Protein Data Bank File : 1by2 Title : EXTRACELLULAR MODULE 23-OCT-98 1BY2 Number of Amino Acid Residues : 112 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ALA VAL ASN ASP GLY ASP MET ARG LEU ALA 10 ASP GLY GLY ALA THR ASN GLN GLY ARG VAL 20 GLU ILE PHE TYR ARG GLY GLN TRP GLY THR 30 VAL CYS ASP ASN LEU TRP ASP LEU THR ASP 40 ALA SER VAL VAL CYS ARG ALA LEU GLY PHE 50 GLU ASN ALA THR GLN ALA LEU GLY ARG ALA 60 ALA PHE GLY GLN GLY SER GLY PRO ILE MET 70 LEU ASP GLU VAL GLN CYS THR GLY THR GLU 80 ALA SER LEU ALA ASP CYS LYS SER LEU GLY 90 TRP LEU LYS SER ASN CYS ARG HIS GLU ARG 100 ASP ALA GLY VAL VAL CYS THR ASN GLU THR 110 THR LEU Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ALA 0.0 87.0 -179.1 2 VAL -113.8 136.4 179.9 -177.4 3 ASN -117.8 164.3 179.0 -60.4 -71.9 4 ASP -53.0 131.4 179.1 -71.8 -10.9 5 GLY 94.9 -9.7 178.4 6 ASP -65.6 141.1 -178.7 -84.2 9.0 7 MET -125.1 164.9 177.0 -60.0 164.7 -69.6 8 ARG -156.0 155.7 177.4 68.9 -176.7 -176.2 -156.6 9 LEU -106.1 136.0 -179.3 -60.3 -174.6 10 ALA -130.7 158.1 178.1 11 ASP 55.2 25.1 -179.4 -63.1 -10.0 12 GLY -93.5 -11.9 -178.2 13 GLY 91.1 -70.8 177.9 14 ALA -84.8 170.1 179.8 15 THR -86.9 -14.5 -179.3 55.1 16 ASN -97.3 23.5 176.7 60.8 -47.8 17 GLN -162.1 153.7 178.9 71.1 171.3 12.5 18 GLY 154.6 -177.1 178.1 19 ARG -76.0 135.5 -179.7 177.5 179.4 59.4 -107.1 20 VAL -80.5 126.1 176.8 176.9 21 GLU -124.7 144.1 -176.4 -61.4 -170.9 -17.3 22 ILE -136.1 145.5 -177.1 -175.1 168.4 23 PHE -95.8 141.7 178.3 -178.6 85.2 24 TYR -157.7 123.7 179.1 -178.0 65.1 25 ARG 42.8 48.2 177.0 -65.5 -170.6 174.2 -179.8 26 GLY 96.9 -8.5 179.3 27 GLN -139.2 158.7 179.5 65.0 -177.0 -24.9 28 TRP -101.0 144.9 179.7 -72.2 86.9 29 GLY -149.3 -179.6 -177.9 30 THR -107.8 -178.7 -178.7 53.6 31 VAL -124.4 130.3 178.8 177.1 32 CYS -74.2 145.0 -177.8 -173.6 33 ASP -76.0 0.3 -179.9 66.0 9.6 34 ASN -62.6 117.6 -179.5 -70.5 -28.6 35 LEU 70.4 10.8 -179.3 -51.8 -175.9 36 TRP -65.7 121.4 -179.4 -173.7 -116.1 37 ASP -130.6 -176.9 -177.9 65.7 20.8 38 LEU -65.3 -30.4 179.1 -160.3 79.1 39 THR -69.4 -38.0 177.3 -55.2 40 ASP -65.8 -46.2 -179.9 -68.0 -16.2 41 ALA -59.9 -38.5 180.0 42 SER -68.2 -28.0 178.2 80.0 43 VAL -66.7 -41.7 178.9 160.7 44 VAL -64.7 -54.3 -179.3 -179.1 45 CYS -55.8 -49.2 -179.9 -68.5 46 ARG -63.9 -38.0 178.6 -60.0 -171.3 96.5 -93.3 47 ALA -63.7 -36.8 180.0 48 LEU -82.8 6.8 177.2 -63.4 -172.6 49 GLY 89.2 17.9 179.3 50 PHE -105.0 160.6 -178.1 -61.7 -76.1 51 GLU -66.8 -36.7 -178.3 -82.1 -179.9 26.2 52 ASN -168.9 177.0 177.3 -145.2 -21.5 53 ALA -103.0 145.5 177.5 54 THR -108.9 -23.0 179.6 58.9 55 GLN -148.8 141.3 177.6 -69.2 160.8 78.7 56 ALA -114.6 112.5 -177.5 57 LEU -109.5 149.8 179.1 -53.4 168.5 58 GLY -126.4 -167.1 178.3 59 ARG 53.0 42.3 179.7 -52.1 -66.0 117.9 100.3 60 ALA 49.6 53.0 179.9 61 ALA -61.0 -30.2 179.0 62 PHE -110.4 32.9 180.0 -64.3 -75.3 63 GLY 86.4 157.6 179.3 64 GLN -80.1 141.3 177.4 -62.1 -175.6 -156.7 65 GLY -92.9 -163.3 -179.4 66 SER -135.1 176.1 179.8 -63.8 67 GLY 84.7 -176.5 -179.8 68 PRO -74.6 157.7 176.1 35.6 -45.2 69 ILE -85.7 111.8 -178.2 -83.3 58.4 70 MET -75.0 -48.0 -178.3 -66.3 -71.6 -161.3 71 LEU -132.1 157.9 -175.6 -64.3 170.4 72 ASP -157.9 150.8 -178.9 -174.8 2.2 73 GLU 51.6 48.5 -179.0 -59.5 -163.9 -0.4 74 VAL -74.0 125.6 -179.4 -179.3 75 GLN -125.2 90.8 -179.3 -64.0 -73.0 77.9 76 CYS -91.7 153.4 178.2 -58.9 77 THR -89.3 -18.4 179.8 65.1 78 GLY 108.3 -15.1 -178.8 79 THR -100.1 3.9 -179.0 71.8 80 GLU -76.6 150.2 179.0 -59.1 87.2 -5.3 81 ALA -78.4 -27.1 -178.3 82 SER -153.0 161.3 177.7 168.9 83 LEU -64.9 -24.3 178.3 -67.1 -174.4 84 ALA -61.1 -24.8 -179.8 85 ASP -94.6 -0.6 178.6 -59.0 -47.3 86 CYS -90.6 163.5 177.9 -59.3 87 LYS -73.3 138.6 178.6 177.9 -159.0 179.1 -170.4 88 SER -156.8 -166.1 177.9 76.1 89 LEU -86.1 -6.6 -179.4 -68.9 165.8 90 GLY 108.9 157.1 -179.9 91 TRP -56.2 129.5 179.2 -71.8 108.7 92 LEU 67.9 9.8 178.6 -57.5 166.7 93 LYS -98.0 109.5 -178.9 -177.7 76.5 -167.4 -158.7 94 SER -173.7 151.3 178.1 176.1 95 ASN -111.2 1.4 -179.2 -97.7 16.9 96 CYS -76.6 163.8 176.5 -51.6 97 ARG -115.2 169.1 -178.9 -72.6 121.1 107.1 -153.7 98 HIS -60.2 -13.5 178.4 -75.4 -75.2 99 GLU -72.8 -7.8 178.4 90.0 -115.2 -89.9 100 ARG -102.9 9.1 -177.9 -60.3 -65.6 -78.2 -131.2 101 ASP -55.6 122.8 -178.4 -73.9 -17.3 102 ALA -77.7 151.2 179.7 103 GLY -141.0 174.4 179.7 104 VAL -144.7 162.7 174.2 -56.2 105 VAL -130.1 120.0 -179.1 -179.6 106 CYS -102.1 169.5 178.3 -51.8 107 THR -68.0 151.2 177.2 43.7 108 ASN -69.0 -32.6 -179.9 -101.0 106.8 109 GLU -67.6 132.9 180.0 6.8 -132.3 26.2 110 THR -97.2 80.7 110.7 -46.7 111 THR -127.0 156.3 -179.1 -170.0 112 LEU -98.2 163.9 0.0 -56.3 151.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ALA 9.126 14.936 29.377 2 VAL 10.258 15.473 25.757 3 ASN 7.947 15.440 22.704 4 ASP 8.369 15.252 18.931 5 GLY 9.749 18.546 17.665 6 ASP 11.419 19.532 20.933 7 MET 14.786 21.197 20.207 8 ARG 18.046 22.027 21.950 9 LEU 21.300 23.806 21.102 10 ALA 24.524 21.896 21.776 11 ASP 28.261 22.458 21.885 12 GLY 27.879 26.227 21.705 13 GLY 29.564 27.229 24.969 14 ALA 26.804 29.709 25.793 15 THR 23.165 28.612 25.964 16 ASN 22.104 30.983 23.209 17 GLN 24.102 29.344 20.399 18 GLY 25.021 25.895 19.178 19 ARG 24.330 22.997 16.854 20 VAL 20.568 22.469 16.453 21 GLU 19.308 19.101 17.717 22 ILE 15.683 17.975 17.527 23 PHE 13.707 15.136 19.071 24 TYR 11.597 12.600 17.204 25 ARG 10.065 9.300 18.282 26 GLY 12.486 8.627 21.045 27 GLN 15.751 9.967 19.669 28 TRP 17.712 13.141 19.066 29 GLY 19.224 13.962 