Protein Data Bank File : 1g2ba Title : METAL BINDING PROTEIN 18-OCT-00 1G2B Number of Amino Acid Residues : 62 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 MET ASP ARG GLN GLY PHE VAL PRO ALA ALA 10 TYR VAL LYS LYS LEU ASP SER GLY THR GLY 20 LYS GLU LEU VAL LEU ALA LEU TYR ASP TYR 30 GLN GLU LYS SER PRO ARG GLU VAL THR MET 40 LYS LYS GLY ASP ILE LEU THR LEU LEU ASN 50 SER THR ASN LYS ASP TRP TRP LYS VAL GLU 60 VAL ASN Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 MET 0.0 -91.1 168.7 95.7 -63.2 112.4 2 ASP -57.1 136.4 179.6 -72.4 -13.9 3 ARG -137.0 150.0 178.1 -52.7 -94.0 173.1 -158.7 4 GLN -129.2 141.0 176.9 -56.4 -173.9 -9.7 5 GLY 172.8 -169.7 -174.1 6 PHE -95.1 141.8 169.3 -68.9 -77.4 7 VAL -128.4 158.3 179.5 -63.3 8 PRO -63.5 129.4 -177.8 -22.3 35.7 9 ALA -55.2 -35.1 -178.5 10 ALA -63.3 -20.3 -169.9 11 TYR -95.2 3.2 179.3 -56.3 -15.0 12 VAL -133.0 155.9 -179.7 -62.4 13 LYS -124.0 125.4 176.7 177.0 179.6 -172.1 171.2 14 LYS -63.3 131.0 165.0 -69.0 -177.9 175.0 -167.7 15 LEU -82.3 149.8 174.7 -53.5 -175.9 16 ASP -55.3 144.4 176.7 -68.3 -0.4 17 SER -61.8 151.4 179.5 -55.6 18 GLY -153.6 -143.4 173.3 19 THR -71.3 135.5 176.5 -56.0 20 GLY 76.1 -147.6 -170.7 21 LYS -77.8 160.4 174.6 -63.0 172.4 -172.7 -178.5 22 GLU -67.6 149.4 -176.7 -59.4 -52.9 -56.8 23 LEU -131.9 147.9 170.6 -61.1 174.2 24 VAL -127.5 156.6 170.5 -62.0 25 LEU -99.8 126.3 173.7 170.2 67.8 26 ALA -73.3 118.4 -179.1 27 LEU -82.7 -22.1 -174.8 -65.1 174.2 28 TYR -145.9 154.3 164.2 -44.6 -67.6 29 ASP -62.8 138.2 177.8 -71.8 -6.0 30 TYR -145.6 113.0 173.4 -176.6 76.4 31 GLN -87.9 133.9 179.1 -170.2 172.1 -31.7 32 GLU -55.5 135.9 -178.6 59.3 -168.7 -1.4 33 LYS -106.2 -10.7 177.9 -54.2 178.2 166.5 -63.5 34 SER -153.4 156.7 -175.6 70.5 35 PRO -54.8 -31.3 -178.1 -23.4 29.4 36 ARG -73.1 -8.3 -179.8 69.0 -169.2 -171.9 -178.2 37 GLU -93.9 179.2 171.0 -62.2 166.3 34.4 38 VAL -139.5 162.0 179.3 -71.2 39 THR -95.7 139.2 176.4 -66.7 40 MET -136.1 158.5 173.9 60.5 -173.8 -177.0 41 LYS -109.9 143.5 175.3 -171.2 173.1 172.1 54.7 42 LYS -50.8 132.8 178.6 179.9 167.7 162.8 44.6 43 GLY 90.6 -10.8 175.7 44 ASP -62.6 144.3 173.9 -72.0 -9.0 45 ILE -104.3 111.7 -171.0 -57.9 -66.2 46 LEU -109.7 139.8 168.2 -48.2 176.9 47 THR -71.8 124.6 -178.2 -58.6 48 LEU -91.6 116.9 -176.6 177.6 57.9 49 LEU -94.2 -37.6 -175.0 -55.4 -177.8 50 ASN -156.6 120.0 177.1 -174.5 -55.2 51 SER -120.6 29.0 -179.4 59.2 52 THR -73.7 -24.7 179.3 63.7 53 ASN -93.3 142.9 -176.8 -172.9 -93.1 54 LYS -75.6 -22.6 -171.8 78.6 174.2 179.6 -158.2 55 ASP -101.5 -35.8 -169.6 -65.2 -46.1 56 TRP -130.3 120.4 179.8 -68.2 101.0 57 TRP -110.0 139.1 -179.3 -71.2 -3.8 58 LYS -90.2 124.6 -179.5 -165.7 -176.5 -178.0 -170.2 59 VAL -128.6 163.8 167.8 -61.5 60 GLU -116.1 129.5 -178.5 172.3 172.8 66.0 61 VAL -113.0 160.4 -179.6 -55.2 62 ASN -90.2 -173.2 0.0 62.1 35.5 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 MET -13.424 -0.540 20.432 2 ASP -11.202 0.653 17.609 3 ARG -10.002 4.212 18.501 4 GLN -8.069 6.900 16.518 5 GLY -5.912 9.745 17.722 6 PHE -2.464 11.029 18.284 7 VAL 0.527 9.483 19.973 8 PRO 4.041 10.891 20.381 9 ALA 6.049 10.129 17.267 10 ALA 9.089 9.129 19.353 11 TYR 7.128 6.275 