Protein Data Bank File : 1stu Title : DOUBLE STRANDED RNA BINDING DOMAIN 16-MAY-95 1STU Number of Amino Acid Residues : 68 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 PRO ILE SER GLN VAL HIS GLU ILE GLY ILE 10 LYS ARG ASN MET THR VAL HIS PHE LYS VAL 20 LEU ARG GLU GLU GLY PRO ALA HIS MET LYS 30 ASN PHE ILE THR ALA CYS ILE VAL GLY SER 40 ILE VAL THR GLU GLY GLU GLY ASN GLY LYS 50 LYS VAL SER LYS LYS ARG ALA ALA GLU LYS 60 MET LEU VAL GLU LEU GLN LYS LEU Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 PRO 0.0 -39.6 179.9 0.1 1.4 2 ILE -76.6 -51.2 -180.0 -39.6 -49.6 3 SER -52.1 -37.5 179.7 177.8 4 GLN -63.2 -53.6 179.0 -77.0 -172.9 -128.7 5 VAL -54.9 -67.9 178.7 -173.0 6 HIS -36.9 -38.9 -179.8 -69.8 -74.3 7 GLU -60.1 -62.3 -179.3 -107.7 -168.4 -18.8 8 ILE -74.1 -51.5 -178.7 53.1 93.7 9 GLY -44.3 -52.4 -179.7 10 ILE -78.0 -37.8 -178.0 -105.3 -58.1 11 LYS -60.7 -16.8 -179.8 -84.1 -74.5 142.1 -89.9 12 ARG -116.3 -44.1 179.9 -169.9 47.3 167.5 164.2 13 ASN 155.5 -15.5 -179.4 -103.8 115.3 14 MET -71.9 111.8 179.7 -91.3 129.6 40.0 15 THR -64.9 121.8 -179.6 3.2 16 VAL -98.2 110.7 178.6 -178.8 17 HIS -136.5 95.5 -179.0 -46.8 -120.9 18 PHE -78.7 135.1 179.1 -76.5 87.0 19 LYS -150.4 110.5 -179.7 -40.4 176.8 -86.5 141.2 20 VAL -78.6 118.4 -178.8 176.8 21 LEU -118.8 10.3 -179.8 34.3 147.0 22 ARG -139.2 166.9 -179.9 -105.3 125.9 -140.6 -37.5 23 GLU -156.9 42.6 -179.6 -33.1 174.4 -13.8 24 GLU -176.3 -169.1 179.8 79.6 -153.0 -1.9 25 GLY -138.5 -148.7 179.9 26 PRO -60.7 -62.1 179.9 -0.4 0.5 27 ALA -174.7 40.4 -179.9 28 HIS 164.4 73.6 -179.9 39.7 -166.4 29 MET 163.3 106.9 180.0 -108.7 168.6 -170.1 30 LYS -68.3 84.4 179.9 -51.4 109.6 -145.9 -119.4 31 ASN -120.1 128.2 179.6 -51.7 -2.9 32 PHE -99.9 127.1 178.8 -74.1 54.2 33 ILE -88.8 97.3 -179.1 -64.7 63.7 34 THR -86.2 118.0 -179.1 -75.2 35 ALA -82.0 114.5 178.9 36 CYS -110.2 113.2 -178.5 6.6 37 ILE -78.8 138.9 179.3 -157.5 -65.9 38 VAL -131.4 146.4 179.5 115.8 39 GLY 42.4 -112.9 -179.4 40 SER -118.7 2.8 179.5 -87.4 41 ILE -120.8 154.1 -179.5 -41.2 101.4 42 VAL -89.9 160.2 179.2 -126.1 43 THR -150.3 90.6 -178.6 -68.9 44 GLU -81.1 -172.8 -179.8 -33.3 -168.4 45.0 45 GLY -169.3 119.6 -178.9 46 GLU -80.4 92.0 178.5 -16.8 93.7 61.3 47 GLY -81.2 120.3 -179.4 48 ASN -61.4 101.4 179.5 -164.5 115.6 49 GLY 133.7 