Protein Data Bank File : 1fl7d Title : HORMONE/GROWTH FACTOR 11-AUG-00 1FL7 Number of Amino Acid Residues : 106 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 CYS GLU LEU THR ASN ILE THR ILE ALA ILE 10 GLU LYS GLU GLU CYS ARG PHE CYS ILE SER 20 ILE ASN THR ALA TRP CYS ALA GLY TYR CYS 30 TYR THR ARG ASP LEU VAL TYR LYS ASP PRO 40 ALA ARG PRO LYS ILE GLN LYS THR CYS THR 50 PHE LYS GLU LEU VAL TYR GLU THR VAL ARG 60 VAL PRO GLY CYS ALA HIS HIS ALA ASP SER 70 LEU TYR THR TYR PRO VAL ALA THR GLN CYS 80 HIS CYS GLY LYS CYS ASP SER ASP SER THR 90 ASP CYS THR VAL ARG GLY LEU GLY PRO SER 100 TYR CYS SER PHE GLY GLU Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 CYS 0.0 101.2 179.2 -179.5 2 GLU -148.0 156.4 179.1 79.5 -93.2 54.6 3 LEU -50.9 128.0 178.9 -77.6 167.8 4 THR -131.6 149.2 179.7 55.3 5 ASN -80.9 125.2 177.3 -118.0 -16.8 6 ILE -130.2 176.9 179.6 81.8 171.6 7 THR -135.0 109.9 179.8 86.6 8 ILE -84.1 -178.8 -179.1 65.2 176.1 9 ALA -121.1 127.2 179.2 10 ILE -96.6 119.1 -177.1 -49.8 163.5 11 GLU -105.7 118.8 179.3 -169.9 172.7 -64.1 12 LYS -100.8 96.3 -179.3 -173.5 57.6 167.2 -62.5 13 GLU -52.7 -62.3 -178.7 -73.4 -158.4 72.8 14 GLU -41.2 -34.5 -178.5 -62.1 71.5 31.2 15 CYS -106.6 12.8 178.9 -59.1 16 ARG 40.9 63.2 178.0 -63.9 177.5 164.7 176.7 17 PHE -171.1 159.5 -179.9 81.8 133.8 18 CYS -127.3 147.7 176.3 -51.1 19 ILE -116.4 162.0 179.4 48.4 -178.6 20 SER -117.2 140.1 177.9 62.5 21 ILE -130.8 134.5 -179.6 -178.7 179.7 22 ASN -77.3 150.8 -178.1 -176.3 -68.5 23 THR -164.0 148.6 -179.6 -167.5 24 ALA -89.6 126.7 178.3 25 TRP -139.8 -175.7 -177.6 -98.5 90.4 26 CYS -95.9 141.4 179.6 -54.8 27 ALA -168.6 141.7 179.6 28 GLY 156.2 -147.2 -179.5 29 TYR -122.2 153.4 178.8 -66.9 76.8 30 CYS -145.7 147.6 -179.4 -60.7 31 TYR -85.9 132.3 178.4 -166.1 96.1 32 THR -139.4 160.8 179.2 18.0 33 ARG -138.0 151.0 -179.4 63.9 174.8 107.1 -70.4 34 ASP -104.5 104.5 -178.4 -169.1 5.4 35 LEU -53.5 126.8 179.4 -58.4 -171.2 36 VAL -78.6 -16.7 178.0 -53.2 37 TYR -122.7 91.8 -178.2 173.0 63.1 38 LYS -109.9 -178.2 178.8 47.8 -178.4 65.9 82.1 39 ASP -130.3 119.0 -179.8 161.5 40.0 40 PRO -55.7 -48.9 -179.4 -30.2 44.0 41 ALA -49.8 -73.2 -179.4 42 ARG -114.8 92.1 179.8 -63.9 -57.7 157.7 -177.2 43 PRO -73.7 164.5 179.4 34.3 -45.2 44 LYS -84.1 138.5 178.7 179.8 -169.2 174.9 -173.0 45 ILE -90.1 130.4 -178.2 -51.4 -61.7 46 GLN -93.6 148.3 -179.9 -57.6 152.1 -69.4 47 LYS -66.2 167.5 179.6 -55.7 -72.4 -169.2 51.0 48 THR -156.9 151.1 177.4 -71.4 49 CYS -68.7 131.0 -178.5 -170.5 50 THR -177.3 164.6 -178.8 171.8 51 PHE -61.7 146.9 178.0 82.8 93.0 52 LYS -109.5 -39.3 178.8 -175.9 177.6 -178.4 58.0 