Protein Data Bank File : 1scfd Title : HORMONE/GROWTH FACTOR 04-JUN-98 1SCF Number of Amino Acid Residues : 101 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ASN VAL LYS ASP VAL THR LYS LEU VAL ALA 10 ASN LEU PRO LYS ASP TYR ILE THR LEU LYS 20 TYR VAL PRO GLY ASP VAL LEU PRO SER HIS 30 CYS TRP ILE SER GLU VAL VAL GLN LEU SER 40 ASP SER LEU THR ASP LEU LEU ASP LYS PHE 50 SER ASN ILE SER GLU GLY LEU SER ASN TYR 60 SER ILE ILE ASP LYS LEU VAL ASN ILE VAL 70 ASP ASP LEU VAL GLU CYS VAL SER PRO GLU 80 PRO ARG LEU PHE THR PRO GLU GLU PHE PHE 90 ARG ILE PHE ASN ARG SER ILE ASP ALA PHE 100 LYS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ASN 0.0 -96.7 -173.0 0.0 0.0 2 VAL -34.5 -60.5 168.9 162.1 3 LYS -44.3 -50.9 176.3 0.0 0.0 0.0 0.0 4 ASP -78.2 -25.5 178.5 -86.2 -4.5 5 VAL -62.2 -43.3 -178.7 163.0 6 THR -66.5 -28.8 -179.6 -91.1 7 LYS -81.4 -38.5 167.7 -165.7 -173.0 -80.9 165.1 8 LEU -61.1 -49.6 174.8 -169.8 62.6 9 VAL -50.5 -46.4 175.0 -179.0 10 ALA -60.2 -27.1 -176.4 11 ASN -102.3 2.0 173.8 -136.5 39.9 12 LEU -103.1 145.4 178.8 -64.2 169.0 13 PRO -59.4 138.2 177.9 -21.3 40.0 14 LYS -61.9 -27.9 175.3 -74.5 153.6 -161.9 166.0 15 ASP -98.5 14.1 166.5 65.4 -20.0 16 TYR -79.6 -164.9 23.3 -174.4 49.3 17 ILE -165.3 132.4 175.1 -54.7 171.6 18 THR -86.2 129.5 175.0 -52.0 19 LEU -135.5 133.4 168.9 176.8 53.2 20 LYS -82.7 103.9 -165.4 -58.2 -168.4 -169.6 -179.5 21 TYR -93.4 137.1 180.0 170.7 89.4 22 VAL -86.4 105.0 177.8 175.1 23 PRO -56.9 141.0 -174.7 -25.7 42.1 24 GLY 83.6 84.2 62.0 25 ASP 32.6 -51.3 -179.8 41.9 8.0 26 VAL -85.0 -33.5 -172.6 -59.0 27 LEU -81.5 158.2 174.5 -58.1 -176.8 28 PRO -74.1 146.3 -178.9 30.7 -40.3 29 SER -40.0 -45.2 179.6 -50.5 30 HIS -57.7 -16.7 180.0 74.9 -90.5 31 CYS -87.1 -14.9 -171.6 -79.5 32 TRP -139.9 -26.7 -167.0 59.9 -97.0 33 ILE -60.8 -34.5 -172.4 -164.3 56.7 34 SER -78.4 -33.7 171.0 80.2 35 GLU -73.2 33.7 81.3 174.7 71.4 -69.3 36 VAL 12.7 -31.6 172.6 -71.2 37 VAL -64.2 -44.9 174.7 166.3 38 GLN -66.5 -33.4 173.8 -67.1 -55.9 -23.3 39 LEU -70.5 -44.7 174.5 -71.6 171.2 40 SER -56.2 -41.5 -178.5 -177.4 41 ASP -60.3 -50.5 -176.9 -161.9 -82.9 42 SER -67.3 -41.6 178.4 -65.7 43 LEU -69.6 -33.0 178.0 -81.4 166.0 44 THR -72.5 -35.3 168.3 -69.2 45 ASP -68.9 -36.5 179.8 -55.2 -17.2 46 LEU -64.5 -43.2 177.1 -168.4 58.9 47 LEU -52.8 -33.0 -177.0 -170.5 69.5 48 ASP -76.6 -10.1 178.9 175.7 76.6 49 LYS -89.5 -5.1 -178.3 -54.4 -60.6 167.5 59.1 50 PHE -120.3 163.5 173.1 -68.2 -74.8 51 SER -134.9 160.7 177.1 88.5 52 ASN -63.2 153.5 177.0 -76.9 -70.2 53 ILE -123.7 162.8 -177.9 61.6 172.9 54 SER -65.0 -30.1 -179.7 57.4 55 GLU -174.9 145.9 164.5 104.3 -60.8 -58.4 56 GLY 115.4 -159.6 -175.7 57 LEU -68.5 124.6 -173.9 -152.1 -169.3 58 SER -132.3 120.9 178.8 173.7 59 ASN -64.7 -38.9 174.6 -71.5 -0.9 60 TYR -51.1 -57.7 -179.1 -171.3 87.1 61 SER -60.8 -35.7 179.0 -52.2 62 ILE -68.2 -46.4 -177.6 -59.8 -178.9 63 ILE -71.2 -39.4 178.9 -62.4 168.1 64 ASP -58.0 -41.3 171.1 -170.1 34.9 65 LYS -66.4 -32.2 175.0 -61.0 -155.3 -151.4 73.8 66 LEU -72.1 -35.6 178.9 -58.4 -169.8 67 VAL -64.5 -45.3 -179.2 167.1 68 ASN -63.5 -31.0 168.7 -62.8 -42.7 69 ILE -65.6 -42.5 179.2 -57.2 163.4 70 VAL -74.0 -23.8 174.5 -164.1 71 ASP -69.2 -46.5 171.1 -93.2 -4.1 72 ASP -53.0 -55.9 177.7 -64.3 -14.9 73 LEU -61.9 -30.5 174.1 -54.0 -177.6 74 VAL -68.2 -36.7 179.3 173.7 75 GLU -77.4 -23.3 172.7 -90.2 154.1 46.1 76 CYS -66.2 -35.5 177.6 -174.6 77 VAL -77.7 -138.2 61.5 0.0 78 SER -129.8 168.7 176.5 -167.8 79 PRO -109.3 149.6 -171.0 41.5 -37.9 80 GLU -90.1 147.4 176.2 0.0 0.0 0.0 81 PRO -55.7 131.6 178.2 -32.8 42.6 82 ARG -137.8 150.5 179.2 -169.2 156.6 158.8 176.4 83 LEU -104.7 128.6 180.0 -50.1 -173.3 84 PHE -124.1 143.8 167.9 -60.0 -82.5 85 THR -70.8 165.3 175.9 56.5 86 PRO -52.1 -51.8 177.0 -37.3 48.6 87 GLU -55.6 -38.1 174.3 59.0 166.6 10.4 88 GLU -70.8 -47.6 178.0 -64.0 162.9 2.8 89 PHE -59.2 -47.0 -177.8 177.7 89.1 90 PHE -77.2 -18.3 166.0 -71.6 -73.1 91 ARG -68.2 -36.9 175.2 -168.0 -172.9 172.2 163.6 92 ILE -68.5 -46.2 169.3 -62.9 166.3 93 PHE -47.3 -53.9 -178.0 174.2 81.0 94 ASN -63.1 -42.0 178.2 -80.1 -37.3 95 ARG -62.4 -40.8 -176.3 172.7 86.7 -165.9 -62.8 96 SER -71.7 -42.6 175.8 -55.4 97 ILE -59.6 -37.0 179.0 -92.1 42.3 98 ASP -69.6 -41.9 -177.7 -179.3 71.4 99 ALA -67.0 -12.0 169.6 100 PHE -68.2 -31.3 167.6 -119.2 -57.0 101 LYS -86.6 -102.2 0.0 0.0 0.0 0.0 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ASN 46.416 43.904 38.273 2 VAL 45.936 42.823 34.490 3 LYS 48.844 40.432 34.132 4 ASP 47.703 38.684 37.372 5 VAL 44.000 39.173 36.672 6 THR 44.166 36.943 33.605 7 LYS 45.958 34.179 35.596 8 LEU 43.391 34.389 38.362 9 VAL 40.479 34.034 35.786 10 ALA 42.319 30.924 34.543 11 ASN 42.665 29.549 38.081 12 LEU 39.069 30.126 39.157 13 PRO 36.365 27.588 38.004 14 LYS 34.492 28.864 34.822 15 ASP 31.146 27.984 36.585 16 TYR 31.978 29.716 39.865 17 ILE 30.838 35.733 42.127 18 THR 28.142 38.118 43.587 19 LEU 28.610 41.845 42.783 20 LYS 26.046 44.522 43.409 21 TYR 26.219 46.004 39.925 22 VAL 25.505 49.613 39.093 23 PRO 23.085 49.608 36.105 