HEADER OXIDOREDUCTASE 17-JAN-19 6J7A
TITLE FUSION PROTEIN OF HEME OXYGENASE-1 AND NADPH CYTOCHROME P450 REDUCTASE
TITLE 2 (17AA)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEME OXYGENASE 1,NADPH--CYTOCHROME P450 REDUCTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HO-1,HSP32,P450R;
COMPND 5 EC: 1.14.14.18,1.6.2.4;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: HMOX1, POR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS FUSION PROTEIN, REDOX COMPLEX, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SUGISHIMA,H.SATO,K.WADA,K.YAMAMOTO
REVDAT 3 22-NOV-23 6J7A 1 REMARK
REVDAT 2 15-MAY-19 6J7A 1 JRNL
REVDAT 1 10-APR-19 6J7A 0
JRNL AUTH M.SUGISHIMA,H.SATO,K.WADA,K.YAMAMOTO
JRNL TITL CRYSTAL STRUCTURE OF A NADPH-CYTOCHROME P450 OXIDOREDUCTASE
JRNL TITL 2 (CYPOR) AND HEME OXYGENASE 1 FUSION PROTEIN IMPLIES A
JRNL TITL 3 CONFORMATIONAL CHANGE IN CYPOR UPON NADPH/NADP+BINDING.
JRNL REF FEBS LETT. V. 593 868 2019
JRNL REFN ISSN 0014-5793
JRNL PMID 30883732
JRNL DOI 10.1002/1873-3468.13360
REMARK 2
REMARK 2 RESOLUTION. 3.27 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.27
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.48
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.7
REMARK 3 NUMBER OF REFLECTIONS : 36317
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.420
REMARK 3 FREE R VALUE TEST SET COUNT : 1970
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 46.4835 - 7.8662 0.90 2579 147 0.1762 0.1904
REMARK 3 2 7.8662 - 6.2485 0.95 2592 149 0.1993 0.2237
REMARK 3 3 6.2485 - 5.4600 0.95 2577 150 0.2194 0.2499
REMARK 3 4 5.4600 - 4.9614 0.94 2551 146 0.2129 0.2197
REMARK 3 5 4.9614 - 4.6062 0.95 2505 143 0.1883 0.2287
REMARK 3 6 4.6062 - 4.3348 0.94 2502 145 0.2092 0.2351
REMARK 3 7 4.3348 - 4.1178 0.94 2498 144 0.2270 0.2291
REMARK 3 8 4.1178 - 3.9387 0.96 2536 143 0.2507 0.2731
REMARK 3 9 3.9387 - 3.7871 0.95 2529 142 0.2628 0.2553
REMARK 3 10 3.7871 - 3.6565 0.97 2559 147 0.2634 0.2845
REMARK 3 11 3.6565 - 3.5422 0.97 2538 146 0.3018 0.3162
REMARK 3 12 3.5422 - 3.4410 0.97 2542 147 0.2930 0.3124
REMARK 3 13 3.4410 - 3.3504 0.87 2290 132 0.2931 0.3333
REMARK 3 14 3.3504 - 3.2687 0.59 1549 89 0.3090 0.3180
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.560
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 13616
REMARK 3 ANGLE : 0.662 18495
REMARK 3 CHIRALITY : 0.040 1943
REMARK 3 PLANARITY : 0.005 2374
REMARK 3 DIHEDRAL : 14.591 8039
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 10 THROUGH 192 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.5247 15.5831 -32.0904
REMARK 3 T TENSOR
REMARK 3 T11: 0.2935 T22: 0.2401
REMARK 3 T33: 0.1943 T12: 0.0473
REMARK 3 T13: -0.0842 T23: -0.0416
REMARK 3 L TENSOR
REMARK 3 L11: 3.6503 L22: 5.2454
REMARK 3 L33: 2.3203 L12: 0.2939
REMARK 3 L13: 0.3691 L23: -1.0044
REMARK 3 S TENSOR
REMARK 3 S11: -0.0937 S12: 0.0485 S13: 0.1877
REMARK 3 S21: -0.0129 S22: 0.0782 S23: -0.1478
REMARK 3 S31: -0.1577 S32: 0.0794 S33: 0.0283
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 193 THROUGH 392 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.9937 14.0214 -56.1228
REMARK 3 T TENSOR
REMARK 3 T11: 0.5155 T22: 0.5081
REMARK 3 T33: 0.4966 T12: -0.0439
REMARK 3 T13: 0.0052 T23: -0.0205
REMARK 3 L TENSOR
REMARK 3 L11: 4.2936 L22: 0.8819
REMARK 3 L33: 2.7085 L12: -1.0023
REMARK 3 L13: -2.1854 L23: 0.7310
REMARK 3 S TENSOR
REMARK 3 S11: 0.1621 S12: 0.2400 S13: 0.4991
REMARK 3 S21: -0.4425 S22: 0.0990 S23: -0.3382
REMARK 3 S31: -0.2107 S32: 0.4583 S33: -0.2697
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 393 THROUGH 729 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.5850 2.9958 -28.9679