53 GLU -140.3 129.3 -179.4 -74.5 -65.4 -48.4 54 LEU -133.7 165.8 179.9 86.8 -162.0 55 VAL -139.2 168.1 179.0 -38.8 56 TYR -110.4 146.2 179.1 -79.2 74.3 57 GLU -132.6 157.0 -179.2 -78.1 -164.9 49.4 58 THR -126.0 148.6 179.3 -60.9 59 VAL -140.3 145.5 179.0 -169.0 60 ARG -88.9 107.5 -179.1 -75.8 -175.2 52.6 -167.5 61 VAL -86.1 138.2 179.9 179.6 62 PRO -60.7 166.1 179.5 32.9 -45.6 63 GLY -119.6 -146.8 179.6 64 CYS -168.1 -174.8 178.8 61.3 65 ALA -61.6 172.4 -179.8 66 HIS 47.9 -2.3 177.6 68.2 -77.3 67 HIS -154.7 124.0 -178.5 -161.7 71.0 68 ALA -71.4 158.6 178.3 69 ASP -68.3 160.0 -178.4 51.8 -80.0 70 SER -145.7 -171.7 179.6 58.1 71 LEU -107.1 146.5 179.0 -60.1 176.2 72 TYR -140.2 110.5 178.9 -175.3 52.0 73 THR -94.9 140.5 -178.6 76.4 74 TYR -143.9 145.5 -179.9 57.5 82.6 75 PRO -70.0 139.4 179.7 36.2 -45.4 76 VAL -129.6 141.9 -177.9 -173.1 77 ALA -82.0 133.9 179.6 78 THR -98.2 -48.5 179.8 -50.1 79 GLN -141.3 136.8 -180.0 -179.3 -176.7 53.8 80 CYS -104.4 155.2 178.6 -61.4 81 HIS -170.4 154.8 177.3 84.4 -55.3 82 CYS -82.1 108.7 -178.9 -70.2 83 GLY -152.7 177.4 -179.4 84 LYS -60.2 147.1 179.2 -157.5 163.2 -65.0 -57.6 85 CYS -79.5 113.7 -178.9 -178.4 86 ASP -64.5 94.6 -179.7 -173.4 13.1 87 SER -51.3 -38.9 -179.0 167.7 88 ASP -61.7 -39.4 -178.6 -92.7 -67.9 89 SER -110.7 -11.9 -177.1 72.1 90 THR -117.9 144.7 176.5 -61.2 91 ASP -93.3 98.0 -177.7 172.3 34.3 92 CYS -78.3 110.8 -175.9 -55.4 93 THR -141.9 169.5 178.2 77.2 94 VAL -84.5 -43.6 -179.6 -168.2 95 ARG -140.3 148.6 178.3 -120.4 -149.7 81.1 157.4 96 GLY -131.6 -169.5 179.7 97 LEU -78.4 -18.6 -179.9 -83.3 178.7 98 GLY 108.2 144.6 -179.6 99 PRO -59.4 -41.6 -178.9 33.9 -44.5 100 SER -93.4 13.3 179.0 51.2 101 TYR -57.1 142.3 178.2 178.6 60.0 102 CYS -134.9 117.0 -179.9 176.9 103 SER -52.9 -20.4 179.8 169.4 104 PHE -119.4 -167.5 -179.0 -44.9 86.0 105 GLY -135.4 155.7 179.1 106 GLU 51.9 107.8 0.0 -147.6 160.5 60.5 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 CYS 14.797 47.110 29.062 2 GLU 15.020 43.611 30.524 3 LEU 16.782 40.287 29.910 4 THR 15.109 38.649 26.965 5 ASN 15.825 35.297 25.396 6 ILE 17.409 35.681 21.978 7 THR 19.264 33.347 19.635 8 ILE 22.632 34.323 18.204 9 ALA 24.532 32.699 15.362 10 ILE 27.729 30.666 15.686 11 GLU 29.789 30.930 12.523 12 LYS 32.304 28.277 11.600 13 GLU 34.411 29.898 8.874 14 GLU 36.519 26.903 7.932 15 CYS 33.331 25.005 7.121 16 ARG 31.373 27.875 5.618 17 PHE 28.271 27.449 7.803 18 CYS 26.575 28.621 11.031 19 ILE 24.769 26.867 13.872 20 SER 22.454 28.659 16.263 21 ILE 22.571 28.704 20.043 22 ASN 19.992 30.363 22.287 23 THR 21.191 32.894 24.826 24 ALA 19.903 35.589 27.176 25 TRP 