Protein Data Bank File : 1u2f Title : RNA-BINDING PROTEIN 26-MAY-99 1U2F Number of Amino Acid Residues : 90 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ALA ARG ARG LEU TYR VAL GLY ASN ILE PRO 10 PHE GLY ILE THR GLU GLU ALA MET MET ASP 20 PHE PHE ASN ALA GLN MET ARG LEU GLY GLY 30 LEU THR GLN ALA PRO GLY ASN PRO VAL LEU 40 ALA VAL GLN ILE ASN GLN ASP LYS ASN PHE 50 ALA PHE LEU GLU PHE ARG SER VAL ASP GLU 60 THR THR GLN ALA MET ALA PHE ASP GLY ILE 70 ILE PHE GLN GLY GLN SER LEU LYS ILE ARG 80 ARG PRO HIS ASP TYR GLN PRO LEU PRO GLY Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ALA 0.0 -48.1 179.8 2 ARG 65.2 9.7 179.8 -55.4 105.3 -137.1 -151.7 3 ARG -102.7 131.7 -179.7 173.5 117.1 59.5 68.9 4 LEU -118.0 157.2 179.8 -81.0 170.6 5 TYR -108.5 147.4 179.4 162.8 -79.3 6 VAL -126.0 153.0 -179.8 -159.4 7 GLY -135.4 170.2 -179.4 8 ASN 62.5 25.6 -179.7 -72.3 -106.7 9 ILE -98.3 141.9 -179.8 81.0 84.4 10 PRO -79.0 88.6 180.0 22.5 -20.3 11 PHE -48.1 167.5 -179.1 159.5 89.7 12 GLY 101.8 -48.2 179.1 13 ILE -47.8 155.6 -178.3 171.7 -101.5 14 THR -82.3 -169.1 -179.7 65.2 15 GLU -90.3 4.9 -179.8 175.6 161.1 -59.1 16 GLU -90.1 -57.9 -179.8 -72.4 163.9 -73.6 17 ALA -44.8 -75.6 -179.9 18 MET -43.6 -56.7 -179.8 -80.2 -69.8 -112.1 19 MET -43.7 -69.1 -179.6 -176.9 174.3 -78.4 20 ASP -62.8 -10.4 -179.7 -179.5 -86.9 21 PHE -82.3 -29.9 -179.6 173.0 53.3 22 PHE -90.9 -41.3 -179.6 -80.7 61.7 23 ASN -76.6 -40.9 179.2 45.3 64.1 24 ALA -47.1 -26.1 179.2 25 GLN -86.7 -32.5 179.4 -63.5 -55.9 -68.0 26 MET -72.7 -24.6 -179.9 -55.4 -135.1 172.4 27 ARG -80.0 -13.3 -179.9 -85.5 -73.7 -55.5 -74.3 28 LEU -44.7 -85.8 -180.0 -94.6 143.3 29 GLY -57.9 -21.9 -179.9 30 GLY 99.4 59.6 -179.9 31 LEU -81.4 -9.7 179.9 -51.6 172.1 32 THR -140.1 131.8 179.7 51.5 33 GLN -133.5 64.2 -179.9 -98.1 -151.9 135.0 34 ALA -132.3 177.3 -180.0 35 PRO -77.6 56.1 180.0 22.3 -20.8 36 GLY 171.2 -161.1 -180.0 37 ASN -122.3 172.6 180.0 -4.0 93.4 38 PRO -77.7 -73.4 179.8 22.1 -20.3 39 VAL -50.2 148.6 -179.0 170.8 40 LEU -126.9 -38.5 -178.8 -171.9 76.2 41 ALA -136.8 104.7 179.3 42 VAL -119.8 72.3 -180.0 -175.3 43 GLN -71.6 157.2 179.8 -90.9 161.7 -90.8 44 ILE -105.7 168.9 -179.8 -56.5 88.9 45 ASN -129.1 144.3 -180.0 -121.8 112.0 46 