Protein Data Bank File : 1i4fb Title : IMMUNE SYSTEM 21-FEB-01 1I4F Number of Amino Acid Residues : 100 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 MET ILE GLN ARG THR PRO LYS ILE GLN VAL 10 TYR SER ARG HIS PRO ALA GLU ASN GLY LYS 20 SER ASN PHE LEU ASN CYS TYR VAL SER GLY 30 PHE HIS PRO SER ASP ILE GLU VAL ASP LEU 40 LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL 50 GLU HIS SER ASP LEU SER PHE SER LYS ASP 60 TRP SER PHE TYR LEU LEU TYR TYR THR GLU 70 PHE THR PRO THR GLU LYS ASP GLU TYR ALA 80 CYS ARG VAL ASN HIS VAL THR LEU SER GLN 90 PRO LYS ILE VAL LYS TRP ASP ARG ASP MET Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 MET 0.0 161.7 177.4 -57.8 178.3 -97.8 2 ILE -78.5 126.9 179.3 76.0 168.0 3 GLN -126.0 129.3 -178.7 -55.6 -161.1 -43.2 4 ARG -128.6 131.4 -173.0 -70.9 174.1 -92.9 178.6 5 THR -81.9 147.0 -178.7 -156.0 6 PRO -71.5 141.9 166.5 23.0 -34.0 7 LYS -86.3 142.7 -174.4 -60.9 167.2 -68.6 174.4 8 ILE -132.8 128.7 168.8 -57.6 166.5 9 GLN -124.4 134.1 179.8 -60.2 -162.2 57.1 10 VAL -123.1 123.6 -168.8 -176.8 11 TYR -163.9 164.2 176.9 57.6 -74.9 12 SER -100.1 155.3 178.5 57.1 13 ARG -66.5 -39.8 -177.6 179.9 -177.2 -60.3 173.8 14 HIS -123.6 166.0 175.2 -57.0 111.4 15 PRO -57.5 138.1 -178.2 -20.5 29.1 16 ALA -71.2 132.8 173.5 17 GLU -137.3 122.8 179.2 -51.8 -67.1 -46.7 18 ASN -56.9 135.3 179.9 -64.0 -52.1 19 GLY 80.3 2.0 178.8 20 LYS -111.8 133.6 -179.7 -58.6 -65.3 -168.0 -42.3 21 SER -60.7 143.8 -176.3 -165.6 22 ASN -157.6 -170.9 176.3 -156.6 -31.4 23 PHE -130.8 133.0 176.5 -63.8 85.3 24 LEU -102.1 126.6 -177.3 -175.9 57.3 25 ASN -116.5 144.2 169.4 -69.1 -32.6 26 CYS -129.8 109.6 -179.9 -179.6 27 TYR -100.3 115.2 -177.4 -177.6 54.4 28 VAL -111.5 131.8 -176.0 -76.9 29 SER -150.0 167.7 176.9 65.9 30 GLY 74.2 14.3 -173.1 31 PHE -105.2 157.4 175.4 57.8 -84.5 32 HIS -162.9 133.3 2.1 -148.6 -68.5 33 PRO -73.0 178.6 -170.8 37.4 -45.9 34 SER -74.4 -25.8 -175.8 60.7 35 ASP -63.8 126.3 -179.4 -69.5 -1.2 36 ILE -156.2 149.8 176.6 -168.0 163.1 37 GLU -116.2 127.1 -179.9 -178.7 173.8 47.1 38 VAL -133.3 127.5 171.7 -177.7 39 ASP -127.1 150.3 170.6 -66.6 -55.7 40 LEU -101.6 138.3 -175.1 -67.9 177.6 41 LEU -120.6 146.4 172.8 -47.9 175.3 42 LYS -123.3 112.5 -177.2 179.6 -180.0 -179.0 177.8 43 ASN 50.7 43.4 176.6 -57.1 -47.7 44 GLY 82.7 -5.3 -179.2 45 GLU -103.4 145.6 179.5 -174.6 179.9 -68.8 46 ARG -66.5 131.5 172.7 -178.6 174.5 177.4 -83.5 47 ILE -78.2 131.3 -179.0 -61.6 168.5 48 GLU -66.2 -51.7 -167.5 -69.9 -64.4 -35.0 49 LYS -99.6 72.2 179.6 -74.2 -55.7 169.4 -178.8 50 VAL -108.4 133.3 178.1 171.2 51 GLU -114.8 165.1 178.7 -67.4 174.3 -82.4 52 HIS -143.2 158.1 178.8 62.1 84.5 53 SER -74.2 165.9 175.5 62.2 54 ASP -79.5 134.8 -177.4 -57.9 -43.7 55 LEU -49.5 122.3 172.0 -170.8 69.4 56 SER -134.2 -177.5 -176.0 -165.3 57 PHE -149.3 162.4 -174.5 55.6 81.3 58 SER -100.8 -177.4 178.6 -55.6 59 LYS -57.3 -30.3 177.6 -174.5 67.1 43.1 -160.6 60 ASP -89.7 10.6 -178.1 65.0 1.6 61 TRP 75.2 -1.0 177.9 -57.6 107.3 62 SER -72.9 149.9 -175.2 67.6 63 PHE -90.2 158.7 172.3 -64.4 -73.9 64 TYR -145.5 147.3 179.6 63.8 -91.8 65 LEU -143.5 149.7 169.6 -66.3 163.0 66 LEU -115.6 124.2 173.2 179.4 64.6 67 TYR -107.1 140.1 -172.9 -76.8 75.5 68 TYR -154.1 155.5 170.8 60.8 -85.1 69 THR -152.8 151.5 169.8 -176.4 70 GLU -70.0 141.9 172.8 -167.5 157.0 66.8 71 PHE -155.4 165.1 176.8 84.7 -49.9 72 THR -126.9 105.6 -175.4 -65.2 73 PRO -72.8 161.7 -178.9 20.9 -35.9 74 THR -149.8 175.6 -174.6 55.8 75 GLU -72.5 -38.1 -170.7 -73.6 -179.6 61.5 76 LYS -86.4 -25.9 -174.9 65.1 178.7 -174.0 172.4 77 ASP -76.1 144.9 175.4 -62.2 -54.5 78 GLU -117.8 146.1 -177.9 -60.9 -66.8 -37.5 79 TYR -128.8 154.9 178.4 -57.8 -98.7 80 ALA -158.9 168.2 166.2 81 CYS -116.6 138.6 179.2 -176.4 82 ARG -116.2 122.4 -176.8 179.5 177.9 62.3 -154.6 83 VAL -122.7 138.0 168.8 -179.1 84 ASN -128.3 139.7 -175.8 -161.0 26.4 85 HIS -153.4 159.8 -178.2 -171.3 -105.4 86 VAL -62.8 -21.5 178.4 61.5 87 THR -81.4 -0.9 179.6 57.2 88 LEU -114.3 138.8 178.1 -61.5 176.8 89 SER -69.3 -33.1 177.6 -57.2 90 GLN -152.8 165.5 -178.6 60.9 -78.2 -48.2 91 PRO -55.5 141.2 -179.4 -25.4 37.5 92 LYS -103.8 125.0 178.0 173.9 64.2 178.5 -179.2 93 ILE -107.2 132.4 177.7 -57.1 179.5 94 VAL -125.7 120.2 179.1 180.0 95 LYS -73.2 141.8 171.8 -179.6 170.8 176.1 179.5 96 TRP -76.5 119.2 173.9 175.8 47.9 97 ASP -106.6 116.7 -178.9 -180.0 -46.7 98 ARG -55.9 -30.2 -179.5 -56.2 -178.9 173.3 -150.4 99 ASP -79.5 13.2 -172.5 -59.2 -50.5 100 MET -144.0 16.6 0.0 -70.3 -153.2 -75.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 MET 5.263 19.779 8.387 2 ILE 4.366 16.087 8.105 3 GLN 2.334 14.707 11.033 4 ARG 1.578 11.033 11.498 5 THR -0.631 9.644 14.176 6 PRO 0.594 6.816 16.411 7 LYS -0.381 3.175 15.930 8 ILE -0.894 1.540 19.340 9 GLN -0.701 -2.064 20.559 10 VAL -1.308 -3.024 24.183 11 TYR -0.354 -6.569 25.179 12 SER 1.422 -8.716 27.724 13 ARG 4.817 -10.270 27.254 14 HIS 3.492 -13.732 28.266 15 PRO -0.020 -15.296 28.446 16 ALA -2.023 -13.799 31.169 17 GLU -2.633 -15.804 34.277 18 ASN -4.373 -14.262 37.234 19 GLY -2.150 -13.867 40.198 20 LYS 1.062 -14.537 38.155 21 SER 3.707 -11.887 37.475 22 ASN 4.016 -10.694 33.856 23 PHE 4.840 -7.576 31.824 24 LEU 2.384 -5.087 30.262 25 ASN 3.509 -3.449 27.070 26 CYS 2.287 -0.489 25.105 27 TYR 4.006 -0.292 21.686 28 VAL 3.540 3.021 19.900 29 SER 4.785 3.364 16.314 30 GLY 4.393 5.192 13.064 31 PHE 4.210 8.640 14.559 32 HIS 5.846 12.006 13.750 33 PRO 6.883 14.316 15.374 34 SER 8.562 12.456 18.236 35 ASP 7.005 14.196 21.247 36 ILE 4.449 11.849 22.759 37 GLU 2.927 11.102 26.162 38 VAL 2.293 7.502 27.157 39 ASP 0.917 6.107 30.380 40 LEU -0.129 2.628 31.380 41 LEU -3.298 2.591 33.520 42 LYS -4.665 0.194 36.145 43 ASN -8.378 0.725 36.765 44 GLY -8.018 4.159 35.249 45 GLU -5.061 5.323 37.333 46 ARG -1.500 5.836 36.098 47 ILE 0.931 3.049 36.988 48 GLU 4.037 4.516 38.634 49 LYS 6.962 2.481 37.639 50 VAL 6.614 2.451 33.853 51 GLU 9.753 2.509 31.766 52 HIS 10.369 3.068 28.098 53 SER 12.762 2.317 25.320 54 ASP 15.101 4.788 23.667 55 LEU 13.631 6.660 20.687 56 SER 14.265 5.075 17.325 57 PHE 12.723 5.189 13.869 58 SER 11.705 3.205 10.841 59 LYS 12.336 3.276 7.107 60 ASP 9.724 5.909 6.542 61 TRP 11.312 8.046 9.289 62 SER 8.407 7.489 11.685 63 PHE 9.209 6.927 15.318 64 TYR 8.581 4.011 17.664 65 LEU 8.741 3.406 21.408 66 LEU 7.929 0.606 23.844 67 TYR 6.525 1.508 27.301 68 TYR 6.384 -1.353 29.849 69 THR 5.931 -2.391 33.412 70 GLU 5.918 -5.515 35.508 71 PHE 2.413 -6.383 36.665 72 THR 0.252 -9.140 38.056 73 PRO -3.143 -9.340 36.336 74 THR -6.369 -10.473 38.038 75 GLU -9.886 -11.066 37.157 76 LYS -11.244 -7.730 38.436 77 ASP -8.479 -5.405 37.297 78 GLU -8.584 -3.584 33.996 79 TYR -5.559 -2.182 32.173 80 ALA -5.035 0.255 29.363 81 CYS -2.575 2.551 27.634 82 ARG -3.206 6.258 27.374 83 VAL -1.450 8.160 24.548 84 ASN -1.312 11.807 23.686 85 HIS 0.280 13.324 20.588 86 VAL -0.206 16.530 18.608 87 THR -2.249 14.594 16.064 88 LEU -4.897 13.725 18.752 89 SER -7.745 16.013 20.037 90 GLN -7.688 14.340 23.415 91 PRO -5.787 11.419 25.000 92 LYS -6.466 8.102 23.276 93 ILE -7.043 5.158 25.592 94 VAL -6.667 1.603 24.378 95 LYS -7.820 -1.247 26.658 96 TRP -5.711 -4.329 27.210 97 ASP -7.492 -7.455 25.823 98 ARG -5.693 -10.574 27.024 99 ASP -6.376 -12.616 23.840 100 MET -4.447 -10.475 21.405 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 10 S S C S S S S S S S 20 S S S/S S S S S S S S/S 30 S S/P S S S S S S S S 40 S/T T T T/S S S S S S/S S 50 S S S S S/S S S S/T T T 60 T/S S S S S S S S S S 70 S S/S S S S S S S S S/S 80 S S S S S S C C C S 90 S S S S S S S