20.671 39.180 26.329 26 CYS 19.265 42.703 26.691 27 ALA 16.403 44.398 24.860 28 GLY 13.641 46.876 25.665 29 TYR 12.964 50.564 26.312 30 CYS 14.649 53.513 27.952 31 TYR 13.686 57.120 28.550 32 THR 15.829 59.738 26.825 33 ARG 15.488 63.445 26.233 34 ASP 16.870 65.725 23.556 35 LEU 18.381 68.712 25.318 36 VAL 16.949 71.927 23.922 37 TYR 20.074 73.709 25.144 38 LYS 23.150 71.787 24.072 39 ASP 26.879 72.067 23.549 40 PRO 28.441 70.914 20.232 41 ALA 31.825 70.189 21.806 42 ARG 30.770 67.840 24.586 43 PRO 27.194 66.562 24.100 44 LYS 25.305 64.579 26.716 45 ILE 25.415 60.787 26.390 46 GLN 21.981 59.147 26.514 47 LYS 21.170 55.828 28.216 48 THR 20.487 52.666 26.198 49 CYS 19.225 49.179 26.901 50 THR 22.270 46.998 27.473 51 PHE 24.082 44.564 29.714 52 LYS 25.184 45.735 33.160 53 GLU 26.886 42.469 34.083 54 LEU 27.797 39.676 31.655 55 VAL 29.573 36.314 31.558 56 TYR 31.108 34.011 28.978 57 GLU 29.992 30.541 27.943 58 THR 31.506 27.922 25.677 59 VAL 30.086 25.397 23.253 60 ARG 31.657 22.656 21.199 61 VAL 30.850 23.554 17.611 62 PRO 30.792 20.816 14.946 63 GLY 33.380 20.585 12.222 64 CYS 33.489 19.119 8.750 65 ALA 36.072 17.400 6.579 66 HIS 39.471 19.132 6.389 67 HIS 38.635 20.848 9.693 68 ALA 38.105 19.567 13.235 69 ASP 35.336 20.588 15.643 70 SER 36.119 23.342 18.127 71 LEU 35.177 25.505 21.082 72 TYR 33.371 28.800 20.843 73 THR 33.086 31.065 23.854 74 TYR 30.510 33.861 23.660 75 PRO 29.314 36.630 26.032 76 VAL 26.000 36.157 27.849 77 ALA 24.012 38.751 29.783 78 THR 23.604 38.380 33.536 79 GLN 21.817 41.672 34.169 80 CYS 20.286 44.360 31.904 81 HIS 19.798 48.086 32.545 82 CYS 19.306 51.445 30.856 83 GLY 22.803 52.873 31.043 84 LYS 25.643 54.480 29.142 85 CYS 26.909 52.345 26.255 86 ASP 30.200 50.906 27.458 87 SER 32.617 51.990 24.735 88 ASP 35.392 49.697 26.005 89 SER 33.509 46.425 25.562 90 THR 30.743 47.521 23.252 91 ASP 30.413 48.548 19.631 92 CYS 27.948 51.380 20.251 93 THR 25.798 51.721 17.160 94 VAL 22.430 52.645 15.692 95 ARG 22.381 49.450 13.633 96 GLY 24.531 46.354 13.404 97 LEU 24.416 43.191 11.325 98 GLY 22.114 41.492 13.786 99 PRO 22.546 38.782 16.450 100 SER 21.592 35.911 14.143 101 TYR 23.482 37.206 11.103 102 CYS 25.301 34.465 9.240 103 SER 28.089 35.223 6.783 104 PHE 26.928 32.147 4.855 105 GLY 23.599 30.564 4.088 106 GLU 21.512 27.509 4.937 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C S S S S S S/S S S S 10 S S/T T T T C S S S S 20 S S S S/S S S S S S S 30 S/S S S S S S/S S S S/T T 40 T T/S S S S S S S S S 50 S S S/S S S S S S S S 60 S S S S/T T T T/S S S S 70 S S S S S S S S S/S S 80 S S C C C T T T T C 90 S S S S/S S S S C C S 100 S S