HEADER OXIDOREDUCTASE(OXYGEN(A)) 30-SEP-93 1GOF 1GOF 2 COMPND GALACTOSE OXIDASE (E.C.1.1.3.9) (PH 4.5) 1GOF 3 SOURCE (DACTYLIUM DENDROIDES) 1GOF 4 AUTHOR N.ITO,S.E.V.PHILLIPS,P.F.KNOWLES 1GOF 5 REVDAT 1 31-JAN-94 1GOF 0 1GOF 6 JRNL AUTH N.ITO,S.E.V.PHILLIPS,C.STEVENS,Z.B.OGEL, 1GOF 7 JRNL AUTH 2 M.J.MC*PHERSON,J.N.KEEN,K.D.S.YADAV,P.F.KNOWLES 1GOF 8 JRNL TITL NOVEL THIOETHER BOND REVEALED BY A 1.7 ANGSTROMS 1GOF 9 JRNL TITL 2 CRYSTAL STRUCTURE OF GALACTOSE OXIDASE 1GOF 10 JRNL REF NATURE V. 350 87 1991 1GOF 11 JRNL REFN ASTM NATUAS UK ISSN 0028-0836 006 1GOF 12 REMARK 1 1GOF 13 REMARK 1 REFERENCE 1 1GOF 14 REMARK 1 AUTH N.ITO,S.E.V.PHILLIPS,K.K.S.YADAV,P.F.KNOWLES 1GOF 15 REMARK 1 TITL THE CRYSTAL STRUCTURE OF A FREE RADICAL ENZYME, 1GOF 16 REMARK 1 TITL 2 GALACTOSE OXIDASE 1GOF 17 REMARK 1 REF TO BE PUBLISHED 1GOF 18 REMARK 1 REFN 353 1GOF 19 REMARK 1 REFERENCE 2 1GOF 20 REMARK 1 AUTH M.J.MC*PHERSON,Z.B.OGEL,C.STEVENS,K.D.S.YADAV, 1GOF 21 REMARK 1 AUTH 2 J.M.KEEN,P.F.KNOWLES 1GOF 22 REMARK 1 TITL GALACTOSE OXIDASE OF DACTYLIUM DENDROIDES: GENE 1GOF 23 REMARK 1 TITL 2 CLONING AND SEQUENCE ANALYSIS 1GOF 24 REMARK 1 REF J.BIOL.CHEM. V. 267 8146 1992 1GOF 25 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 1GOF 26 REMARK 2 1GOF 27 REMARK 2 RESOLUTION. 1.7 ANGSTROMS. 1GOF 28 REMARK 3 1GOF 29 REMARK 3 REFINEMENT. 1GOF 30 REMARK 3 PROGRAM PROLSQ 1GOF 31 REMARK 3 AUTHORS KONNERT,HENDRICKSON 1GOF 32 REMARK 3 R VALUE 0.177 1GOF 33 REMARK 3 RMSD BOND DISTANCES 0.018 ANGSTROMS 1GOF 34 REMARK 3 RMSD BOND ANGLE DISTANCES 0.05 ANGSTROMS 1GOF 35 REMARK 3 1GOF 36 REMARK 3 RESOLUTION RANGE 10.0 - 1.7 ANGSTROMS 1GOF 37 REMARK 3 DATA CUTOFF 0.0 SIGMA(F) 1GOF 38 REMARK 3 PERCENT COMPLETION 79.1 1GOF 39 REMARK 3 1GOF 40 REMARK 3 NUMBER OF PROTEIN ATOMS 4830 1GOF 41 REMARK 3 NUMBER OF SOLVENT ATOMS 325 1GOF 42 REMARK 4 1GOF 43 REMARK 4 UNUSUAL COVALENT LINKAGE IS OBSERVED BETWEEN SG OF CYS 228 1GOF 44 REMARK 4 AND CE1 OF TYR 272. THE REFINEMENT WAS CARRIED OUT 1GOF 45 REMARK 4 WITHOUT ASSUMING THIS BOND AS A RESTRAINT, ALTHOUGH THE 1GOF 46 REMARK 4 NON-BONDED INTERACTION TERMS BETWEEN THESE TWO SIDE CHAINS 1GOF 47 REMARK 4 WERE REMOVED. 