HEADER ALKALINE PHOSPHATASE 03-MAR-93 1ALK 1ALK 2 COMPND ALKALINE PHOSPHATASE (E.C.3.1.3.1) 1ALK 3 SOURCE (ESCHERICHIA COLI) 1ALK 4 AUTHOR E.E.KIM,W.WYCKOFF 1ALK 5 REVDAT 1 31-JAN-94 1ALK 0 1ALK 6 REMARK 1 1ALK 7 REMARK 1 REFERENCE 1 1ALK 8 REMARK 1 AUTH E.E.KIM,H.W.WYCKOFF 1ALK 9 REMARK 1 TITL REACTION MECHANISM OF ALKALINE PHOSPHATASE BASED 1ALK 10 REMARK 1 TITL 2 ON CRYSTAL STRUCTURES. TWO METAL ION CATALYSIS 1ALK 11 REMARK 1 REF J.MOL.BIOL. V. 218 449 1991 1ALK 12 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1ALK 13 REMARK 1 REFERENCE 2 1ALK 14 REMARK 1 AUTH F.M.HULETT,E.E.KIM,C.BOOKSTEIN,N.V.KAPP, 1ALK 15 REMARK 1 AUTH 2 C.W.EDWARDS,H.W.WYCKOFF 1ALK 16 REMARK 1 TITL BACILLUS SUBTILIS ALKALINE PHOSPHATASES III AND IV. 1ALK 17 REMARK 1 TITL 2 CLONING, SEQUENCING, AND COMPARISONS OF DEDUCED 1ALK 18 REMARK 1 TITL 3 AMINO ACID SEQUENCE WITH ESCHERICHIA COLI ALKALINE 1ALK 19 REMARK 1 TITL 4 PHOSPHATASE THREE-DIMENSIONAL STRUCTURE 1ALK 20 REMARK 1 REF J.BIOL.CHEM. V. 266 1077 1991 1ALK 21 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 1ALK 22 REMARK 1 REFERENCE 3 1ALK 23 REMARK 1 AUTH E.E.KIM,H.W.WYCKOFF 1ALK 24 REMARK 1 TITL STRUCTURE OF ALKALINE PHOSPHATASES 1ALK 25 REMARK 1 REF CLIN.CHIM.ACTA V. 186 175 1989 1ALK 26 REMARK 1 REFN ASTM CCATAR NE ISSN 0009-8981 769 1ALK 27 REMARK 1 REFERENCE 4 1ALK 28 REMARK 1 AUTH J.M.SOWADSKI,M.D.HANDSCHUMACHER,H.M.K.MURTHY, 1ALK 29 REMARK 1 AUTH 2 B.A.FOSTER,H.W.WYCKOFF 1ALK 30 REMARK 1 TITL REFINED STRUCTURE OF ALKALINE PHOSPHATASE 1ALK 31 REMARK 1 REF J.MOL.BIOL. V. 186 417 1985 1ALK 32 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1ALK 33 REMARK 2 1ALK 34 REMARK 2 RESOLUTION. 2.0 ANGSTROMS. 1ALK 35 REMARK 3 1ALK 36 REMARK 3 REFINEMENT. 1ALK 37 REMARK 3 PROGRAM 1 X-PLOR 1ALK 38 REMARK 3 AUTHORS 1 BRUNGER 1ALK 39 REMARK 3 PROGRAM 2 PROFFT 1ALK 40 REMARK 3 AUTHORS 2 KONNERT,HENDRICKSON,FINZEL 1ALK 41 REMARK 3 R VALUE 0.177 1ALK 42 REMARK 3 1ALK 43 REMARK 3 NUMBER OF PROTEIN ATOMS 6608 1ALK 44 REMARK 3 NUMBER OF SOLVENT ATOMS 6 1ALK 45 REMARK 4 1ALK 46 REMARK 4 THE STRUCTURE IS OF THE NATIVE ENZYME, I.E. TWO ZN AND ONE 1ALK 47 REMARK 4 MG AT THE ACTIVE SITE, COMPLEXED WITH AN INORGANIC 1ALK 48 REMARK 4 PHOSPHATE BOUND IN EACH OF THE TWO ACTIVE SITES. PHOSPHATE 1ALK 49 REMARK 4 IS A STRONG COMPETITIVE INHIBITOR OF THE ENZYME. 1ALK 50 REMARK 5 1ALK 51 REMARK 5 THERE IS A DIMER (IDENTICAL CHAIN OF 449 RESIDUES) PER 1ALK 52 REMARK 5 ASYMMETRIC UNIT AND THEY ARE REFINED INDEPENDENTLY. 