GLN -88.5 -149.8 179.9 -39.1 121.1 -135.0 47 ASP 61.6 -125.6 179.9 -62.9 -35.6 48 LYS -52.3 -19.7 -179.9 -109.0 -80.2 93.8 142.2 49 ASN 80.6 97.3 179.5 -40.9 -51.5 50 PHE -153.4 168.9 -179.0 39.8 -72.2 51 ALA -139.3 167.8 179.2 52 PHE -134.4 149.7 -180.0 -94.0 -82.2 53 LEU -123.2 116.2 -178.9 -37.9 129.5 54 GLU -96.0 122.0 179.4 -162.8 171.3 6.4 55 PHE -107.9 121.2 179.9 -39.7 -36.6 56 ARG -90.4 -1.0 -179.7 -129.1 -142.5 145.9 -150.9 57 SER -161.0 -35.0 -179.1 -148.7 58 VAL -43.0 124.1 179.8 97.9 59 ASP -96.5 43.3 -179.5 -110.9 65.7 60 GLU -123.4 1.1 -179.7 -158.7 145.7 48.3 61 THR -43.2 -26.0 -179.6 170.9 62 THR -86.6 -43.5 -179.6 -161.2 63 GLN -86.3 -16.4 179.7 -39.6 174.5 -67.8 64 ALA -49.0 -30.9 178.9 65 MET -57.4 -19.4 179.6 -62.7 164.1 61.6 66 ALA -57.1 -32.4 179.3 67 PHE -81.0 4.0 179.9 -48.2 -64.5 68 ASP -39.8 102.3 -179.3 171.2 28.5 69 GLY 102.9 -73.2 179.4 70 ILE 39.2 -132.0 179.9 -165.9 -175.7 71 ILE -152.3 115.1 180.0 -76.0 -59.3 72 PHE -122.9 129.7 179.9 -171.2 62.7 73 GLN 45.3 39.1 -179.9 -160.1 173.3 137.7 74 GLY 58.3 60.8 -179.9 75 GLN -168.8 127.9 180.0 179.4 81.5 -68.6 76 SER -51.2 161.0 -179.9 -159.2 77 LEU -129.9 -171.8 179.8 -43.7 170.7 78 LYS -160.1 95.9 180.0 163.7 136.6 -112.4 176.9 79 ILE -79.7 149.5 -179.8 -69.1 -146.2 80 ARG -130.0 -177.6 179.9 -72.8 -124.6 133.6 -178.0 81 ARG -117.5 95.3 -179.9 -73.9 -146.7 -105.2 148.9 82 PRO -77.2 49.9 179.9 22.4 -21.4 83 HIS -129.9 -32.9 -179.9 -162.8 105.3 84 ASP 40.7 56.0 -179.9 45.7 76.3 85 TYR -78.6 159.6 180.0 88.9 -51.3 86 GLN 45.5 91.5 -180.0 -75.6 179.4 -27.2 87 PRO -77.7 94.3 -179.9 22.3 -21.0 88 LEU -42.4 102.6 179.9 -170.0 115.2 89 PRO -78.5 171.5 180.0 22.5 -20.6 90 GLY 138.8 -147.0 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ALA -5.554 8.716 6.406 2 ARG -2.870 8.067 3.762 3 ARG -3.470 4.360 4.489 4 LEU -4.262 2.043 1.562 5 TYR -5.471 -1.577 1.507 6 VAL -3.993 -4.348 -0.662 7 GLY -5.435 -7.731 -1.685 8 ASN -4.191 -10.912 -3.394 9 ILE -1.081 -10.463 -1.247 10 PRO 0.889 -13.449 0.067 11 PHE 0.621 -12.937 3.846 12 GLY 3.677 -14.090 5.832 13 ILE 6.051 -11.715 4.028 14 THR 7.609 -9.139 6.421 15 GLU 6.959 -5.374 6.486 16 GLU 10.060 -4.742 4.341 17 ALA 9.171 -6.377 1.001 18 MET 5.732 -4.744 0.606 