REMARK 3 T TENSOR
REMARK 3 T11: 0.2966 T22: 0.8348
REMARK 3 T33: 0.7625 T12: 0.1259
REMARK 3 T13: -0.1445 T23: -0.2002
REMARK 3 L TENSOR
REMARK 3 L11: 1.6284 L22: 1.7457
REMARK 3 L33: 1.9725 L12: 0.7141
REMARK 3 L13: -0.1894 L23: 0.2452
REMARK 3 S TENSOR
REMARK 3 S11: 0.1520 S12: 0.0294 S13: -0.0794
REMARK 3 S21: 0.2836 S22: 0.2474 S23: -0.7045
REMARK 3 S31: 0.0475 S32: 0.8782 S33: -0.1666
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 730 THROUGH 855 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.8795 -19.7787 -29.7004
REMARK 3 T TENSOR
REMARK 3 T11: 0.6567 T22: 0.3298
REMARK 3 T33: 0.5109 T12: 0.1262
REMARK 3 T13: -0.1948 T23: 0.0178
REMARK 3 L TENSOR
REMARK 3 L11: 2.4090 L22: 1.9026
REMARK 3 L33: 3.4449 L12: 0.5647
REMARK 3 L13: 0.6066 L23: -0.1345
REMARK 3 S TENSOR
REMARK 3 S11: 0.2301 S12: 0.0207 S13: -0.6546
REMARK 3 S21: 0.2344 S22: 0.1625 S23: -0.1678
REMARK 3 S31: 0.7340 S32: 0.4837 S33: -0.3391
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 10 THROUGH 192 )
REMARK 3 ORIGIN FOR THE GROUP (A): -38.4056 -29.1382 -65.8649
REMARK 3 T TENSOR
REMARK 3 T11: 0.3678 T22: 0.2539
REMARK 3 T33: 0.2256 T12: -0.0126
REMARK 3 T13: -0.1549 T23: -0.0239
REMARK 3 L TENSOR
REMARK 3 L11: 2.4327 L22: 4.0376
REMARK 3 L33: 2.5122 L12: -0.2666
REMARK 3 L13: -0.7365 L23: -0.5442
REMARK 3 S TENSOR
REMARK 3 S11: -0.0670 S12: 0.0803 S13: -0.0539
REMARK 3 S21: -0.2422 S22: 0.0597 S23: 0.0525
REMARK 3 S31: 0.2085 S32: -0.0542 S33: 0.0101
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 193 THROUGH 411 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.7253 -28.0551 -55.6637
REMARK 3 T TENSOR
REMARK 3 T11: 0.5634 T22: 0.4968
REMARK 3 T33: 0.6997 T12: 0.1672
REMARK 3 T13: -0.1375 T23: -0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 3.6386 L22: 0.8250
REMARK 3 L33: 1.7285 L12: 1.1501
REMARK 3 L13: 0.5845 L23: -0.2842
REMARK 3 S TENSOR
REMARK 3 S11: 0.2402 S12: 0.1430 S13: -0.1075
REMARK 3 S21: 0.1427 S22: -0.2292 S23: -0.5537
REMARK 3 S31: 0.2326 S32: 0.6776 S33: 0.0190
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 412 THROUGH 673 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.6867 -18.7787 -87.1760
REMARK 3 T TENSOR
REMARK 3 T11: 0.8293 T22: 0.8497
REMARK 3 T33: 0.5769 T12: 0.2886
REMARK 3 T13: 0.2206 T23: 0.1486
REMARK 3 L TENSOR
REMARK 3 L11: 3.6579 L22: 2.2092
REMARK 3 L33: 1.7444 L12: -0.4994
REMARK 3 L13: 0.6920 L23: 0.0814
REMARK 3 S TENSOR
REMARK 3 S11: 0.2110 S12: 0.4041 S13: -0.2101
REMARK 3 S21: -0.6112 S22: -0.2713 S23: -0.6682
REMARK 3 S31: 0.2550 S32: 0.6653 S33: 0.0407
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 674 THROUGH 855 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.3718 2.5103 -75.9278
REMARK 3 T TENSOR
REMARK 3 T11: 0.6292 T22: 0.3634
REMARK 3 T33: 0.4027 T12: 0.0655
REMARK 3 T13: -0.0747 T23: 0.1038
REMARK 3 L TENSOR
REMARK 3 L11: 1.0322 L22: 2.3053
REMARK 3 L33: 4.2045 L12: -0.4673
REMARK 3 L13: -0.3180 L23: 1.0983
REMARK 3 S TENSOR
REMARK 3 S11: 0.1061 S12: 0.2486 S13: 0.2918
REMARK 3 S21: -0.6221 S22: -0.0764 S23: -0.0151
REMARK 3 S31: -0.4510 S32: 0.2679 S33: -0.0205
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6J7A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1300010608.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-DEC-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36941
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.250
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.45500
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 6J79
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 20000, MES-NAOH, ETHYL ACETATE, PH
