Protein Data Bank File : 1gyf Title : IMMUNE SYSTEM 30-APR-99 1GYF Number of Amino Acid Residues : 62 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ASP VAL MET TRP GLU TYR LYS TRP GLU ASN 10 THR GLY ASP ALA GLU LEU TYR GLY PRO PHE 20 THR SER ALA GLN MET GLN THR TRP VAL SER 30 GLU GLY TYR PHE PRO ASP GLY VAL TYR CYS 40 ARG LYS LEU ASP PRO PRO GLY GLY GLN PHE 50 TYR ASN SER LYS ARG ILE ASP PHE ASP LEU 60 TYR THR Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ASP 0.0 56.2 -180.0 55.4 23.7 2 VAL -69.5 110.5 179.9 -172.1 3 MET -90.5 147.0 -179.4 -131.6 62.4 157.5 4 TRP -132.5 -174.4 179.7 -70.1 73.1 5 GLU -156.9 160.7 -179.5 47.3 180.0 -20.8 6 TYR -144.9 133.4 179.2 67.7 83.1 7 LYS -114.6 123.5 -179.8 -168.8 145.7 59.4 70.1 8 TRP -55.2 -48.1 -180.0 -69.1 116.2 9 GLU -98.5 -177.4 179.9 -86.0 -109.3 -50.0 10 ASN -124.7 38.6 -179.9 49.5 86.1 11 THR -105.1 165.2 179.3 83.8 12 GLY -78.6 -4.0 -180.0 13 ASP -114.3 -23.7 -179.9 -58.9 87.2 14 ALA -43.5 137.2 179.6 15 GLU -64.4 137.1 -179.3 -39.0 -138.4 38.3 16 LEU -114.3 136.1 179.4 -139.1 -172.2 17 TYR -141.8 -156.5 179.5 -40.6 -69.7 18 GLY 85.6 16.3 179.6 19 PRO -70.4 54.6 -179.9 26.2 -32.8 20 PHE -123.3 166.2 -179.6 -37.8 -89.9 21 THR -55.4 144.2 179.5 77.6 22 SER -46.7 -30.3 179.1 74.8 23 ALA -66.2 -44.7 179.7 24 GLN -62.7 -26.2 179.3 -163.3 91.6 81.1 25 MET -72.3 -43.2 179.4 -81.6 -59.0 -42.1 26 GLN -61.3 -33.9 179.6 -115.8 -76.2 -63.4 27 THR -62.9 -58.7 179.7 -58.9 28 TRP -57.7 -46.3 179.8 -79.8 -55.4 29 VAL -64.2 -44.6 179.9 -179.8 30 SER -75.3 -32.4 -179.9 -60.8 31 GLU -64.8 -39.6 180.0 -177.0 -87.4 -9.9 32 GLY 123.1 2.1 -180.0 33 TYR -55.7 -26.0 179.9 -133.6 81.5 34 PHE -121.9 78.7 -179.9 -35.6 -41.3 35 PRO -66.1 -30.8 180.0 22.8 -32.2 36 ASP -105.2 4.9 -179.9 -179.2 63.2 37 GLY 83.6 162.3 -180.0 38 VAL -137.5 164.8 179.7 -74.8 39 TYR -78.0 83.5 -179.3 -114.6 38.1 40 CYS -76.0 144.9 179.8 -92.4 41 ARG -158.8 159.3 179.9 -107.0 -103.2 115.6 -155.9 42 LYS -95.7 133.3 -179.9 -84.1 -164.6 -117.6 159.9 43 LEU -64.9 -66.3 180.0 -37.9 -173.2 44 ASP -119.6 126.4 0.1 -158.7 61.2 45 PRO -79.4 139.1 180.0 30.4 -32.5 46 PRO -76.3 135.6 -179.9 29.1 -33.0 47 GLY -144.0 -101.8 -179.9 48 GLY -178.4 -149.5 180.0 49 GLN 48.9 69.2 -179.7 -125.7 163.8 114.9 50 PHE -54.6 163.5 -179.8 -84.3 71.9 51 TYR -146.1 129.8 179.9 -112.6 -60.5 52 ASN -58.3 135.1 179.9 -154.8 -13.9 53 SER -52.8 -28.3 179.8 71.9 54 LYS -81.0 -1.4 -180.0 -131.5 128.0 -96.4 116.6 55 ARG -120.5 5.0 179.8 -96.1 149.9 -157.3 -72.1 56 ILE -103.3 151.8 -180.0 -58.9 -174.4 57 ASP -98.6 115.5 179.9 -160.1 -49.2 58 PHE -98.6 30.4 180.0 -64.8 85.4 59 ASP -134.3 29.1 179.8 -126.8 -61.0 60 LEU -147.0 30.6 -179.9 -36.9 163.5 61 TYR -138.5 -52.0 -180.0 -65.5 -71.0 62 THR -111.4 -51.1 0.0 171.9 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ASP -2.449 3.361 -14.306 2 VAL -1.863 4.501 -10.725 3 MET 0.810 2.204 -9.291 4 TRP 1.198 1.632 -5.550 5 GLU 3.305 -0.241 -2.988 6 TYR 2.952 -1.743 0.497 7 LYS 5.370 -2.285 3.383 8 TRP 4.560 -4.840 6.086 9 GLU 6.526 -2.872 8.673 10 ASN 7.040 0.861 9.190 11 THR 10.838 0.980 9.310 12 GLY 13.348 2.637 7.009 13 ASP 14.784 -0.795 6.227 14 ALA 11.572 -2.848 6.008 15 GLU 11.198 -4.547 2.629 16 LEU 8.843 -2.709 0.293 17 TYR 6.596 -4.273 -2.334 18 GLY 3.178 -3.801 -3.873 19 PRO 4.389 -2.394 -7.252 20 PHE 1.075 -3.447 -8.774 21 THR -1.939 -1.607 -10.181 22 SER -4.061 0.220 -7.600 23 ALA -6.622 -2.432 -8.487 24 GLN -4.288 -5.254 -7.474 25 MET -3.870 -3.450 -4.156 26 GLN -7.603 -3.410 -3.458 27 THR -7.629 -7.156 -4.092 28 TRP -4.965 -8.022 -1.523 29 VAL -6.373 -5.462 0.908 30 SER -9.952 -6.581 0.282 31 GLU -8.942 -10.244 0.098 32 GLY -7.490 -10.131 3.599 33 TYR -3.765 -10.367 2.871 34 PHE -3.402 -7.364 5.186 35 PRO -5.548 -8.009 8.309 36 ASP -3.605 -5.387 10.260 37 GLY -3.049 -3.105 7.275 38 VAL 0.153 -2.233 5.440 39 TYR 2.296 0.800 4.636 40 CYS 0.669 1.727 1.327 41 ARG 2.335 4.256 -0.965 42 LYS 2.360 5.423 -4.578 43 LEU 5.296 4.512 -6.810 44 ASP 5.168 7.414 -9.263 45 PRO 5.434 10.138 -8.361 46 PRO 7.571 8.934 -5.400 47 GLY 7.419 10.989 -2.219 48 GLY 6.793 9.928 1.359 49 GLN 4.375 10.149 4.278 50 PHE 3.206 6.541 4.130 51 TYR -0.439 5.685 4.794 52 ASN -2.049 2.550 6.228 53 SER -4.026 0.605 3.620 54 LYS -6.935 0.837 6.061 55 ARG -6.673 4.640 5.903 56 ILE -6.395 5.046 2.124 57 ASP -9.239 5.580 -0.345 58 PHE -9.382 3.009 -3.144 59 ASP -12.328 4.753 -4.807 60 LEU -10.663 7.908 -6.119 61 TYR -7.952 6.590 -8.435 62 THR -9.289 3.810 -10.660 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S S C S S S 10 S C C S S S S S C C 20 H H H H H H H H H H 30 H H C T T T T S S S 40 S S S S/P S S S S S/S S 50 S S/T T T T/S S S S/T T T 60 T/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 e E E E E e S 10 S S S S e E E S 20 h H H H H H H H H H 30 H h t t T T t e E E 40 E E e S S 50 E E e G G g S S S 60 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ASP 0.0 0.0 91.1 2 VAL 77.3 65.1 64.6 3 MET 93.0 58.3 62.1 4 TRP 194.6 94.9 33.2 5 GLU 109.5 79.0 43.6 6 TYR 160.6 88.8 32.2 7 LYS 160.0 92.2 49.3 8 TRP 103.7 50.6 58.8 9 GLU 41.9 30.2 70.0 10 ASN 38.3 31.7 69.6 11 THR 54.9 51.4 76.6 12 GLY 0.0 0.0 85.0 13 ASP 0.0 0.0 90.4 14 ALA 57.3 78.9 64.0 15 GLU 21.2 15.3 81.5 16 LEU 107.6 72.8 57.0 17 TYR 94.2 52.0 66.5 18 GLY 34.8 100.0 30.1 19 PRO 63.0 50.6 54.1 20 PHE 99.1 59.4 55.5 21 THR 41.2 38.5 62.2 22 SER 77.6 92.8 47.7 23 ALA 22.1 30.5 77.9 24 GLN 71.3 48.0 62.3 25 MET 159.3 100.0 32.4 26 GLN 79.8 53.7 65.0 27 THR 35.1 32.9 74.1 28 TRP 150.1 73.2 41.9 29 VAL 107.6 90.6 49.5 30 SER 35.7 42.6 79.6 31 GLU 47.0 33.9 68.7 32 GLY 8.8 25.2 83.6 33 TYR 67.6 37.4 69.1 34 PHE 166.2 99.6 33.1 35 PRO 31.3 25.2 82.5 36 ASP 0.0 0.0 86.2 37 GLY 34.8 100.0 69.5 38 VAL 116.1 97.7 38.1 39 TYR 109.1 60.3 59.7 40 CYS 99.1 99.9 35.8 41 ARG 156.3 74.8 58.6 42 LYS 114.4 66.0 56.6 43 LEU 106.5 72.1 57.1 44 ASP 14.0 12.7 72.8 45 PRO 24.7 19.9 80.7 46 PRO 40.8 32.8 83.7 47 GLY 4.6 13.1 84.5 48 GLY 13.1 37.6 67.8 49 GLN 0.0 0.0 88.9 50 PHE 129.0 77.4 48.1 51 TYR 55.6 30.7 74.7 52 ASN 74.0 61.2 62.9 53 SER 83.6 100.0 40.2 54 LYS 82.0 47.3 79.5 55 ARG 44.7 21.4 80.1 56 ILE 129.8 90.4 46.7 57 ASP 49.5 44.8 57.6 58 PHE 151.1 90.6 48.3 59 ASP 7.5 6.7 86.3 60 LEU 40.4 27.4 78.3 61 TYR 123.9 68.5 59.8 62 THR 46.0 43.0 80.8