19 MET 7.070 -1.498 2.113 20 ASP 9.988 -1.228 -0.328 21 PHE 7.596 -2.711 -2.915 22 PHE 5.252 0.316 -2.894 23 ASN 7.772 3.150 -2.429 24 ALA 10.402 1.581 -4.690 25 GLN 7.790 2.393 -7.347 26 MET 7.175 5.907 -6.003 27 ARG 10.939 6.558 -6.179 28 LEU 10.901 5.744 -9.914 29 GLY 10.283 9.242 -11.329 30 GLY 11.585 10.499 -7.963 31 LEU 8.500 11.551 -5.970 32 THR 10.626 11.686 -2.796 33 GLN 14.173 13.022 -2.320 34 ALA 14.925 12.858 1.418 35 PRO 17.009 10.804 3.855 36 GLY 14.365 8.050 4.051 37 ASN 11.318 6.664 2.206 38 PRO 7.687 7.696 1.731 39 VAL 5.626 4.756 3.046 40 LEU 6.225 4.297 6.790 41 ALA 4.034 1.444 8.110 42 VAL 2.794 -1.354 5.814 43 GLN 1.771 -4.200 8.147 44 ILE 0.222 -7.328 6.594 45 ASN -2.941 -9.198 7.650 46 GLN -3.609 -12.952 7.936 47 ASP -6.965 -14.703 7.397 48 LYS -8.181 -13.743 3.885 49 ASN -4.574 -12.527 3.479 50 PHE -4.323 -8.773 2.814 51 ALA -1.977 -5.855 3.571 52 PHE -2.074 -2.103 4.291 53 LEU 0.436 0.652 3.424 54 GLU 0.828 3.594 5.822 55 PHE 2.353 6.748 4.311 56 ARG 3.612 9.374 6.764 57 SER 4.401 11.791 3.909 58 VAL 3.999 10.141 0.474 59 ASP 1.472 12.348 -1.359 60 GLU 0.320 9.464 -3.572 61 THR -2.196 7.822 -1.204 62 THR -4.705 8.806 -3.918 63 GLN -2.756 7.622 -6.986 64 ALA -1.178 4.713 -5.081 65 MET -4.275 2.829 -6.259 66 ALA -2.514 3.074 -9.630 67 PHE -0.378 0.109 -8.512 68 ASP -3.667 -1.741 -7.879 69 GLY -2.388 -5.250 -8.654 70 ILE 1.068 -4.400 -10.048 71 ILE 3.299 -7.408 -9.152 72 PHE 4.269 -8.628 -5.667 73 GLN 6.294 -11.803 -5.009 74 GLY 5.259 -12.863 -8.533 75 GLN 1.504 -12.603 -7.875 76 SER -1.215 -10.139 -8.937 77 LEU -2.458 -7.814 -6.171 78 LYS -5.602 -5.783 -5.389 79 ILE -5.459 -2.338 -3.743 80 ARG -8.664 -0.984 -2.152 81 ARG -9.910 2.294 -0.632 82 PRO -10.048 2.034 3.167 83 HIS -11.874 5.384 3.438 84 ASP -15.491 4.695 2.381 85 TYR -16.092 8.457 2.084 86 GLN -19.581 9.789 1.278 87 PRO -21.804 6.893 2.355 88 LEU -24.264 6.570 -0.559 89 PRO -27.489 6.964 1.442 90 GLY -30.887 5.634 0.296 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 10 S S/S S S S H H H H H 20 H H H H H H H H C C 30 S S S S S/S S S S S S 40 S S S S S S/T T T T S 50 S S S S S S/S S S S H 60 H H H H 3 3 3 S S S 70 S/T T T T/S S S S S S S 80 S S S C C C 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 