2 4 TRP 79.1 38.6 59.4 5 GLU 49.7 35.9 76.9 6 ARG 76.1 36.4 76.9 7 LYS 45.3 26.1 73.7 8 VAL 67.6 56.9 58.7 9 ASP 29.9 27.0 71.8 10 PHE 33.6 20.1 78.2 11 LEU 52.6 35.6 66.2 12 GLU 36.3 26.2 81.7 13 GLU 22.3 16.1 80.0 14 ASN 63.7 52.7 54.2 15 ILE 57.0 39.7 61.7 16 THR 60.4 56.5 75.1 17 ALA 25.9 35.7 79.7 18 LEU 55.0 37.2 79.1 19 LEU 36.6 24.8 72.9 20 GLU 34.7 25.0 72.5 21 GLU 37.6 27.1 69.1 22 ALA 24.4 33.7 71.5 23 GLN 26.1 17.6 77.9 24 ILE 23.5 16.4 79.0 25 GLN 50.7 34.1 74.1 26 GLN 41.4 27.9 79.2 27 GLU 62.9 45.4 62.3 28 LYS 61.7 35.6 86.6 29 ASN 53.0 43.9 75.5 30 MET 70.7 44.3 75.6 31 TYR 51.1 28.2 86.5 32 GLU 46.8 33.8 78.7 33 LEU 19.3 13.1 83.8 34 GLN 46.4 31.3 70.8