S/S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 B E E E E 10 E E e S t T T t 20 E E E E E E E E E 30 E B S S E E E E 40 E E e T E E e S S 50 E E e E E e T T 60 t e E E E E E E E E 70 E S S e E E 80 E E E E t T T t S S 90 E E E E e t T T t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 MET 0.0 0.0 93.6 2 ILE 39.1 27.2 78.3 3 GLN 88.8 59.8 54.7 4 ARG 148.8 71.2 59.5 5 THR 44.8 41.9 65.2 6 PRO 124.1 99.7 42.3 7 LYS 35.9 20.7 82.6 8 ILE 133.9 93.3 38.7 9 GLN 38.9 26.1 70.1 10 VAL 118.4 99.6 41.0 11 TYR 122.1 67.4 66.6 12 SER 76.8 91.9 61.5 13 ARG 104.7 50.1 68.3 14 HIS 57.7 38.4 67.2 15 PRO 19.5 15.7 80.6 16 ALA 70.9 97.6 54.6 17 GLU 46.2 33.4 74.1 18 ASN 78.0 64.5 71.1 19 GLY 7.1 20.5 68.2 20 LYS 40.0 23.0 82.1 21 SER 36.6 43.8 76.8 22 ASN 116.5 96.3 56.1 23 PHE 116.0 69.5 67.1 24 LEU 147.8 100.0 33.1 25 ASN 109.5 90.6 45.2 26 CYS 99.2 100.0 30.2 27 TYR 111.9 61.8 61.3 28 VAL 118.8 100.0 30.9 29 SER 71.7 85.8 52.2 30 GLY 27.5 78.9 65.9 31 PHE 166.8 100.0 40.1 32 HIS 105.9 70.5 53.7 33 PRO 76.6 61.5 61.5 34 SER 58.3 69.8 46.4 35 ASP 0.0 0.0 87.5 36 ILE 138.2 96.3 38.1 37 GLU 38.6 27.9 80.3 38 VAL 118.8 100.0 33.1 39 ASP 98.0 88.7 60.8 40 LEU 147.8 100.0 34.4 41 LEU 141.7 95.9 50.1 42 LYS 87.7 50.6 72.5 43 ASN 57.5 47.6 71.5 44 GLY 7.0 20.2 69.4 45 GLU 6.6 4.8 88.9 46 ARG 106.4 50.9 79.4 47 ILE 113.0 78.8 53.5 48 GLU 27.1 19.5 83.1 49 LYS 6.4 3.7 85.0 50 VAL 112.5 94.7 52.6 51 GLU 33.3 24.0 75.2 52 HIS 67.2 44.7 66.0 53 SER 42.9 51.3 68.2 54 ASP 0.0 0.0 89.1 55 LEU 89.2 60.4 59.7 56 SER 39.9 47.7 68.4 57 PHE 78.8 47.2 61.2 58 SER 38.1 45.6 74.3 59 LYS 0.0 0.0 91.9 60 ASP 34.3 31.0 77.7 61 TRP 40.3 19.6 82.6 62 SER 80.0 95.7 62.9 63 PHE 138.6 83.1 46.9 64 TYR 107.8 59.5 66.4 65 LEU 136.7 92.5 48.0 66 LEU 94.8 64.1 60.3 67 TYR 159.4 88.0 41.2 68 TYR 118.5 65.5 63.5 69 THR 99.2 92.8 44.0 70 GLU 43.4 31.3 73.8 71 PHE 150.1 90.0 39.8 72 THR 58.1 54.4 67.3 73 PRO 124.4 99.9 52.8 74 THR 67.6 63.2 68.9 75 GLU 11.0 8.0 88.6 76 LYS 10.5 6.1 89.9 77 ASP 103.9 94.0 59.1 78 GLU 58.3 42.1 77.1 79 TYR 177.2 97.9 38.7 80 ALA 61.1 84.2 47.5 81 CYS 99.2 100.0 31.8 82 ARG 138.5 66.3 51.6 83 VAL 118.8 100.0 31.9 84 ASN 71.5 59.1 61.3 85 HIS 145.4 96.8 46.6 86 VAL 45.6 38.4 72.5 87 THR 87.0 81.4 58.9 88 LEU 116.4 78.8 67.1 89 SER 8.5 10.2 86.9 90 GLN 29.0 19.5 78.6 91 PRO 71.5 57.4 59.3 92 LYS 62.0 35.8 67.9 93 ILE 67.3 46.9 59.6 94 VAL 78.4 66.0 57.7 95 LYS 51.7 29.8 79.1 96 TRP 196.9 96.1 43.3 97 ASP 47.5 43.0 66.7 98 ARG 139.1 66.6 68.2 99 ASP 4.2 3.8 83.6 100 MET 33.5 21.0 86.1