HEADER OXIDOREDUCTASE 06-JUL-94 1PBE 1PBE 2 COMPND P-HYDROXYBENZOATE HYDROXYLASE (PHBH) (E.C.1.14.13.2) 1PBE 3 COMPND 2 COMPLEXED WITH P-HYDROXYBENZOIC ACID 1PBE 4 SOURCE (PSEUDOMONAS FLUORESCENS) 1PBE 5 AUTHOR H.A.SCHREUDER,W.G.J.HOL,J.DRENTH 1PBE 6 REVDAT 1 30-SEP-94 1PBE 0 1PBE 7 JRNL AUTH H.A.SCHREUDER,P.A.J.PRICK,R.K.WIERENGA,G.VRIEND, 1PBE 8 JRNL AUTH 2 K.S.WILSON,W.G.J.HOL,J.DRENTH 1PBE 9 JRNL TITL CRYSTAL STRUCTURE OF THE P-HYDROXYBENZOATE 1PBE 10 JRNL TITL 2 HYDROXYLASE-SUBSTRATE COMPLEX REFINED AT 1.9 1PBE 11 JRNL TITL 3 ANGSTROMS RESOLUTION. ANALYSIS OF THE 1PBE 12 JRNL TITL 4 ENZYME-SUBSTRATE AND ENZYME-PRODUCT COMPLEXES 1PBE 13 JRNL REF J.MOL.BIOL. V. 208 679 1989 1PBE 14 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 0070 1PBE 15 REMARK 1 1PBE 16 REMARK 1 REFERENCE 1 1PBE 17 REMARK 1 AUTH H.A.SCHREUDER,J.M.VAN DER LAAN,M.B.A.SWARTE, 1PBE 18 REMARK 1 AUTH 2 K.H.KALK,W.G.J.HOL,J.DRENTH 1PBE 19 REMARK 1 TITL CRYSTAL STRUCTURE OF THE REDUCED FORM OF 1PBE 20 REMARK 1 TITL 2 P-HYDROXYBENZOATE HYDROXYLASE REFINED AT 2.3 1PBE 21 REMARK 1 TITL 3 ANGSTROMS RESOLUTION 1PBE 22 REMARK 1 REF PROTEINS.STRUCT.,FUNCT., V. 14 178 1992 1PBE 23 REMARK 1 REF 2 GENET. 1PBE 24 REMARK 1 REFN ASTM PSFGEY US ISSN 0887-3585 0867 1PBE 25 REMARK 1 REFERENCE 2 1PBE 26 REMARK 1 AUTH J.M.VAN DER LAAN,M.B.A.SWARTE,H.GROENDIJK, 1PBE 27 REMARK 1 AUTH 2 W.G.J.HOL,J.DRENTH 1PBE 28 REMARK 1 TITL THE INFLUENCE OF PURIFICATION AND PROTEIN 1PBE 29 REMARK 1 TITL 2 HETEROGENEITY ON THE CRYSTALLIZATION OF 1PBE 30 REMARK 1 TITL 3 P-HYDROXYBENZOATE HYDROXYLASE 1PBE 31 REMARK 1 REF EUR.J.BIOCHEM. V. 179 715 1989 1PBE 32 REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 0262 1PBE 33 REMARK 1 REFERENCE 3 1PBE 34 REMARK 1 AUTH J.M.VAN DER LAAN,H.A.SCHREUDER,M.B.A.SWARTE, 1PBE 35 REMARK 1 AUTH 2 R.K.WIERENGA,K.H.KALK,W.G.J.HOL,J.DRENTH 1PBE 36 REMARK 1 TITL THE COENZYME ANALOGUE ADENOSINE 5-DIPHOSPHORIBOSE 1PBE 37 REMARK 1 TITL 2 DISPLACES FAD IN THE ACTIVE SITE OF 1PBE 38 REMARK 1 TITL 3 P-HYDROXYBENZOATE HYDROXYLASE. AN X-RAY 1PBE 39 REMARK 1 TITL 4 CRYSTALLOGRAPHIC INVESTIGATION 1PBE 40 REMARK 1 REF BIOCHEMISTRY V. 28 7199 1989 1PBE 41 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 0033 1PBE 42 REMARK 1 REFERENCE 4 1PBE 43 REMARK 1 AUTH H.A.SCHREUDER,W.G.J.HOL,J.DRENTH 1PBE 44 REMARK 1 TITL ANALYSIS OF THE ACTIVE SITE OF THE FLAVOPROTEIN 1PBE 45 REMARK 1 TITL 2 P-HYDROXYBENZOATE HYDROXYLASE AND SOME IDEAS