Protein Data Bank File : 2pvba Title : METAL BINDING PROTEIN 02-OCT-98 2PVB Number of Amino Acid Residues : 107 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 SER PHE ALA GLY LEU LYS ASP ALA ASP VAL 10 ALA ALA ALA LEU ALA ALA CYS SER ALA ALA 20 ASP SER PHE LYS HIS LYS GLU PHE PHE ALA 30 LYS VAL GLY LEU ALA SER LYS SER LEU ASP 40 ASP VAL LYS LYS ALA PHE TYR VAL ILE ASP 50 GLN ASP LYS SER GLY PHE ILE GLU GLU ASP 60 GLU LEU LYS LEU PHE LEU GLN ASN PHE SER 70 PRO SER ALA ARG ALA LEU THR ASP ALA GLU 80 THR LYS ALA PHE LEU ALA ASP GLY ASP LYS 90 ASP GLY ASP GLY MET ILE GLY VAL ASP GLU 100 PHE ALA ALA MET ILE LYS ALA Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 SER 0.0 148.8 179.5 76.3 2 PHE -157.4 121.7 -172.1 -168.0 -86.2 3 ALA -51.5 136.0 -179.6 4 GLY 92.7 -18.7 -179.8 5 LEU -106.7 160.3 177.2 -55.8 179.4 6 LYS -82.1 131.7 -179.5 -172.3 167.4 156.7 -163.2 7 ASP -52.8 -42.7 -175.6 -68.5 -0.6 8 ALA -64.8 -34.6 178.7 9 ASP -68.0 -42.4 178.3 -67.6 -25.3 10 VAL -61.0 -47.6 -179.1 176.9 11 ALA -62.5 -37.7 178.2 12 ALA -67.5 -40.5 179.5 13 ALA -63.0 -40.3 177.1 14 LEU -65.8 -41.4 177.0 -71.3 166.9 15 ALA -61.9 -37.0 -175.4 16 ALA -68.0 -20.6 176.5 17 CYS -113.9 26.8 -178.0 64.4 18 SER -61.9 -34.7 179.1 58.4 19 ALA -78.4 136.5 175.0 20 ALA -57.6 137.7 179.3 21 ASP 74.8 8.8 172.7 -69.8 -48.2 22 SER -94.8 -7.0 -179.1 76.2 23 PHE -68.4 135.8 174.0 175.2 79.0 24 LYS -133.4 105.8 -172.2 -64.1 174.5 176.1 59.2 25 HIS -54.8 -40.7 -177.8 51.3 -79.2 26 LYS -68.6 -33.5 174.9 -74.9 175.7 172.1 161.2 27 GLU -67.3 -42.2 177.9 -66.4 -167.8 -0.6 28 PHE -59.9 -46.1 -179.7 -175.7 -86.3 29 PHE -55.3 -41.7 178.7 -60.6 -28.0 30 ALA -68.2 -51.1 -172.9 31 LYS -62.8 -38.7 -177.4 -171.2 62.8 -178.1 169.4 32 VAL -79.9 -9.9 175.8 -63.6 33 GLY 102.6 -1.8 -177.9 34 LEU -68.0 -35.7 179.0 -82.1 166.0 35 ALA -62.1 -22.6 -180.0 36 SER -93.8 -6.3 177.9 -67.2 37 LYS -78.3 154.9 171.5 -74.1 -75.7 -170.3 170.0 38 SER -60.4 159.3 173.2 64.9 39 LEU -56.7 -42.6 177.4 177.9 59.7 40 ASP -53.5 -47.5 -177.9 172.8 49.8 41 ASP -69.9 -34.6 175.6 -71.1 -12.6 42 VAL -64.4 -40.7 175.3 170.5 43 LYS -58.5 -42.5 178.4 -69.6 178.1 175.7 176.0 44 LYS -58.0 -41.2 -179.9 -63.0 171.7 -166.8 167.1 45 ALA -62.9 -38.2 178.3 46 PHE -53.5 -49.3 -172.9 171.5 78.6 47 TYR -67.5 -27.6 172.7 -65.8 -75.0 48 VAL -67.0 -46.1 -176.7 171.2 49 ILE -64.3 -33.3 172.3 -53.9 -59.4 50 ASP -72.8 79.0 -168.4 172.2 23.9 51 GLN -66.6 -32.8 178.3 -66.2 -165.7 65.1 52 ASP -90.5 4.9 175.4 71.6 -1.7 53 LYS 61.3 34.6 179.3 -47.1 -53.1 155.3 -175.1 54 SER -84.7 -11.7 -174.7 65.2 55 GLY 93.0 -5.2 178.7 56 PHE -136.9 150.9 165.6 -64.0 88.4 57 ILE -89.6 109.5 176.9 -60.1 165.9 58 GLU -84.0 171.3 -175.6 -64.4 84.3 20.8 59 GLU -59.7 -38.0 179.8 -156.1 175.6 -28.7 60 ASP -63.7 -31.9 175.6 58.6 -9.3 61 GLU -75.3 -28.0 168.8 -69.2 168.9 -13.8 62 LEU -68.3 -44.2 -179.1 -66.2 173.2 63 LYS -58.4 -37.8 -179.1 -177.5 161.8 -175.1 79.2 64 LEU -100.1 21.8 -179.2 -61.3 -178.9 65 PHE -49.8 -46.3 -174.3 172.4 78.4 66 LEU -66.1 -22.6 -179.6 -59.9 175.8 67 GLN -64.9 -20.5 175.5 -69.3 -163.4 -71.6 68 ASN -70.0 -19.0 -179.3 -61.5 -76.7 69 PHE -101.2 -31.4 169.8 -61.8 86.9 70 SER -154.1 127.3 -177.3 174.3 71 PRO -60.5 -27.9 -178.1 24.9 -37.0 72 SER -88.3 0.4 176.5 56.9 73 ALA -64.7 155.4 -178.1 74 ARG -68.8 156.2 163.0 68.0 179.3 -178.4 84.7 75 ALA -66.0 149.3 163.9 76 LEU -69.0 147.3 173.6 -61.5 -173.0 77 THR -68.4 163.6 175.0 66.5 78 ASP -57.5 -36.8 177.3 -69.8 -13.1 79 ALA -63.1 -47.7 179.0 80 GLU -61.8 -41.4 -178.2 -73.4 165.6 -24.0 81 THR -61.0 -49.7 -178.9 -60.9 82 LYS -67.9 -31.8 175.7 -81.3 -75.9 -153.5 -69.9 83 ALA -66.6 -41.2 176.7 84 PHE -58.8 -50.0 179.9 -166.0 -7.7 85 LEU -58.9 -49.7 -174.5 178.6 62.9 86 ALA -63.3 -37.0 179.7 87 ASP -68.2 -36.5 -174.5 -171.7 62.0 88 GLY -91.1 -22.8 -168.9 89 ASP -85.7 70.7 -177.3 -177.4 18.9 90 LYS -65.0 -21.9 178.8 -73.9 -14.4 179.7 48.6 91 ASP -104.0 -0.9 169.6 65.2 13.9 92 GLY 76.8 12.2 -178.2 93 ASP -84.9 4.1 175.8 68.1 -4.9 94 GLY 84.6 8.1 -175.1 95 MET -143.0 169.3 174.7 -49.9 178.9 -77.9 96 ILE -118.2 123.2 177.2 -70.1 174.1 97 GLY -94.5 175.7 -171.0 98 VAL -61.9 -41.9 -178.5 62.5 99 ASP -67.3 -37.2 176.3 -68.0 -19.6 100 GLU -64.7 -39.7 178.6 -75.4 168.4 -27.2 101 PHE -62.9 -48.4 178.7 -178.6 82.6 102 ALA -62.1 -38.6 -178.2 103 ALA -62.3 -36.6 179.4 104 MET -68.6 -33.2 -172.9 -84.2 -174.7 -67.9 105 ILE -85.6 -38.0 -176.7 -68.0 164.8 106 LYS -98.4 11.9 178.6 -60.9 -56.4 -55.5 -165.1 107 ALA -50.0 143.4 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 SER 5.448 18.370 18.030 2 PHE 7.323 21.172 19.687 3 ALA 9.159 20.776 22.973 4 GLY 7.151 22.063 25.901 5 LEU 3.808 21.906 24.058 6 LYS 1.357 19.030 23.804 7 ASP 1.608 17.088 20.572 8 ALA -2.166 16.932 20.185 9 ASP -2.413 20.756 20.440 10 VAL 0.327 21.195 17.840 11 ALA -1.346 18.721 15.505 12 ALA -4.722 20.457 15.968 13 ALA -3.219 23.859 15.283 14 LEU -1.640 22.566 12.085 15 ALA -4.951 21.037 10.980 16 ALA -6.726 24.348 11.684 17 CYS -4.503 26.160 9.139 18 SER -4.374 23.412 6.552 19 ALA -5.968 25.588 3.847 20 ALA -3.758 28.172 2.158 21 ASP -4.531 31.687 3.446 22 SER -6.247 30.345 6.587 23 PHE -3.237 30.799 8.875 24 LYS -3.748 33.411 11.603 25 HIS -0.600 33.599 13.734 26 LYS -2.373 34.783 16.869 27 GLU -4.906 31.951 16.556 