S t 10 T T t t T h H H H H 20 H H H H H H h T T T 30 t S S S e E E 40 E e E E T T T T E 50 E E E E E e S t T T 60 T T g G G G G g S 70 S S S S B 80 t T T t S Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ALA 32.6 44.8 84.6 2 ARG 65.4 31.3 82.2 3 ARG 104.0 49.8 65.1 4 LEU 141.7 95.9 40.4 5 TYR 135.4 74.8 42.4 6 VAL 118.8 100.0 30.6 7 GLY 30.9 88.9 56.2 8 ASN 42.2 34.9 67.5 9 ILE 143.5 100.0 36.8 10 PRO 87.2 70.1 57.6 11 PHE 92.8 55.7 58.8 12 GLY 8.8 25.2 63.0 13 ILE 122.8 85.5 52.0 14 THR 25.5 23.9 79.2 15 GLU 87.2 62.9 57.5 16 GLU 14.2 10.2 81.5 17 ALA 31.2 43.0 57.7 18 MET 159.4 100.0 19.2 19 MET 123.1 77.2 63.4 20 ASP 23.6 21.4 78.5 21 PHE 134.7 80.8 45.1 22 PHE 165.0 98.9 25.1 23 ASN 113.3 93.7 38.8 24 ALA 41.7 57.5 75.1 25 GLN 95.9 64.6 52.1 26 MET 159.2 99.9 31.6 27 ARG 91.8 44.0 80.8 28 LEU 40.3 27.3 85.9 29 GLY 0.0 0.0 76.4 30 GLY 21.0 60.3 74.4 31 LEU 68.4 46.3 73.6 32 THR 79.2 74.1 52.5 33 GLN 9.8 6.6 89.0 34 ALA 20.8 28.7 69.5 35 PRO 6.2 5.0 78.9 36 GLY 4.8 13.8 81.4 37 ASN 45.5 37.6 70.8 38 PRO 122.8 98.6 36.6 39 VAL 118.8 100.0 34.7 40 LEU 60.2 40.8 65.2 41 ALA 51.3 70.6 65.3 42 VAL 118.8 100.0 40.3 43 GLN 20.9 14.1 83.5 44 ILE 131.5 91.7 47.6 45 ASN 64.8 53.6 58.0 46 GLN 48.4 32.6 70.4 47 ASP 10.5 9.5 81.2 48 LYS 10.1 5.8 83.3 49 ASN 58.4 48.3 70.0 50 PHE 130.0 78.0 58.9 51 ALA 72.4 99.8 32.5 52 PHE 120.7 72.3 49.6 53 LEU 147.8 100.0 23.9 54 GLU 72.6 52.4 61.7 55 PHE 166.8 100.0 39.4 56 ARG 35.4 16.9 77.0 57 SER 7.4 8.8 84.3 58 VAL 116.2 97.8 34.5 59 ASP 0.0 0.0 87.9 60 GLU 119.2 86.0 39.9 61 THR 68.2 63.8 50.8 62 THR 20.2 18.9 71.9 63 GLN 43.1 29.0 74.4 64 ALA 72.6 100.0 33.6 65 MET 101.8 63.9 62.6 66 ALA 16.4 22.5 73.6 67 PHE 130.3 78.1 48.0 68 ASP 58.3 52.8 66.6 69 GLY 27.3 78.5 73.4 70 ILE 102.1 71.1 46.7 71 ILE 42.0 29.2 72.1 72 PHE 159.0 95.3 29.9 73 GLN 51.0 34.3 65.2 74 GLY 0.6 1.8 71.7 75 GLN 44.4 29.9 82.7 76 SER 21.5 25.8 73.0 77 LEU 147.7 99.9 40.4 78 LYS 84.1 48.5 80.2 79 ILE 143.1 99.7 39.8 80 ARG 68.9 33.0 69.6 81 ARG 72.3 34.6 62.4 82 PRO 96.3 77.4 56.5 83 HIS 46.3 30.8 71.4 84 ASP 0.0 0.0 88.7 85 TYR 59.3 32.8 81.7 86 GLN 32.8 22.1 70.5 87 PRO 10.2 8.2 87.5 88 LEU 0.0 0.0 85.4 89 PRO 16.3 13.1 84.9 90 GLY 0.0 0.0 85.3