REMARK File generated by Swiss-PdbViewer 4.00b0 REMARK http://www.expasy.org/spdbv/ REMARK File generated by Swiss-PdbViewer 4.00b0 REMARK http://www.expasy.org/spdbv/ HEADER LYASE TITLE 3 SCHIFF BASE INTERMEDIATE COMPND MOL_ID: 1; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B KEYWDS ALIEN LYASE EXPDTA X-RAY DIFFRACTION AUTHOR MEB REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0019 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE REMARK 3 RIDING POSITIONS REMARK 4 REMARK 100 REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.7 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.59 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5M POTASSIUM PHOSHPATE DIBASIC/ REMARK 280 SODIUM PHOSPHATE MONOBASIC, PH 7.7, VAPOR DIFFUSION, HANGING REMARK 280 DROP, TEMPERATURE 281K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 X+2/3,Y+1/3,Z+1/3 REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3 REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3 REMARK 290 7555 X+1/3,Y+2/3,Z+2/3 REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3 REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 52.83050 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.50170 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 84.28467 REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 52.83050 REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 30.50170 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 84.28467 REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 52.83050 REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 30.50170 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 84.28467 REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 61.00341 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 168.56933 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 61.00341 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 168.56933 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 61.00341 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 168.56933 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 48390 ANGSTROM**2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 500 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PNH A 247 REMARK 900 DBREF XXXX A 1 246 UNP Q7NSA6 ADC_CHRVO 1 246 DBREF XXXX B 1 246 UNP Q7NSA6 ADC_CHRVO 1 246 CRYST1 105.661 105.661 252.854 90.00 90.00 120.00 H 3 36 ATOM 1 N PHE A 27 13.774 -31.230 -17.054 1.00 30.03 ATOM 2 CA PHE A 27 13.660 -30.543 -15.774 1.00 29.36 ATOM 3 C PHE A 27 15.041 -30.334 -15.133 1.00 29.34 ATOM 4 O PHE A 27 15.814 -31.281 -14.955 1.00 29.04 ATOM 5 CB PHE A 27 12.727 -31.310 -14.813 1.00 29.37 ATOM 6 CG PHE A 27 11.284 -31.301 -15.234 1.00 29.46 ATOM 7 CD1 PHE A 27 10.409 -30.318 -14.745 1.00 28.18 ATOM 8 CD2 PHE A 27 10.810 -32.229 -16.151 1.00 30.08 ATOM 