REMARK 280 6.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 41.34300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 94.41600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 80.09550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 94.41600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.34300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 80.09550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 GLU A 2
REMARK 465 ARG A 3
REMARK 465 PRO A 4
REMARK 465 GLN A 5
REMARK 465 LEU A 6
REMARK 465 ASP A 7
REMARK 465 SER A 8
REMARK 465 MET A 9
REMARK 465 GLU A 223
REMARK 465 GLU A 224
REMARK 465 HIS A 225
REMARK 465 LYS A 226
REMARK 465 ASP A 227
REMARK 465 GLN A 228
REMARK 465 SER A 229
REMARK 465 ALA A 230
REMARK 465 SER A 231
REMARK 465 GLN A 232
REMARK 465 THR A 233
REMARK 465 GLU A 234
REMARK 465 PHE A 235
REMARK 465 LEU A 236
REMARK 465 ARG A 237
REMARK 465 MET A 238
REMARK 465 GLN A 239
REMARK 465 THR A 240
REMARK 465 THR A 241
REMARK 465 ALA A 242
REMARK 465 PRO A 243
REMARK 465 PRO A 244
REMARK 465 VAL A 245
REMARK 465 LYS A 246
REMARK 465 GLU A 247
REMARK 465 ALA A 677
REMARK 465 GLY A 678
REMARK 465 GLU A 679
REMARK 465 ASN A 680
REMARK 465 GLY A 681
REMARK 465 GLY A 682
REMARK 465 ARG A 683
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 ARG B 3
REMARK 465 PRO B 4
REMARK 465 GLN B 5
REMARK 465 LEU B 6
REMARK 465 ASP B 7
REMARK 465 SER B 8
REMARK 465 MET B 9
REMARK 465 GLU B 223
REMARK 465 GLU B 224
REMARK 465 HIS B 225
REMARK 465 LYS B 226
REMARK 465 ASP B 227
REMARK 465 GLN B 228
REMARK 465 SER B 229
REMARK 465 ALA B 230
REMARK 465 SER B 231
REMARK 465 GLN B 232
REMARK 465 THR B 233
REMARK 465 GLU B 234
REMARK 465 PHE B 235
REMARK 465 LEU B 236
REMARK 465 ARG B 237
REMARK 465 MET B 238
REMARK 465 GLN B 239
REMARK 465 THR B 240
REMARK 465 THR B 241
REMARK 465 ALA B 242
REMARK 465 PRO B 243
REMARK 465 PRO B 244
REMARK 465 VAL B 245
REMARK 465 LYS B 246
REMARK 465 GLU B 247
REMARK 465 GLU B 415
REMARK 465 ALA B 416
REMARK 465 SER B 417
REMARK 465 SER B 418
REMARK 465 ALA B 677
REMARK 465 GLY B 678
REMARK 465 GLU B 679
REMARK 465 ASN B 680
REMARK 465 GLY B 681
REMARK 465 GLY B 682
REMARK 465 ARG B 683
REMARK 465 GLN B 776
REMARK 465 ALA B 777
REMARK 465 HIS B 778
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 HIS A 284 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A 285 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 341 CG OD1 OD2
REMARK 470 GLU A 395 CG CD OE1 OE2
REMARK 470 GLU A 415 CG CD OE1 OE2
REMARK 470 ARG A 811 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 339 CG CD OE1 OE2
REMARK 470 LYS B 357 CG CD CE NZ
REMARK 470 LYS B 581 CG CD CE NZ
REMARK 470 LYS B 779 CG CD CE NZ
REMARK 470 ARG B 811 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU B 337 CA - CB - CG ANGL. DEV. = 16.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLN A 41 78.81 -109.99
REMARK 500 SER A 43 159.08 63.58
REMARK 500 HIS A 100 41.52 -104.46
REMARK 500 ARG A 136 -64.34 -93.23
REMARK 500 SER A 142 -83.25 -115.91
REMARK 500 MET A 288 -159.41 -100.41
REMARK 500 GLU A 297 36.93 -90.48
REMARK 500 LEU A 300 2.06 -66.65
REMARK 500 GLU A 323 56.69 -98.93
REMARK 500 GLN A 338 -72.74 -69.61
REMARK 500 ASP A 341 26.56 -146.03
REMARK 500 LEU A 344 54.31 -106.89
REMARK 500 SER A 417 117.17 64.78
REMARK 500 ASP A 454 -155.71 -152.07
REMARK 500 ASN A 466 74.11 -162.24
REMARK 500 LEU A 528 30.49 -88.06
REMARK 500 ASN A 533 3.35 -67.60
REMARK 500 ILE A 554 18.54 44.07
REMARK 500 GLU A 588 5.63 -66.02
REMARK 500 GLU A 654 118.67 -162.81
REMARK 500 ARG A 744 -75.45 -86.47
REMARK 500 GLU A 748 -71.23 -108.50