20.900 12 VAL 6.430 4.378 17.653 13 LYS 8.658 2.988 14.885 14 LYS 7.624 2.978 11.221 15 LEU 7.550 -0.393 9.617 16 ASP 8.552 -0.547 5.952 17 SER 5.737 0.124 3.543 18 GLY 4.021 -2.913 2.028 19 THR 0.577 -3.960 0.966 20 GLY -2.265 -1.718 2.281 21 LYS -1.893 0.880 4.913 22 GLU 1.203 2.158 6.675 23 LEU 2.057 0.446 10.026 24 VAL 4.022 1.350 13.110 25 LEU 5.331 -0.650 16.088 26 ALA 4.473 0.712 19.565 27 LEU 7.764 0.917 21.435 28 TYR 6.264 1.694 24.893 29 ASP 2.998 1.580 26.770 30 TYR 1.350 4.961 26.443 31 GLN -1.899 5.951 28.146 32 GLU -3.621 8.861 26.477 33 LYS -3.057 12.153 28.396 34 SER -5.642 14.291 26.531 35 PRO -8.766 13.531 24.472 36 ARG -7.015 14.039 21.144 37 GLU -4.663 11.123 21.942 38 VAL -5.165 7.321 22.105 39 THR -3.770 4.575 24.278 40 MET -1.348 1.923 23.022 41 LYS 0.479 -1.040 24.546 42 LYS 4.134 -1.886 23.966 43 GLY 4.381 -4.281 21.008 44 ASP 1.118 -3.248 19.352 45 ILE 1.111 -3.049 15.569 46 LEU -0.802 0.119 14.745 47 THR -2.247 1.472 11.514 48 LEU -0.521 4.763 10.828 49 LEU -3.008 7.396 9.566 50 ASN -0.951 10.580 9.493 51 SER 2.754 11.227 10.104 52 THR 2.970 14.775 8.713 53 ASN 3.715 16.352 12.108 54 LYS 7.131 15.700 13.684 55 ASP 5.782 15.420 17.250 56 TRP 2.351 13.798 16.976 57 TRP 1.346 10.945 14.674 58 LYS -2.266 9.877 14.156 59 VAL -2.812 6.116 14.592 60 GLU -5.612 3.605 14.979 61 VAL -5.378 1.342 18.086 62 ASN -7.321 -1.593 19.211 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S S C T T T 10 T/S S S S S S/S S S S S 20 S S S S S S S S/S S S 30 S S C C C S S S S S 40 S S S S S S S/S S S S 50 C C T T T T/S S S S S 60 S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 E E E E E E e T 10 e E E E e S S 20 S e E E E E e S B 30 S t T T B B 40 t T T e E E E E E E 50 S S e E E E E E 60 E Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 MET 41.2 25.8 90.9 2 ASP 46.8 42.3 62.8 3 ARG 52.8 25.3 81.1 4 GLN 82.3 55.4 65.0 5 GLY 30.1 86.6 50.9 6 PHE 102.9 61.7 53.0 7 VAL 118.8 100.0 31.2 8 PRO 105.4 84.7 41.8 9 ALA 64.2 88.4 60.2 10 ALA 7.6 10.4 73.5 11 TYR 101.1 55.9 49.4 12 VAL 118.8 100.0 33.0 13 LYS 44.9 25.9 71.0 14 LYS 77.2 44.5 64.6 15 LEU 92.1 62.3 60.1 16 ASP 0.0 0.0 91.1 17 SER 28.2 33.7 88.2 18 GLY 0.0 0.0 84.8 19 THR 0.0 0.0 88.1 20 GLY 0.0 0.0 74.1 21 LYS 36.5 21.0 80.5 22 GLU 69.7 50.3 73.9 23 LEU 81.3 55.0 63.6 24 VAL 118.8 100.0 33.6 25 LEU 94.0 63.6 54.2 26 ALA 72.6 100.0 48.8 27 LEU 99.6 67.4 59.7 28 TYR 65.9 36.4 67.9 29 ASP 37.3 33.7 71.8 30 TYR 161.7 89.3 45.8 31 GLN 17.8 11.9 81.0 32 GLU 71.7 51.7 74.3 33 LYS 29.6 17.1 85.7 34 SER 47.0 56.2 64.0 35 PRO 6.5 5.2 83.1 36 ARG 52.0 24.9 78.2 37 GLU 129.7 93.5 52.9 38 VAL 113.6 95.7 49.6 39 THR 49.8 46.6 67.3 40 MET 157.3 98.7 38.8 41 LYS 35.6 20.5 86.0 42 LYS 50.2 29.0 78.3 43 GLY 10.2 29.2 69.4 44 ASP 85.4 77.3 57.6 45 ILE 71.3 49.7 60.1 46 LEU 145.1 98.1 43.7 47 THR 80.9 75.7 54.4 48 LEU 140.5 95.0 42.6 49 LEU 110.4 74.7 60.1 50 ASN 55.4 45.8 69.3 51 SER 67.3 80.5 55.4 52 THR 12.8 12.0 87.8 53 ASN 45.0 37.3 80.5 54 LYS 9.9 5.7 92.1 55 ASP 36.2 32.7 70.8 56 TRP 132.9 64.8 63.4 57 TRP 171.6 83.7 49.8 58 LYS 100.7 58.1 55.7 59 VAL 118.8 100.0 33.5 60 GLU 96.9 69.9 61.2 61 VAL 114.4 96.3 47.3 62 ASN 17.5 14.4 87.6