WITH 1PBE 46 REMARK 1 TITL 3 RESPECT TO ITS REACTION MECHANISM 1PBE 47 REMARK 1 REF BIOCHEMISTRY V. 29 3101 1989 1PBE 48 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 0033 1PBE 49 REMARK 1 REFERENCE 5 1PBE 50 REMARK 1 AUTH H.A.SCHREUDER,W.G.J.HOL,J.DRENTH 1PBE 51 REMARK 1 TITL MOLECULAR MODELING REVEALS THE POSSIBLE IMPORTANCE 1PBE 52 REMARK 1 TITL 2 OF A CARBONYL OXYGEN BINDING POCKET FOR THE 1PBE 53 REMARK 1 TITL 3 CATALYTIC MECHANISM OF P-HYDROXYBENZOATE 1PBE 54 REMARK 1 TITL 4 HYDROXYLASE 1PBE 55 REMARK 1 REF J.BIOL.CHEM. V. 263 3131 1988 1PBE 56 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 0071 1PBE 57 REMARK 1 REFERENCE 6 1PBE 58 REMARK 1 AUTH H.A.SCHREUDER,J.M.VAN DER LAAN,W.G.J.HOL,J.DRENTH 1PBE 59 REMARK 1 TITL CRYSTAL STRUCTURE OF P-HYDROXYBENZOATE HYDROXYLASE 1PBE 60 REMARK 1 TITL 2 COMPLEXED WITH ITS REACTION PRODUCT 1PBE 61 REMARK 1 TITL 3 3,4-DIHYDROXYBENZOATE 1PBE 62 REMARK 1 REF J.MOL.BIOL. V. 199 637 1988 1PBE 63 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070 1PBE 64 REMARK 1 REFERENCE 7 1PBE 65 REMARK 1 AUTH R.K.WIERENGA,J.DRENTH,G.E.SCHULZ 1PBE 66 REMARK 1 TITL COMPARISON OF THE THREE-DIMENSIONAL PROTEIN AND 1PBE 67 REMARK 1 TITL 2 NUCLEOTIDE STRUCTURE OF THE FAD-BINDING DOMAIN 1PBE 68 REMARK 1 TITL 3 OF P-HYDROXYBENZOATE HYDROXYLASE WITH THE FAD- 1PBE 69 REMARK 1 TITL 4 AS WELL AS NADPH-BINDING DOMAINS OF GLUTATHIONE 1PBE 70 REMARK 1 TITL 5 REDUCTASE 1PBE 71 REMARK 1 REF J.MOL.BIOL. V. 167 725 1983 1PBE 72 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070 1PBE 73 REMARK 1 REFERENCE 8 1PBE 74 REMARK 1 AUTH R.K.WIERENGA,R.J.DE JONG,K.H.KALK,W.G.J.HOL, 1PBE 75 REMARK 1 AUTH 2 J.DRENTH 1PBE 76 REMARK 1 TITL CRYSTAL STRUCTURE OF P-HYDROXYBENZOATE HYDROXYLASE 1PBE 77 REMARK 1 REF J.MOL.BIOL. V. 131 55 1979 1PBE 78 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070 1PBE 79 REMARK 1 REFERENCE 9 1PBE 80 REMARK 1 AUTH J.DRENTH,W.G.J.HOL,R.K.WIERENGA 1PBE 81 REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY INVESTIGATION 1PBE 82 REMARK 1 TITL 2 OF P-HYDROXYBENZOATE HYDROXYLASE FROM PSEUDOMONAS 1PBE 83 REMARK 1 TITL 3 FLUORESCENS 1PBE 84 REMARK 1 REF J.BIOL.CHEM. V. 250 5268 1975 1PBE 85 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 0071 1PBE 86 REMARK 2 1PBE 87 REMARK 2 RESOLUTION. 1.9 ANGSTROMS. 1PBE 88 REMARK 3 1PBE 89 REMARK 3 REFINEMENT. 