Protein Data Bank File : 1elwb Title : CHAPERONE 14-MAR-00 1ELW Number of Amino Acid Residues : 115 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 MET GLU GLN VAL ASN GLU LEU LYS GLU LYS 10 GLY ASN LYS ALA LEU SER VAL GLY ASN ILE 20 ASP ASP ALA LEU GLN CYS TYR SER GLU ALA 30 ILE LYS LEU ASP PRO HIS ASN HIS VAL LEU 40 TYR SER ASN ARG SER ALA ALA TYR ALA LYS 50 LYS GLY ASP TYR GLN LYS ALA TYR GLU ASP 60 GLY CYS LYS THR VAL ASP LEU LYS PRO ASP 70 TRP GLY LYS GLY TYR SER ARG LYS ALA ALA 80 ALA LEU GLU PHE LEU ASN ARG PHE GLU GLU 90 ALA LYS ARG THR TYR GLU GLU GLY LEU LYS 100 HIS GLU ALA ASN ASN PRO GLN LEU LYS GLU 110 GLY LEU GLN ASN MET Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 MET 0.0 -94.9 179.0 0.0 0.0 0.0 2 GLU -68.1 -32.2 -179.3 0.0 0.0 0.0 3 GLN -64.3 -39.0 179.5 -171.1 173.0 3.5 4 VAL -70.3 -48.3 180.0 171.9 5 ASN -61.9 -39.4 179.6 -65.4 -39.9 6 GLU -61.0 -46.2 179.8 165.7 170.4 41.7 7 LEU -66.3 -38.4 178.8 -78.0 170.4 8 LYS -62.3 -45.9 -179.2 -174.5 -165.3 68.4 150.3 9 GLU -63.7 -40.4 178.4 -71.1 175.7 56.0 10 LYS -63.0 -41.2 179.0 -76.4 -168.2 51.5 177.1 11 GLY -64.4 -42.5 179.8 12 ASN -61.9 -42.0 -179.6 -75.9 -178.9 13 LYS -63.2 -46.4 179.7 -178.3 176.5 160.6 -176.6 14 ALA -60.1 -42.9 179.9 15 LEU -64.8 -36.2 -178.8 -161.1 65.4 16 SER -62.5 -25.0 178.6 77.4 17 VAL -106.4 16.6 177.3 -65.9 18 GLY 74.5 12.4 178.6 19 ASN -93.6 80.7 -175.8 -69.0 -24.8 20 ILE -65.0 -42.1 179.4 -53.2 171.8 21 ASP -61.1 -41.8 179.6 -72.9 159.8 22 ASP -62.9 -41.9 179.9 -73.7 -17.2 23 ALA -60.9 -48.0 -179.6 24 LEU -57.8 -40.4 179.5 -71.0 169.8 25 GLN -63.4 -46.6 179.6 -178.6 158.5 -59.7 26 CYS -60.4 -47.9 -179.3 -69.2 27 TYR -64.3 -39.0 -180.0 -63.1 -38.8 28 SER -64.8 -41.0 178.0 -65.1 29 GLU -64.9 -37.1 178.9 -71.2 -60.2 -48.8 30 ALA -67.2 -40.5 -179.6 31 ILE -65.0 -32.9 179.1 -76.9 166.1 32 LYS -66.7 -36.9 179.1 -72.3 -49.2 -174.0 174.6 33 LEU -75.5 -32.4 -177.6 -64.0 174.3 34 ASP -139.9 77.4 -179.4 -172.7 7.6 35 PRO -65.6 -3.0 178.6 33.0 -42.8 36 HIS -110.1 13.1 -178.6 -80.8 -92.8 37 ASN -91.0 101.0 -178.4 -169.4 -31.2 38 HIS -59.2 -29.0 -179.7 52.8 -71.7 39 VAL -65.7 -35.0 -179.7 172.2 40 LEU -68.3 -40.6 178.6 -55.9 176.3 41 TYR -68.8 -34.9 179.7 -68.4 -81.2 42 SER -66.5 -46.7 179.9 176.5 43 ASN -63.2 -42.8 -179.5 -75.0 2.1 44 ARG -65.7 -33.9 177.8 -160.2 173.5 59.4 -178.6 45 SER -61.0 -45.1 177.4 177.1 46 ALA -58.3 -44.5 -179.1 47 ALA -64.3 -42.7 178.9 48 TYR -64.0 -35.7 180.0 -85.0 -52.4 49 ALA -66.1 -41.4 -179.8 50 LYS -68.3 -27.2 -179.9 -75.6 179.3 166.9 177.0 51 LYS -78.5 -24.3 -178.2 -179.5 62.9 176.7 -179.2 52 GLY 93.2 10.0 178.3 53 ASP -95.5 79.4 -176.9 -168.2 -32.6 54 TYR -65.2 -31.8 178.5 -55.0 -49.4 55 GLN -61.8 -47.5 179.8 -178.8 54.0 44.4 56 LYS -70.9 -32.9 177.1 -70.0 -171.8 -177.3 174.7 57 ALA -61.5 -42.7 179.2 58 TYR -63.5 -47.9 -179.9 173.2 64.4 59 GLU -58.8 -41.3 178.7 -58.8 173.0 -13.5 60 ASP -69.7 -34.8 177.9 -81.2 -13.5 61 GLY -65.4 -40.5 178.9 62 CYS -62.6 -41.8 -179.8 -73.2 63 LYS -64.4 -37.9 179.2 -177.6 59.2 174.8 -159.5 64 THR -61.1 -46.7 178.8 -55.4 65 VAL -63.4 -39.9 -179.9 171.5 66 ASP -64.0 -39.4 -179.8 -63.1 -30.6 67 LEU -72.9 -40.0 -177.0 -73.2 165.1 68 LYS -132.6 75.8 -179.3 -72.3 -66.5 -97.0 -175.1 69 PRO -59.5 -17.4 179.2 27.8 -36.7 70 ASP -93.4 -9.5 -176.6 -65.1 -42.2 71 TRP -82.9 114.9 -177.0 -167.8 42.4 72 GLY -58.1 -36.9 -176.6 73 LYS -60.7 -32.3 179.0 -156.1 152.7 -171.6 -172.2 74 GLY -63.1 -35.8 179.5 75 TYR -69.9 -35.0 177.6 -67.5 -87.1 76 SER -64.0 -40.4 179.0 -66.7 77 ARG -62.9 -48.7 -177.4 -64.6 -55.3 -176.4 -161.4 78 LYS -63.4 -46.3 -178.0 -177.8 172.7 178.2 176.7 79 ALA -68.4 -37.7 -179.9 80 ALA -64.7 -39.8 -179.4 81 ALA -64.2 -42.2 179.1 82 LEU -61.2 -40.2 178.6 -75.7 165.3 83 GLU -62.7 -41.8 -179.7 -69.9 -170.1 52.2 84 PHE -64.8 -28.8 179.3 -76.0 122.8 85 LEU -85.8 4.6 -179.6 -68.4 167.5 86 ASN 61.9 31.6 177.9 -66.4 -52.9 87 ARG -106.6 68.1 -175.0 -71.5 168.3 60.2 -179.8 88 PHE -63.7 -41.6 179.8 -54.5 -68.1 89 GLU -66.9 -36.2 178.0 -61.8 -62.4 159.0 90 GLU -67.6 -35.9 178.1 -70.8 171.7 88.6 91 ALA -62.1 -44.1 178.5 92 LYS -58.3 -49.4 -179.6 -177.8 172.9 -173.2 -68.0 93 ARG -59.0 -36.6 -178.2 -74.0 -67.3 -165.4 176.4 94 THR -67.9 -44.9 176.9 -59.0 95 TYR -61.2 -40.3 -178.2 -73.4 122.1 96 GLU -65.3 -36.4 179.1 -64.3 178.8 -25.1 97 GLU -67.0 -42.9 179.2 -80.5 -56.9 -51.7 98 GLY -60.2 -35.8 -179.4 99 LEU -72.9 -19.4 176.3 -71.2 165.1 100 LYS -71.0 -29.3 179.8 -71.3 175.8 -175.7 -178.1 101 HIS -88.6 -30.2 179.2 -69.7 -100.8 102 GLU -146.6 87.0 -175.5 -177.4 169.7 -72.5 103 ALA -58.0 -28.1 -178.5 104 ASN -101.7 23.2 179.2 63.5 -30.9 105 ASN -72.3 112.1 -179.6 -173.2 -68.6 106 PRO -62.4 -36.5 -179.3 36.3 -44.2 107 GLN -68.6 -36.3 179.3 -64.3 69.1 45.0 108 LEU -71.2 -40.0 179.5 -69.6 -177.7 109 LYS -63.3 -41.3 -179.9 -71.0 -179.1 -171.9 175.2 110 GLU -69.1 -43.9 179.8 0.0 0.0 0.0 111 GLY -58.3 -45.3 -180.0 112 LEU -67.2 -34.3 -179.6 175.4 59.3 113 GLN -75.4 -48.0 -179.3 165.7 -170.6 -59.9 114 ASN -62.8 -13.6 179.6 -66.9 -21.3 115 MET -92.5 116.4 0.0 -179.0 -177.7 45.8 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 MET 65.895 91.007 25.027 2 GLU 67.766 88.046 26.475 3 GLN 64.354 86.718 27.472 4 VAL 63.159 86.661 23.864 5 ASN 66.357 85.058 22.554 6 GLU 66.351 82.544 25.409 7 LEU 62.795 81.485 24.558 8 LYS 63.524 81.332 20.835 9 GLU 66.523 79.103 21.515 10 LYS 64.501 76.912 23.878 11 GLY 61.821 76.572 21.215 12 ASN 64.430 75.719 18.599 13 LYS 65.889 73.083 20.935 14 ALA 62.468 71.530 21.624 15 LEU 61.772 71.428 17.918 16 SER 65.201 69.826 17.349 17 VAL 64.169 66.871 19.509 18 GLY 60.702 66.624 18.013 19 ASN 58.850 68.088 20.972 20 ILE 56.592 70.265 18.877 21 ASP 54.085 71.275 21.540 22 ASP 56.947 72.484 23.747 23 ALA 58.381 74.402 20.806 24 LEU 55.029 76.072 20.110 25 GLN 54.746 77.107 23.755 26 CYS 58.230 78.641 23.755 27 TYR 57.666 80.545 20.536 28 SER 54.249 81.767 21.676 29 GLU 55.704 83.064 24.954 30 ALA 58.442 84.820 22.971 31 ILE 55.880 86.361 20.596 32 LYS 53.956 87.736 23.549 33 LEU 57.136 89.503 24.690 34 ASP 58.109 90.680 21.182 35 PRO 55.078 90.667 18.860 36 HIS 57.040 92.311 16.028 37 ASN 59.765 89.694 15.744 38 HIS 59.270 88.058 12.349 39 VAL 61.725 85.287 13.197 40 LEU 59.454 84.065 15.983 41 TYR 56.437 83.885 13.697 42 SER 58.475 82.148 11.013 43 ASN 59.727 79.577 13.517 44 ARG 56.276 79.094 14.961 45 SER 54.865 78.637 11.441 46 ALA 57.403 75.824 10.970 47 ALA 56.343 74.256 14.297 48 TYR 52.636 74.443 13.424 49 ALA 53.379 72.863 10.062 50 LYS 55.221 70.041 11.824 51 LYS 52.232 69.768 14.214 52 GLY 49.871 69.530 11.276 53 ASP 47.983 72.723 12.176 54 TYR 48.266 74.142 8.686 55 GLN 45.796 76.939 9.331 56 LYS 47.956 78.362 12.125 57 ALA 51.116 77.692 10.080 58 TYR 49.525 79.820 7.329 59 GLU 48.505 82.594 9.713 60 ASP 52.052 82.805 11.143 61 GLY 53.506 82.742 7.639 62 CYS 51.200 85.626 6.769 63 LYS 52.328 87.564 9.820 64 THR 55.957 86.989 8.853 65 VAL 55.367 88.431 5.386 66 ASP 53.442 