Protein Data Bank File : 1bqhh Title : IMMUNE SYSTEM 16-AUG-98 1BQH Number of Amino Acid Residues : 125 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 LYS PRO GLN ALA PRO GLU LEU ARG ILE PHE 10 PRO LYS LYS MET ASP ALA GLU LEU GLY GLN 20 LYS VAL ASP LEU VAL CYS GLU VAL LEU GLY 30 SER VAL SER GLN GLY CYS SER TRP LEU PHE 40 GLN ASN SER SER SER LYS LEU PRO GLN PRO 50 THR PHE VAL VAL TYR MET ALA SER SER HIS 60 ASN LYS ILE THR TRP ASP GLU LYS LEU ASN 70 SER SER LYS LEU PHE SER ALA MET ARG ASP 80 THR ASN ASN LYS TYR VAL LEU THR LEU ASN 90 LYS PHE SER LYS GLU ASN GLU GLY TYR TYR 100 PHE CYS SER VAL ILE SER ASN SER VAL MET 110 TYR PHE SER SER VAL VAL PRO VAL LEU GLN 120 LYS VAL SER SER ALA Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 LYS 0.0 71.6 -179.8 -76.3 54.9 -174.5 176.5 2 PRO -71.4 -164.7 -179.5 29.1 -32.4 3 GLN -56.4 158.6 179.9 -73.3 -89.4 -29.9 4 ALA -152.9 110.6 179.9 5 PRO -54.8 168.7 179.6 -21.7 31.5 6 GLU -135.3 112.3 -179.3 -168.9 177.4 -46.6 7 LEU -94.1 132.2 179.5 -80.6 52.6 8 ARG -129.3 126.6 -179.6 -71.9 -173.5 -175.1 171.7 9 ILE -111.0 161.9 -179.9 19.3 59.1 10 PHE -160.3 129.4 0.2 166.7 69.6 11 PRO -80.5 170.6 179.4 5.2 1.9 12 LYS -76.7 -23.9 179.6 -93.4 63.1 -177.0 -171.7 13 LYS -145.7 157.7 179.5 -71.3 -144.9 170.2 -172.0 14 MET -176.0 161.5 -179.0 -173.7 50.5 118.9 15 ASP -170.4 147.9 -179.3 34.3 69.1 16 ALA -157.0 179.2 179.7 17 GLU -62.4 135.7 178.1 -32.4 95.0 -3.3 18 LEU -54.3 105.7 179.3 -73.8 -166.6 19 GLY 121.8 19.2 -177.7 20 GLN -109.6 155.8 179.1 145.7 -151.3 119.5 21 LYS -79.9 104.2 179.8 -175.6 -160.0 -73.6 59.3 22 VAL -95.3 118.0 179.1 173.8 23 ASP -113.9 127.1 -179.6 39.3 -67.5 24 LEU -119.9 125.0 180.0 -59.3 165.9 25 VAL -106.1 144.8 179.7 -45.8 26 CYS -123.3 121.1 179.9 176.3 27 GLU -102.6 117.3 179.9 178.2 176.7 -17.9 28 VAL -99.0 125.4 179.5 -172.0 29 LEU -105.6 129.4 179.0 -62.2 -172.8 30 GLY 118.5 149.3 -179.7 31 SER -101.2 11.0 -179.1 59.8 32 VAL -91.7 26.5 -179.9 -66.5 33 SER 173.0 124.3 179.9 77.1 34 GLN -100.0 165.2 -179.8 77.1 -102.9 -10.1 35 GLY 69.1 178.8 179.9 36 CYS -165.8 146.3 179.8 159.3 37 SER -121.9 137.6 179.4 -89.2 38 TRP -105.3 121.6 179.8 -90.7 108.9 39 LEU -106.8 170.4 -179.3 -63.4 -165.4 40 PHE -151.4 136.9 178.3 167.8 55.1 41 GLN -116.8 98.7 -179.1 -74.3 -119.5 176.4 42 ASN -43.9 135.5 179.8 -158.0 -33.4 43 SER -62.4 -39.8 179.8 -164.0 44 SER -81.7 95.8 179.8 60.5 45 SER 175.0 147.4 179.6 176.0 46 LYS -96.2 -41.4 179.4 62.0 -70.4 -55.5 -51.0 47 LEU -93.3 