Protein Data Bank File : 1dszb Title : TRANSCRIPTION/DNA 10-JAN-00 1DSZ Number of Amino Acid Residues : 84 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLY SER PHE THR LYS HIS ILE CYS ALA ILE 10 CYS GLY ASP ARG SER SER GLY LYS HIS TYR 20 GLY VAL TYR SER CYS GLU GLY CYS LYS GLY 30 PHE PHE LYS ARG THR VAL ARG LYS ASP LEU 40 THR TYR THR CYS ARG ASP ASN LYS ASP CYS 50 LEU ILE ASP LYS ARG GLN ARG ASN ARG CYS 60 GLN TYR CYS ARG TYR GLN LYS CYS LEU ALA 70 MET GLY MET LYS ARG GLU ALA VAL GLN GLU 80 GLU ARG GLN ARG Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLY 0.0 -166.2 174.4 2 SER -61.1 147.6 175.3 174.1 3 PHE -72.2 -16.0 172.6 -172.7 -103.8 4 THR -91.0 115.9 167.5 -65.9 5 LYS -115.1 -81.9 174.2 -47.2 -116.7 -148.8 173.0 6 HIS -131.8 178.1 -178.2 -59.5 110.9 7 ILE -130.3 141.0 178.4 -68.6 -70.2 8 CYS -67.4 124.4 179.1 177.8 9 ALA -71.7 -18.7 -178.5 10 ILE -85.6 -46.1 -170.1 -57.0 -22.5 11 CYS -129.6 -6.4 175.9 77.3 12 GLY 92.2 -5.6 177.5 13 ASP -71.6 170.1 176.4 -165.8 -170.7 14 ARG -61.7 148.6 -179.2 -66.7 -172.1 -73.5 150.1 15 SER -142.4 141.7 178.1 168.1 16 SER -90.2 -16.0 -177.6 74.2 17 GLY 163.6 -167.1 -178.8 18 LYS -80.8 149.6 172.6 -61.9 -172.9 -176.2 -176.4 19 HIS -139.6 129.0 -179.8 -55.8 -81.9 20 TYR 54.5 30.1 174.3 -46.6 -58.2 21 GLY 102.6 -5.2 -168.9 22 VAL -142.0 139.0 172.3 169.4 23 TYR -53.9 120.6 -177.0 -72.1 -56.7 24 SER -150.3 156.5 178.1 46.7 25 CYS -83.8 169.8 176.6 68.6 26 GLU -55.9 -42.5 177.2 -65.6 -80.9 -166.4 27 GLY -60.7 -53.2 -172.4 28 CYS -72.8 -37.5 173.6 -64.1 29 LYS -54.1 -49.8 -176.6 141.6 -174.8 -166.2 -167.5 30 GLY -64.9 -45.1 -178.6 31 PHE -62.0 -42.7 177.6 167.4 83.7 32 PHE -63.8 -48.6 177.4 -173.2 79.6 33 LYS -54.6 -49.1 -177.9 -177.9 -173.5 60.1 168.5 34 ARG -64.7 -41.2 178.4 -67.8 -171.6 -59.0 -91.8 35 THR -56.7 -48.6 -179.7 -58.4 36 VAL -67.8 -48.8 -177.5 173.6 37 ARG -59.8 -39.8 -178.3 -69.5 -93.0 -174.0 88.2 38 LYS -99.0 2.7 -174.9 -56.1 -173.1 -101.9 149.9 39 ASP 43.5 52.7 177.5 -175.3 27.2 40 LEU -73.9 144.5 174.8 -51.3 170.4 41 THR -115.3 131.3 -178.4 -62.9 42 TYR -119.4 157.1 172.7 -52.3 123.2 43 THR -128.9 139.3 176.7 64.2 44 CYS -85.8 128.3 177.5 -177.7 45 ARG -83.5 3.7 179.8 0.0 0.0 0.0 0.0 46 ASP -123.7 -119.8 -173.5 0.0 0.0 47 ASN -119.9 24.3 177.1 -35.0 71.1 48 LYS 61.0 30.0 178.2 -60.9 178.1 172.6 81.1 49 ASP -144.5 33.1 176.3 61.0 2.1 50 CYS -55.9 143.1 -179.5 -65.2 51 LEU -77.4 129.7 179.9 157.0 91.4 52 ILE -111.3 113.3 173.1 -45.4 -67.8 53 ASP -141.5 177.7 -170.7 65.9 -157.3 54 LYS -59.7 -42.1 -174.6 -172.4 -175.9 177.3 169.7 55 ARG -78.5 -24.1 178.9 132.3 -145.0 -129.5 62.7 56 GLN -116.5 15.8 -173.1 62.5 -177.1 -114.8 57 ARG -60.4 -24.1 -178.4 70.3 -166.1 168.6 -165.7 58 ASN -89.1 -8.0 -175.7 -67.1 -58.4 59 ARG -63.4 -40.2 -179.2 -158.8 150.1 79.6 167.0 60 CYS -132.6 103.5 179.5 -175.0 61 GLN -65.8 -40.5 176.4 -65.3 