91.363 6.842 67 LEU 56.285 92.199 9.193 68 LYS 59.090 91.678 6.681 69 PRO 57.758 91.899 3.146 70 ASP 61.238 91.688 1.658 71 TRP 62.237 88.519 3.560 72 GLY 62.013 85.460 1.367 73 LYS 61.615 82.958 4.163 74 GLY 58.262 84.346 5.260 75 TYR 56.932 83.601 1.789 76 SER 58.309 80.065 2.053 77 ARG 56.389 79.629 5.343 78 LYS 53.190 81.025 3.909 79 ALA 53.413 79.082 0.659 80 ALA 54.333 75.811 2.345 81 ALA 51.282 76.143 4.587 82 LEU 49.150 76.845 1.540 83 GLU 50.467 73.715 -0.150 84 PHE 49.565 71.661 2.946 85 LEU 46.084 73.245 2.762 86 ASN 45.857 72.163 -0.899 87 ARG 45.638 75.815 -1.950 88 PHE 48.152 75.347 -4.730 89 GLU 47.463 78.375 -6.903 90 GLU 47.722 80.614 -3.859 91 ALA 50.984 78.857 -2.947 92 LYS 52.234 79.604 -6.446 93 ARG 51.231 83.277 -6.166 94 THR 52.985 83.477 -2.798 95 TYR 56.313 82.150 -4.073 96 GLU 55.949 84.575 -6.969 97 GLU 55.315 87.506 -4.627 98 GLY 58.390 86.658 -2.600 99 LEU 60.398 86.625 -5.822 100 LYS 59.166 90.110 -6.653 101 HIS 60.988 91.223 -3.460 102 GLU 64.117 89.057 -3.783 103 ALA 64.440 87.719 -7.311 104 ASN 67.482 85.540 -6.658 105 ASN 66.145 83.771 -3.595 106 PRO 67.139 80.121 -4.169 107 GLN 64.593 78.707 -1.713 108 LEU 61.668 80.507 -3.326 109 LYS 62.728 79.451 -6.814 110 GLU 63.033 75.834 -5.639 111 GLY 59.767 75.889 -3.723 112 LEU 57.939 77.209 -6.770 113 GLN 59.736 74.693 -8.984 114 ASN 59.282 71.654 -6.729 115 MET 55.559 72.292 -6.743 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 H H H H H H H 20 H H H H H H H H H H 30 H H H H C C H H H H 40 H H H H H H H H H H 50 H H H H H H H H H H 60 H H H H H H H H H C 70 H H H H 3 3/H H H H H 80 H H H H H H H H H H 90 H H H H H H H H H H 100 H H C C H H H H H H 110 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 H H H h T h H 20 H H H H H H H H H H 30 H H H h T T h H H H 40 H H H H H H H H H H 50 H h h H H H H H H H 60 H H H H H H H h T T 70 h H H H H H H H H H 80 H H H H h T h H H H 90 H H H H H H H H H H 100 H h T T h H H H H H 110 H H H H h Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 MET 79.0 49.6 88.0 2 GLU 64.6 46.6 81.6 3 GLN 45.3 30.5 69.6 4 VAL 106.4 89.6 56.7 5 ASN 40.4 33.4 73.1 6 GLU 35.0 25.2 70.5 7 LEU 119.2 80.6 50.3 8 LYS 112.8 65.1 61.4 9 GLU 37.0 26.7 74.0 10 LYS 64.7 37.3 66.2 11 GLY 34.8 100.0 51.3 12 ASN 68.2 56.4 68.5 13 LYS 19.6 11.3 84.6 14 