128.3 -179.9 -64.4 173.6 48 PRO -61.6 86.8 179.7 3.6 -2.9 49 GLN -106.9 102.8 179.9 -177.7 68.4 33.8 50 PRO -65.5 150.0 179.7 4.1 -1.8 51 THR -130.2 120.6 179.6 57.1 52 PHE -65.5 122.7 177.7 172.3 79.8 53 VAL -95.7 -75.6 -175.5 152.5 54 VAL -146.3 158.3 178.2 81.0 55 TYR -123.3 137.8 179.8 176.5 75.8 56 MET -135.3 138.3 179.0 -72.5 -169.5 -99.2 57 ALA -86.6 152.2 -179.7 58 SER -85.5 -6.0 -179.7 69.5 59 SER -115.4 -75.0 180.0 48.8 60 HIS -78.8 147.7 -179.7 61.4 79.9 61 ASN -75.9 11.1 179.9 -56.1 171.6 62 LYS -83.0 126.7 -178.8 -173.2 176.5 145.4 -6.2 63 ILE -115.6 138.2 178.9 54.8 -72.8 64 THR -118.9 112.6 -179.5 -66.1 65 TRP -100.2 -173.3 173.8 -57.6 85.3 66 ASP -124.7 114.2 -179.3 -146.9 33.8 67 GLU -58.9 9.2 -179.2 82.1 -97.3 86.0 68 LYS -81.4 143.6 -177.4 -176.7 175.7 141.9 -174.1 69 LEU 26.5 52.3 -179.5 -147.9 34.7 70 ASN -11.8 100.9 -179.2 169.0 -12.1 71 SER -113.2 27.6 -179.7 -38.5 72 SER -76.1 93.2 -179.4 -84.7 73 LYS 168.4 -27.5 -179.8 -107.8 -61.5 -176.8 66.4 74 LEU -103.3 -17.8 -179.4 36.9 156.3 75 PHE -111.5 133.8 179.3 -70.7 -45.4 76 SER -154.5 135.4 -179.2 -168.2 77 ALA -148.5 143.1 179.8 78 MET -132.2 173.2 -179.7 57.0 161.5 79.4 79 ARG -122.4 124.7 -179.5 -169.9 -102.6 -92.6 70.7 80 ASP -92.9 -149.0 -178.6 -81.9 3.5 81 THR -62.9 -118.4 -178.7 -42.2 82 ASN -56.9 95.4 -179.6 -66.4 103.3 83 ASN 37.1 43.9 -179.3 -72.2 21.0 84 LYS -103.2 111.5 -179.9 -56.4 -71.2 -176.5 94.1 85 TYR -109.8 108.4 -179.3 -66.7 86.3 86 VAL -92.6 136.8 179.3 -170.3 87 LEU -131.3 104.9 -180.0 174.1 73.0 88 THR -99.4 143.7 179.8 66.7 89 LEU -104.8 121.2 179.4 -53.2 -172.2 90 ASN -78.9 103.8 -179.8 -47.1 51.3 91 LYS 65.9 94.7 179.6 174.9 -137.7 172.3 -65.6 92 PHE -57.2 90.7 179.3 179.6 -9.7 93 SER -94.4 -175.6 -180.0 70.7 94 LYS -69.7 -30.1 179.8 -150.2 158.2 -178.8 -179.4 95 GLU -71.8 -9.1 -179.3 -66.4 85.0 -85.6 96 ASN -96.0 -28.2 -179.5 -59.5 -15.8 97 GLU -54.4 132.1 179.9 -179.3 -178.9 41.6 98 GLY 159.2 -155.3 -179.5 99 TYR -116.1 128.2 -179.3 -45.9 80.5 100 TYR -114.6 153.9 -179.9 -69.0 66.0 101 PHE -173.0 140.7 -179.4 70.5 -59.2 102 CYS -94.9 150.8 -179.6 53.9 103 SER -130.7 155.7 -179.8 -171.7 104 VAL -148.5 157.4 179.9 170.9 105 ILE -122.1 120.6 179.3 -71.9 -171.3 106 SER -123.3 120.3 179.7 167.2 107 ASN 47.7 56.4 179.8 -73.8 -64.5 108 SER 69.9 -20.1 179.6 -67.6 109 VAL -86.4 131.0 -179.9 -70.2 110 MET -88.3 128.8 180.0 -58.9 -172.1 45.6 111 TYR -112.2 142.3 -179.9 -62.1 -86.3 112 PHE -128.0 138.0 178.5 -50.1 -89.4 113 SER -75.8 