1PBE 90 REMARK 3 PROGRAM PROLSQ 1PBE 91 REMARK 3 AUTHORS KONNERT,HENDRICKSON 1PBE 92 REMARK 3 R VALUE 0.156 1PBE 93 REMARK 3 1PBE 94 REMARK 3 NUMBER OF REFLECTIONS 31148 1PBE 95 REMARK 3 RESOLUTION RANGE 6.0 - 1.9 ANGSTROMS 1PBE 96 REMARK 3 DATA CUTOFF 0.0 SIGMA(F) 1PBE 97 REMARK 3 PERCENT COMPLETION 88.1 1PBE 98 REMARK 3 1PBE 99 REMARK 3 NUMBER OF ATOMS PRESENT IN ENTRY. 1PBE 100 REMARK 3 NUMBER OF PROTEIN ATOMS 3098 1PBE 101 REMARK 3 NUMBER OF NUCLEIC ACID ATOMS 0 1PBE 102 REMARK 3 NUMBER OF SOLVENT ATOMS 330 1PBE 103 REMARK 3 NUMBER OF HETEROGEN ATOMS 63 1PBE 104 REMARK 3 1PBE 105 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES (THE VALUES OF 1PBE 106 REMARK 3 SIGMA, IN PARENTHESES, ARE THE INPUT ESTIMATED 1PBE 107 REMARK 3 STANDARD DEVIATIONS THAT DETERMINE THE RELATIVE 1PBE 108 REMARK 3 WEIGHTS OF THE CORRESPONDING RESTRAINTS) 1PBE 109 REMARK 3 DISTANCE RESTRAINTS (ANGSTROMS) 1PBE 110 REMARK 3 BOND DISTANCE 0.018(0.020) 1PBE 111 REMARK 3 ANGLE DISTANCE 0.039(0.030) 1PBE 112 REMARK 3 PLANAR 1-4 DISTANCE 0.047(0.040) 1PBE 113 REMARK 3 PLANE RESTRAINT (ANGSTROMS) 0.017(0.020) 1PBE 114 REMARK 3 CHIRAL-CENTER RESTRAINT (ANGSTROMS**3) 0.185(0.150) 1PBE 115 REMARK 3 NON-BONDED CONTACT RESTRAINTS (ANGSTROMS) 1PBE 116 REMARK 3 SINGLE TORSION CONTACT 0.189(0.350) 1PBE 117 REMARK 3 MULTIPLE TORSION CONTACT 0.222(0.350) 1PBE 118 REMARK 3 POSSIBLE HYDROGEN BOND 0.241(0.350) 1PBE 119 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS (ANGSTROMS**2) 1PBE 120 REMARK 3 MAIN-CHAIN BOND 3.725(5.000) 1PBE 121 REMARK 3 MAIN-CHAIN ANGLE 4.514(5.000) 1PBE 122 REMARK 3 SIDE-CHAIN BOND 7.752(7.000) 1PBE 123 REMARK 3 SIDE-CHAIN ANGLE 10.535(10.000) 1PBE 124 REMARK 4 1PBE 125 REMARK 4 CROSS REFERENCE TO SEQUENCE DATABASE 1PBE 126 REMARK 4 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 1PBE 127 REMARK 4 PHHY_PSEFL 1PBE 128 REMARK 4 1PBE 129 REMARK 4 RESIDUES MISSING FROM THE C-TERMINUS 1PBE 130 REMARK 4 SEQUENCE NUMBER IS THAT FROM SWISS-PROT ENTRY 1PBE 131 REMARK 4 GLU 392 1PBE 132 REMARK 4 ILE 393 1PBE 133 REMARK 4 GLU 394 1PBE 134 REMARK 5 1PBE 135 REMARK 5 THERE ARE A FEW SHORT CRYSTAL PACKING CONTACTS WHICH MAINLY 1PBE 136 REMARK 5 OCCUR IN POORLY DEFINED REGIONS. 