24 GLY 24.265 51.891 33.338 25 ASP 28.357 50.446 30.370 26 VAL 26.665 53.462 28.719 27 LEU 27.031 56.231 31.341 28 PRO 30.141 58.383 32.244 29 SER 32.266 57.360 35.166 30 HIS 31.018 60.127 37.567 31 CYS 27.521 58.516 37.662 32 TRP 28.763 55.094 38.789 33 ILE 32.444 54.851 39.687 34 SER 32.421 55.538 43.500 35 GLU 29.656 53.051 44.230 36 VAL 34.605 50.504 43.671 37 VAL 32.754 50.149 46.945 38 GLN 30.807 47.154 45.522 39 LEU 33.966 45.728 44.057 40 SER 35.913 45.942 47.377 41 ASP 33.021 44.038 49.030 42 SER 32.933 41.258 46.504 43 LEU 36.638 40.884 46.345 44 THR 36.864 40.818 50.189 45 ASP 34.293 38.066 50.220 46 LEU 36.099 36.331 47.383 47 LEU 39.332 36.428 49.431 48 ASP 37.705 34.524 52.363 49 LYS 37.048 31.574 50.058 50 PHE 40.797 30.938 49.594 51 SER 43.703 30.208 51.822 52 ASN 47.479 30.684 51.746 53 ILE 49.778 28.029 50.363 54 SER 53.442 27.347 51.233 55 GLU 54.755 28.626 47.914 56 GLY 53.784 29.192 44.320 57 LEU 50.768 30.474 42.415 58 SER 48.132 31.561 44.977 59 ASN 44.604 32.871 44.335 60 TYR 44.709 34.222 47.893 61 SER 47.786 36.498 47.221 62 ILE 46.470 37.645 43.893 63 ILE 43.023 38.678 45.220 64 ASP 44.561 40.150 48.321 65 LYS 46.692 42.534 46.222 66 LEU 43.570 43.462 44.247 67 VAL 41.624 44.124 47.462 68 ASN 44.375 46.498 48.626 69 ILE 44.088 48.469 45.268 70 VAL 40.240 48.859 45.486 71 ASP 40.753 49.840 49.206 72 ASP 43.039 52.689 48.095 73 LEU 40.526 53.903 45.456 74 VAL 37.680 53.589 47.958 75 GLU 39.548 55.935 50.387 76 CYS 40.273 58.307 47.528 77 VAL 36.453 58.684 47.150 78 SER 21.629 51.156 45.958 79 PRO 22.366 48.292 43.470 80 GLU 20.971 44.880 43.417 81 PRO 22.855 41.549 43.686 82 ARG 23.966 39.882 40.479 83 LEU 25.996 36.697 39.565 84 PHE 29.031 36.804 37.333 85 THR 31.539 34.192 36.176 86 PRO 35.219 35.126 36.935 87 GLU 35.905 36.456 33.395 88 GLU 32.837 38.649 33.596 89 PHE 33.464 39.892 37.125 90 PHE 37.102 40.718 36.297 91 ARG 36.293 42.421 32.990 92 ILE 34.052 44.753 35.121 93 PHE 36.853 45.059 37.683 94 ASN 39.325 45.994 34.955 95 ARG 36.824 48.438 33.431 96 SER 36.147 50.153 36.820 97 ILE 39.853 50.468 37.718 98 ASP 40.562 52.125 34.333 99 ALA 37.731 54.649 34.586 100 PHE 39.342 56.063 37.709 101 LYS 42.055 57.566 35.420 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 C C C C/X X/S S S S/S 20 S S S S/X X/C C C T T T 30 T C C C C/X X/H H H H H 40 H H H H H H H H H 3/S 50 S S S S/S S S S H H H 60 H H H H H H H H H H 70 H H H H H H H/X X/S S S 80 S S S S S/H H H H H H 90 H H H H H H H H H H/S 100 S 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 