28 PHE -2.081 29.450 16.018 29 PHE -0.253 30.781 19.092 30 ALA -3.342 30.170 21.221 31 LYS -4.215 26.743 19.808 32 VAL -0.756 25.292 20.149 33 GLY -0.499 26.533 23.746 34 LEU 2.189 29.217 23.396 35 ALA -0.136 32.049 24.442 36 SER -0.559 30.202 27.813 37 LYS 3.203 29.712 28.341 38 SER 5.347 31.791 30.636 39 LEU 7.496 34.538 29.147 40 ASP 10.565 32.384 29.799 41 ASP 9.109 29.568 27.772 42 VAL 7.977 31.877 24.986 43 LYS 11.550 33.168 24.719 44 LYS 12.787 29.587 24.322 45 ALA 10.426 29.120 21.397 46 PHE 11.754 32.236 19.671 47 TYR 15.304 30.930 19.547 48 VAL 14.117 27.686 18.016 49 ILE 12.087 29.545 15.259 50 ASP 15.272 31.557 14.554 51 GLN 16.651 28.612 12.593 52 ASP 19.883 30.273 11.443 53 LYS 20.738 31.618 14.921 54 SER 20.947 35.132 13.627 55 GLY 19.073 36.549 16.613 56 PHE 16.042 37.523 14.522 57 ILE 13.237 35.733 12.780 58 GLU 13.636 36.908 9.182 59 GLU 10.909 36.685 6.575 60 ASP 12.138 33.360 5.190 61 GLU 11.865 31.869 8.730 62 LEU 8.320 33.250 8.990 63 LYS 7.453 31.667 5.678 64 LEU 8.675 28.305 7.007 65 PHE 7.347 28.900 10.525 66 LEU 5.154 25.796 10.512 67 GLN 8.123 23.515 9.744 68 ASN 9.307 24.022 13.341 69 PHE 6.128 22.181 14.398 70 SER 6.159 19.522 11.676 71 PRO 8.796 19.255 8.932 72 SER 6.145 18.285 6.413 73 ALA 3.879 21.262 7.191 74 ARG 3.158 23.721 4.443 75 ALA 4.926 26.998 3.797 76 LEU 2.952 30.084 4.633 77 THR 1.781 31.908 1.547 78 ASP 3.530 35.166 0.726 79 ALA 0.384 36.944 1.941 80 GLU 0.391 35.100 5.267 81 THR 4.113 35.694 5.683 82 LYS 3.858 39.423 5.149 83 ALA 0.849 39.738 7.385 84 PHE 2.738 37.916 10.187 85 LEU 5.712 40.252 9.702 86 ALA 3.633 43.442 9.673 87 ASP 1.768 42.529 12.820 88 GLY 4.878 41.656 14.770 89 ASP 7.492 44.090 13.495 90 LYS 6.816 46.897 15.992 91 ASP 10.207 48.551 15.415 92 GLY 10.092 48.437 11.632 93 ASP 13.413 46.765 10.927 94 GLY 11.880 44.113 8.669 95 MET 12.496 41.285 11.151 96 ILE 11.135 39.972 14.431 97 GLY 13.281 40.058 17.536 98 VAL 12.678 38.150 20.771 99 ASP 10.736 40.893 22.533 100 GLU 8.527 41.415 19.460 101 PHE 7.870 37.683 19.301 102 ALA 6.870 37.544 22.939 103 ALA 4.671 40.643 22.527 104 MET 2.620 38.983 19.770 105 ILE 2.062 35.882 21.863 106 LYS 1.468 37.427 25.265 107 ALA -0.696 40.304 24.011 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C T T T T H H H H H 10 H H H H H H H H T T 20 T T C H H H H H H H 30 H H H/T T T T C H H H 40 H H H H H H H H H H/T 50 T T T C S S S S/H H H 60 H H H H H/H H H H 3 3 70 C S S S S S H H H H 80 H H H H H H H H H/T T 90 T T C S S S S/H H H H 100 H H H H H H H Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 t T T t h H H H H 10 H H H H H H h t t T 20 T t h H H H H H H 