1ALK 53 REMARK 6 1ALK 54 REMARK 6 THERE ARE THREE WATER MOLECULES COORDINATING TO THE THIRD 1ALK 55 REMARK 6 METAL, NAMELY MG (RESIDUE NUMBER 452 ), AND THESE ARE 1ALK 56 REMARK 6 NUMBERED 454 - 456. 1ALK 57 REMARK 7 1ALK 58 REMARK 7 SEQUENCE ADVISORY NOTICE: 1ALK 59 REMARK 7 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. 1ALK 60 REMARK 7 1ALK 61 REMARK 7 SWISS-PROT ENTRY NAME: PPB_ECOLI 1ALK 62 REMARK 7 1ALK 63 REMARK 7 SWISS-PROT RESIDUE PDB SEQRES 1ALK 64 REMARK 7 NAME NUMBER NAME CHAIN SEQ/INSERT CODE 1ALK 65 REMARK 7 ASP 37 ASN 15 1ALK 66 REMARK 7 ASP 57 ASN 35 1ALK 67 REMARK 7 LYS 198 GLN 176 1ALK 68 REMARK 7 LYS 250 GLU 228 1ALK 69 REMARK 7 LYS 252 GLU 230 1ALK 70 SEQRES 1 A 449 THR PRO GLU MET PRO VAL LEU GLU ASN ARG ALA ALA GLN 1ALK 71 SEQRES 2 A 449 GLY ASN ILE THR ALA PRO GLY GLY ALA ARG ARG LEU THR 1ALK 72 SEQRES 3 A 449 GLY ASP GLN THR ALA ALA LEU ARG ASN SER LEU SER ASP 1ALK 73 SEQRES 4 A 449 LYS PRO ALA LYS ASN ILE ILE LEU LEU ILE GLY ASP GLY 1ALK 74 SEQRES 5 A 449 MET GLY ASP SER GLU ILE THR ALA ALA ARG ASN TYR ALA 1ALK 75 SEQRES 6 A 449 GLU GLY ALA GLY GLY PHE PHE LYS GLY ILE ASP ALA LEU 1ALK 76 SEQRES 7 A 449 PRO LEU THR GLY GLN TYR THR HIS TYR ALA LEU ASN LYS 1ALK 77 SEQRES 8 A 449 LYS THR GLY LYS PRO ASP TYR VAL THR ASP SER ALA ALA 1ALK 78 SEQRES 9 A 449 SER ALA THR ALA TRP SER THR GLY VAL LYS THR TYR ASN 1ALK 79 SEQRES 10 A 449 GLY ALA LEU GLY VAL ASP ILE HIS GLU LYS ASP HIS PRO 1ALK 80 SEQRES 11 A 449 THR ILE LEU GLU MET ALA LYS ALA ALA GLY LEU ALA THR 1ALK 81 SEQRES 12 A 449 GLY ASN VAL SER THR ALA GLU LEU GLN ASP ALA THR PRO 1ALK 82 SEQRES 13 A 449 ALA ALA LEU VAL ALA HIS VAL THR SER ARG LYS CYS TYR 1ALK 83 SEQRES 14 A 449 GLY PRO SER ALA THR SER GLN LYS CYS PRO GLY ASN ALA 1ALK 84 SEQRES 15 A 449 LEU GLU LYS GLY GLY LYS GLY SER ILE THR GLU GLN LEU 1ALK 85 SEQRES 16 A 449 LEU ASN ALA ARG ALA ASP VAL THR LEU GLY GLY GLY ALA 1ALK 86 SEQRES 17 A 449 LYS THR PHE ALA GLU THR ALA THR ALA GLY GLU TRP GLN 1ALK 87 SEQRES 18 A 449 GLY LYS THR LEU ARG GLU GLU ALA GLU ALA ARG GLY TYR 1ALK 88 SEQRES 19 A 449 GLN LEU VAL SER ASP ALA ALA SER LEU ASN SER VAL THR 1ALK 89 SEQRES 20 A 449 GLU ALA ASN GLN GLN LYS PRO LEU LEU GLY LEU PHE ALA 1ALK 90 SEQRES 21 A 449 ASP GLY ASN MET PRO VAL ARG TRP LEU GLY PRO LYS ALA 1ALK 91 SEQRES 22 A 449 THR TYR HIS GLY ASN ILE ASP LYS PRO ALA VAL THR