HEADER OXIDOREDUCTASE(OXYGENASE) 04-JUN-91 2CP4 2CP4 2 COMPND CYTOCHROME P450CAM (CAMPHOR MONOOXYGENASE) (E.C.1.14.15.1) 2CP4 3 COMPND 2 MUTANT WITH THR 252 REPLACED BY ALA (/T252A$) WITH BOUND 2CP4 4 COMPND 3 CAMPHOR 2CP4 5 SOURCE (PSEUDOMONAS $PUTIDA) RECOMBINANT FORM EXPRESSED IN 2CP4 6 SOURCE 2 (ESCHERICHIA $COLI) 2CP4 7 AUTHOR R.RAAG,T.L.POULOS 2CP4 8 REVDAT 1 15-JAN-93 2CP4 0 2CP4 9 JRNL AUTH R.RAAG,S.MARTINIS,S.G.SLIGAR,T.L.POULOS, 2CP4 10 JRNL TITL CRYSTAL STRUCTURE OF THE CYTOCHROME P-450CAM 2CP4 11 JRNL TITL 2 ACTIVE SITE MUTANT THR252ALA 2CP4 12 JRNL REF BIOCHEMISTRY V. 33 11420 1991 2CP4 13 JRNL REFN ASTM BICHAW US ISSN 0006-2960 033 2CP4 14 REMARK 1 2CP4 15 REMARK 1 REFERENCE 1 2CP4 16 REMARK 1 AUTH R.RAAG,T.L.POULOS 2CP4 17 REMARK 1 TITL X-*RAY CRYSTALLOGRAPHIC STRUCTURAL STUDIES OF 2CP4 18 REMARK 1 TITL 2 CYTOCHROME P-450=/CAM$=+ 2CP4 19 REMARK 1 REF TO BE PUBLISHED 2CP4 20 REMARK 1 REFN ASTM 353 2CP4 21 REMARK 1 REFERENCE 2 2CP4 22 REMARK 1 AUTH R.RAAG,T.L.POULOS 2CP4 23 REMARK 1 TITL CRYSTAL STRUCTURES OF CYTOCHROME P-450=/CAM$= 2CP4 24 REMARK 1 TITL 2 COMPLEXED WITH CAMPHANE, THIOCAMPHOR, AND 2CP4 25 REMARK 1 TITL 3 ADAMANTANE: FACTORS CONTROLLING P-450 SUBSTRATE 2CP4 26 REMARK 1 TITL 4 HYDROXYLATION 2CP4 27 REMARK 1 REF BIOCHEMISTRY V. 30 2674 1991 2CP4 28 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 2CP4 29 REMARK 1 REFERENCE 3 2CP4 30 REMARK 1 AUTH R.RAAG,T.L.POULOS 2CP4 31 REMARK 1 TITL CRYSTAL STRUCTURE OF THE CARBON 2CP4 32 REMARK 1 TITL 2 MONOXY-*SUBSTRATE-*CYTOCHROME P-450=/CAM$= TERNARY 2CP4 33 REMARK 1 TITL 3 COMPLEX 2CP4 34 REMARK 1 REF BIOCHEMISTRY V. 28 7586 1989 2CP4 35 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 2CP4 36 REMARK 1 REFERENCE 4 2CP4 37 REMARK 1 AUTH R.RAAG,T.L.POULOS 2CP4 38 REMARK 1 TITL THE STRUCTURAL BASIS FOR SUBSTRATE-INDUCED 2CP4 39 REMARK 1 TITL 2 CHANGES IN REDOX POTENTIAL AND SPIN EQUILIBRIUM 2CP4 40 REMARK 1 TITL 3 IN CYTOCHROME P-450(CAM) 2CP4 41 REMARK 1 REF BIOCHEMISTRY V. 28 917 1989 2CP4 42 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 2CP4 43 REMARK 2 2CP4 44 REMARK 2 RESOLUTION. 2.1 ANGSTROMS. 2CP4 45 REMARK 3 2CP4 46 REMARK 3 REFINEMENT. BY THE RESTRAINED LEAST-SQUARES PROCEDURE OF J. 2CP4 47 REMARK 3 KONNERT AND W. HENDRICKSON (PROGRAM *PROFFT*). THE R 2CP4 48 REMARK 3 VALUE IS 0.179. THE RMS DEVIATION FROM IDEALITY OF THE 2CP4 49 REMARK 3 BOND LENGTHS IS 0.020 ANGSTROMS. THE RMS DEVIATION FROM 2CP4 50 REMARK 3 IDEALITY OF THE BOND ANGLE DISTANCES IS 0.034 ANGSTROMS. 