Protein Data Bank File : 2hsp Title : PHOSPHORIC DIESTER HYDROLASE 13-JUN-94 2HSP Number of Amino Acid Residues : 71 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLY SER PRO THR PHE LYS CYS ALA VAL LYS 10 ALA LEU PHE ASP TYR LYS ALA GLN ARG GLU 20 ASP GLU LEU THR PHE ILE LYS SER ALA ILE 30 ILE GLN ASN VAL GLU LYS GLN GLU GLY GLY 40 TRP TRP ARG GLY ASP TYR GLY GLY LYS LYS 50 GLN LEU TRP PHE PRO SER ASN TYR VAL GLU 60 GLU MET VAL ASN PRO GLU GLY ILE HIS ARG 70 ASP Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLY 0.0 -112.3 180.0 2 SER -144.3 69.6 -180.0 -78.3 3 PRO -68.4 118.7 -179.9 5.1 -2.5 4 THR -146.0 170.5 180.0 9.5 5 PHE -58.5 -163.6 -180.0 -132.0 79.7 6 LYS 55.7 156.6 179.8 -93.5 79.4 177.3 -68.6 7 CYS -84.5 108.3 -179.8 -163.9 8 ALA -116.3 -175.3 -180.0 9 VAL -147.0 -178.7 179.6 -28.0 10 LYS -137.6 88.9 -179.9 171.5 159.6 -108.3 51.9 11 ALA -38.6 120.9 179.8 12 LEU -92.9 -27.6 180.0 -39.5 171.4 13 PHE -106.7 168.3 -179.9 -65.6 1.1 14 ASP -102.5 138.9 179.9 176.2 18.8 15 TYR -116.1 170.4 179.6 -160.1 -81.1 16 LYS -148.9 78.4 179.5 -152.7 -169.0 -169.6 67.0 17 ALA -125.3 -50.8 180.0 18 GLN 76.3 -38.7 -180.0 -163.1 -168.6 148.3 19 ARG -175.6 74.0 -179.9 58.7 -137.5 -157.5 -122.2 20 GLU -131.1 4.6 -179.2 95.9 85.7 7.5 21 ASP 112.5 -7.9 179.7 -64.4 15.5 22 GLU -129.5 162.2 -180.0 -145.3 -69.8 -13.4 23 LEU -126.9 164.1 -180.0 -26.4 119.2 24 THR -88.6 25.2 180.0 175.9 25 PHE -44.9 142.0 -179.5 58.4 77.2 26 ILE -104.9 166.2 -180.0 29.7 63.7 27 LYS -55.5 123.7 179.9 168.4 -103.7 -92.3 173.6 28 SER 110.3 -6.0 179.9 71.5 29 ALA -62.9 145.2 -180.0 30 ILE -119.9 120.3 -179.7 -32.4 92.3 31 ILE -108.3 151.7 -179.7 -54.3 -178.9 32 GLN -114.3 165.9 -179.9 -60.3 -122.4 -39.1 33 ASN 46.9 87.7 -179.4 -85.9 138.6 34 VAL -123.8 154.2 -179.9 116.0 35 GLU -174.6 107.3 179.8 -160.3 -116.2 -85.6 36 LYS -47.7 137.4 -179.9 5.7 173.4 166.2 42.8 37 GLN -109.9 146.4 -179.7 153.2 -82.4 -27.6 38 GLU -32.1 81.7 179.6 -59.8 -88.1 60.9 39 GLY 157.0 -20.5 -179.9 40 GLY 97.0 44.0 -180.0 41 TRP -133.6 142.8 -178.8 -65.5 75.2 42 TRP -110.0 152.6 179.6 -64.3 42.4 43 ARG -113.2 174.4 -180.0 -119.2 179.6 -160.8 171.3 44 GLY 134.5 145.5 -179.9 45 ASP -69.8 146.5 179.8 88.3 67.6 46 TYR -156.5 93.3 -179.8 -165.7 55.4 47 GLY 100.8 -141.0 180.0 48 GLY -84.8 3.9 179.9 49 LYS -92.4 179.9 179.8 -43.1 -67.0 -141.7 -42.0 50 LYS -153.0 101.7 179.8 -144.9 -158.4 -149.8 79.4 51 GLN 71.9 68.7 179.5 -44.1 -151.5 -101.9 52 LEU -97.7 -136.4 179.9 -68.9 -141.0 53 TRP -141.7 145.0 179.2 -77.2 105.7 54 PHE -145.7 131.5 180.0 0.1 -66.7 55 PRO -51.4 153.2 179.5 -14.8 13.9 56 SER -97.5 8.7 -180.0 73.3 57 ASN -107.2 -16.9 -179.9 -117.0 -63.0 58 TYR -107.2 -46.7 -179.5 -79.7 57.5 59 VAL -87.7 170.9 179.8 -49.6 60 GLU -155.4 120.7 -179.7 -101.1 -66.8 -48.0 61 GLU -56.6 82.1 179.6 45.0 144.1 -70.8 62 MET 38.5 100.3 179.8 -86.5 -105.6 134.9 63 VAL -88.2 22.2 179.9 -167.1 64 ASN -136.3 94.9 180.0 -68.4 74.7 65 PRO -56.6 -140.9 -179.9 -13.1 19.4 66 GLU 55.6 166.9 -180.0 -88.9 164.8 -69.9 67 GLY 169.4 137.6 179.9 68 ILE -110.8 160.0 -179.9 -58.3 148.9 69 HIS -105.8 135.3 180.0 5.4 -84.6 70 ARG -68.1 -132.5 179.9 -164.2 101.3 142.8 166.9 71 ASP -103.3 128.7 0.0 -75.4 -35.1 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLY 0.419 -1.442 -0.383 2 SER 0.933 -2.137 -4.088 3 PRO -1.731 -0.432 -6.201 4 THR -1.342 -1.515 -9.824 5 PHE -3.370 -2.177 -12.964 6 LYS -5.138 -5.507 -13.561 7 CYS -7.738 -6.730 -11.094 8 ALA -5.847 -7.696 -7.945 9 VAL -6.578 -8.318 -4.283 10 LYS -4.914 -8.222 -0.893 11 ALA -5.107 -11.551 0.956 12 LEU -6.490 -10.752 4.373 13 PHE -6.074 -14.294 5.661 14 ASP -3.050 -16.619 5.551 15 TYR -2.806 -19.699 3.339 16 LYS -0.394 -22.609 3.221 17 ALA 0.043 -24.343 -0.132 18 GLN 3.040 -22.660 -1.632 19 ARG 2.434 -24.582 -4.836 20 GLU -0.571 -26.903 -4.951 21 ASP -2.600 -24.999 -7.525 22 GLU -3.199 -22.823 -4.512 23 LEU -0.374 -20.830 -2.715 24 THR 0.797 -20.232 0.825 25 PHE 0.428 -16.604 0.153 26 ILE 0.263 -14.732 3.456 27 LYS -1.926 -11.902 4.629 28 SER -0.990 -8.869 2.588 29 ALA -0.155 -10.900 -0.488 30 ILE -1.183 -9.242 -3.736 31 ILE -2.401 -11.351 -6.652 32 GLN -3.133 -10.118 -10.228 33 ASN -5.686 -11.011 -12.897 34 VAL -8.365 -12.320 -10.649 35 GLU -11.862 -13.753 -11.089 36 LYS -13.919 -15.982 -8.748 37 GLN -14.648 -19.315 -10.384 38 GLU -17.862 -21.364 -10.112 39 GLY -17.392 -22.396 -6.473 40 GLY -16.000 -19.358 -4.685 41 TRP -12.325 -19.712 -5.612 42 TRP -10.133 -17.123 -7.237 43 ARG -7.366 -17.320 -9.871 44 GLY -4.362 -15.045 -10.607 45 ASP -0.532 -15.088 -10.495 46 TYR 1.426 -14.870 -7.219 47 GLY 5.204 -15.365 -7.328 48 GLY 6.838 -17.505 -10.032 49 LYS 3.449 -19.144 -10.597 50 LYS 0.628 -18.046 -12.869 51 GLN -3.066 -18.311 -12.024 52 LEU -3.249 -20.686 -9.085 53 TRP -6.125 -20.586 -6.554 54 PHE -7.242 -18.602 -3.564 55 PRO -10.477 -18.832 -1.511 56 