CYS 1ALK 92 SEQRES 23 A 449 THR PRO ASN PRO GLN ARG ASN ASP SER VAL PRO THR LEU 1ALK 93 SEQRES 24 A 449 ALA GLN MET THR ASP LYS ALA ILE GLU LEU LEU SER LYS 1ALK 94 SEQRES 25 A 449 ASN GLU LYS GLY PHE PHE LEU GLN VAL GLU GLY ALA SER 1ALK 95 SEQRES 26 A 449 ILE ASP LYS GLN ASP HIS ALA ALA ASN PRO CYS GLY GLN 1ALK 96 SEQRES 27 A 449 ILE GLY GLU THR VAL ASP LEU ASP GLU ALA VAL GLN ARG 1ALK 97 SEQRES 28 A 449 ALA LEU GLU PHE ALA LYS LYS GLU GLY ASN THR LEU VAL 1ALK 98 SEQRES 29 A 449 ILE VAL THR ALA ASP HIS ALA HIS ALA SER GLN ILE VAL 1ALK 99 SEQRES 30 A 449 ALA PRO ASP THR LYS ALA PRO GLY LEU THR GLN ALA LEU 1ALK 100 SEQRES 31 A 449 ASN THR LYS ASP GLY ALA VAL MET VAL MET SER TYR GLY 1ALK 101 SEQRES 32 A 449 ASN SER GLU GLU ASP SER GLN GLU HIS THR GLY SER GLN 1ALK 102 SEQRES 33 A 449 LEU ARG ILE ALA ALA TYR GLY PRO HIS ALA ALA ASN VAL 1ALK 103 SEQRES 34 A 449 VAL GLY LEU THR ASP GLN THR ASP LEU PHE TYR THR MET 1ALK 104 SEQRES 35 A 449 LYS ALA ALA LEU GLY LEU LYS 1ALK 105 SEQRES 1 B 449 THR PRO GLU MET PRO VAL LEU GLU ASN ARG ALA ALA GLN 1ALK 106 SEQRES 2 B 449 GLY ASN ILE THR ALA PRO GLY GLY ALA ARG ARG LEU THR 1ALK 107 SEQRES 3 B 449 GLY ASP GLN THR ALA ALA LEU ARG ASN SER LEU SER ASP 1ALK 108 SEQRES 4 B 449 LYS PRO ALA LYS ASN ILE ILE LEU LEU ILE GLY ASP GLY 1ALK 109 SEQRES 5 B 449 MET GLY ASP SER GLU ILE THR ALA ALA ARG ASN TYR ALA 1ALK 110 SEQRES 6 B 449 GLU GLY ALA GLY GLY PHE PHE LYS GLY ILE ASP ALA LEU 1ALK 111 SEQRES 7 B 449 PRO LEU THR GLY GLN TYR THR HIS TYR ALA LEU ASN LYS 1ALK 112 SEQRES 8 B 449 LYS THR GLY LYS PRO ASP TYR VAL THR ASP SER ALA ALA 1ALK 113 SEQRES 9 B 449 SER ALA THR ALA TRP SER THR GLY VAL LYS THR TYR ASN 1ALK 114 SEQRES 10 B 449 GLY ALA LEU GLY VAL ASP ILE HIS GLU LYS ASP HIS PRO 1ALK 115 SEQRES 11 B 449 THR ILE LEU GLU MET ALA LYS ALA ALA GLY LEU ALA THR 1ALK 116 SEQRES 12 B 449 GLY ASN VAL SER THR ALA GLU LEU GLN ASP ALA THR PRO 1ALK 117 SEQRES 13 B 449 ALA ALA LEU VAL ALA HIS VAL THR SER ARG LYS CYS TYR 1ALK 118 SEQRES 14 B 449 GLY PRO SER ALA THR SER GLN LYS CYS PRO GLY ASN ALA 1ALK 119 SEQRES 15 B 449 LEU GLU LYS GLY GLY LYS GLY SER ILE THR GLU GLN LEU 1ALK 120 SEQRES 16 B 449 LEU ASN ALA ARG ALA ASP VAL THR LEU GLY GLY GLY ALA 1ALK 121 SEQRES 17 B 449 LYS THR PHE ALA GLU THR ALA THR ALA GLY GLU TRP GLN 1ALK 122 SEQRES 18 B 449 GLY LYS THR LEU ARG GLU GLU ALA GLU ALA ARG GLY TYR 1ALK 123 SEQRES 19 B 449 GLN LEU VAL SER ASP ALA ALA SER LEU