HEADER OXIDOREDUCTASE(OXYGENASE) 23-NOV-93 1CPT 1CPT 2 COMPND CYTOCHROME P450-TERP 1CPT 3 SOURCE (PSEUDOMONAS SP.) RECOMBINANT FORM EXPRESSED IN 1CPT 4 SOURCE 2 (ESCHERICHIA COLI) 1CPT 5 AUTHOR C.A.HASEMANN,K.G.RAVICHANDRAN,J.A.PETERSON,J.DEISENHOFER 1CPT 6 REVDAT 1 31-JAN-94 1CPT 0 1CPT 7 JRNL AUTH C.A.HASEMANN,K.G.RAVICHANDRAN,J.A.PETERSON, 1CPT 8 JRNL AUTH 2 J.DEISENHOFER 1CPT 9 JRNL TITL CRYSTAL STRUCTURE AND REFINEMENT OF CYTOCHROME 1CPT 10 JRNL TITL 2 P450=TERP= AT 2.3 ANGSTROMS RESOLUTION 1CPT 11 JRNL REF TO BE PUBLISHED 1CPT 12 JRNL REFN 353 1CPT 13 REMARK 1 1CPT 14 REMARK 1 REFERENCE 1 1CPT 15 REMARK 1 AUTH S.S.BODDUPALLI,C.A.HASEMANN,K.G.RAVICHANDRAN, 1CPT 16 REMARK 1 AUTH 2 J.-Y.LU,E.J.GOLDSMITH,J.DEISENHOFER,J.A.PETERSON 1CPT 17 REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION 1CPT 18 REMARK 1 TITL 2 ANALYSIS OF P450=TERP= AND THE HEMOPROTEIN DOMAIN 1CPT 19 REMARK 1 TITL 3 OF P450=BM-3=, ENZYMES BELONGING TO TWO DISTINCT 1CPT 20 REMARK 1 TITL 4 CLASSES OF THE CYTOCHROME P450 SUPERFAMILY 1CPT 21 REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 89 5567 1992 1CPT 22 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 1CPT 23 REMARK 1 REFERENCE 2 1CPT 24 REMARK 1 AUTH J.A.PETERSON,J.-Y.LU,J.GEISSELSODER, 1CPT 25 REMARK 1 AUTH 2 S.GRAHAM-LORENCE,C.CARMONA,F.WITNEY,M.C.LORENCE 1CPT 26 REMARK 1 TITL CYTOCHROME P-450=TERP=: ISOLATION AND PURIFICATION 1CPT 27 REMARK 1 TITL 2 OF THE PROTEIN AND CLONING AND SEQUENCING OF ITS 1CPT 28 REMARK 1 TITL 3 OPERON 1CPT 29 REMARK 1 REF J.BIOL.CHEM. V. 267 14193 1992 1CPT 30 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 1CPT 31 REMARK 2 1CPT 32 REMARK 2 RESOLUTION. 2.3 ANGSTROMS. 1CPT 33 REMARK 3 1CPT 34 REMARK 3 REFINEMENT. 1CPT 35 REMARK 3 PROGRAM X-PLOR 1CPT 36 REMARK 3 AUTHORS BRUNGER 1CPT 37 REMARK 3 R VALUE 0.189 1CPT 38 REMARK 3 RMSD BOND DISTANCES 0.016 ANGSTROMS 1CPT 39 REMARK 3 RMSD BOND ANGLES 2.98 DEGREES 1CPT 40 REMARK 4 1CPT 41 REMARK 4 THE MODEL INCLUDES RESIDUES 1 - 428, WITH THE EXCEPTION OF 1CPT 42 REMARK 4 RESIDUES 191 - 207. NO INTERPRETABLE ELECTRON DENSITY WAS 1CPT 43 REMARK 4 FOUND FOR THIS LOOP BETWEEN HELICES F AND G. 220 1CPT 44 REMARK 4 CRYSTALLOGRAPHICALLY ORDERED WATER MOLECULES ARE INCLUDED. 