1GOF 48 REMARK 5 1GOF 49 REMARK 5 IN THE SITE RECORDS BELOW, CU DENOTES THE COPPER BINDING 1GOF 50 REMARK 5 SITE AND NA DENOTES THE SODIUM BINDING SITE. 1GOF 51 REMARK 6 1GOF 52 REMARK 6 THE SHEET PRESENTED AS *S9* ON SHEET RECORDS BELOW IS 1GOF 53 REMARK 6 ACTUALLY A SEVEN-STRANDED BETA-BARREL. THIS IS REPRESENTED 1GOF 54 REMARK 6 BY AN EIGHT-STRANDED SHEET IN WHICH THE FIRST AND LAST 1GOF 55 REMARK 6 STRANDS ARE IDENTICAL. 1GOF 56 REMARK 7 1GOF 57 REMARK 7 DOMAIN 3 (RESIDUES 553 - 639) HAS A VERY COMPLICATED 1GOF 58 REMARK 7 HYDROGEN BONDING NETWORK WHICH IS DIFFICULT TO DESCRIBE. 1GOF 59 REMARK 7 IN THE SHEET RECORDS BELOW, THIS IS SIMPLIFIED BY REGARDING 1GOF 60 REMARK 7 SEVERAL PAIRS OF BETA-STRANDS AS ONE. 1GOF 61 REMARK 8 1GOF 62 REMARK 8 THE COORDINATES IN THIS ENTRY ARE PRESENTED IN THE 1GOF 63 REMARK 8 A*, B, C COORDINATE FRAME. 1GOF 64 REMARK 9 1GOF 65 REMARK 9 THERE IS SOME UNCERTAINTY AS TO THE EXACT TYPING OF THE 1GOF 66 REMARK 9 FUNGUS DACTYLIUM DENDROIDES. (SEE REFERENCE 2). 1GOF 67 SEQRES 1 639 ALA SER ALA PRO ILE GLY SER ALA ILE SER ARG ASN ASN 1GOF 68 SEQRES 2 639 TRP ALA VAL THR CYS ASP SER ALA GLN SER GLY ASN GLU 1GOF 69 SEQRES 3 639 CYS ASN LYS ALA ILE ASP GLY ASN LYS ASP THR PHE TRP 1GOF 70 SEQRES 4 639 HIS THR PHE TYR GLY ALA ASN GLY ASP PRO LYS PRO PRO 1GOF 71 SEQRES 5 639 HIS THR TYR THR ILE ASP MET LYS THR THR GLN ASN VAL 1GOF 72 SEQRES 6 639 ASN GLY LEU SER MET LEU PRO ARG GLN ASP GLY ASN GLN 1GOF 73 SEQRES 7 639 ASN GLY TRP ILE GLY ARG HIS GLU VAL TYR LEU SER SER 1GOF 74 SEQRES 8 639 ASP GLY THR ASN TRP GLY SER PRO VAL ALA SER GLY SER 1GOF 75 SEQRES 9 639 TRP PHE ALA ASP SER THR THR LYS TYR SER ASN PHE GLU 1GOF 76 SEQRES 10 639 THR ARG PRO ALA ARG TYR VAL ARG LEU VAL ALA ILE THR 1GOF 77 SEQRES 11 639 GLU ALA ASN GLY GLN PRO TRP THR SER ILE ALA GLU ILE 1GOF 78 SEQRES 12 639 ASN VAL PHE GLN ALA SER SER TYR THR ALA PRO GLN PRO 1GOF 79 SEQRES 13 639 GLY LEU GLY ARG TRP GLY PRO THR ILE ASP LEU PRO ILE 1GOF 80 SEQRES 14 639 VAL PRO ALA ALA ALA ALA ILE GLU PRO THR SER GLY ARG 1GOF 81 SEQRES 15 639 VAL LEU MET TRP SER SER TYR ARG ASN ASP ALA PHE GLY 1GOF 82 SEQRES 16 639 GLY SER PRO GLY GLY ILE THR LEU THR SER SER TRP ASP 1GOF 83 SEQRES 17 639 PRO SER THR GLY ILE VAL SER ASP ARG THR VAL THR VAL 1GOF 84 SEQRES 18 639 THR LYS HIS ASP MET PHE CYS PRO GLY ILE SER MET ASP 1GOF 85 SEQRES 19 639 GLY ASN GLY GLN ILE VAL VAL THR GLY GLY ASN ASP ALA 1GOF 86 SEQRES 20 639 LYS LYS THR SER LEU TYR ASP SER SER SER ASP SER TRP 1GOF 87 SEQRES 21 639 ILE PRO GLY PRO ASP MET