SER -13.206 -16.279 -1.863 57 ASN -13.412 -16.785 1.838 58 TYR -9.865 -15.616 2.332 59 VAL -9.259 -12.923 -0.334 60 GLU -11.079 -9.697 -1.139 61 GLU -10.798 -7.644 -4.350 62 MET -9.045 -4.632 -2.821 63 VAL -11.352 -3.225 -0.171 64 ASN -9.534 0.018 -0.717 65 PRO -10.412 1.903 -3.950 66 GLU -8.366 4.850 -5.153 67 GLY -5.141 4.419 -7.133 68 ILE -2.283 6.500 -8.574 69 HIS -0.391 6.146 -11.863 70 ARG 3.392 5.734 -12.018 71 ASP 5.340 7.194 -14.933 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 S/S S S S S S C T T 20 T T C S S S S S S S 30 S S S/S S S S S/T T T T/S 40 S S S S S T T T T S 50 S S S S S/T T T T/S S S 60 S C S S S S S S S S 70 S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S E E 10 e S S S S 20 S S t T T e E 30 E B S B T T e 40 E E B S S 50 S E E e T T t 60 S S 70 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLY 6.9 19.7 80.8 2 SER 34.3 41.1 61.3 3 PRO 62.5 50.2 73.8 4 THR 34.7 32.5 87.4 5 PHE 0.0 0.0 83.3 6 LYS 70.0 40.4 76.4 7 CYS 29.3 29.5 75.6 8 ALA 66.8 92.0 55.6 9 VAL 118.8 100.0 38.7 10 LYS 116.4 67.1 53.1 11 ALA 72.6 100.0 46.9 12 LEU 85.1 57.6 56.1 13 PHE 63.3 37.9 70.2 14 ASP 45.7 41.3 69.9 15 TYR 129.9 71.8 49.9 16 LYS 11.2 6.5 83.3 17 ALA 65.1 89.7 51.7 18 GLN 60.1 40.5 68.6 19 ARG 74.7 35.7 79.4 20 GLU 42.6 30.7 73.9 21 ASP 21.1 19.1 69.2 22 GLU 133.2 96.1 36.3 23 LEU 143.3 96.9 41.2 24 THR 64.6 60.5 53.5 25 PHE 163.6 98.1 31.4 26 ILE 53.0 36.9 80.9 27 LYS 46.2 26.6 75.0 28 SER 39.2 46.9 60.1 29 ALA 71.3 98.2 45.0 30 ILE 96.8 67.5 68.5 31 ILE 143.5 100.0 34.9 32 GLN 103.8 69.9 65.0 33 ASN 50.3 41.6 72.9 34 VAL 114.0 96.0 40.1 35 GLU 24.2 17.4 79.7 36 LYS 58.8 33.9 70.8 37 GLN 79.2 53.3 64.9 38 GLU 0.0 0.0 87.6 39 GLY 4.1 11.8 78.6 40 GLY 16.5 47.3 68.9 41 TRP 112.6 54.9 62.5 42 TRP 193.7 94.5 36.4 43 ARG 88.7 42.5 70.9 44 GLY 34.8 100.0 53.7 45 ASP 66.8 60.4 62.8 46 TYR 133.4 73.7 51.1 47 GLY 0.0 0.0 83.4 48 GLY 0.0 0.0 79.8 49 LYS 108.6 62.6 61.5 50 LYS 27.0 15.6 76.9 51 GLN 74.0 49.8 62.8 52 LEU 120.6 81.6 54.2 53 TRP 150.9 73.6 50.0 54 PHE 166.8 100.0 32.4 55 PRO 123.1 98.8 30.1 56 SER 60.9 72.8 59.4 57 ASN 15.1 12.5 77.3 58 TYR 106.5 58.9 54.6 59 VAL 118.8 100.0 31.7 60 GLU 66.7 48.1 54.2 61 GLU 49.6 35.8 66.2 62 MET 109.0 68.4 65.3 63 VAL 38.3 32.3 75.7 64 ASN 15.6 12.9 74.7 65 PRO 14.9 11.9 84.9 66 GLU 0.0 0.0 86.6 67 GLY 14.6 41.8 65.0 68 ILE 12.0 8.3 83.3 69 HIS 2.1 1.4 86.3 70 ARG 0.0 0.0 90.0 71 ASP 0.0 0.0 83.8