30 H h g G G G g h H H 40 H H H H H H H H H h 50 T T t S S S B h H H 60 H H H h G G G G g t 70 T T t h H H H 80 H H H H H H H H h T 90 T t S S S B h H H H 100 H H H H H H h Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 SER 26.6 31.8 78.4 2 PHE 150.7 90.3 39.9 3 ALA 0.0 0.0 87.8 4 GLY 4.6 13.3 77.5 5 LEU 141.7 95.9 43.1 6 LYS 41.1 23.7 83.0 7 ASP 26.0 23.5 74.0 8 ALA 18.2 25.1 69.2 9 ASP 65.6 59.3 68.3 10 VAL 118.6 99.8 43.8 11 ALA 17.6 24.2 72.7 12 ALA 38.1 52.4 67.4 13 ALA 72.1 99.3 44.6 14 LEU 121.4 82.1 45.5 15 ALA 14.5 20.0 78.9 16 ALA 18.8 25.9 78.7 17 CYS 92.8 93.5 56.4 18 SER 18.6 22.2 84.0 19 ALA 11.7 16.2 84.5 20 ALA 26.7 36.8 73.3 21 ASP 45.4 41.1 68.4 22 SER 56.2 67.3 76.1 23 PHE 165.2 99.0 36.2 24 LYS 62.9 36.3 80.3 25 HIS 129.8 86.4 35.5 26 LYS 87.7 50.6 68.7 27 GLU 29.8 21.5 73.3 28 PHE 160.5 96.2 29.3 29 PHE 164.7 98.8 28.8 30 ALA 25.7 35.5 73.3 31 LYS 67.6 39.0 72.5 32 VAL 118.8 100.0 35.3 33 GLY 17.9 51.5 74.8 34 LEU 142.9 96.7 25.4 35 ALA 48.2 66.5 64.2 36 SER 8.4 10.1 84.1 37 LYS 120.2 69.3 63.1 38 SER 28.2 33.7 79.5 39 LEU 63.3 42.9 61.5 40 ASP 26.8 24.3 75.1 41 ASP 78.8 71.4 69.7 42 VAL 118.8 100.0 38.2 43 LYS 90.4 52.1 58.9 44 LYS 55.2 31.8 83.9 45 ALA 69.7 96.0 38.8 46 PHE 166.4 99.7 38.4 47 TYR 73.8 40.7 65.4 48 VAL 46.9 39.5 74.0 49 ILE 142.3 99.2 37.0 50 ASP 108.4 98.1 58.6 51 GLN 78.2 52.6 77.1 52 ASP 37.9 34.3 81.8 53 LYS 59.1 34.1 86.2 54 SER 50.6 60.5 84.8 55 GLY 10.7 30.7 69.6 56 PHE 95.5 57.2 66.7 57 ILE 142.6 99.4 36.7 58 GLU 97.4 70.3 66.5 59 GLU 82.3 59.4 59.3 60 ASP 17.4 15.7 73.1 61 GLU 127.7 92.2 67.5 62 LEU 146.6 99.2 33.4 63 LYS 107.7 62.1 64.7 64 LEU 78.8 53.3 71.5 65 PHE 165.7 99.3 28.1 66 LEU 145.9 98.7 34.4 67 GLN 90.5 60.9 69.9 68 ASN 107.0 88.5 53.0 69 PHE 166.7 99.9 28.0 70 SER 55.9 66.9 58.7 71 PRO 19.7 15.8 85.2 72 SER 4.2 5.0 86.6 73 ALA 58.9 81.2 61.9 74 ARG 154.8 74.1 66.3 75 ALA 44.8 61.6 63.5 76 LEU 147.8 100.0 45.4 77 THR 71.7 67.1 70.8 78 ASP 13.9 12.6 80.7 79 ALA 12.2 16.8 83.6 80 GLU 128.7 92.9 60.8 81 THR 102.7 96.1 47.2 82 LYS 60.3 34.7 80.1 83 ALA 17.6 24.2 77.4 84 PHE 165.8 99.4 29.4 85 LEU 127.9 86.5 52.1 86 ALA 12.2 16.8 79.0 87 ASP 66.1 59.8 69.7 88 GLY 34.4 98.8 51.8 89 ASP 100.3 90.8 65.3 90 LYS 50.2 29.0 84.5 91 ASP 33.6 30.4 85.1 92 GLY 6.2 17.9 86.9 93 ASP 61.9 56.0 70.8 94 GLY 8.3 23.9 70.8 95 MET 107.9 67.7 58.4 96 ILE 143.4 99.9 37.5 97 GLY 22.5 64.6 55.9 98 VAL 87.0 73.2 50.5 99 ASP 11.7 10.6 74.2 100 GLU 119.4 86.2 63.6 101 PHE 164.5 98.6 29.7 102 ALA 65.0 89.5 45.2 103 ALA 19.9 27.4 77.1 104 MET 152.7 95.8 43.6 105 ILE 143.2 99.8 31.9 106 LYS 108.3 62.5 68.8 107 ALA 25.7 35.4 85.2