161.0 175.8 44.9 114 SER -68.5 138.3 -179.5 57.3 115 VAL -62.8 154.9 180.0 56.7 116 VAL -131.7 113.8 179.8 -56.9 117 PRO -60.9 130.2 179.5 -3.6 8.9 118 VAL -134.8 65.9 -178.6 -166.9 119 LEU -101.9 179.7 179.5 -33.1 138.5 120 GLN -75.3 134.9 -178.5 146.5 84.7 48.6 121 LYS -57.9 95.7 179.7 71.7 171.2 -175.0 27.8 122 VAL 36.4 10.8 179.5 76.4 123 SER 52.5 16.4 -179.0 -58.3 124 SER -103.0 173.4 -179.3 66.1 125 ALA 95.8 -163.3 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 LYS 5.412 35.935 31.716 2 PRO 7.109 32.777 30.265 3 GLN 9.463 31.980 27.355 4 ALA 9.474 33.715 23.991 5 PRO 11.227 32.343 20.867 6 GLU 13.442 34.606 18.756 7 LEU 13.124 34.697 14.990 8 ARG 16.038 36.064 12.959 9 ILE 15.884 36.478 9.203 10 PHE 18.589 37.047 6.663 11 PRO 19.034 39.118 4.771 12 LYS 16.844 41.895 6.266 13 LYS 16.470 43.444 2.778 14 MET 17.012 42.407 -0.860 15 ASP 16.082 43.017 -4.465 16 ALA 17.073 41.689 -7.808 17 GLU 17.070 41.214 -11.487 18 LEU 13.879 39.800 -12.819 19 GLY 14.860 36.090 -12.691 20 GLN 17.170 35.268 -9.791 21 LYS 17.256 32.547 -7.029 22 VAL 16.429 34.397 -3.798 23 ASP 17.062 32.289 -0.697 24 LEU 15.820 33.541 2.654 25 VAL 16.776 31.835 5.903 26 CYS 14.988 32.067 9.228 27 GLU 16.853 31.249 12.443 28 VAL 14.638 30.240 15.344 29 LEU 16.188 30.453 18.792 30 GLY 14.698 28.397 21.578 31 SER 13.263 25.010 22.377 32 VAL 9.827 26.450 23.144 33 SER 8.449 25.837 19.654 34 GLN 9.185 23.442 16.795 35 GLY 8.758 23.909 13.074 36 CYS 8.475 27.171 11.160 37 SER 6.179 28.935 8.699 38 TRP 7.168 31.355 5.957 39 LEU 4.652 34.106 5.214 40 PHE 4.361 36.651 2.423 41 GLN 2.586 40.004 1.979 42 ASN 2.128 40.557 -1.767 43 SER 3.607 43.837 -2.966 44 SER 0.495 44.457 -5.053 45 SER -2.144 45.327 -2.442 46 LYS -3.562 48.232 -0.424 47 LEU -4.757 46.183 2.553 48 PRO -2.042 44.177 4.350 49 GLN -3.251 40.725 3.419 50 PRO -0.697 38.082 4.437 51 THR -0.357 35.007 2.326 52 PHE 0.691 31.660 3.718 53 VAL 3.595 30.278 1.723 54 VAL 4.973 27.334 3.556 55 TYR 5.374 25.234 6.685 56 MET 8.321 23.047 7.733 57 ALA 8.774 20.656 10.668 58 SER 11.903 20.787 12.847 59 SER 12.005 16.999 12.835 60 HIS 10.499 15.476 9.732 61 ASN 11.433 16.611 6.275 62 LYS 7.738 16.872 5.559 63 ILE 6.704 20.196 4.231 64 THR 3.227 21.530 3.989 65 TRP 2.709 24.284 1.283 66 ASP -0.412 26.075 -0.157 67 GLU -2.131 24.723 -3.281 68 LYS -3.577 28.131 -3.977 69 LEU -3.133 29.818 -7.429 70 ASN -0.694 26.940 -7.678 71 SER 2.567 28.693 -7.645 72 SER 4.501 25.482 -7.343 73 LYS 7.451 26.330 -9.489 74 LEU 8.554 