ALA 60.5 83.3 54.8 15 LEU 129.0 87.3 54.1 16 SER 24.7 29.5 73.8 17 VAL 41.7 35.1 81.2 18 GLY 6.3 18.1 75.5 19 ASN 45.6 37.7 72.8 20 ILE 108.5 75.6 51.0 21 ASP 34.0 30.8 74.1 22 ASP 36.6 33.1 66.7 23 ALA 72.6 100.0 42.7 24 LEU 128.6 87.0 46.5 25 GLN 23.0 15.5 81.3 26 CYS 86.4 87.1 51.7 27 TYR 180.3 99.6 44.3 28 SER 54.5 65.2 70.6 29 GLU 46.9 33.8 65.9 30 ALA 72.6 100.0 42.6 31 ILE 134.0 93.4 52.4 32 LYS 29.2 16.8 85.0 33 LEU 89.1 60.3 66.0 34 ASP 66.8 60.4 56.9 35 PRO 57.4 46.1 77.4 36 HIS 28.8 19.2 73.8 37 ASN 87.0 71.9 57.2 38 HIS 107.4 71.5 43.3 39 VAL 72.5 61.0 64.7 40 LEU 147.8 100.0 43.7 41 TYR 165.0 91.1 49.9 42 SER 82.2 98.4 52.6 43 ASN 96.5 79.8 59.6 44 ARG 171.3 82.0 50.0 45 SER 82.1 98.2 53.0 46 ALA 58.1 80.1 64.7 47 ALA 72.6 100.0 37.1 48 TYR 154.3 85.3 52.2 49 ALA 56.1 77.3 50.7 50 LYS 69.4 40.0 67.0 51 LYS 91.0 52.5 67.7 52 GLY 18.7 53.8 72.8 53 ASP 67.4 61.0 55.5 54 TYR 117.8 65.1 57.3 55 GLN 65.7 44.2 66.6 56 LYS 74.9 43.2 73.2 57 ALA 72.0 99.2 48.5 58 TYR 142.9 79.0 53.8 59 GLU 55.9 40.3 69.1 60 ASP 103.2 93.4 53.0 61 GLY 34.8 100.0 60.7 62 CYS 72.3 72.9 60.7 63 LYS 95.0 54.8 63.6 64 THR 106.9 100.0 44.4 65 VAL 104.0 87.5 56.9 66 ASP 29.5 26.7 72.8 67 LEU 127.6 86.3 54.6 68 LYS 77.7 44.8 67.3 69 PRO 61.6 49.5 75.8 70 ASP 22.1 20.0 76.3 71 TRP 130.2 63.5 56.8 72 GLY 34.4 99.0 56.4 73 LYS 70.4 40.6 75.5 74 GLY 34.8 99.9 47.9 75 TYR 172.2 95.1 43.4 76 SER 58.8 70.3 53.8 77 ARG 153.0 73.2 60.3 78 LYS 125.6 72.4 52.0 79 ALA 72.6 100.0 48.4 80 ALA 35.2 48.4 71.4 81 ALA 72.2 99.5 49.2 82 LEU 145.8 98.7 46.8 83 GLU 96.0 69.3 55.7 84 PHE 80.2 48.1 64.4 85 LEU 111.9 75.7 59.3 86 ASN 29.0 24.0 75.7 87 ARG 123.8 59.3 68.1 88 PHE 70.5 42.3 71.8 89 GLU 12.8 9.2 76.9 90 GLU 64.6 46.6 67.0 91 ALA 72.6 100.0 43.3 92 LYS 82.1 47.4 70.7 93 ARG 37.0 17.7 85.1 94 THR 97.1 90.8 42.2 95 TYR 170.6 94.3 47.4 96 GLU 95.3 68.7 57.9 97 GLU 71.0 51.2 67.6 98 GLY 34.8 100.0 44.6 99 LEU 122.1 82.6 53.8 100 LYS 52.1 30.0 84.7 101 HIS 93.9 62.5 74.9 102 GLU 71.1 51.3 82.4 103 ALA 9.8 13.5 82.2 104 ASN 16.7 13.8 78.9 105 ASN 108.4 89.7 54.2 106 PRO 47.5 38.2 81.5 107 GLN 38.6 26.0 76.9 108 LEU 147.7 100.0 50.7 109 LYS 71.6 41.3 70.9 110 GLU 100.0 72.2 78.7 111 GLY 20.0 57.5 68.0 112 LEU 108.9 73.7 49.2 113 GLN 22.7 15.3 86.4 114 ASN 31.5 26.0 77.8 115 MET 132.8 83.3 53.6