REMARK 500 GLN A 776 -155.39 -145.16
REMARK 500 ASP A 789 30.42 -84.91
REMARK 500 GLN B 41 70.17 -108.47
REMARK 500 HIS B 100 42.90 -105.07
REMARK 500 ARG B 136 -64.74 -93.21
REMARK 500 SER B 142 -80.87 -114.76
REMARK 500 ALA B 156 70.69 54.37
REMARK 500 ARG B 285 31.79 -90.77
REMARK 500 GLU B 297 36.38 -90.08
REMARK 500 LEU B 300 1.68 -67.99
REMARK 500 GLU B 323 56.49 -98.84
REMARK 500 GLN B 338 -70.06 -66.83
REMARK 500 ASP B 341 26.42 -147.26
REMARK 500 LEU B 344 54.76 -104.58
REMARK 500 ASP B 454 -156.70 -152.07
REMARK 500 ASN B 466 74.20 -162.24
REMARK 500 LEU B 528 30.54 -87.47
REMARK 500 ASN B 533 4.55 -68.60
REMARK 500 GLU B 654 118.50 -163.08
REMARK 500 ARG B 744 -76.22 -86.54
REMARK 500 GLU B 748 -72.04 -108.22
REMARK 500 ALA B 810 -89.97 -52.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 901 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 25 NE2
REMARK 620 2 HEM A 901 NA 89.6
REMARK 620 3 HEM A 901 NB 85.9 85.0
REMARK 620 4 HEM A 901 NC 81.7 169.3 88.1
REMARK 620 5 HEM A 901 ND 82.6 90.9 167.9 94.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 901 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 25 NE2
REMARK 620 2 HEM B 901 NA 91.1
REMARK 620 3 HEM B 901 NB 88.6 84.9
REMARK 620 4 HEM B 901 NC 80.7 169.3 88.1
REMARK 620 5 HEM B 901 ND 80.1 90.9 167.9 94.4
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMN A 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMN B 903
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6J79 RELATED DB: PDB
REMARK 900 PDB ENTRIES FOR THE SAME CITATION
DBREF 6J7A A 1 237 UNP P06762 HMOX1_RAT 1 237
DBREF 6J7A A 239 855 UNP P00388 NCPR_RAT 58 678
DBREF 6J7A B 1 237 UNP P06762 HMOX1_RAT 1 237
DBREF 6J7A B 239 855 UNP P00388 NCPR_RAT 58 678
SEQADV 6J7A MET A -19 UNP P06762 INITIATING METHIONINE
SEQADV 6J7A GLY A -18 UNP P06762 EXPRESSION TAG
SEQADV 6J7A SER A -17 UNP P06762 EXPRESSION TAG
SEQADV 6J7A SER A -16 UNP P06762 EXPRESSION TAG
SEQADV 6J7A HIS A -15 UNP P06762 EXPRESSION TAG
SEQADV 6J7A HIS A -14 UNP P06762 EXPRESSION TAG
SEQADV 6J7A HIS A -13 UNP P06762 EXPRESSION TAG
SEQADV 6J7A HIS A -12 UNP P06762 EXPRESSION TAG
SEQADV 6J7A HIS A -11 UNP P06762 EXPRESSION TAG
SEQADV 6J7A HIS A -10 UNP P06762 EXPRESSION TAG
SEQADV 6J7A SER A -9 UNP P06762 EXPRESSION TAG
SEQADV 6J7A SER A -8 UNP P06762 EXPRESSION TAG
SEQADV 6J7A GLY A -7 UNP P06762 EXPRESSION TAG
SEQADV 6J7A LEU A -6 UNP P06762 EXPRESSION TAG
SEQADV 6J7A VAL A -5 UNP P06762 EXPRESSION TAG
SEQADV 6J7A PRO A -4 UNP P06762 EXPRESSION TAG
SEQADV 6J7A ARG A -3 UNP P06762 EXPRESSION TAG
SEQADV 6J7A GLY A -2 UNP P06762 EXPRESSION TAG
SEQADV 6J7A SER A -1 UNP P06762 EXPRESSION TAG
SEQADV 6J7A HIS A 0 UNP P06762 EXPRESSION TAG
SEQADV 6J7A PRO A 222 UNP P06762 THR 222 ENGINEERED MUTATION
SEQADV 6J7A ALA A 230 UNP P06762 PRO 230 ENGINEERED MUTATION
SEQADV 6J7A MET A 238 UNP P06762 LINKER
SEQADV 6J7A A UNP P00388 THR 236 DELETION
SEQADV 6J7A A UNP P00388 GLY 237 DELETION
SEQADV 6J7A A UNP P00388 GLU 238 DELETION
SEQADV 6J7A A UNP P00388 GLU 239 DELETION
SEQADV 6J7A MET B -19 UNP P06762 INITIATING METHIONINE
SEQADV 6J7A GLY B -18 UNP P06762 EXPRESSION TAG
SEQADV 6J7A SER B -17 UNP P06762 EXPRESSION TAG
SEQADV 6J7A SER B -16 UNP P06762 EXPRESSION TAG
SEQADV 6J7A HIS B -15 UNP P06762 EXPRESSION TAG
SEQADV 6J7A HIS B -14 UNP P06762 EXPRESSION TAG
SEQADV 6J7A HIS B -13 UNP P06762 EXPRESSION TAG
SEQADV 6J7A HIS B -12 UNP P06762 EXPRESSION TAG
SEQADV 6J7A HIS B -11 UNP P06762 EXPRESSION TAG
SEQADV 6J7A HIS B -10 UNP P06762 EXPRESSION TAG
SEQADV 6J7A SER B -9 UNP P06762 EXPRESSION TAG
SEQADV 6J7A SER B -8 UNP P06762 EXPRESSION TAG
SEQADV 6J7A GLY B -7 UNP P06762 EXPRESSION TAG