t T T t e E E E 20 e S g G G 30 G g T T t h H H H H 40 H H H H H H H h T t 50 S S S h H H 60 H H H H H H H H H H 70 H H H H H H h e 80 E E E e h H H H H H 90 H H H H H H H H H h 100 t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ASN 104.6 86.5 51.3 2 VAL 18.6 15.6 78.2 3 LYS 98.3 56.7 82.3 4 ASP 71.1 64.3 66.8 5 VAL 115.9 97.6 44.7 6 THR 15.3 14.4 78.4 7 LYS 79.5 45.9 68.8 8 LEU 147.8 100.0 34.3 9 VAL 83.1 69.9 53.7 10 ALA 14.6 20.2 81.2 11 ASN 67.3 55.6 72.1 12 LEU 147.6 99.8 31.3 13 PRO 49.0 39.4 72.6 14 LYS 0.0 0.0 91.2 15 ASP 3.9 3.5 79.2 16 TYR 111.7 61.7 50.6 17 ILE 132.1 92.0 43.3 18 THR 51.3 48.0 61.7 19 LEU 142.6 96.5 38.2 20 LYS 89.0 51.3 66.9 21 TYR 137.3 75.9 55.3 22 VAL 89.4 75.2 48.6 23 PRO 37.1 29.8 71.6 24 GLY 23.6 67.7 64.9 25 ASP 32.6 29.5 83.0 26 VAL 19.7 16.6 76.9 27 LEU 72.9 49.3 60.4 28 PRO 48.5 38.9 71.4 29 SER 50.2 60.0 59.7 30 HIS 31.7 21.1 68.8 31 CYS 52.8 53.3 62.2 32 TRP 180.7 88.1 58.2 33 ILE 122.3 85.2 42.0 34 SER 27.5 32.8 63.1 35 GLU 81.5 58.8 60.0 36 VAL 118.8 100.0 36.3 37 VAL 55.3 46.6 69.6 38 GLN 122.8 82.6 55.5 39 LEU 142.2 96.2 37.9 40 SER 67.0 80.2 62.1 41 ASP 30.8 27.9 84.4 42 SER 78.0 93.3 57.9 43 LEU 147.8 100.0 29.1 44 THR 44.0 41.2 69.4 45 ASP 37.1 33.6 79.1 46 LEU 144.7 97.9 32.4 47 LEU 124.7 84.3 52.1 48 ASP 10.6 9.6 81.5 49 LYS 76.5 44.1 77.4 50 PHE 125.8 75.4 52.9 51 SER 10.1 12.0 78.9 52 ASN 36.2 29.9 73.6 53 ILE 69.5 48.4 80.9 54 SER 4.1 4.9 87.1 55 GLU 9.8 7.1 87.1 56 GLY 4.0 11.4 75.0 57 LEU 77.0 52.1 66.9 58 SER 75.2 89.9 64.4 59 ASN 104.8 86.7 43.6 60 TYR 130.5 72.1 66.6 61 SER 39.4 47.2 70.7 62 ILE 133.8 93.2 47.9 63 ILE 143.5 100.0 28.6 64 ASP 66.7 60.3 60.9 65 LYS 51.3 29.6 80.4 66 LEU 145.0 98.1 30.6 67 VAL 107.5 90.5 58.9 68 ASN 43.2 35.8 79.2 69 ILE 79.4 55.3 60.8 70 VAL 118.8 100.0 36.1 71 ASP 51.7 46.8 77.2 72 ASP 20.9 18.9 78.7 73 LEU 112.4 76.0 41.0 74 VAL 80.7 68.0 55.2 75 GLU 11.9 8.6 85.9 76 CYS 22.8 23.0 75.6 77 VAL 95.6 80.5 58.3 78 SER 16.8 20.1 87.6 79 PRO 118.7 95.3 55.1 80 GLU 73.8 53.3 71.5 81 PRO 57.5 46.1 60.3 82 ARG 71.6 34.3 69.4 83 LEU 24.9 16.8 81.6 84 PHE 155.4 93.1 50.2 85 THR 63.4 59.3 70.9 86 PRO 122.3 98.3 43.9 87 GLU 31.3 22.6 72.3 88 GLU 60.9 44.0 68.7 89 PHE 166.8 100.0 28.2 90 PHE 165.7 99.4 26.7 91 ARG 16.5 7.9 89.1 92 ILE 102.9 71.7 47.7 93 PHE 166.6 99.9 27.0 94 ASN 78.9 65.3 49.9 95 ARG 99.5 47.6 72.4 96 SER 76.7 91.8 39.7 97 ILE 107.8 75.1 42.0 98 ASP 10.1 9.2 82.3 99 ALA 58.3 80.3 66.4 100 PHE 129.3 77.5 49.9 101 LYS 103.4 59.6 83.0