179.1 -61.1 62 TYR -52.4 -54.5 -171.9 175.9 84.4 63 CYS -73.8 -28.3 175.8 -72.5 64 ARG -65.3 -47.6 179.6 -177.0 -173.3 -163.8 175.5 65 TYR -64.5 -41.3 179.4 -179.0 66.0 66 GLN -62.1 -34.3 179.5 -70.2 -57.7 -44.0 67 LYS -75.5 -34.2 174.0 -172.2 170.3 -175.0 176.2 68 CYS -54.5 -47.4 179.0 -75.1 69 LEU -66.6 -44.3 -173.7 -64.8 171.6 70 ALA -69.3 -24.5 175.6 71 MET -86.1 -8.0 171.1 -59.4 -50.9 -68.8 72 GLY 122.9 3.5 -174.7 73 MET -66.7 137.0 -174.3 -75.1 -166.8 169.9 74 LYS -102.2 111.6 -179.9 -56.5 174.7 -176.4 161.5 75 ARG -54.4 -37.9 -173.6 -71.8 161.5 29.9 -147.8 76 GLU -73.7 -12.2 173.8 76.3 -84.9 18.3 77 ALA -79.5 -13.8 169.1 78 VAL -75.6 127.9 -175.4 175.8 79 GLN -96.9 177.3 175.3 -60.9 -178.1 -1.0 80 GLU -76.6 160.9 178.2 -61.1 173.1 -84.6 81 GLU -57.7 148.0 175.7 -76.1 -165.3 97.6 82 ARG -119.4 -179.0 170.9 -92.2 172.2 -149.5 -180.0 83 GLN -147.3 -38.8 178.3 0.0 0.0 0.0 84 ARG 60.1 89.1 0.0 0.0 0.0 0.0 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLY 25.862 -18.911 16.982 2 SER 28.779 -19.705 19.255 3 PHE 28.416 -18.715 22.940 4 THR 31.775 -17.029 22.403 5 LYS 31.426 -13.715 20.535 6 HIS 33.773 -11.091 22.043 7 ILE 35.159 -10.164 25.448 8 CYS 35.102 -6.855 27.304 9 ALA 38.530 -5.305 27.276 10 ILE 37.765 -3.474 30.479 11 CYS 36.510 -6.253 32.770 12 GLY 36.517 -9.557 30.955 13 ASP 32.734 -10.046 30.775 14 ARG 31.000 -11.112 27.543 15 SER 30.703 -8.608 24.714 16 SER 28.647 -8.410 21.526 17 GLY 31.039 -5.983 19.855 18 LYS 32.692 -2.603 20.166 19 HIS 31.215 0.392 21.928 20 TYR 32.817 3.845 21.827 21 GLY 35.788 2.250 20.077 22 VAL 36.487 -0.787 22.244 23 TYR 35.180 -4.302 22.820 24 SER 33.016 -3.865 25.866 25 CYS 30.212 -5.325 27.901 26 GLU 26.750 -3.878 28.507 27 GLY 27.972 -2.794 31.934 28 CYS 31.106 -1.000 30.842 29 LYS 29.372 0.593 27.759 30 GLY 26.597 1.945 29.971 31 PHE 28.918 3.138 32.733 32 PHE 31.096 4.987 30.238 33 LYS 28.116 6.656 28.488 34 ARG 26.662 7.810 31.802 35 THR 30.023 9.096 33.037 36 VAL 30.532 11.171 29.899 37 ARG 26.899 12.468 29.611 38 LYS 26.756 13.584 33.233 39 ASP 30.457 14.594 33.486 40 LEU 30.845 12.560 36.671 41 THR 34.073 12.782 38.667 42 TYR 35.329 9.852 40.705 43 THR 38.078 9.382 43.334 44 CYS 40.000 6.203 44.123 45 ARG 40.158 5.228 47.810 46 ASP 43.349 3.253 47.151 47 ASN 46.295 3.734 44.823 48 LYS 44.641 4.394 41.447 49 ASP 45.550 0.915 40.184 50 CYS 42.556 -1.170 41.313 51 LEU 42.029 -4.459 39.518 52 ILE 39.103 -4.432 37.089 53 ASP 37.357 -7.734 36.420 54 LYS 33.775 -8.872 36.221 55 ARG 33.345 -9.492 39.919 56 GLN 34.869 -6.260 41.257 57 ARG 34.276 -3.769 38.424 58 ASN 31.873 -1.727 40.563 59 ARG 34.164 -1.432 43.607 60 CYS 36.157 1.554 42.264 61 GLN 34.435 3.819 39.715 62 TYR 37.616 5.880 39.303 63 CYS 39.714 2.944 38.199 64 ARG 36.924 1.454 36.048 65 TYR 36.609 4.718 34.106 66 GLN 40.374 5.157 33.805 67 LYS 40.557 1.609 32.344 68 CYS 