SEQADV 6J7A LEU B -6 UNP P06762 EXPRESSION TAG
SEQADV 6J7A VAL B -5 UNP P06762 EXPRESSION TAG
SEQADV 6J7A PRO B -4 UNP P06762 EXPRESSION TAG
SEQADV 6J7A ARG B -3 UNP P06762 EXPRESSION TAG
SEQADV 6J7A GLY B -2 UNP P06762 EXPRESSION TAG
SEQADV 6J7A SER B -1 UNP P06762 EXPRESSION TAG
SEQADV 6J7A HIS B 0 UNP P06762 EXPRESSION TAG
SEQADV 6J7A PRO B 222 UNP P06762 THR 222 ENGINEERED MUTATION
SEQADV 6J7A ALA B 230 UNP P06762 PRO 230 ENGINEERED MUTATION
SEQADV 6J7A MET B 238 UNP P06762 LINKER
SEQADV 6J7A B UNP P00388 THR 236 DELETION
SEQADV 6J7A B UNP P00388 GLY 237 DELETION
SEQADV 6J7A B UNP P00388 GLU 238 DELETION
SEQADV 6J7A B UNP P00388 GLU 239 DELETION
SEQRES 1 A 875 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 875 LEU VAL PRO ARG GLY SER HIS MET GLU ARG PRO GLN LEU
SEQRES 3 A 875 ASP SER MET SER GLN ASP LEU SER GLU ALA LEU LYS GLU
SEQRES 4 A 875 ALA THR LYS GLU VAL HIS ILE ARG ALA GLU ASN SER GLU
SEQRES 5 A 875 PHE MET ARG ASN PHE GLN LYS GLY GLN VAL SER ARG GLU
SEQRES 6 A 875 GLY PHE LYS LEU VAL MET ALA SER LEU TYR HIS ILE TYR
SEQRES 7 A 875 THR ALA LEU GLU GLU GLU ILE GLU ARG ASN LYS GLN ASN
SEQRES 8 A 875 PRO VAL TYR ALA PRO LEU TYR PHE PRO GLU GLU LEU HIS
SEQRES 9 A 875 ARG ARG ALA ALA LEU GLU GLN ASP MET ALA PHE TRP TYR
SEQRES 10 A 875 GLY PRO HIS TRP GLN GLU ALA ILE PRO TYR THR PRO ALA
SEQRES 11 A 875 THR GLN HIS TYR VAL LYS ARG LEU HIS GLU VAL GLY GLY
SEQRES 12 A 875 THR HIS PRO GLU LEU LEU VAL ALA HIS ALA TYR THR ARG
SEQRES 13 A 875 TYR LEU GLY ASP LEU SER GLY GLY GLN VAL LEU LYS LYS
SEQRES 14 A 875 ILE ALA GLN LYS ALA MET ALA LEU PRO SER SER GLY GLU
SEQRES 15 A 875 GLY LEU ALA PHE PHE THR PHE PRO SER ILE ASP ASN PRO
SEQRES 16 A 875 THR LYS PHE LYS GLN LEU TYR ARG ALA ARG MET ASN THR
SEQRES 17 A 875 LEU GLU MET THR PRO GLU VAL LYS HIS ARG VAL THR GLU
SEQRES 18 A 875 GLU ALA LYS THR ALA PHE LEU LEU ASN ILE GLU LEU PHE
SEQRES 19 A 875 GLU GLU LEU GLN ALA LEU LEU PRO GLU GLU HIS LYS ASP
SEQRES 20 A 875 GLN SER ALA SER GLN THR GLU PHE LEU ARG MET GLN THR
SEQRES 21 A 875 THR ALA PRO PRO VAL LYS GLU SER SER PHE VAL GLU LYS
SEQRES 22 A 875 MET LYS LYS THR GLY ARG ASN ILE ILE VAL PHE TYR GLY
SEQRES 23 A 875 SER GLN THR GLY THR ALA GLU GLU PHE ALA ASN ARG LEU
SEQRES 24 A 875 SER LYS ASP ALA HIS ARG TYR GLY MET ARG GLY MET SER
SEQRES 25 A 875 ALA ASP PRO GLU GLU TYR ASP LEU ALA ASP LEU SER SER
SEQRES 26 A 875 LEU PRO GLU ILE ASP LYS SER LEU VAL VAL PHE CYS MET
SEQRES 27 A 875 ALA THR TYR GLY GLU GLY ASP PRO THR ASP ASN ALA GLN
SEQRES 28 A 875 ASP PHE TYR ASP TRP LEU GLN GLU THR ASP VAL ASP LEU
SEQRES 29 A 875 THR GLY VAL LYS PHE ALA VAL PHE GLY LEU GLY ASN LYS
SEQRES 30 A 875 THR TYR GLU HIS PHE ASN ALA MET GLY LYS TYR VAL ASP
SEQRES 31 A 875 GLN ARG LEU GLU GLN LEU GLY ALA GLN ARG ILE PHE GLU
SEQRES 32 A 875 LEU GLY LEU GLY ASP ASP ASP GLY ASN LEU GLU GLU ASP
SEQRES 33 A 875 PHE ILE THR TRP ARG GLU GLN PHE TRP PRO ALA VAL CYS
SEQRES 34 A 875 GLU PHE PHE GLY VAL GLU ALA SER SER ILE ARG GLN TYR
SEQRES 35 A 875 GLU LEU VAL VAL HIS GLU ASP MET ASP VAL ALA LYS VAL
SEQRES 36 A 875 TYR THR GLY GLU MET GLY ARG LEU LYS SER TYR GLU ASN
SEQRES 37 A 875 GLN LYS PRO PRO PHE ASP ALA LYS ASN PRO PHE LEU ALA
SEQRES 38 A 875 ALA VAL THR ALA ASN ARG LYS LEU ASN GLN GLY THR GLU
SEQRES 39 A 875 ARG HIS LEU MET HIS LEU GLU LEU ASP ILE SER ASP SER
SEQRES 40 A 875 LYS ILE ARG TYR GLU SER GLY ASP HIS VAL ALA VAL TYR
SEQRES 41 A 875 PRO ALA ASN ASP SER ALA LEU VAL ASN GLN ILE GLY GLU
SEQRES 42 A 875 ILE LEU GLY ALA ASP LEU ASP VAL ILE MET SER LEU ASN
SEQRES 43 A 875 ASN LEU ASP GLU GLU SER ASN LYS LYS HIS PRO PHE PRO
SEQRES 44 A 875 CYS PRO THR THR TYR ARG THR ALA LEU THR TYR TYR LEU