15.706 30 THR 20.585 16.899 13.725 31 VAL 19.455 19.179 10.879 32 CYS 21.238 19.442 7.513 33 ASP 22.318 22.936 6.421 34 ASN 20.803 22.718 2.921 35 LEU 18.642 25.843 2.503 36 TRP 19.171 26.644 6.206 37 ASP 18.414 30.342 6.607 38 LEU 17.824 33.105 9.128 39 THR 14.082 32.515 9.169 40 ASP 14.678 28.858 10.118 41 ALA 17.191 29.926 12.781 42 SER 14.712 32.412 14.299 43 VAL 12.101 29.633 14.706 44 VAL 14.630 27.669 16.791 45 CYS 15.747 30.681 18.864 46 ARG 12.246 31.937 19.663 47 ALA 11.116 28.415 20.595 48 LEU 14.064 28.199 22.963 49 GLY 13.004 31.514 24.456 50 PHE 15.295 34.055 22.839 51 GLU 14.042 37.109 21.004 52 ASN 15.549 36.236 17.641 53 ALA 18.373 34.638 15.709 54 THR 21.332 36.727 14.647 55 GLN 23.034 34.006 12.570 56 ALA 22.106 30.793 10.729 57 LEU 25.272 28.679 10.457 58 GLY 26.092 25.589 8.410 59 ARG 28.968 23.177 7.793 60 ALA 29.062 21.914 11.377 61 ALA 30.095 25.338 12.719 62 PHE 29.648 23.988 16.262 63 GLY 31.099 20.559 15.540 64 GLN 29.539 17.494 14.020 65 GLY 26.768 15.853 15.997 66 SER 25.749 12.191 16.158 67 GLY 22.566 10.241 15.522 68 PRO 20.355 10.411 12.419 69 ILE 19.955 13.540 10.313 70 MET 16.370 14.405 11.252 71 LEU 15.404 17.281 8.932 72 ASP 16.830 18.773 5.703 73 GLU 15.882 21.573 3.290 74 VAL 13.852 23.261 6.027 75 GLN 11.709 26.161 4.778 76 CYS 9.979 27.985 7.671 77 THR 7.681 31.003 7.332 78 GLY 8.926 32.234 10.678 79 THR 5.682 31.763 12.657 80 GLU 6.191 28.094 13.507 81 ALA 6.510 26.701 17.011 82 SER 9.081 24.117 15.920 83 LEU 11.105 23.098 12.876 84 ALA 8.803 20.039 12.848 85 ASP 6.004 22.336 11.635 86 CYS 8.042 23.872 8.803 87 LYS 8.207 22.557 5.244 88 SER 11.115 20.109 4.763 89 LEU 11.826 16.795 2.953 90 GLY 10.135 14.941 5.831 91 TRP 11.432 13.262 9.019 92 LEU 14.630 11.302 8.497 93 LYS 14.785 12.120 4.789 94 SER 18.267 13.326 3.867 95 ASN 21.492 12.511 2.010 96 CYS 23.701 14.792 4.137 97 ARG 26.356 13.735 6.590 98 HIS 27.084 15.344 9.952 99 GLU 29.661 17.633 8.399 100 ARG 26.647 19.611 7.153 101 ASP 25.123 20.020 10.656 102 ALA 23.306 23.363 11.026 103 GLY 23.702 25.748 13.954 104 VAL 22.380 29.112 15.158 105 VAL 23.404 32.146 17.183 106 CYS 20.466 33.698 19.087 107 THR 20.059 37.070 20.735 108 ASN 21.434 37.307 24.266 109 GLU 18.043 38.829 25.066 110 THR 15.358 36.438 26.233 111 THR 23.614 31.583 1.804 112 LEU 23.274 27.845 2.550 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S S S S S S 10 S C C T T T T S S S 20 S S S/T T T T/S S S S S 30 S S S S C C H H H H 40 H H H H H H H H H C 50 C S S S S/S S S S S T 60 T T T/S S S S S S S S 70 S C S S S S S C C C 80 C T T T T/S S S S S C 90 C S S S S/S S S S C S 100 S S S S S S S S C S/X 110 SXS S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 t T T e E E E E 10 S S t T e E E E E 20 E E