29.671 -8.012 75 PHE 8.616 28.488 -4.408 76 SER 11.077 26.036 -2.857 77 ALA 12.294 25.600 0.740 78 MET 14.593 23.393 2.854 79 ARG 15.789 23.213 6.468 80 ASP 19.445 23.574 7.486 81 THR 21.450 23.212 10.681 82 ASN 20.753 25.187 13.868 83 ASN 17.039 25.998 13.656 84 LYS 17.761 27.329 10.154 85 TYR 14.764 27.409 7.808 86 VAL 15.650 28.339 4.222 87 LEU 13.054 29.550 1.695 88 THR 14.338 29.919 -1.861 89 LEU 12.520 31.637 -4.739 90 ASN 12.763 30.019 -8.151 91 LYS 13.375 33.011 -10.503 92 PHE 12.498 36.351 -8.912 93 SER 9.433 37.196 -11.107 94 LYS 6.799 39.916 -10.565 95 GLU 4.514 37.489 -8.716 96 ASN 7.304 37.100 -6.154 97 GLU 7.847 40.768 -5.342 98 GLY 6.697 41.728 -1.946 99 TYR 7.430 41.322 1.726 100 TYR 8.445 38.000 3.292 101 PHE 8.715 36.970 6.925 102 CYS 8.770 33.892 9.138 103 SER 6.485 32.925 11.953 104 VAL 6.536 30.275 14.681 105 ILE 4.118 29.200 17.423 106 SER 5.107 28.748 21.059 107 ASN 2.559 27.749 23.696 108 SER -0.306 28.913 21.549 109 VAL 1.177 32.467 20.973 110 MET 2.271 33.394 17.384 111 TYR 5.585 35.138 16.855 112 PHE 6.594 37.065 13.737 113 SER 10.006 38.107 12.331 114 SER 10.708 41.569 11.032 115 VAL 9.579 41.724 7.381 116 VAL 12.140 41.604 4.590 117 PRO 11.689 43.554 1.310 118 VAL 12.028 41.533 -1.946 119 LEU 11.206 44.108 -4.640 120 GLN 12.783 44.762 -8.131 121 LYS 16.285 46.261 -7.911 122 VAL 15.522 49.982 -8.272 123 SER 14.290 49.146 -11.804 124 SER 17.463 50.725 -13.222 125 ALA 20.280 50.185 -15.706 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/P 10 S C C C C C C S S S 20 S/S S S S S S S S S S 30 C S S S S/S S S S S S 40 S S S S S S S/S S S S 50 S S S S/S S S S/T T T T 60 S S S S S S S/T T T T 70 T T T T/S S S S/S S S S 80 S S S S S S S S S S 90 S C T T T T S S S S 100 S S S S S/T T T T/S S S 110 S S S S/S S S S S S S 120 C C S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 E E E E E 10 S E E E t T T t 20 E E E E E E E E 30 S S E E E E E 40 E E e S S S e E 50 E E E E E E e S S S 60 e E E E e g G G G 70 g T T e E E E E E e 80 t T e E E E E E E e 90 S t T T T e E E E 100 E E E E E E T T E E 110 E E e E E E E E 120 e T T t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 LYS 0.0 0.0 90.5 2 PRO 21.5 17.3 86.3 3 GLN 36.0 24.3 71.7 4 ALA 29.6 40.8 70.0 5 PRO 122.8 98.7 47.0 6 GLU 58.7 42.3 73.1 7 LEU 144.5 97.7 42.1 8 ARG 89.9 43.1 74.5 9 ILE 140.1 97.6 47.2 10 PHE 37.3 22.3 70.8 11 PRO 92.8 74.5 53.9 12 LYS 62.5 36.1 69.2 13 LYS 32.6 18.8 75.6 14 MET 78.4 49.2 65.2 15 ASP 52.6 47.6 59.3 16 