2CP4 51 REMARK 4 2CP4 52 REMARK 4 N-TERMINAL RESIDUES 1-9 ARE NOT VISIBLE IN ELECTRON DENSITY 2CP4 53 REMARK 4 MAPS AND ARE OMITTED FROM THIS MODEL. 2CP4 54 SEQRES 1 414 THR THR GLU THR ILE GLN SER ASN ALA ASN LEU ALA PRO 2CP4 55 SEQRES 2 414 LEU PRO PRO HIS VAL PRO GLU HIS LEU VAL PHE ASP PHE 2CP4 56 SEQRES 3 414 ASP MET TYR ASN PRO SER ASN LEU SER ALA GLY VAL GLN 2CP4 57 SEQRES 4 414 GLU ALA TRP ALA VAL LEU GLN GLU SER ASN VAL PRO ASP 2CP4 58 SEQRES 5 414 LEU VAL TRP THR ARG CYS ASN GLY GLY HIS TRP ILE ALA 2CP4 59 SEQRES 6 414 THR ARG GLY GLN LEU ILE ARG GLU ALA TYR GLU ASP TYR 2CP4 60 SEQRES 7 414 ARG HIS PHE SER SER GLU CYS PRO PHE ILE PRO ARG GLU 2CP4 61 SEQRES 8 414 ALA GLY GLU ALA TYR ASP PHE ILE PRO THR SER MET ASP 2CP4 62 SEQRES 9 414 PRO PRO GLU GLN ARG GLN PHE ARG ALA LEU ALA ASN GLN 2CP4 63 SEQRES 10 414 VAL VAL GLY MET PRO VAL VAL ASP LYS LEU GLU ASN ARG 2CP4 64 SEQRES 11 414 ILE GLN GLU LEU ALA CYS SER LEU ILE GLU SER LEU ARG 2CP4 65 SEQRES 12 414 PRO GLN GLY GLN CYS ASN PHE THR GLU ASP TYR ALA GLU 2CP4 66 SEQRES 13 414 PRO PHE PRO ILE ARG ILE PHE MET LEU LEU ALA GLY LEU 2CP4 67 SEQRES 14 414 PRO GLU GLU ASP ILE PRO HIS LEU LYS TYR LEU THR ASP 2CP4 68 SEQRES 15 414 GLN MET THR ARG PRO ASP GLY SER MET THR PHE ALA GLU 2CP4 69 SEQRES 16 414 ALA LYS GLU ALA LEU TYR ASP TYR LEU ILE PRO ILE ILE 2CP4 70 SEQRES 17 414 GLU GLN ARG ARG GLN LYS PRO GLY THR ASP ALA ILE SER 2CP4 71 SEQRES 18 414 ILE VAL ALA ASN GLY GLN VAL ASN GLY ARG PRO ILE THR 2CP4 72 SEQRES 19 414 SER ASP GLU ALA LYS ARG MET CYS GLY LEU LEU LEU VAL 2CP4 73 SEQRES 20 414 GLY GLY LEU ASP ALA VAL VAL ASN PHE LEU SER PHE SER 2CP4 74 SEQRES 21 414 MET GLU PHE LEU ALA LYS SER PRO GLU HIS ARG GLN GLU 2CP4 75 SEQRES 22 414 LEU ILE GLU ARG PRO GLU ARG ILE PRO ALA ALA CYS GLU 2CP4 76 SEQRES 23 414 GLU LEU LEU ARG ARG PHE SER LEU VAL ALA ASP GLY ARG 2CP4 77 SEQRES 24 414 ILE LEU THR SER ASP TYR GLU PHE HIS GLY VAL GLN LEU 2CP4 78 SEQRES 25 414 LYS LYS GLY ASP GLN ILE LEU LEU PRO GLN MET LEU SER 2CP4 79 SEQRES 26 414 GLY LEU ASP GLU ARG GLU ASN ALA CYS PRO MET HIS VAL 2CP4 80 SEQRES 27 414 ASP PHE SER ARG GLN LYS VAL SER HIS THR THR PHE GLY 2CP4 81 SEQRES 28 414 HIS GLY SER HIS LEU CYS LEU GLY GLN HIS LEU ALA ARG 2CP4 82 SEQRES 29 414 ARG GLU ILE ILE VAL THR LEU LYS GLU TRP LEU THR ARG 2CP4 83 SEQRES 30 414 ILE PRO ASP PHE SER ILE ALA PRO GLY ALA GLN ILE GLN 2CP4 84 SEQRES 31 414 HIS LYS SER GLY ILE VAL SER GLY VAL GLN ALA LEU PRO 2CP4 85 SEQRES 32 414 LEU VAL TRP ASP PRO ALA THR THR LYS ALA VAL 2CP4 86 FTNOTE 1 2CP4 87 FTNOTE 1 RESIDUES PRO 89, PRO 100, AND PRO 106 ARE CIS PROLINES. 