GLN VAL ALA ARG GLY TYR GLN 1GOF 88 SEQRES 22 639 SER SER ALA THR MET SER ASP GLY ARG VAL PHE THR ILE 1GOF 89 SEQRES 23 639 GLY GLY SER TRP SER GLY GLY VAL PHE GLU LYS ASN GLY 1GOF 90 SEQRES 24 639 GLU VAL TYR SER PRO SER SER LYS THR TRP THR SER LEU 1GOF 91 SEQRES 25 639 PRO ASN ALA LYS VAL ASN PRO MET LEU THR ALA ASP LYS 1GOF 92 SEQRES 26 639 GLN GLY LEU TYR ARG SER ASP ASN HIS ALA TRP LEU PHE 1GOF 93 SEQRES 27 639 GLY TRP LYS LYS GLY SER VAL PHE GLN ALA GLY PRO SER 1GOF 94 SEQRES 28 639 THR ALA MET ASN TRP TYR TYR THR SER GLY SER GLY ASP 1GOF 95 SEQRES 29 639 VAL LYS SER ALA GLY LYS ARG GLN SER ASN ARG GLY VAL 1GOF 96 SEQRES 30 639 ALA PRO ASP ALA MET CYS GLY ASN ALA VAL MET TYR ASP 1GOF 97 SEQRES 31 639 ALA VAL LYS GLY LYS ILE LEU THR PHE GLY GLY SER PRO 1GOF 98 SEQRES 32 639 ASP TYR GLN ASP SER ASP ALA THR THR ASN ALA HIS ILE 1GOF 99 SEQRES 33 639 ILE THR LEU GLY GLU PRO GLY THR SER PRO ASN THR VAL 1GOF 100 SEQRES 34 639 PHE ALA SER ASN GLY LEU TYR PHE ALA ARG THR PHE HIS 1GOF 101 SEQRES 35 639 THR SER VAL VAL LEU PRO ASP GLY SER THR PHE ILE THR 1GOF 102 SEQRES 36 639 GLY GLY GLN ARG ARG GLY ILE PRO PHE GLU ASP SER THR 1GOF 103 SEQRES 37 639 PRO VAL PHE THR PRO GLU ILE TYR VAL PRO GLU GLN ASP 1GOF 104 SEQRES 38 639 THR PHE TYR LYS GLN ASN PRO ASN SER ILE VAL ARG VAL 1GOF 105 SEQRES 39 639 TYR HIS SER ILE SER LEU LEU LEU PRO ASP GLY ARG VAL 1GOF 106 SEQRES 40 639 PHE ASN GLY GLY GLY GLY LEU CYS GLY ASP CYS THR THR 1GOF 107 SEQRES 41 639 ASN HIS PHE ASP ALA GLN ILE PHE THR PRO ASN TYR LEU 1GOF 108 SEQRES 42 639 TYR ASN SER ASN GLY ASN LEU ALA THR ARG PRO LYS ILE 1GOF 109 SEQRES 43 639 THR ARG THR SER THR GLN SER VAL LYS VAL GLY GLY ARG 1GOF 110 SEQRES 44 639 ILE THR ILE SER THR ASP SER SER ILE SER LYS ALA SER 1GOF 111 SEQRES 45 639 LEU ILE ARG TYR GLY THR ALA THR HIS THR VAL ASN THR 1GOF 112 SEQRES 46 639 ASP GLN ARG ARG ILE PRO LEU THR LEU THR ASN ASN GLY 1GOF 113 SEQRES 47 639 GLY ASN SER TYR SER PHE GLN VAL PRO SER ASP SER GLY 1GOF 114 SEQRES 48 639 VAL ALA LEU PRO GLY TYR TRP MET LEU PHE VAL MET ASN 1GOF 115 SEQRES 49 639 SER ALA GLY VAL PRO SER VAL ALA SER THR ILE ARG VAL 1GOF 116 SEQRES 50 639 THR GLN 1GOF 117 FTNOTE 1 1GOF 118 FTNOTE 1 CIS PROLINE - PRO 52 1GOF 119 FTNOTE 2 1GOF 120 FTNOTE 2 CIS PROLINE - PRO 163 1GOF 121 FTNOTE 3 1GOF 122 FTNOTE 3 CIS PROLINE - PRO 350 1GOF 123 HET CU 700 1 