E E T T E E E E 30 E e t T T t h H H H 40 H H H H H H H h T t 50 S e E E E E E t T T 60 T T t S e E E 70 E S B S 80 S g G G G g B S t 90 T T t g G G G 100 B e E E E E e S 110 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ALA 0.0 0.0 93.4 2 VAL 70.1 59.0 62.5 3 ASN 18.3 15.1 81.9 4 ASP 55.5 50.2 60.1 5 GLY 33.6 96.7 54.7 6 ASP 59.0 53.4 65.1 7 MET 155.1 97.3 41.0 8 ARG 106.1 50.8 60.5 9 LEU 144.4 97.7 44.9 10 ALA 50.6 69.7 73.8 11 ASP 36.0 32.6 84.3 12 GLY 34.6 99.4 61.3 13 GLY 0.0 0.0 86.4 14 ALA 26.7 36.7 81.6 15 THR 0.0 0.0 83.7 16 ASN 103.3 85.4 51.9 17 GLN 98.7 66.4 54.2 18 GLY 34.8 100.0 45.4 19 ARG 193.3 92.5 56.2 20 VAL 118.8 100.0 33.2 21 GLU 126.8 91.5 57.4 22 ILE 143.5 100.0 35.5 23 PHE 140.4 84.2 56.0 24 TYR 152.1 84.0 44.1 25 ARG 38.8 18.6 82.3 26 GLY 6.8 19.5 65.0 27 GLN 59.3 39.9 65.0 28 TRP 155.2 75.7 55.9 29 GLY 33.7 96.8 58.0 30 THR 106.7 99.8 55.3 31 VAL 118.8 100.0 38.7 32 CYS 98.8 99.6 52.1 33 ASP 110.5 100.0 48.0 34 ASN 82.3 68.1 72.7 35 LEU 71.9 48.6 77.5 36 TRP 204.4 99.7 36.9 37 ASP 57.1 51.7 75.8 38 LEU 61.9 41.9 72.7 39 THR 56.6 52.9 76.6 40 ASP 110.4 99.9 49.2 41 ALA 72.6 100.0 43.2 42 SER 68.5 82.0 61.9 43 VAL 117.5 98.9 57.2 44 VAL 118.8 100.0 26.8 45 CYS 99.2 100.0 41.2 46 ARG 72.7 34.8 86.9 47 ALA 50.9 70.1 70.0 48 LEU 110.6 74.8 55.4 49 GLY 5.2 15.0 76.0 50 PHE 143.7 86.1 61.5 51 GLU 46.0 33.2 71.6 52 ASN 50.2 41.5 62.7 53 ALA 72.6 100.0 46.1 54 THR 53.7 50.2 63.0 55 GLN 63.3 42.6 62.6 56 ALA 66.8 92.0 51.8 57 LEU 100.0 67.6 54.6 58 GLY 34.8 99.9 48.5 59 ARG 98.3 47.1 76.8 60 ALA 65.7 90.4 66.7 61 ALA 43.7 60.1 65.0 62 PHE 138.5 83.0 59.1 63 GLY 3.2 9.2 79.4 64 GLN 62.0 41.7 67.9 65 GLY 31.6 90.9 70.9 66 SER 3.4 4.1 83.3 67 GLY 10.7 30.8 66.5 68 PRO 84.4 67.8 58.0 69 ILE 127.2 88.6 64.2 70 MET 159.1 99.8 44.3 71 LEU 143.7 97.2 39.7 72 ASP 106.8 96.7 49.3 73 GLU 81.2 58.6 57.7 74 VAL 118.6 99.9 40.7 75 GLN 78.4 52.8 69.4 76 CYS 99.2 100.0 43.6 77 THR 21.4 20.0 83.1 78 GLY 26.5 76.2 62.8 79 THR 5.8 5.5 88.6 80 GLU 116.0 83.7 59.9 81 ALA 2.3 3.2 85.1 82 SER 69.9 83.6 51.9 83 LEU 147.8 100.0 23.7 84 ALA 59.0 81.2 55.8 85 ASP 38.1 34.5 71.3 86 CYS 98.5 99.3 52.8 87 LYS 23.0 13.2 83.4 88 SER 77.5 92.7 60.1 89 LEU 82.1 55.6 72.3 90 GLY 2.5 7.2 80.0 91 TRP 158.2 77.2 45.0 92 LEU 83.3 56.4 62.8 93 LYS 39.1 22.5 81.4 94 SER 80.0 95.7 54.7 95 ASN 0.0 0.0 91.3 96 CYS 88.8 89.5 57.5 97 ARG 34.5 16.5 86.7 98 HIS 121.5 80.9 67.6 99 GLU 72.8 52.5 66.9 100 ARG 133.6 64.0 74.0 101 ASP 110.3 99.8 54.3 102 ALA 72.6 100.0 51.2 103 GLY 34.1 98.1 50.3 104 VAL 118.8 100.0 35.3 105 VAL 95.6 80.5 63.5 106 CYS 99.2 100.0 39.6 107 THR 83.0 77.6 55.4 108 ASN 9.6 7.9 85.5 109 GLU 33.0 23.8 78.4 110 THR 23.9 22.4 73.5 111 THR 0.0 0.0 90.4 112 LEU 116.5 78.8 70.6