SEQRES 45 A 875 ASP ILE THR ASN PRO PRO ARG THR ASN VAL LEU TYR GLU
SEQRES 46 A 875 LEU ALA GLN TYR ALA SER GLU PRO SER GLU GLN GLU HIS
SEQRES 47 A 875 LEU HIS LYS MET ALA SER SER SER GLY GLU GLY LYS GLU
SEQRES 48 A 875 LEU TYR LEU SER TRP VAL VAL GLU ALA ARG ARG HIS ILE
SEQRES 49 A 875 LEU ALA ILE LEU GLN ASP TYR PRO SER LEU ARG PRO PRO
SEQRES 50 A 875 ILE ASP HIS LEU CYS GLU LEU LEU PRO ARG LEU GLN ALA
SEQRES 51 A 875 ARG TYR TYR SER ILE ALA SER SER SER LYS VAL HIS PRO
SEQRES 52 A 875 ASN SER VAL HIS ILE CYS ALA VAL ALA VAL GLU TYR GLU
SEQRES 53 A 875 ALA LYS SER GLY ARG VAL ASN LYS GLY VAL ALA THR SER
SEQRES 54 A 875 TRP LEU ARG ALA LYS GLU PRO ALA GLY GLU ASN GLY GLY
SEQRES 55 A 875 ARG ALA LEU VAL PRO MET PHE VAL ARG LYS SER GLN PHE
SEQRES 56 A 875 ARG LEU PRO PHE LYS SER THR THR PRO VAL ILE MET VAL
SEQRES 57 A 875 GLY PRO GLY THR GLY ILE ALA PRO PHE MET GLY PHE ILE
SEQRES 58 A 875 GLN GLU ARG ALA TRP LEU ARG GLU GLN GLY LYS GLU VAL
SEQRES 59 A 875 GLY GLU THR LEU LEU TYR TYR GLY CYS ARG ARG SER ASP
SEQRES 60 A 875 GLU ASP TYR LEU TYR ARG GLU GLU LEU ALA ARG PHE HIS
SEQRES 61 A 875 LYS ASP GLY ALA LEU THR GLN LEU ASN VAL ALA PHE SER
SEQRES 62 A 875 ARG GLU GLN ALA HIS LYS VAL TYR VAL GLN HIS LEU LEU
SEQRES 63 A 875 LYS ARG ASP ARG GLU HIS LEU TRP LYS LEU ILE HIS GLU
SEQRES 64 A 875 GLY GLY ALA HIS ILE TYR VAL CYS GLY ASP ALA ARG ASN
SEQRES 65 A 875 MET ALA LYS ASP VAL GLN ASN THR PHE TYR ASP ILE VAL
SEQRES 66 A 875 ALA GLU PHE GLY PRO MET GLU HIS THR GLN ALA VAL ASP
SEQRES 67 A 875 TYR VAL LYS LYS LEU MET THR LYS GLY ARG TYR SER LEU
SEQRES 68 A 875 ASP VAL TRP SER
SEQRES 1 B 875 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 875 LEU VAL PRO ARG GLY SER HIS MET GLU ARG PRO GLN LEU
SEQRES 3 B 875 ASP SER MET SER GLN ASP LEU SER GLU ALA LEU LYS GLU
SEQRES 4 B 875 ALA THR LYS GLU VAL HIS ILE ARG ALA GLU ASN SER GLU
SEQRES 5 B 875 PHE MET ARG ASN PHE GLN LYS GLY GLN VAL SER ARG GLU
SEQRES 6 B 875 GLY PHE LYS LEU VAL MET ALA SER LEU TYR HIS ILE TYR
SEQRES 7 B 875 THR ALA LEU GLU GLU GLU ILE GLU ARG ASN LYS GLN ASN
SEQRES 8 B 875 PRO VAL TYR ALA PRO LEU TYR PHE PRO GLU GLU LEU HIS
SEQRES 9 B 875 ARG ARG ALA ALA LEU GLU GLN ASP MET ALA PHE TRP TYR
SEQRES 10 B 875 GLY PRO HIS TRP GLN GLU ALA ILE PRO TYR THR PRO ALA
SEQRES 11 B 875 THR GLN HIS TYR VAL LYS ARG LEU HIS GLU VAL GLY GLY
SEQRES 12 B 875 THR HIS PRO GLU LEU LEU VAL ALA HIS ALA TYR THR ARG
SEQRES 13 B 875 TYR LEU GLY ASP LEU SER GLY GLY GLN VAL LEU LYS LYS
SEQRES 14 B 875 ILE ALA GLN LYS ALA MET ALA LEU PRO SER SER GLY GLU
SEQRES 15 B 875 GLY LEU ALA PHE PHE THR PHE PRO SER ILE ASP ASN PRO
SEQRES 16 B 875 THR LYS PHE LYS GLN LEU TYR ARG ALA ARG MET ASN THR
SEQRES 17 B 875 LEU GLU MET THR PRO GLU VAL LYS HIS ARG VAL THR GLU
SEQRES 18 B 875 GLU ALA LYS THR ALA PHE LEU LEU ASN ILE GLU LEU PHE
SEQRES 19 B 875 GLU GLU LEU GLN ALA LEU LEU PRO GLU GLU HIS LYS ASP
SEQRES 20 B 875 GLN SER ALA SER GLN THR GLU PHE LEU ARG MET GLN THR
SEQRES 21 B 875 THR ALA PRO PRO VAL LYS GLU SER SER PHE VAL GLU LYS
SEQRES 22 B 875 MET LYS LYS THR GLY ARG ASN ILE ILE VAL PHE TYR GLY
SEQRES 23 B 875 SER GLN THR GLY THR ALA GLU GLU PHE ALA ASN ARG LEU
SEQRES 24 B 875 SER LYS ASP ALA HIS ARG TYR GLY MET ARG GLY MET SER
SEQRES 25 B 875 ALA ASP PRO GLU GLU TYR ASP LEU ALA ASP LEU SER SER
SEQRES 26 B 875 LEU PRO GLU ILE ASP LYS SER LEU VAL VAL PHE CYS MET
SEQRES 27 B 875 ALA THR TYR GLY GLU GLY ASP PRO THR ASP ASN ALA GLN
SEQRES 28 B 875 ASP PHE TYR ASP TRP LEU GLN GLU THR ASP VAL ASP LEU
SEQRES 29 B 875 THR GLY VAL LYS PHE ALA VAL PHE GLY LEU GLY ASN LYS
SEQRES 30 B 875 THR TYR GLU HIS PHE ASN ALA MET GLY LYS TYR VAL ASP