1CPT 45 REMARK 5 1CPT 46 REMARK 5 BY REQUEST OF THE DEPOSITORS, THE SIDE-CHAIN ATOM NAMES OF 1CPT 47 REMARK 5 SEVERAL RESIDUES DO NOT FOLLOW IUPAC/IUB SPECIFICATIONS 1CPT 48 REMARK 5 WITH RESPECT TO THE DESIGNATION OF 1 AND 2 FOR BRANCHED 1CPT 49 REMARK 5 SIDE CHAINS. THE AFFECTED RESIDUES ARE GLU 9, TYR 28, 1CPT 50 REMARK 5 PHE 31, GLU 46, ASP 49, PHE 70, GLU 74, GLU 77, TYR 80, 1CPT 51 REMARK 5 GLU 85, TYR 113, PHE 121, PHE 147, GLU 150, ASP 156, 1CPT 52 REMARK 5 TYR 160, ASP 175, ASP 186, PHE 188, GLU 214, PHE 219, 1CPT 53 REMARK 5 TYR 220, PHE 223, PHE 226, ASP 229, ASP 236, ASP 237, 1CPT 54 REMARK 5 ASP 248, TYR 251, ASP 253, TYR 256, TYR 260, TYR 261, 1CPT 55 REMARK 5 PHE 317, GLU 326, TYR 342, ASP 348, PHE 352, GLU 357, 1CPT 56 REMARK 5 PHE 363, PHE 370, GLU 386, PHE 391, GLU 402, AND PHE 425. 1CPT 57 SEQRES 1 412 MET ASP ALA ARG ALA THR ILE PRO GLU HIS ILE ALA ARG 1CPT 58 SEQRES 2 412 THR VAL ILE LEU PRO GLN GLY TYR ALA ASP ASP GLU VAL 1CPT 59 SEQRES 3 412 ILE TYR PRO ALA PHE LYS TRP LEU ARG ASP GLU GLN PRO 1CPT 60 SEQRES 4 412 LEU ALA MET ALA HIS ILE GLU GLY TYR ASP PRO MET TRP 1CPT 61 SEQRES 5 412 ILE ALA THR LYS HIS ALA ASP VAL MET GLN ILE GLY LYS 1CPT 62 SEQRES 6 412 GLN PRO GLY LEU PHE SER ASN ALA GLU GLY SER GLU ILE 1CPT 63 SEQRES 7 412 LEU TYR ASP GLN ASN ASN GLU ALA PHE MET ARG SER ILE 1CPT 64 SEQRES 8 412 SER GLY GLY CYS PRO HIS VAL ILE ASP SER LEU THR SER 1CPT 65 SEQRES 9 412 MET ASP PRO PRO THR HIS THR ALA TYR ARG GLY LEU THR 1CPT 66 SEQRES 10 412 LEU ASN TRP PHE GLN PRO ALA SER ILE ARG LYS LEU GLU 1CPT 67 SEQRES 11 412 GLU ASN ILE ARG ARG ILE ALA GLN ALA SER VAL GLN ARG 1CPT 68 SEQRES 12 412 LEU LEU ASP PHE ASP GLY GLU CYS ASP PHE MET THR ASP 1CPT 69 SEQRES 13 412 CYS ALA LEU TYR TYR PRO LEU HIS VAL VAL MET THR ALA 1CPT 70 SEQRES 14 412 LEU GLY VAL PRO GLU ASP ASP GLU PRO LEU MET LEU LYS 1CPT 71 SEQRES 15 412 LEU THR GLN ASP PHE PHE GLY VAL GLU ALA ALA ARG ARG 1CPT 72 SEQRES 16 412 PHE HIS GLU THR ILE ALA THR PHE TYR ASP TYR PHE ASN 1CPT 73 SEQRES 17 412 GLY PHE THR VAL ASP ARG ARG SER CYS PRO LYS ASP ASP 1CPT 74 SEQRES 18 412 VAL MET SER LEU LEU ALA ASN SER LYS LEU ASP GLY ASN 1CPT 75 SEQRES 19 412 TYR ILE ASP ASP LYS TYR ILE ASN ALA TYR TYR VAL ALA 1CPT 76 SEQRES 20 412 ILE ALA THR ALA GLY HIS ASP THR THR SER SER SER SER 1CPT 77 SEQRES 21 412 GLY GLY ALA ILE ILE GLY LEU SER ARG ASN PRO GLU GLN 1CPT 78 SEQRES 22 412 LEU ALA LEU ALA LYS SER ASP PRO ALA LEU ILE PRO ARG 1CPT 79 SEQRES 23 412 LEU VAL ASP GLU ALA VAL ARG TRP THR ALA PRO VAL LYS 1CPT 80 SEQRES 24 412 SER PHE MET ARG THR ALA LEU ALA ASP THR GLU VAL ARG 1CPT 81 SEQRES 25 412 GLY GLN ASN ILE LYS ARG GLY ASP ARG ILE MET LEU SER 1CPT 82 SEQRES 26 412 TYR PRO SER ALA ASN ARG ASP GLU GLU VAL PHE SER ASN 1CPT 83 SEQRES 27 412 PRO ASP GLU PHE ASP ILE THR ARG PHE PRO ASN ARG HIS 1CPT 84 SEQRES 28 412 LEU GLY PHE GLY TRP GLY ALA HIS MET CYS LEU GLY GLN 1CPT 85 SEQRES 29 412 HIS LEU ALA LYS LEU GLU MET LYS ILE