ASN SER VAL THR 1ALK 124 SEQRES 20 B 449 GLU ALA ASN GLN GLN LYS PRO LEU LEU GLY LEU PHE ALA 1ALK 125 SEQRES 21 B 449 ASP GLY ASN MET PRO VAL ARG TRP LEU GLY PRO LYS ALA 1ALK 126 SEQRES 22 B 449 THR TYR HIS GLY ASN ILE ASP LYS PRO ALA VAL THR CYS 1ALK 127 SEQRES 23 B 449 THR PRO ASN PRO GLN ARG ASN ASP SER VAL PRO THR LEU 1ALK 128 SEQRES 24 B 449 ALA GLN MET THR ASP LYS ALA ILE GLU LEU LEU SER LYS 1ALK 129 SEQRES 25 B 449 ASN GLU LYS GLY PHE PHE LEU GLN VAL GLU GLY ALA SER 1ALK 130 SEQRES 26 B 449 ILE ASP LYS GLN ASP HIS ALA ALA ASN PRO CYS GLY GLN 1ALK 131 SEQRES 27 B 449 ILE GLY GLU THR VAL ASP LEU ASP GLU ALA VAL GLN ARG 1ALK 132 SEQRES 28 B 449 ALA LEU GLU PHE ALA LYS LYS GLU GLY ASN THR LEU VAL 1ALK 133 SEQRES 29 B 449 ILE VAL THR ALA ASP HIS ALA HIS ALA SER GLN ILE VAL 1ALK 134 SEQRES 30 B 449 ALA PRO ASP THR LYS ALA PRO GLY LEU THR GLN ALA LEU 1ALK 135 SEQRES 31 B 449 ASN THR LYS ASP GLY ALA VAL MET VAL MET SER TYR GLY 1ALK 136 SEQRES 32 B 449 ASN SER GLU GLU ASP SER GLN GLU HIS THR GLY SER GLN 1ALK 137 SEQRES 33 B 449 LEU ARG ILE ALA ALA TYR GLY PRO HIS ALA ALA ASN VAL 1ALK 138 SEQRES 34 B 449 VAL GLY LEU THR ASP GLN THR ASP LEU PHE TYR THR MET 1ALK 139 SEQRES 35 B 449 LYS ALA ALA LEU GLY LEU LYS 1ALK 140 FTNOTE 1 1ALK 141 FTNOTE 1 RESIDUES 1-4 AND 404-409 ARE NOT WELL DEFINED IN THE 1ALK 142 FTNOTE 1 ELECTRON DENSITY MAPS. 1ALK 143 HET ZN A 450 1 ZINC 1ALK 144 HET ZN A 451 1 ZINC 1ALK 145 HET MG A 452 1 MAGNESIUM ++ 1ALK 146 HET PO4 A 453 5 PHOSPHATE GROUP 1ALK 147 HET ZN B 450 1 ZINC 1ALK 148 HET ZN B 451 1 ZINC 1ALK 149 HET MG B 452 1 MAGNESIUM ++ 1ALK 150 HET PO4 B 453 5 PHOSPHATE GROUP 1ALK 151 FORMUL 3 ZN 4(ZN1 ++) 1ALK 152 FORMUL 4 MG 2(MG1) 1ALK 153 FORMUL 5 PO4 2(O4 P1) 1ALK 154 FORMUL 6 HOH *6(H2 O1) 1ALK 155 HELIX 1 H1 GLN A 29 LEU A 37 1 1ALK 156 HELIX 2 H2 GLY A 54 GLU A 66 1 1ALK 157 HELIX 3 H3 PHE A 72 LEU A 78 1 1ALK 158 HELIX 4 H4 ASP A 101 GLY A 112 1 1ALK 159 HELIX 5 H5 THR A 131 GLY A 140 1 1ALK 160 HELIX 6 H6 ASP A 153 VAL A 160 1 1ALK 161 HELIX 7 H7 GLY A 170 LYS A 177 1 1ALK 162 HELIX 8 H8 SER A 190 ARG A 199 1 1ALK 163 HELIX 9 H9 GLY A 207 GLU A 213 1 1ALK 164 HELIX 10 H10 THR A 224 GLY A 233 1 1ALK 165 HELIX 11 H11 ASP A 239 VAL A 246 1 1ALK 166 HELIX 12 H12 HIS A 276 LYS A 281 1 1ALK 167 HELIX 13 H13 THR A 298 ASN A 313 1 1ALK 168 HELIX 14 H14 SER A 325 ALA A 333 1 1ALK 169 HELIX 15 H15 ASN A 334 GLY A 360 1 1ALK 170 HELIX 16 H16 ASP