2CP4 88 HET HEM 1 43 PROTOPORPHYRIN IX GROUP CONTAINS FE+++ 2CP4 89 HET CAM 2 11 CAMPHOR SUBSTRATE 2CP4 90 FORMUL 2 HEM C34 H32 N4 O4 FE1 +++ 2CP4 91 FORMUL 3 CAM C10 H9 O1 2CP4 92 FORMUL 4 HOH *232(H2 O1) 2CP4 93 HELIX 1 A GLY 37 GLN 46 1 2CP4 94 HELIX 2 B ARG 67 ASP 77 1 2CP4 95 HELIX 3 BND ASP 77 PHE 81 5 2CP4 96 HELIX 4 BPR PRO 89 TYR 96 1 2CP4 97 HELIX 5 C PRO 106 LYS 126 1 2CP4 98 HELIX 6 D LEU 127 GLN 145 1 2CP4 99 HELIX 7 E ASN 149 LEU 169 1 2CP4 100 HELIX 8 F ASP 173 THR 185 1 2CP4 101 HELIX 9 G THR 192 LYS 214 1 2CP4 102 HELIX 10 H ASP 218 ASN 225 1 2CP4 103 HELIX 11 I THR 234 SER 267 1 2CP4 104 HELIX 12 J SER 267 GLU 276 1 2CP4 105 HELIX 13 K ARG 280 PHE 292 1 2CP4 106 HELIX 14 310 LEU 324 ASP 328 5 2CP4 107 HELIX 15 L GLY 359 ILE 378 1 2CP4 108 SHEET 1 B1 2 ASP 52 CYS 58 0 2CP4 109 SHEET 2 B1 2 GLY 60 THR 66 -1 2CP4 110 SHEET 1 B5 3 GLY 146 PHE 150 0 2CP4 111 SHEET 2 B5 3 ILE 395 VAL 405 -1 2CP4 112 SHEET 3 B5 3 SER 382 SER 397 -1 2CP4 113 SHEET 1 B2 2 GLY 226 VAL 228 0 2CP4 114 SHEET 2 B2 2 GLY 230 ILE 233 -1 2CP4 115 SHEET 1 B3 2 VAL 295 LEU 301 0 2CP4 116 SHEET 2 B3 2 GLY 315 MET 323 -1 2CP4 117 SHEET 1 B4 2 TYR 305 HIS 308 0 2CP4 118 SHEET 2 B4 2 VAL 310 LEU 312 -1 2CP4 119 TURN 1 T1 PRO 15 VAL 18 TYPE I 2CP4 120 TURN 2 T2 ASP 27 ASN 30 TYPE I 2CP4 121 TURN 3 T3 ASN 33 ALA 36 TYPE I 2CP4 122 TURN 4 T4 GLU 47 VAL 50 TYPE I 2CP4 123 TURN 5 T5 CYS 58 GLY 61 TYPE I(PRIME) 2CP4 124 TURN 6 T6 PHE 98 SER 102 CIS-PRO 2CP4 125 TURN 7 T7 ASP 104 GLN 108 CIS-PRO 2CP4 126 TURN 8 T8 PRO 170 ASP 173 TYPE I 2CP4 127 TURN 9 T9 VAL 228 ARG 231 TYPE I(PRIME) 2CP4 128 TURN 10 T10 ARG 277 ILE 281 TYPE I 2CP4 129 TURN 11 T11 PHE 307 VAL 310 TYPE I(PRIME) 2CP4 130 TURN 12 T12 ASP 328 GLU 331 TYPE I 2CP4 131 TURN 13 T13 CYS 334 HIS 337 TYPE I 2CP4 132 TURN 14 T14 THR 348 GLY 351 TYPE I 2CP4 133 TURN 15 T15 GLY 353 LEU 356 TYPE I 2CP4 134 TURN 16 T16 ALA 384 ALA 387 TYPE II 2CP4 135 CRYST1 108.670 103.900 36.380 90.00 90.00 90.00 P 21 21 21 4 2CP4 136 ORIGX1 1.000000 0.000000 0.000000 0.00000 2CP4 137 ORIGX2 0.000000 1.000000 0.000000 0.00000 2CP4 138 ORIGX3 0.000000 0.000000 1.000000 0.00000 2CP4 139 SCALE1 0.009202 0.000000 0.000000 0.00000 2CP4 140 SCALE2 0.000000 0.009625 0.000000 0.00000 2CP4 141 SCALE3 0.000000 0.000000 0.027488 0.00000 2CP4 142