177.1 -179.9 50 LYS -94.3 -46.5 179.9 66.9 -172.4 -131.2 -86.3 51 LYS -84.1 -9.7 -180.0 175.1 178.2 -128.9 -165.7 52 VAL -84.8 -39.3 -179.2 95.2 53 SER -35.6 -30.0 -179.9 -143.3 54 LYS -76.3 -49.7 -179.7 -101.1 -163.1 -169.1 80.1 55 LYS -63.7 -35.7 -179.5 -177.5 145.7 105.8 114.0 56 ARG -76.9 -40.3 179.7 -147.2 77.5 97.7 164.6 57 ALA -61.8 -51.7 -179.0 58 ALA -63.0 -56.4 179.6 59 GLU -46.8 -43.6 179.3 -85.2 -141.8 32.2 60 LYS -60.0 -43.2 180.0 -116.8 -84.6 -174.3 115.5 61 MET -65.1 -70.4 -179.9 169.4 145.7 -70.4 62 LEU -47.7 -62.6 178.5 -56.1 -128.7 63 VAL -44.3 -38.3 -179.5 174.4 64 GLU -58.0 -57.3 -178.3 -119.9 74.6 -54.8 65 LEU -110.0 24.0 179.6 45.4 -79.0 66 GLN -112.2 -20.4 180.0 -77.0 -69.9 17.8 67 LYS -98.6 -33.4 -179.8 -111.4 92.1 118.6 103.4 68 LEU -80.9 12.3 0.0 -45.7 -169.1 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 PRO -2.835 6.939 4.102 2 ILE -4.003 3.598 5.540 3 SER -7.236 4.870 7.125 4 GLN -8.126 6.337 3.707 5 VAL -7.664 3.012 1.909 6 HIS -9.450 0.998 4.600 7 GLU -12.153 3.653 4.149 8 ILE -12.751 3.105 0.409 9 GLY -11.303 -0.409 0.130 10 ILE -13.811 -1.639 2.722 11 LYS -16.497 0.917 1.847 12 ARG -16.735 -0.681 -1.604 13 ASN -15.393 -4.239 -1.211 14 MET -11.595 -3.973 -1.613 15 THR -10.122 -5.592 1.521 16 VAL -7.473 -3.157 2.823 17 HIS -4.637 -4.958 4.641 18 PHE -1.301 -3.102 4.793 19 LYS 1.771 -5.201 5.667 20 VAL 5.359 -3.953 5.216 21 LEU 7.481 -6.937 4.153 22 ARG 10.550 -5.125 2.770 23 GLU 13.119 -2.526 3.890 24 GLU 15.454 -1.800 0.952 25 GLY 15.754 -1.667 -2.858 26 PRO 18.028 -2.929 -5.642 27 ALA 21.334 -1.777 -4.115 28 HIS 21.139 1.943 -3.263 29 MET 17.841 3.394 -1.986 30 LYS 16.089 2.910 1.376 31 ASN 12.700 1.904 -0.076 32 PHE 10.247 -0.322 1.800 33 ILE 7.842 -2.366 -0.339 34 THR 4.689 -2.220 1.743 35 ALA 2.234 -4.855 0.530 36 CYS -1.303 -3.465 0.708 37 ILE -3.920 -6.117 -0.062 38 VAL -7.006 -4.908 -1.923 39 GLY -10.190 -6.824 -2.844 40 SER -8.826 -10.330 -3.551 41 ILE -5.454 -9.362 -5.085 42 VAL -2.447 -7.736 -3.368 43 THR -0.998 -4.347 -4.294 44 GLU 2.291 -3.412 -2.581 45 GLY 4.204 -0.134 -2.977 46 GLU 7.884 0.692 -2.372 47 GLY 7.683 3.907 -0.322 48 ASN 11.181 5.458 -0.124 49 GLY 11.755 5.436 3.659 50 LYS 10.594 3.490 6.737 51 LYS 7.589 5.583 7.830 52 VAL 6.802 6.385 4.178 53 SER 6.336 2.754 3.039 54 LYS 2.802 