COPPER ++ ION 1GOF 124 HET ACY 701 4 ACETATE ION 1GOF 125 HET NA 702 1 SODIUM +1 COUNTER ION 1GOF 126 HET ACY 703 4 ACETATE ION 1GOF 127 FORMUL 2 CU CU1 ++ 1GOF 128 FORMUL 3 ACY 2(C2 H3 O2 -) 1GOF 129 FORMUL 4 NA NA1 + 1GOF 130 FORMUL 5 HOH *316(H2 O1) 1GOF 131 HELIX 1 H1 LEU 328 SER 331 1 THE ONLY A-HELIX 1GOF 132 SHEET 1 S1 9 ALA 15 CYS 18 0 1GOF 133 SHEET 2 S1 9 HIS 53 ASP 58 -1 N THR 56 O THR 17 1GOF 134 SHEET 3 S1 9 TYR 123 ALA 128 -1 N LEU 126 O TYR 55 1GOF 135 SHEET 4 S1 9 ARG 84 SER 90 -1 N TYR 88 O ARG 125 1GOF 136 SHEET 5 S1 9 ALA 101 SER 104 -1 N GLY 103 O HIS 85 1GOF 137 SHEET 6 S1 9 ARG 160 ASP 166 1 N ASP 166 O SER 102 1GOF 138 SHEET 7 S1 9 ASP 524 THR 529 -1 N ILE 527 O PRO 163 1GOF 139 SHEET 8 S1 9 VAL 507 GLY 511 -1 N ASN 509 O GLN 526 1GOF 140 SHEET 9 S1 9 SER 497 LEU 501 -1 N LEU 500 O PHE 508 1GOF 141 SHEET 1 S2 3 LYS 112 ALA 121 0 1GOF 142 SHEET 2 S2 3 GLN 63 LEU 71 -1 N LEU 68 O SER 114 1GOF 143 SHEET 3 S2 3 GLU 142 GLN 147 -1 N PHE 146 O GLY 67 1GOF 144 SHEET 1 S3 5 VAL 214 VAL 219 0 1GOF 145 SHEET 2 S3 5 THR 202 TRP 207 -1 N SER 206 O SER 215 1GOF 146 SHEET 3 S3 5 VAL 183 TRP 186 -1 N MET 185 O SER 205 1GOF 147 SHEET 4 S3 5 ALA 173 ILE 176 -1 N ALA 175 O LEU 184 1GOF 148 SHEET 5 S3 5 THR 578 THR 580 -1 N ALA 579 O ALA 174 1GOF 149 SHEET 1 S4 4 GLY 230 MET 233 0 1GOF 150 SHEET 2 S4 4 GLN 238 THR 242 -1 N VAL 240 O SER 232 1GOF 151 SHEET 3 S4 4 THR 250 ASP 254 -1 N TYR 253 O ILE 239 1GOF 152 SHEET 4 S4 4 SER 259 PRO 262 -1 N ILE 261 O LEU 252 1GOF 153 SHEET 1 S5 4 SER 274 THR 277 0 1GOF 154 SHEET 2 S5 4 VAL 283 ILE 286 -1 N PHE 284 O ALA 276 1GOF 155 SHEET 3 S5 4 GLY 299 SER 303 -1 N TYR 302 O VAL 283 1GOF 156 SHEET 4 S5 4 THR 308 LEU 312 -1 N THR 310 O VAL 301 1GOF 157 SHEET 1 S6 4 LEU 337 GLY 339 0 1GOF 158 SHEET 2 S6 4 VAL 345 GLN 347 -1 N PHE 346 O PHE 338 1GOF 159 SHEET 3 S6 4 ALA 353 TYR 358 -1 N TYR 357 O VAL 345 1GOF 160 SHEET 4 S6 4 ASP 364 LYS 370 -1 N LYS 366 O TRP 356 1GOF 161 SHEET 1 S7 4 ASN 385 ASP 390 0 1GOF 162 SHEET 2 S7 4 LYS 395 PHE 399 -1 N LEU 397 O VAL 387 1GOF 163 SHEET 3 S7 4 ALA 414 THR 418 -1 N ILE 417 O ILE 396 1GOF 164 SHEET 4 S7 4 ASN 427 PHE 430 -1 N VAL 429 O ILE 416 1GOF 165 SHEET 1 S8 4 THR 443 VAL 446 0 1GOF 166 SHEET 2 S8 4 SER 451 THR 455 -1 N PHE 453 O VAL 445 1GOF 167 SHEET 3 S8 4 GLU 474 VAL 477 -1 N TYR 476 O THR 452 1GOF 168 SHEET 4 S8 4 