PHE PHE GLU GLU 1CPT 86 SEQRES 30 412 LEU LEU PRO LYS LEU LYS SER VAL GLU LEU SER GLY PRO 1CPT 87 SEQRES 31 412 PRO ARG LEU VAL ALA THR ASN PHE VAL GLY GLY PRO LYS 1CPT 88 SEQRES 32 412 ASN VAL PRO ILE ARG PHE THR LYS ALA 1CPT 89 FTNOTE 1 1CPT 90 FTNOTE 1 CIS PROLINE - PRO 108 1CPT 91 FTNOTE 2 1CPT 92 FTNOTE 2 FOR RESIDUE 207 NO DENSITY WAS SEEN FOR SIDE CHAIN ATOMS 1CPT 93 FTNOTE 2 BEYOND CA. 1CPT 94 FTNOTE 3 1CPT 95 FTNOTE 3 ASPARTATES 236 AND 253 WERE MODELLED IN ALTERNATE 1CPT 96 FTNOTE 3 CONFORMATIONS. 1CPT 97 FTNOTE 4 1CPT 98 FTNOTE 4 CIS PROLINE - PRO 364 1CPT 99 FTNOTE 5 1CPT 100 FTNOTE 5 WATER 440 IS AN AXIAL LIGAND TO THE HEME IRON. 1CPT 101 HET HEM 430 43 PROTOPORPHYRIN IX CONTAINS FE(II) 1CPT 102 FORMUL 2 HEM C34 H32 N4 O4 FE1 ++ 1CPT 103 FORMUL 3 HOH *221(H2 O1) 1CPT 104 HELIX 1 A3 GLN 19 ALA 22 5 1CPT 105 HELIX 2 A' GLU 9 ILE 16 1 1CPT 106 HELIX 3 A ASP 24 GLU 37 1 1CPT 107 HELIX 4 B HIS 57 LYS 65 1 1CPT 108 HELIX 5 B' GLN 82 ILE 91 1 1CPT 109 HELIX 6 B3 LEU 102 SER 104 5 1CPT 110 HELIX 7 C PRO 108 LEU 118 1 1CPT 111 HELIX 8 C' PRO 123 ILE 126 1 1CPT 112 HELIX 9 C3 ARG 127 LEU 129 5 1CPT 113 HELIX 10 D GLU 130 LEU 145 1 1CPT 114 HELIX 11 E' PHE 153 ASP 156 1 1CPT 115 HELIX 12 E TYR 160 LEU 170 1 1CPT 116 HELIX 13 D3 GLU 174 ASP 176 5 1CPT 117 HELIX 14 F GLU 177 GLN 185 1 1CPT 118 HELIX 15 G ALA 208 ARG 231 1 1CPT 119 HELIX 16 H VAL 238 ASN 244 1 1CPT 120 HELIX 17 I ASP 254 ARG 285 1 1CPT 121 HELIX 18 J PRO 287 SER 295 1 1CPT 122 HELIX 19 E3 PRO 297 LEU 299 5 1CPT 123 HELIX 20 K ILE 300 THR 311 1 1CPT 124 HELIX 21 K' TYR 342 ASN 346 1 1CPT 125 HELIX 22 L GLN 380 LEU 394 1 1CPT 126 HELIX 23 F3 LEU 395 LYS 397 5 1CPT 127 SHEET 1 1 5 PRO 39 ALA 43 0 1CPT 128 SHEET 2 1 5 PRO 50 THR 55 -1 1CPT 129 SHEET 3 1 5 GLY 335 SER 341 1 1CPT 130 SHEET 4 1 5 PHE 317 LEU 322 -1 1CPT 131 SHEET 5 1 5 LEU 69 SER 71 -1 1CPT 132 SHEET 1 2 2 THR 325 VAL 327 0 1CPT 133 SHEET 2 2 2 GLN 330 ILE 332 -1 1CPT 134 SHEET 1 3 3 GLY 149 PHE 153 0 1CPT 135 SHEET 2 3 3 VAL 421 ALA 428 -1 1CPT 136 SHEET 3 3 3 LYS 397 SER 404 -1 1CPT 137 SHEET 1 4 2 ARG 408 VAL 410 0 1CPT 138 SHEET 2 4 2 GLY 417 ASN 420 -1 1CPT 139 SHEET 1 5 2 SER 245 LEU 247 0 1CPT 140 SHEET 2 5 2 ASN 250 ILE 252 -1 1CPT 141 CRYST1 69.440 69.440 456.550 90.00 90.00 120.00 P 61 2 2 12 1CPT 142 ORIGX1 1.000000 0.000000 0.000000 0.00000 1CPT 143 ORIGX2 0.000000 1.000000 0.000000 0.00000 1CPT 144 ORIGX3 0.000000 0.000000 1.000000 0.00000 1CPT 145 SCALE1 0.014401 0.008314 0.000000 0.00000 1CPT 146 SCALE2 0.000000 0.016629 0.000000 0.00000 1CPT 147 SCALE3 0.000000 0.000000 0.002190 0.00000 1CPT 148