ALA 71.4 98.4 51.6 17 GLU 56.1 40.4 66.9 18 LEU 62.6 42.4 77.8 19 GLY 24.4 70.1 63.1 20 GLN 97.5 65.6 66.5 21 LYS 48.1 27.7 80.8 22 VAL 112.7 94.9 39.2 23 ASP 49.2 44.5 60.1 24 LEU 146.4 99.0 32.1 25 VAL 84.0 70.7 50.1 26 CYS 99.2 100.0 35.3 27 GLU 99.3 71.6 56.0 28 VAL 117.1 98.6 46.3 29 LEU 88.6 59.9 76.3 30 GLY 13.1 37.6 76.1 31 SER 0.0 0.0 84.9 32 VAL 90.9 76.5 63.0 33 SER 76.3 91.2 55.2 34 GLN 19.8 13.3 87.6 35 GLY 34.8 100.0 59.3 36 CYS 97.7 98.5 36.7 37 SER 61.8 73.9 46.8 38 TRP 204.8 99.9 34.3 39 LEU 125.3 84.8 42.4 40 PHE 155.0 93.0 55.7 41 GLN 105.4 71.0 50.5 42 ASN 69.5 57.5 68.0 43 SER 64.2 76.8 61.0 44 SER 9.6 11.5 85.7 45 SER 57.3 68.6 68.8 46 LYS 20.9 12.1 79.6 47 LEU 18.6 12.6 72.8 48 PRO 37.8 30.4 81.5 49 GLN 27.7 18.6 80.8 50 PRO 73.4 58.9 67.3 51 THR 68.7 64.2 69.7 52 PHE 102.6 61.5 67.1 53 VAL 110.5 93.0 32.6 54 VAL 118.6 99.8 28.9 55 TYR 105.9 58.5 64.8 56 MET 156.0 97.9 42.5 57 ALA 67.4 92.8 65.8 58 SER 54.6 65.3 65.8 59 SER 13.6 16.3 78.3 60 HIS 59.8 39.8 70.9 61 ASN 12.6 10.4 89.2 62 LYS 52.4 30.2 77.1 63 ILE 86.3 60.2 65.4 64 THR 43.6 40.8 73.6 65 TRP 140.6 68.6 54.4 66 ASP 67.8 61.4 68.9 67 GLU 3.2 2.3 86.2 68 LYS 37.0 21.3 79.1 69 LEU 0.0 0.0 86.5 70 ASN 30.3 25.1 82.2 71 SER 55.8 66.7 57.9 72 SER 18.8 22.5 80.9 73 LYS 9.0 5.2 87.2 74 LEU 110.9 75.0 58.2 75 PHE 140.6 84.3 47.2 76 SER 39.7 47.5 77.0 77 ALA 71.3 98.3 41.4 78 MET 38.9 24.4 74.3 79 ARG 170.8 81.8 66.7 80 ASP 48.6 44.0 60.1 81 THR 10.1 9.4 75.0 82 ASN 11.5 9.5 71.0 83 ASN 62.3 51.6 69.6 84 LYS 106.7 61.6 61.8 85 TYR 176.7 97.7 42.4 86 VAL 106.9 89.9 47.5 87 LEU 147.8 100.0 28.8 88 THR 84.8 79.3 45.8 89 LEU 147.8 100.0 42.0 90 ASN 59.4 49.2 72.0 91 LYS 72.2 41.6 72.5 92 PHE 166.1 99.6 49.5 93 SER 68.8 82.3 63.0 94 LYS 21.0 12.1 85.6 95 GLU 25.4 18.3 80.1 96 ASN 120.9 100.0 49.1 97 GLU 100.9 72.8 54.3 98 GLY 34.8 100.0 44.5 99 TYR 92.7 51.2 57.2 100 TYR 181.0 100.0 27.6 101 PHE 143.1 85.8 45.3 102 CYS 99.2 100.0 32.8 103 SER 80.3 96.0 39.2 104 VAL 113.7 95.7 46.1 105 ILE 60.7 42.3 67.0 106 SER 82.4 98.6 49.9 107 ASN 22.6 18.7 80.4 108 SER 2.4 2.8 79.8 109 VAL 40.8 34.4 76.9 110 MET 79.8 50.0 61.8 111 TYR 127.9 70.7 55.9 112 PHE 93.8 56.2 58.4 113 SER 80.5 96.3 48.3 114 SER 19.1 22.9 74.1 115 VAL 55.8 47.0 59.9 116 VAL 117.9 99.2 41.1 117 PRO 107.3 86.2 47.0 118 VAL 118.6 99.9 35.2 119 LEU 88.1 59.6 62.9 120 GLN 112.5 75.7 60.0 121 LYS 104.3 60.2 69.1 122 VAL 12.2 10.3 85.3 123 SER 20.3 24.3 77.0 124 SER 28.9 34.6 71.7 125 ALA 2.8 3.8 79.3