THR 482 LYS 485 -1 N TYR 484 O ILE 475 1GOF 169 SHEET 1 S9 8 ILE 546 LYS 555 0 1GOF 170 SHEET 2 S9 8 ARG 559 THR 564 -1 N SER 563 O ARG 548 1GOF 171 SHEET 3 S9 8 SER 601 GLN 605 -1 N TYR 602 O ILE 562 1GOF 172 SHEET 4 S9 8 ARG 589 ASN 596 -1 N THR 595 O SER 603 1GOF 173 SHEET 5 S9 8 LYS 570 ARG 575 -1 N LEU 573 O ILE 590 1GOF 174 SHEET 6 S9 8 GLY 616 MET 623 -1 N PHE 621 O SER 572 1GOF 175 SHEET 7 S9 8 SER 633 THR 638 -1 N SER 633 O LEU 620 1GOF 176 SHEET 8 S9 8 ILE 546 LYS 555 1 N VAL 554 O ARG 636 1GOF 177 TURN 1 T1 GLN 22 ASN 25 TYPE II 1GOF 178 TURN 2 T2 ASN 34 THR 37 TYPE I 1GOF 179 TURN 3 T3 GLN 78 TRP 81 TYPE II 1GOF 180 TURN 4 T4 GLU 131 GLY 134 TYPE I 1GOF 181 TURN 5 T5 GLN 155 LEU 158 TYPE II 1GOF 182 TURN 6 T6 PHE 194 SER 197 TYPE II 1GOF 183 TURN 7 T7 THR 220 LYS 223 TYPE I 1GOF 184 TURN 8 T8 ASP 234 GLY 237 TYPE I 1GOF 185 TURN 9 T9 GLY 243 ASP 246 TYPE II' 1GOF 186 TURN 10 T10 ASP 246 LYS 249 TYPE I 1GOF 187 TURN 11 T11 MET 278 GLY 281 TYPE I 1GOF 188 TURN 12 T12 LEU 312 ALA 315 TYPE I 1GOF 189 TURN 13 T13 ASP 324 GLY 327 TYPE I 1GOF 190 TURN 14 T14 SER 360 GLY 363 TYPE II' 1GOF 191 TURN 15 T15 SER 373 GLY 376 TYPE I 1GOF 192 TURN 16 T16 ALA 381 GLY 384 TYPE II 1GOF 193 TURN 17 T17 GLU 421 THR 424 TYPE II 1GOF 194 TURN 18 T18 ALA 431 GLY 434 TYPE II' 1GOF 195 TURN 19 T19 LEU 447 GLY 450 TYPE I 1GOF 196 TURN 20 T20 ILE 462 GLU 465 TYPE II 1GOF 197 TURN 21 T21 PRO 478 ASP 481 TYPE I 1GOF 198 TURN 22 T22 VAL 494 SER 497 TYPE II 1GOF 199 TURN 23 T23 LEU 502 GLY 505 TYPE I 1GOF 200 TURN 24 T24 CYS 515 CYS 518 TYPE II' 1GOF 201 TURN 25 T25 ASN 535 GLY 538 TYPE I 1GOF 202 TURN 26 T26 LYS 555 GLY 558 TYPE II 1GOF 203 TURN 27 T27 THR 580 VAL 583 TYPE I' 1GOF 204 TURN 28 T28 ASN 624 GLY 627 TYPE I 1GOF 205 SSBOND 1 CYS 18 CYS 27 1GOF 206 SSBOND 2 CYS 515 CYS 518 1GOF 207 SITE 1 CU 5 TYR 272 TYR 495 HIS 496 HIS 581 1GOF 208 SITE 2 CU 5 ACY 703 1GOF 209 SITE 1 NA 6 LYS 29 ASP 32 ASN 34 THR 37 1GOF 210 SITE 2 NA 6 ALA 141 GLU 142 1GOF 211 CRYST1 98.000 89.400 86.700 90.00 117.80 90.00 C 2 4 1GOF 212 ORIGX1 1.000000 0.000000 0.000000 0.00000 1GOF 213 ORIGX2 0.000000 1.000000 0.000000 0.00000 1GOF 214 ORIGX3 0.000000 0.000000 1.000000 0.00000 1GOF 215 SCALE1 0.011535 0.000000 0.000000 0.00000 1GOF 216 SCALE2 0.000000 0.011186 0.000000 0.00000 1GOF 217 SCALE3 0.006081 0.000000 0.011534 0.00000 1GOF 218