37.742 2.432 29.917 69 LEU 39.918 5.250 28.659 70 ALA 43.205 3.315 28.718 71 MET 41.745 0.494 26.660 72 GLY 40.687 3.050 24.059 73 MET 37.189 4.354 24.691 74 LYS 36.431 7.606 22.899 75 ARG 34.524 10.294 24.793 76 GLU 33.594 11.953 21.485 77 ALA 31.846 8.772 20.301 78 VAL 29.203 9.435 22.956 79 GLN 26.460 11.436 21.209 80 GLU 23.899 13.992 22.338 81 GLU 20.567 12.907 23.780 82 ARG 18.041 12.077 21.196 83 GLN 14.538 11.821 21.502 84 ARG 14.270 11.551 17.826 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C S S S S C T T T 10 T/S S S S C C C T T T 20 T S S S S/H H H H H H 30 H H H H H H H H H/S S 40 S S S S/T T T T S S S 50 S C T T T T/T T T T H 60 H H H H H H H H H H 70 H H C T T T T/S S S S 80 S/S S S/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S E E e T T 10 T t e E E S e E E T 20 T E E e h H H H H H 30 H H H H H H H H h t 40 S S S 50 t T T T T T T h 60 H H H H H H H H H H 70 h T t g G G G g 80 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLY 0.0 0.0 92.2 2 SER 19.6 23.4 83.8 3 PHE 21.2 12.7 88.1 4 THR 14.8 13.8 84.1 5 LYS 49.5 28.5 83.8 6 HIS 81.5 54.2 66.8 7 ILE 55.5 38.7 70.7 8 CYS 99.2 100.0 43.2 9 ALA 44.3 61.0 56.9 10 ILE 143.5 100.0 29.4 11 CYS 98.6 99.4 41.5 12 GLY 11.9 34.1 71.2 13 ASP 89.8 81.3 56.0 14 ARG 65.7 31.4 75.0 15 SER 80.4 96.1 61.0 16 SER 17.2 20.6 79.4 17 GLY 20.0 57.5 70.2 18 LYS 69.4 40.0 72.3 19 HIS 109.1 72.6 68.4 20 TYR 152.3 84.1 42.7 21 GLY 24.0 68.9 63.9 22 VAL 108.1 91.0 51.7 23 TYR 103.7 57.3 62.1 24 SER 83.6 100.0 42.8 25 CYS 96.9 97.6 53.7 26 GLU 13.1 9.5 82.3 27 GLY 13.2 37.8 76.4 28 CYS 99.2 100.0 38.6 29 LYS 107.9 62.2 66.1 30 GLY 24.4 70.1 68.4 31 PHE 157.1 94.2 57.4 32 PHE 166.8 100.0 34.4 33 LYS 105.2 60.7 62.8 34 ARG 91.0 43.5 66.9 35 THR 104.2 97.5 48.0 36 VAL 90.8 76.4 53.8 37 ARG 131.6 63.0 60.6 38 LYS 69.7 40.2 65.3 39 ASP 3.0 2.7 91.0 40 LEU 88.6 59.9 69.1 41 THR 13.0 12.1 82.0 42 TYR 160.6 88.7 48.5 43 THR 6.4 6.0 78.3 44 CYS 99.1 99.9 43.6 45 ARG 128.3 61.4 86.8 46 ASP 69.7 63.1 70.5 47 ASN 16.6 13.7 78.7 48 LYS 58.3 33.6 72.1 49 ASP 16.6 15.0 83.0 50 CYS 67.5 68.0 51.4 51 LEU 45.3 30.7 83.8 52 ILE 140.2 97.7 45.8 53 ASP 67.0 60.7 56.4 54 LYS 63.5 36.6 79.8 55 ARG 21.3 10.2 90.8 56 GLN 112.0 75.4 67.4 57 ARG 166.3 79.6 57.0 58 ASN 27.2 22.5 86.4 59 ARG 35.9 17.2 87.2 60 CYS 85.6 86.2 52.6 61 GLN 61.8 41.6 62.9 62 TYR 134.3 74.2 48.6 63 CYS 93.8 94.6 43.2 64 ARG 199.0 95.3 41.4 65 TYR 149.2 82.4 40.4 66 GLN 76.1 51.2 60.7 67 LYS 111.1 64.1 62.5 68 CYS 99.2 100.0 33.1 69 LEU 101.4 68.6 65.2 70 ALA 15.6 21.4 76.6 71 MET 89.5 56.1 61.0 72 GLY 6.9 19.7 75.2 73 MET 159.4 100.0 38.0 74 LYS 65.4 37.7 77.6 75 ARG 60.6 29.0 73.3 76 GLU 17.3 12.5 77.8 77 ALA 41.0 56.5 61.2 78 VAL 115.3 97.0 47.5 79 GLN 44.3 29.8 91.0 80 GLU 0.0 0.0 89.9 81 GLU 17.6 12.7 87.0 82 ARG 49.1 23.5 84.1 83 GLN 72.3 48.7 79.9 84 ARG 146.8 70.3 68.5