SEQRES 31 B 875 GLN ARG LEU GLU GLN LEU GLY ALA GLN ARG ILE PHE GLU
SEQRES 32 B 875 LEU GLY LEU GLY ASP ASP ASP GLY ASN LEU GLU GLU ASP
SEQRES 33 B 875 PHE ILE THR TRP ARG GLU GLN PHE TRP PRO ALA VAL CYS
SEQRES 34 B 875 GLU PHE PHE GLY VAL GLU ALA SER SER ILE ARG GLN TYR
SEQRES 35 B 875 GLU LEU VAL VAL HIS GLU ASP MET ASP VAL ALA LYS VAL
SEQRES 36 B 875 TYR THR GLY GLU MET GLY ARG LEU LYS SER TYR GLU ASN
SEQRES 37 B 875 GLN LYS PRO PRO PHE ASP ALA LYS ASN PRO PHE LEU ALA
SEQRES 38 B 875 ALA VAL THR ALA ASN ARG LYS LEU ASN GLN GLY THR GLU
SEQRES 39 B 875 ARG HIS LEU MET HIS LEU GLU LEU ASP ILE SER ASP SER
SEQRES 40 B 875 LYS ILE ARG TYR GLU SER GLY ASP HIS VAL ALA VAL TYR
SEQRES 41 B 875 PRO ALA ASN ASP SER ALA LEU VAL ASN GLN ILE GLY GLU
SEQRES 42 B 875 ILE LEU GLY ALA ASP LEU ASP VAL ILE MET SER LEU ASN
SEQRES 43 B 875 ASN LEU ASP GLU GLU SER ASN LYS LYS HIS PRO PHE PRO
SEQRES 44 B 875 CYS PRO THR THR TYR ARG THR ALA LEU THR TYR TYR LEU
SEQRES 45 B 875 ASP ILE THR ASN PRO PRO ARG THR ASN VAL LEU TYR GLU
SEQRES 46 B 875 LEU ALA GLN TYR ALA SER GLU PRO SER GLU GLN GLU HIS
SEQRES 47 B 875 LEU HIS LYS MET ALA SER SER SER GLY GLU GLY LYS GLU
SEQRES 48 B 875 LEU TYR LEU SER TRP VAL VAL GLU ALA ARG ARG HIS ILE
SEQRES 49 B 875 LEU ALA ILE LEU GLN ASP TYR PRO SER LEU ARG PRO PRO
SEQRES 50 B 875 ILE ASP HIS LEU CYS GLU LEU LEU PRO ARG LEU GLN ALA
SEQRES 51 B 875 ARG TYR TYR SER ILE ALA SER SER SER LYS VAL HIS PRO
SEQRES 52 B 875 ASN SER VAL HIS ILE CYS ALA VAL ALA VAL GLU TYR GLU
SEQRES 53 B 875 ALA LYS SER GLY ARG VAL ASN LYS GLY VAL ALA THR SER
SEQRES 54 B 875 TRP LEU ARG ALA LYS GLU PRO ALA GLY GLU ASN GLY GLY
SEQRES 55 B 875 ARG ALA LEU VAL PRO MET PHE VAL ARG LYS SER GLN PHE
SEQRES 56 B 875 ARG LEU PRO PHE LYS SER THR THR PRO VAL ILE MET VAL
SEQRES 57 B 875 GLY PRO GLY THR GLY ILE ALA PRO PHE MET GLY PHE ILE
SEQRES 58 B 875 GLN GLU ARG ALA TRP LEU ARG GLU GLN GLY LYS GLU VAL
SEQRES 59 B 875 GLY GLU THR LEU LEU TYR TYR GLY CYS ARG ARG SER ASP
SEQRES 60 B 875 GLU ASP TYR LEU TYR ARG GLU GLU LEU ALA ARG PHE HIS
SEQRES 61 B 875 LYS ASP GLY ALA LEU THR GLN LEU ASN VAL ALA PHE SER
SEQRES 62 B 875 ARG GLU GLN ALA HIS LYS VAL TYR VAL GLN HIS LEU LEU
SEQRES 63 B 875 LYS ARG ASP ARG GLU HIS LEU TRP LYS LEU ILE HIS GLU
SEQRES 64 B 875 GLY GLY ALA HIS ILE TYR VAL CYS GLY ASP ALA ARG ASN
SEQRES 65 B 875 MET ALA LYS ASP VAL GLN ASN THR PHE TYR ASP ILE VAL
SEQRES 66 B 875 ALA GLU PHE GLY PRO MET GLU HIS THR GLN ALA VAL ASP
SEQRES 67 B 875 TYR VAL LYS LYS LEU MET THR LYS GLY ARG TYR SER LEU
SEQRES 68 B 875 ASP VAL TRP SER
HET HEM A 901 43
HET FAD A 902 53
HET FMN A 903 31
HET HEM B 901 43
HET FAD B 902 53
HET FMN B 903 31
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETSYN HEM HEME
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 FAD 2(C27 H33 N9 O15 P2)
FORMUL 5 FMN 2(C17 H21 N4 O9 P)
FORMUL 9 HOH *3(H2 O)
HELIX 1 AA1 ASP A 12 THR A 21 1 10
HELIX 2 AA2 THR A 21 ASN A 30 1 10
HELIX 3 AA3 SER A 31 LYS A 39 1 9
HELIX 4 AA4 SER A 43 ASN A 68 1 26
HELIX 5 AA5 TYR A 74 TYR A 78 5 5
HELIX 6 AA6 PHE A 79 HIS A 84 1 6
HELIX 7 AA7 ARG A 85 GLY A 98 1 14
HELIX 8 AA8 HIS A 100 ILE A 105 1 6
HELIX 9 AA9 THR A 108 HIS A 125 1 18
HELIX 10 AB1 LEU A 128 LEU A 141 1 14
HELIX 11 AB2 GLY A 143 ALA A 156 1 14
HELIX 12 AB3 LEU A 164 THR A 168 5 5
HELIX 13 AB4 ASN A 174 THR A 188 1 15
HELIX 14 AB5 THR A 192 LEU A 220 1 29
HELIX 15 AB6 SER A 249 GLY A 258 1 10
HELIX 16 AB7 GLY A 270 ARG A 285 1 16
HELIX 17 AB8 ASP A 299 SER A 304 5 6
HELIX 18 AB9 SER A 305 ILE A 309 5 5
HELIX 19 AC1 ALA A 330 LEU A 337 1 8
HELIX 20 AC2 ASN A 363 GLU A 374 1 12
HELIX 21 AC3 ASN A 392 GLY A 413 1 22