9 CE1 PHE A 27 9.081 -30.265 -15.153 1.00 27.87 ATOM 10 CE2 PHE A 27 9.470 -32.190 -16.577 1.00 30.75 ATOM 11 CZ PHE A 27 8.601 -31.208 -16.076 1.00 29.24 ATOM 12 N ARG A 30 14.795 -29.681 -10.171 1.00 29.34 ATOM 13 CA ARG A 30 13.552 -30.108 -9.530 1.00 30.00 ATOM 14 C ARG A 30 13.837 -30.277 -8.033 1.00 30.52 ATOM 15 O ARG A 30 14.788 -30.957 -7.686 1.00 30.20 ATOM 16 CB ARG A 30 13.130 -31.436 -10.121 1.00 29.72 ATOM 17 CG ARG A 30 11.680 -31.547 -10.397 1.00 31.28 ATOM 18 CD ARG A 30 11.329 -32.932 -10.806 1.00 33.95 ATOM 19 NE ARG A 30 10.497 -32.913 -11.992 1.00 36.72 ATOM 20 CZ ARG A 30 9.262 -33.389 -12.071 1.00 35.95 ATOM 21 NH1 ARG A 30 8.687 -33.971 -11.040 1.00 38.00 ATOM 22 NH2 ARG A 30 8.611 -33.291 -13.212 1.00 39.12 ATOM 23 N GLU A 62 3.810 -35.172 -1.502 1.00 28.89 ATOM 24 CA GLU A 62 4.918 -34.450 -2.096 1.00 29.22 ATOM 25 C GLU A 62 4.640 -32.985 -2.352 1.00 28.48 ATOM 26 O GLU A 62 3.521 -32.586 -2.658 1.00 27.97 ATOM 27 CB GLU A 62 5.422 -35.137 -3.383 1.00 28.86 ATOM 28 CG GLU A 62 4.471 -35.060 -4.546 1.00 30.50 ATOM 29 CD GLU A 62 4.790 -36.018 -5.719 1.00 31.98 ATOM 30 OE1 GLU A 62 5.642 -36.931 -5.542 1.00 32.72 ATOM 31 OE2 GLU A 62 4.172 -35.819 -6.823 1.00 34.60 ATOM 32 N MET A 66 9.517 -26.824 -9.587 1.00 32.36 ATOM 33 CA MET A 66 10.076 -27.005 -10.936 1.00 34.53 ATOM 34 C MET A 66 10.407 -25.646 -11.580 1.00 33.55 ATOM 35 O MET A 66 9.687 -25.192 -12.477 1.00 34.51 ATOM 36 CB MET A 66 9.094 -27.764 -11.825 1.00 34.11 ATOM 37 CG MET A 66 9.071 -29.251 -11.558 1.00 37.38 ATOM 38 SD MET A 66 7.409 -29.908 -11.425 1.00 40.59 ATOM 39 CE MET A 66 6.876 -28.994 -10.014 1.00 39.13 ATOM 40 N TYR A 75 7.237 -23.487 -12.302 1.00 30.84 ATOM 41 CA TYR A 75 6.044 -23.759 -11.480 1.00 30.98 ATOM 42 C TYR A 75 6.285 -24.684 -10.275 1.00 31.53 ATOM 43 O TYR A 75 7.421 -25.093 -9.994 1.00 32.19 ATOM 44 CB TYR A 75 4.891 -24.289 -12.352 1.00 30.29 ATOM 45 CG TYR A 75 5.154 -25.637 -12.987 1.00 30.39 ATOM 46 CD1 TYR A 75 4.607 -26.812 -12.436 1.00 27.59 ATOM 47 CD2 TYR A 75 5.981 -25.756 -14.138 1.00 31.17 ATOM 48 CE1 TYR A 75 4.845 -28.071 -13.029 1.00 28.57 ATOM 49 CE2 TYR A 75 6.233 -27.025 -14.735 1.00 30.35 ATOM 50 CZ TYR A 75 5.655 -28.175 -14.172 1.00 30.37 ATOM 51 OH TYR A 75 5.884 -29.421 -14.744 1.00 29.23 ATOM 52 N GLU A 77 4.273 -27.857 -7.631 1.00 31.66 ATOM 53 CA GLU A 77 3.333 -28.975 -7.655 1.00 31.61 ATOM 54 C GLU A 77 3.182 -29.480 -6.224 1.00 31.17 ATOM 55 O GLU A 77 4.107 -29.401 -5.432 1.00 31.53 ATOM 56 CB GLU A 77 3.874 -30.092 -8.585 1.00 31.60 ATOM 57 CG GLU A 77 2.990 -31.369 -8.773 1.00 33.54 ATOM 58 CD GLU A 77 3.309 -32.535 -7.786 1.00 39.70 ATOM 59 OE1 GLU A 77 4.024 -32.329 -6.774 1.00 44.87 ATOM 60 OE2 GLU A 77 2.836 -33.672 -8.007 1.00 41.50 ATOM 61 N MET A 97 -2.972 -34.285 -7.882 1.00 27.14 ATOM 62 CA MET A 97 -1.870 -33.364 -8.143 1.00 27.94 ATOM 63 C MET A 97 -2.448 -31.988 -8.342 1.00 27.06 ATOM 64 O MET A 97 -3.531 -31.854 -8.893 1.00 26.52 ATOM 65 CB MET A 97 -1.163 -33.698 -9.458 1.00 27.94 ATOM 66 CG MET A 97 -0.124 -34.756 -9.389 1.00 30.72 ATOM 67 SD MET A 97 0.754 -34.844 -10.981 1.00 31.39 ATOM 68 CE MET A 97 2.255 -35.662 -10.464 1.00 30.18 ATOM 69 N LEU A 99 -1.239 -27.819 -9.392 1.00 28.52 ATOM 70 CA LEU A 99 -0.202 -27.083 -10.131 1.00 29.96 ATOM 71 C LEU A 99 -0.600 -25.618 -10.233 1.00 30.57 ATOM 72 O LEU A 99 -1.794 -25.303 -10.252 1.00 30.57 ATOM 73 CB LEU A 99 -0.079 -27.667 -11.562 1.00 29.95 ATOM 74 CG LEU A 99 1.175 -28.464 -11.986 1.00 32.60 ATOM 75 CD1 LEU A 99 1.422 -29.745 -11.217 1.00 33.61 ATOM 76 CD2 LEU A 99 1.167 -28.790 -13.473 1.00 31.45 ATOM 77 N PRO A 104 1.712 -26.944 -18.203 1.00 30.70 ATOM 78 CA PRO A 104 1.937 -28.301 -17.641 1.00 29.99 ATOM 79 C PRO A 104 0.665 -28.955 -17.059 1.00 29.01 ATOM 80 O PRO A 104 0.619 -30.177 -16.905 1.00 28.88 ATOM 81 CB PRO A 104 2.977 -28.060 -16.547 1.00 29.39 ATOM 82 CG PRO A 104 2.755 -26.645 -16.123 1.00 30.29 ATOM 83 CD PRO A 104 2.348 -25.902 -17.366 1.00 30.72 ATOM 84 N GLY A 108 -0.028 -32.157 -18.841 1.00 22.77 ATOM 85 CA GLY A 108 -0.036 -33.348 -18.020 1.00 23.31 ATOM 86 C GLY A 108 -1.296 -34.179 -18.155 1.00 23.07 ATOM 87 O GLY A 108 -1.214 -35.401 -18.261 1.00 22.36 ATOM 88 N PHE A 124 -2.054 -37.317 -16.123 1.00 24.65 ATOM 89 CA PHE A 124 -1.846 -36.881 -14.753 1.00 24.15 ATOM 90 C PHE A 124 -3.174 -36.293 -14.254 1.00 24.55 ATOM 91 O PHE A 124 -3.811 -35.510 -14.959 1.00 26.12 ATOM 92 CB PHE A 124 -0.745 -35.826 -14.635 1.00 22.64 ATOM 93 CG PHE A 124 0.662 -36.361 -14.722 1.00 21.06 ATOM 94 CD1 PHE A 124 1.270 -36.984 -13.628 1.00 18.47 ATOM 95 CD2 PHE A 124 1.415 -36.155 -15.875 1.00 23.18 ATOM 96 CE1 PHE A 124 2.602 -37.444 -13.711 1.00 19.54 ATOM 97 CE2 PHE A 124 2.730 -36.607 -15.973 1.00 23.53 ATOM 98 CZ PHE A 124 3.326 -37.251 -14.873 1.00 20.79 ATOM 99 N ALA A 125 -3.574 -36.624 -13.055 1.00 24.73 ATOM 100 CA ALA A 125 -4.823 -36.150 -12.487 1.00 24.30 ATOM 101 C ALA A 125 -4.771 -34.714 -11.927 1.00 24.24 ATOM 102 O ALA A 125 -4.955 -34.498 -10.788 1.00 24.63 ATOM 103 CB ALA A 125 -5.028 -37.149 -11.377 1.00 23.94 ATOM 104 N LYS A 126 -4.505 -33.751 -12.763 1.00 20.03 ATOM 105 CA LYS A 126 -4.096 -32.449 -12.280 1.00 20.20 ATOM 106 C LYS A 126 -5.269 -31.503 -12.120 1.00 20.38 ATOM 107 O LYS A 126 -6.145 -31.487 -12.932 1.00 20.24 ATOM 108 CB LYS A 126 -3.015 -31.850 -13.184 1.00 19.86 ATOM 109 CG LYS A 126 -1.622 -32.362 -12.966 1.00 19.78 ATOM 110 CD LYS A 126 -0.708 -32.118 -14.103 1.00 20.53 ATOM 111 CE LYS A 126 0.730 -32.347 -13.780 1.00 25.49 ATOM 112 NZ LYS A 126 1.743 -32.201 -14.847 1.00 28.92 ATOM 113 N LYS A 127 -5.253 -30.752 -11.034 1.00 27.47 ATOM 114 CA LYS A 127 -6.098 -29.592 -10.809 1.00 27.29 ATOM 115 C LYS A 127 -5.246 -28.348 -10.490 1.00 27.77 ATOM 116 O LYS A 127 -4.059 -28.450 -10.339 1.00 27.80 ATOM 117 CB LYS A 127 -7.107 -29.880 -9.712 1.00 26.98 ATOM 118 CG LYS A 127 -8.089 -30.939 -9.986 1.00 24.43 ATOM 119 CD LYS A 127 -8.607 -31.510 -8.739 1.00 26.78 ATOM 120 CE LYS A 127 -9.861 -32.239 -8.954 1.00 24.96 ATOM 121 NZ LYS A 127 -10.292 -32.855 -7.756 1.00 24.75 ATOM 122 N LEU A 211 -13.390 -30.311 -3.161 1.00 34.12 ATOM 123 CA LEU A 211 -12.849 -30.433 -4.525 1.00 33.39 ATOM 124 C LEU A 211 -11.369 -30.841 -4.595 1.00 32.21 ATOM 125 O LEU A 211 -10.830 -31.021 -5.671 1.00 32.16 ATOM 126 CB LEU A 211 -13.065 -29.105 -5.271 1.00 33.37 ATOM 127 CG LEU A 211 -14.383 -28.876 -6.026 1.00 33.65 ATOM 128 CD1 LEU A 211 -15.608 -29.585 -5.455 1.00 33.25 ATOM 129 CD2 LEU A 211 -14.653 -27.398 -6.265 1.00 33.76 ATOM 130 N LEU A 234 11.090 -36.185 -18.026 1.00 29.32 ATOM 131 CA LEU A 234 9.799 -36.871 -17.971 1.00 29.80 ATOM 132 C LEU A 234 9.542 -37.498 -19.332 1.00 30.27 ATOM 133 O LEU A 234 9.182 -36.780 -20.275 1.00 30.12 ATOM 134 CB LEU A 234 8.699 -35.857 -17.702 1.00 29.62 ATOM 135 CG LEU A 234 7.463 -36.154 -16.858 1.00 29.20 ATOM 136 CD1 LEU A 234 6.410 -35.030 -17.019 1.00 26.02 ATOM 137 CD2 LEU A 234 6.898 -37.418 -17.200 1.00 27.05 ATOM 138 N SER B 17 -12.542 -37.923 -8.028 1.00 30.80 ATOM 139 CA SER B 17 -12.866 -36.541 -7.687 1.00 30.12 ATOM 140 C SER B 17 -12.660 -35.685 -8.937 1.00 28.89 ATOM 141 O SER B 17 -11.726 -34.894 -8.998 1.00 27.85 ATOM 142 CB SER B 17 -11.976 -36.078 -6.532 1.00 29.61 ATOM 143 OG SER B 17 -12.219 -34.734 -6.200 1.00 32.81 HETATM 144 C1 D A 247 3.804 -31.954 -16.146 1.00 37.46 HETATM 145 C3 D A 247 3.451 -33.326 -13.883 1.00 41.32 HETATM 146 C4 D A 247 4.851 -33.187 -13.339 1.00 46.98 HETATM 147 O6 D A 247 5.603 -32.334 -13.787 1.00 49.72 HETATM 148 N D A 247 5.268 -34.150 -12.245 1.00 48.07 HETATM 149 C2 D A 247 2.982 -32.335 -14.932 1.00 35.90 CONECT 144 149 CONECT 145 146 149 CONECT 146 147 148 CONECT 149 112 SPDBVT 1.0000000000 0.0000000000 0.0000000000 SPDBVT 0.0000000000 1.0000000000 0.0000000000 SPDBVT 0.0000000000 0.0000000000 1.0000000000 SPDBVT 0.0000000000 0.0000000000 0.0000000000 SPDBVT 0.0000000000 0.0000000000 0.0000000000 SPDBVV default; SPDBVV 50.327543725854 3969.897273732397 20.000000000000 SPDBVV -0.9847823233 -0.0296702206 0.1712409231 SPDBVV -0.1480689309 -0.3726356931 -0.9160885503 SPDBVV 0.0909910295 -0.9275032713 0.3625718057 SPDBVV 0.1030000001 -30.7049999237 -10.8885002136 SPDBVV 0.0000000000 0.0000000000 0.0000000000 SPDBVf 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 SPDBVo 144d d SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVb 0.00 0.00 0.00 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 SPDBVi 1 1 1 0 1 0 1 1 0 1 0 1 1 0 0 SPDBVp 243365 END