S/S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 E E E E E E E E E 10 E E G G G g E E E E 20 E E E E E E E 30 S S S 40 S S E E E 50 E E E E E E E E E E 60 E B T T B E 70 E E E E E E E E E E 80 E E E t T T T t 90 S S t T T 100 t S S Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 CYS 97.1 97.8 54.5 2 GLU 31.8 22.9 77.4 3 LEU 93.3 63.1 62.5 4 THR 61.9 57.9 68.9 5 ASN 33.7 27.9 81.0 6 ILE 100.6 70.1 55.2 7 THR 45.8 42.8 69.7 8 ILE 115.9 80.8 43.7 9 ALA 67.1 92.4 56.3 10 ILE 139.7 97.3 31.6 11 GLU 97.1 70.0 55.7 12 LYS 159.7 92.1 58.4 13 GLU 25.7 18.5 81.3 14 GLU 62.3 44.9 61.9 15 CYS 94.1 94.9 44.5 16 ARG 28.8 13.8 80.3 17 PHE 110.6 66.3 56.0 18 CYS 92.9 93.6 47.6 19 ILE 96.3 67.1 46.8 20 SER 24.6 29.4 75.1 21 ILE 110.7 77.1 50.1 22 ASN 57.1 47.2 65.8 23 THR 98.7 92.3 49.5 24 ALA 43.1 59.4 67.2 25 TRP 154.4 75.3 45.0 26 CYS 97.4 98.2 41.3 27 ALA 29.7 40.9 70.5 28 GLY 21.3 61.2 60.7 29 TYR 0.0 0.0 86.3 30 CYS 88.0 88.7 51.1 31 TYR 21.7 12.0 89.6 32 THR 63.9 59.8 70.9 33 ARG 80.3 38.4 75.5 34 ASP 20.2 18.2 84.7 35 LEU 90.1 60.9 62.4 36 VAL 0.0 0.0 87.9 37 TYR 1.0 0.5 89.0 38 LYS 76.8 44.3 77.3 39 ASP 48.0 43.4 63.4 40 PRO 13.1 10.5 86.7 41 ALA 11.3 15.6 79.9 42 ARG 12.5 6.0 86.5 43 PRO 59.7 48.0 78.8 44 LYS 77.7 44.8 68.3 45 ILE 55.8 38.9 74.2 46 GLN 67.2 45.2 72.3 47 LYS 72.8 42.0 75.3 48 THR 41.4 38.7 67.5 49 CYS 88.0 88.7 46.8 50 THR 87.0 81.4 55.0 51 PHE 144.7 86.8 53.2 52 LYS 80.1 46.2 69.0 53 GLU 33.8 24.4 74.7 54 LEU 107.7 72.9 47.1 55 VAL 48.6 40.9 70.4 56 TYR 65.1 35.9 66.7 57 GLU 56.2 40.5 69.1 58 THR 68.2 63.8 50.3 59 VAL 72.7 61.2 58.6 60 ARG 52.4 25.1 79.6 61 VAL 116.1 97.7 38.8 62 PRO 64.8 52.0 54.9 63 GLY 32.2 92.6 60.9 64 CYS 58.8 59.3 63.0 65 ALA 0.3 0.4 83.3 66 HIS 28.3 18.8 77.9 67 HIS 90.5 60.3 65.8 68 ALA 2.6 3.5 83.8 69 ASP 55.6 50.4 77.1 70 SER 40.3 48.2 73.6 71 LEU 50.1 33.9 66.0 72 TYR 91.7 50.7 59.6 73 THR 44.4 41.6 65.4 74 TYR 172.4 95.2 39.5 75 PRO 74.4 59.8 51.6 76 VAL 105.0 88.4 63.0 77 ALA 72.6 100.0 38.7 78 THR 44.7 41.8 62.1 79 GLN 58.6 39.5 62.1 80 CYS 97.8 98.6 44.3 81 HIS 95.7 63.7 64.8 82 CYS 67.6 68.1 54.3 83 GLY 31.1 89.3 57.1 84 LYS 68.1 39.3 72.4 85 CYS 76.7 77.3 50.8 86 ASP 42.6 38.5 73.9 87 SER 7.8 9.3 84.9 88 ASP 0.0 0.0 90.4 89 SER 40.1 48.0 71.4 90 THR 75.5 70.6 64.1 91 ASP 6.4 5.8 76.2 92 CYS 64.4 65.0 59.5 93 THR 65.0 60.8 79.1 94 VAL 0.0 0.0 85.9 95 ARG 30.5 14.6 87.7 96 GLY 4.6 13.3 83.3 97 LEU 40.3 27.3 74.8 98 GLY 10.5 30.2 66.3 99 PRO 48.5 39.0 64.5 100 SER 28.9 34.6 74.1 101 TYR 81.8 45.2 71.0 102 CYS 75.6 76.2 56.8 103 SER 48.5 58.1 62.7 104 PHE 119.0 71.3 64.4 105 GLY 2.7 7.8 73.1 106 GLU 0.0 0.0 89.0