1PBE 137 SEQRES 1 394 MET LYS THR GLN VAL ALA ILE ILE GLY ALA GLY PRO SER 1PBE 138 SEQRES 2 394 GLY LEU LEU LEU GLY GLN LEU LEU HIS LYS ALA GLY ILE 1PBE 139 SEQRES 3 394 ASP ASN VAL ILE LEU GLU ARG GLN THR PRO ASP TYR VAL 1PBE 140 SEQRES 4 394 LEU GLY ARG ILE ARG ALA GLY VAL LEU GLU GLN GLY MET 1PBE 141 SEQRES 5 394 VAL ASP LEU LEU ARG GLU ALA GLY VAL ASP ARG ARG MET 1PBE 142 SEQRES 6 394 ALA ARG ASP GLY LEU VAL HIS GLU GLY VAL GLU ILE ALA 1PBE 143 SEQRES 7 394 PHE ALA GLY GLN ARG ARG ARG ILE ASP LEU LYS ARG LEU 1PBE 144 SEQRES 8 394 SER GLY GLY LYS THR VAL THR VAL TYR GLY GLN THR GLU 1PBE 145 SEQRES 9 394 VAL THR ARG ASP LEU MET GLU ALA ARG GLU ALA CYS GLY 1PBE 146 SEQRES 10 394 ALA THR THR VAL TYR GLN ALA ALA GLU VAL ARG LEU HIS 1PBE 147 SEQRES 11 394 ASP LEU GLN GLY GLU ARG PRO TYR VAL THR PHE GLU ARG 1PBE 148 SEQRES 12 394 ASP GLY GLU ARG LEU ARG LEU ASP CYS ASP TYR ILE ALA 1PBE 149 SEQRES 13 394 GLY CYS ASP GLY PHE HIS GLY ILE SER ARG GLN SER ILE 1PBE 150 SEQRES 14 394 PRO ALA GLU ARG LEU LYS VAL PHE GLU ARG VAL TYR PRO 1PBE 151 SEQRES 15 394 PHE GLY TRP LEU GLY LEU LEU ALA ASP THR PRO PRO VAL 1PBE 152 SEQRES 16 394 SER HIS GLU LEU ILE TYR ALA ASN HIS PRO ARG GLY PHE 1PBE 153 SEQRES 17 394 ALA LEU CYS SER GLN ARG SER ALA THR ARG SER ARG TYR 1PBE 154 SEQRES 18 394 TYR VAL GLN VAL PRO LEU THR GLU LYS VAL GLU ASP TRP 1PBE 155 SEQRES 19 394 SER ASP GLU ARG PHE TRP THR GLU LEU LYS ALA ARG LEU 1PBE 156 SEQRES 20 394 PRO ALA GLU VAL ALA GLU LYS LEU VAL THR GLY PRO SER 1PBE 157 SEQRES 21 394 LEU GLU LYS SER ILE ALA PRO LEU ARG SER PHE VAL VAL 1PBE 158 SEQRES 22 394 GLU PRO MET GLN HIS GLY ARG LEU PHE LEU ALA GLY ASP 1PBE 159 SEQRES 23 394 ALA ALA HIS ILE VAL PRO PRO THR GLY ALA LYS GLY LEU 1PBE 160 SEQRES 24 394 ASN LEU ALA ALA SER ASP VAL SER THR LEU TYR ARG LEU 1PBE 161 SEQRES 25 394 LEU LEU LYS ALA TYR ARG GLU GLY ARG GLY GLU LEU LEU 1PBE 162 SEQRES 26 394 GLU ARG TYR SER ALA ILE CYS LEU ARG ARG ILE TRP LYS 1PBE 163 SEQRES 27 394 ALA GLU ARG PHE SER TRP TRP MET THR SER VAL LEU HIS 1PBE 164 SEQRES 28 394 ARG PHE PRO ASP THR ASP ALA PHE SER GLN ARG ILE GLN 1PBE 165 SEQRES 29 394 GLN THR GLU LEU GLU TYR TYR LEU GLY SER GLU ALA GLY 1PBE 166 SEQRES 30 394 LEU ALA THR ILE ALA GLU ASN TYR VAL GLY LEU PRO TYR 1PBE 167 SEQRES 31 394 GLU GLU ILE GLU 1PBE 168 FTNOTE 1 1PBE 169 FTNOTE 1 CIS PROLINE - PRO 275 1PBE 170 HET FAD 395 53 FLAVIN-ADENINE DINUCLEOTIDE 1PBE 171 HET PHB 396 10 P-HYDROXYBENZOIC ACID 1PBE 172 FORMUL 2 FAD C27 H33 N9 O15 P2 1PBE 173 FORMUL 3 PHB C7 H6 O3 1PBE 174 FORMUL 4 HOH *330(H2 O1) 1PBE 175 HELIX 1 H1 PRO 12 LYS 23 1 1PBE 176 HELIX 2 H2 PRO 36 LEU 40 1 1PBE 177 HELIX 3 H3 GLN 50 GLU 58 1 1PBE 178 HELIX 4 H4 ARG 63 ASP 68 1 1PBE 179 HELIX 5 H5 LEU 88 LEU 91 1 1PBE 180 HELIX 6 H6 GLN 102 CYS 116 1 