3.186 4.434 55 LYS 1.934 6.377 2.520 56 ARG 3.479 4.935 -0.672 57 ALA 1.878 1.488 -0.317 58 ALA -1.596 2.999 0.234 59 GLU -1.266 5.780 -2.376 60 LYS -0.236 2.974 -4.722 61 MET -3.351 1.019 -3.679 62 LEU -6.009 3.752 -3.794 63 VAL -4.359 5.318 -6.840 64 GLU -4.386 1.739 -8.209 65 LEU -8.188 1.237 -8.099 66 GLN -9.227 4.859 -7.517 67 LYS -8.217 6.345 -10.890 68 LEU -9.307 3.467 -13.150 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 H/S S S S S S S S 20 S S S S T T T T C S 30 S S S S S S S S/T T T 40 T/S S S S S S S S C C 50 C H H H H H H H H H 60 H H H H H H H H 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 h t E E E E 20 e S S S e 30 E E E E E E E E T T 40 E E E E E E E E e T 50 h H H H H H H H H H 60 H H H H H H h Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 PRO 65.4 52.5 60.2 2 ILE 115.8 80.7 41.6 3 SER 6.5 7.8 74.2 4 GLN 37.2 25.0 76.9 5 VAL 118.8 100.0 28.7 6 HIS 85.3 56.8 57.4 7 GLU 34.7 25.0 74.5 8 ILE 95.6 66.6 50.8 9 GLY 34.8 100.0 44.6 10 ILE 55.0 38.3 79.4 11 LYS 40.9 23.6 75.0 12 ARG 25.5 12.2 86.8 13 ASN 3.5 2.9 85.8 14 MET 124.5 78.1 42.8 15 THR 57.8 54.0 61.6 16 VAL 118.8 100.0 46.4 17 HIS 69.4 46.2 58.3 18 PHE 160.7 96.3 34.9 19 LYS 60.3 34.8 69.3 20 VAL 84.9 71.4 62.5 21 LEU 83.2 56.3 74.0 22 ARG 89.9 43.0 68.9 23 GLU 35.7 25.7 67.8 24 GLU 32.8 23.7 86.1 25 GLY 25.7 74.0 57.0 26 PRO 38.6 31.0 74.5 27 ALA 6.1 8.4 78.7 28 HIS 27.1 18.0 75.5 29 MET 50.4 31.6 78.5 30 LYS 17.9 10.3 82.4 31 ASN 98.3 81.3 52.4 32 PHE 133.2 79.9 52.3 33 ILE 111.5 77.7 53.2 34 THR 106.9 100.0 46.0 35 ALA 68.9 95.0 43.8 36 CYS 99.2 100.0 41.8 37 ILE 113.3 78.9 54.0 38 VAL 107.8 90.7 36.5 39 GLY 20.5 58.8 62.6 40 SER 3.0 3.6 77.5 41 ILE 16.9 11.8 79.4 42 VAL 52.8 44.5 61.1 43 THR 84.0 78.6 55.2 44 GLU 85.9 61.9 55.2 45 GLY 33.8 97.1 52.9 46 GLU 61.3 44.2 63.9 47 GLY 34.8 100.0 58.1 48 ASN 62.2 51.4 70.1 49 GLY 16.5 47.4 69.0 50 LYS 26.4 15.2 72.8 51 LYS 2.0 1.1 89.0 52 VAL 81.8 68.8 64.6 53 SER 83.5 99.8 56.5 54 LYS 68.2 39.3 62.8 55 LYS 65.8 37.9 67.8 56 ARG 93.3 44.7 68.9 57 ALA 72.6 100.0 48.6 58 ALA 71.7 98.7 42.0 59 GLU 54.8 39.5 66.7 60 LYS 82.2 47.4 76.6 61 MET 159.4 100.0 35.6 62 LEU 126.8 85.8 42.0 63 VAL 60.4 50.8 60.8 64 GLU 85.2 61.5 57.6 65 LEU 116.7 79.0 42.9 66 GLN 92.0 61.9 52.3 67 LYS 44.7 25.8 74.3 68 LEU 18.6 12.6 87.8