A 434 GLY A 447 1 1ALK 171 HELIX 17 G1 GLN B 29 LEU B 37 1 1ALK 172 HELIX 18 G2 GLY B 54 GLU B 66 1 1ALK 173 HELIX 19 G3 PHE B 72 LEU B 78 1 1ALK 174 HELIX 20 G4 ASP B 101 GLY B 112 1 1ALK 175 HELIX 21 G5 THR B 131 GLY B 140 1 1ALK 176 HELIX 22 G6 ASP B 153 VAL B 160 1 1ALK 177 HELIX 23 G7 GLY B 170 LYS B 177 1 1ALK 178 HELIX 24 G8 SER B 190 ARG B 199 1 1ALK 179 HELIX 25 G9 GLY B 207 GLU B 213 1 1ALK 180 HELIX 26 G10 THR B 224 GLY B 233 1 1ALK 181 HELIX 27 G11 ASP B 239 VAL B 246 1 1ALK 182 HELIX 28 G12 HIS B 276 LYS B 281 1 1ALK 183 HELIX 29 G13 THR B 298 ASN B 313 1 1ALK 184 HELIX 30 G14 SER B 325 ALA B 333 1 1ALK 185 HELIX 31 G15 ASN B 334 GLY B 360 1 1ALK 186 HELIX 32 G16 ASP B 434 GLY B 447 1 1ALK 187 SHEET 1 S1A10 ASN A 44 GLY A 50 0 1ALK 188 SHEET 2 S1A10 LEU A 80 THR A 85 1 1ALK 189 SHEET 3 S1A10 ALA A 142 THR A 148 1 1ALK 190 SHEET 4 S1A10 ASP A 201 GLY A 205 1 1ALK 191 SHEET 5 S1A10 GLN A 235 VAL A 237 1 1ALK 192 SHEET 6 S1A10 PRO A 254 PHE A 259 1 1ALK 193 SHEET 7 S1A10 GLY A 316 GLY A 323 1 1ALK 194 SHEET 8 S1A10 ASN A 361 THR A 367 1 1ALK 195 SHEET 9 S1A10 LEU A 417 TYR A 422 -1 1ALK 196 SHEET 10 S1A10 GLY A 431 ASP A 434 1 1ALK 197 SHEET 1 S2A 3 GLN A 375 VAL A 377 0 1ALK 198 SHEET 2 S2A 3 LEU A 386 ASN A 391 1 1ALK 199 SHEET 3 S2A 3 VAL A 397 TYR A 402 -1 1ALK 200 SHEET 1 S1B10 ASN B 44 GLY B 50 0 1ALK 201 SHEET 2 S1B10 LEU B 80 THR B 85 1 1ALK 202 SHEET 3 S1B10 ALA B 142 THR B 148 1 1ALK 203 SHEET 4 S1B10 ASP B 201 GLY B 205 1 1ALK 204 SHEET 5 S1B10 GLN B 235 VAL B 237 1 1ALK 205 SHEET 6 S1B10 PRO B 254 PHE B 259 1 1ALK 206 SHEET 7 S1B10 GLY B 316 GLY B 323 1 1ALK 207 SHEET 8 S1B10 ASN B 361 THR B 367 1 1ALK 208 SHEET 9 S1B10 LEU B 417 TYR B 422 -1 1ALK 209 SHEET 10 S1B10 GLY B 431 ASP B 434 1 1ALK 210 SHEET 1 S2B 3 GLN B 375 VAL B 377 0 1ALK 211 SHEET 2 S2B 3 LEU B 386 ASN B 391 1 1ALK 212 SHEET 3 S2B 3 VAL B 397 TYR B 402 -1 1ALK 213 SSBOND 1 CYS A 168 CYS A 178 1ALK 214 SSBOND 2 CYS A 286 CYS A 336 1ALK 215 SSBOND 3 CYS B 168 CYS B 178 1ALK 216 SSBOND 4 CYS B 286 CYS B 336 1ALK 217 CRYST1 195.300 167.400 76.700 90.00 90.00 90.00 I 2 2 2 16 1ALK 218 ORIGX1 1.000000 0.000000 0.000000 0.00000 1ALK 219 ORIGX2 0.000000 1.000000 0.000000 0.00000 1ALK 220 ORIGX3 0.000000 0.000000 1.000000 0.00000 1ALK 221 SCALE1 0.005120 0.000000 0.000000 0.00000 1ALK 222 SCALE2 0.000000 0.005974 0.000000 0.00000 1ALK 223 SCALE3 0.000000 0.000000 0.013038 0.00000 1ALK 224