1PBE 181 HELIX 7 H7 ILE 164 GLN 167 1 1PBE 182 HELIX 8 H7A ALA 171 ARG 173 5 1PBE 183 HELIX 9 H7B VAL 231 ASP 233 5 1PBE 184 HELIX 10 H8 ASP 236 ARG 246 1 1PBE 185 HELIX 11 H9 ALA 249 LYS 254 1 1PBE 186 HELIX 12 H9A GLY 285 ALA 287 5 1PBE 187 HELIX 13 H9B PRO 293 GLY 295 5 1PBE 188 HELIX 14 H10 GLY 298 ARG 318 1 1PBE 189 HELIX 15 HH1 GLY 322 ARG 327 5 PART OF H11 1PBE 190 HELIX 16 H11 TYR 328 LEU 350 1 1PBE 191 HELIX 17 H12 ALA 358 TYR 371 1 1PBE 192 HELIX 18 H13 GLU 375 VAL 386 1 1PBE 193 SHEET 1 A 6 THR 119 VAL 121 0 1PBE 194 SHEET 2 A 6 ASN 28 LEU 31 1 O ILE 30 N VAL 121 1PBE 195 SHEET 3 A 6 VAL 5 ILE 8 1 O ILE 7 N LEU 31 1PBE 196 SHEET 4 A 6 TYR 154 GLY 157 1 O ALA 156 N ILE 8 1PBE 197 SHEET 5 A 6 LEU 281 LEU 283 1 O PHE 282 N GLY 157 1PBE 198 SHEET 6 A 6 GLN 277 HIS 278 -1 O HIS 278 N LEU 281 1PBE 199 SHEET 1 B 7 GLN 82 ASP 87 0 1PBE 200 SHEET 2 B 7 GLY 74 PHE 79 -1 O VAL 75 N ILE 86 1PBE 201 SHEET 3 B 7 ILE 200 ASN 203 1 N TYR 201 O GLU 76 1PBE 202 SHEET 4 B 7 ALA 209 SER 215 -1 N CYS 211 O ILE 200 1PBE 203 SHEET 5 B 7 ARG 218 VAL 225 -1 N TYR 222 O LEU 210 1PBE 204 SHEET 6 B 7 PHE 183 ALA 190 -1 N LEU 188 O TYR 221 1PBE 205 SHEET 7 B 7 SER 260 PRO 267 -1 N LEU 261 O LEU 189 1PBE 206 SHEET 1 C 4 LYS 2 THR 3 0 1PBE 207 SHEET 2 C 4 GLU 146 ASP 151 1 O ASP 151 N THR 3 1PBE 208 SHEET 3 C 4 TYR 138 ARG 143 -1 O PHE 141 N LEU 148 1PBE 209 SHEET 4 C 4 ALA 125 HIS 130 1 O ARG 128 N THR 140 1PBE 210 SHEET 1 D 3 LYS 175 PRO 182 0 1PBE 211 SHEET 2 D 3 LEU 268 GLU 274 -1 N SER 270 O ARG 179 1PBE 212 SHEET 3 D 3 HIS 289 ILE 290 -1 N ILE 290 O PHE 271 1PBE 213 SHEET 1 E 3 VAL 47 GLU 49 0 1PBE 214 SHEET 2 E 3 VAL 97 VAL 99 -1 O THR 98 N LEU 48 1PBE 215 SHEET 3 E 3 LEU 70 HIS 72 -1 O LEU 70 N VAL 99 1PBE 216 TURN 1 T1 HIS 22 GLY 25 1PBE 217 TURN 2 T2 PHE 79 GLN 82 1PBE 218 TURN 3 T3 ASP 131 GLY 134 1PBE 219 TURN 4 T4 ARG 143 GLU 146 1PBE 220 TURN 5 T5 GLY 160 GLY 163 1PBE 221 TURN 6 T6 HIS 204 GLY 207 1PBE 222 TURN 7 T7 SER 215 ARG 218 NO O 215 - N 218 H-BOND 1PBE 223 TURN 8 T8 PRO 226 GLU 229 1PBE 224 TURN 9 T9 HIS 278 LEU 281 1PBE 225 CRYST1 71.500 145.800 88.200 90.00 90.00 90.00 C 2 2 21 8 1PBE 226 ORIGX1 1.000000 0.000000 0.000000 0.00000 1PBE 227 ORIGX2 0.000000 1.000000 0.000000 0.00000 1PBE 228 ORIGX3 0.000000 0.000000 1.000000 0.00000 1PBE 229 SCALE1 0.013986 0.000000 0.000000 0.00000 1PBE 230 SCALE2 0.000000 0.006859 0.000000 0.00000 1PBE 231 SCALE3 0.000000 0.000000 0.011338 0.00000 1PBE 232