HELIX 22 AC4 ASP A 431 VAL A 435 5 5
HELIX 23 AC5 ASP A 504 GLY A 516 1 13
HELIX 24 AC6 TYR A 544 TYR A 551 1 8
HELIX 25 AC7 ARG A 559 GLN A 568 1 10
HELIX 26 AC8 GLU A 572 MET A 582 1 11
HELIX 27 AC9 GLY A 587 VAL A 597 1 11
HELIX 28 AD1 HIS A 603 TYR A 611 1 9
HELIX 29 AD2 PRO A 617 LEU A 625 1 9
HELIX 30 AD3 GLY A 665 ALA A 673 1 9
HELIX 31 AD4 ILE A 714 GLN A 730 1 17
HELIX 32 AD5 TYR A 752 ASP A 762 1 11
HELIX 33 AD6 TYR A 781 ASP A 789 1 9
HELIX 34 AD7 ASP A 789 GLU A 799 1 11
HELIX 35 AD8 ASN A 812 GLY A 829 1 18
HELIX 36 AD9 GLU A 832 LYS A 846 1 15
HELIX 37 AE1 ASP B 12 THR B 21 1 10
HELIX 38 AE2 THR B 21 ASN B 30 1 10
HELIX 39 AE3 SER B 31 LYS B 39 1 9
HELIX 40 AE4 SER B 43 ASN B 68 1 26
HELIX 41 AE5 TYR B 74 TYR B 78 5 5
HELIX 42 AE6 PHE B 79 HIS B 84 1 6
HELIX 43 AE7 ARG B 85 GLY B 98 1 14
HELIX 44 AE8 HIS B 100 ILE B 105 1 6
HELIX 45 AE9 THR B 108 HIS B 125 1 18
HELIX 46 AF1 LEU B 128 LEU B 141 1 14
HELIX 47 AF2 GLY B 143 ALA B 156 1 14
HELIX 48 AF3 LEU B 164 THR B 168 5 5
HELIX 49 AF4 ASN B 174 LEU B 189 1 16
HELIX 50 AF5 THR B 192 ALA B 219 1 28
HELIX 51 AF6 SER B 249 GLY B 258 1 10
HELIX 52 AF7 GLY B 270 ARG B 285 1 16
HELIX 53 AF8 ASP B 299 SER B 304 5 6
HELIX 54 AF9 ALA B 330 GLU B 339 1 10
HELIX 55 AG1 ASN B 363 LEU B 376 1 14
HELIX 56 AG2 ASN B 392 PHE B 412 1 21
HELIX 57 AG3 ASP B 431 VAL B 435 5 5
HELIX 58 AG4 ASP B 504 GLY B 516 1 13
HELIX 59 AG5 TYR B 544 TYR B 551 1 8
HELIX 60 AG6 ARG B 559 ALA B 567 1 9
HELIX 61 AG7 GLN B 568 ALA B 570 5 3
HELIX 62 AG8 GLU B 572 MET B 582 1 11
HELIX 63 AG9 GLU B 588 VAL B 597 1 10
HELIX 64 AH1 HIS B 603 TYR B 611 1 9
HELIX 65 AH2 PRO B 617 LEU B 625 1 9
HELIX 66 AH3 GLY B 665 LYS B 674 1 10
HELIX 67 AH4 ILE B 714 GLN B 730 1 17
HELIX 68 AH5 TYR B 752 ASP B 762 1 11
HELIX 69 AH6 TYR B 781 ASP B 789 1 9
HELIX 70 AH7 ASP B 789 GLU B 799 1 11
HELIX 71 AH8 ASN B 812 PHE B 828 1 17
HELIX 72 AH9 GLU B 832 LYS B 846 1 15
SHEET 1 AA1 5 GLY A 290 ALA A 293 0
SHEET 2 AA1 5 ILE A 261 GLY A 266 1 N VAL A 263 O MET A 291
SHEET 3 AA1 5 LEU A 313 TYR A 321 1 O CYS A 317 N GLY A 266
SHEET 4 AA1 5 LYS A 348 GLY A 355 1 O LYS A 348 N VAL A 314
SHEET 5 AA1 5 GLN A 379 ARG A 380 1 O GLN A 379 N PHE A 349
SHEET 1 AA2 4 ASP A 325 PRO A 326 0
SHEET 2 AA2 4 LEU A 313 TYR A 321 -1 N TYR A 321 O ASP A 325
SHEET 3 AA2 4 LYS A 348 GLY A 355 1 O LYS A 348 N VAL A 314
SHEET 4 AA2 4 GLY A 385 ASP A 388 1 O GLY A 385 N GLY A 353
SHEET 1 AA3 3 TYR A 422 VAL A 426 0
SHEET 2 AA3 3 ILE A 522 ASN A 527 -1 O ASN A 526 N GLU A 423
SHEET 3 AA3 3 THR A 542 THR A 543 -1 O THR A 542 N MET A 523
SHEET 1 AA4 6 ARG A 631 SER A 634 0
SHEET 2 AA4 6 HIS A 496 VAL A 499 -1 N VAL A 497 O TYR A 633
SHEET 3 AA4 6 LEU A 685 ARG A 691 -1 O ARG A 691 N HIS A 496
SHEET 4 AA4 6 PHE A 459 LYS A 468 -1 N PHE A 459 O MET A 688
SHEET 5 AA4 6 LEU A 477 ASP A 483 -1 O ASP A 483 N ALA A 462
SHEET 6 AA4 6 SER A 645 VAL A 651 -1 O ALA A 650 N MET A 478
SHEET 1 AA5 2 GLU A 654 GLU A 656 0
SHEET 2 AA5 2 VAL A 662 LYS A 664 -1 O ASN A 663 N TYR A 655
SHEET 1 AA6 5 GLN A 767 PHE A 772 0
SHEET 2 AA6 5 THR A 737 CYS A 743 1 N TYR A 741 O ALA A 771
SHEET 3 AA6 5 VAL A 705 PRO A 710 1 N MET A 707 O LEU A 738
SHEET 4 AA6 5 HIS A 803 GLY A 808 1 O TYR A 805 N ILE A 706
SHEET 5 AA6 5 TYR A 849 VAL A 853 1 O SER A 850 N ILE A 804
SHEET 1 AA7 5 GLY B 290 ALA B 293 0
SHEET 2 AA7 5 ILE B 261 GLY B 266 1 N VAL B 263 O MET B 291
SHEET 3 AA7 5 LEU B 313 TYR B 321 1 O CYS B 317 N GLY B 266
SHEET 4 AA7 5 LYS B 348 LEU B 354 1 O PHE B 352 N PHE B 316
SHEET 5 AA7 5 GLN B 379 ARG B 380 1 O GLN B 379 N PHE B 349
SHEET 1 AA8 4 ASP B 325 PRO B 326 0
SHEET 2 AA8 4 LEU B 313 TYR B 321 -1 N TYR B 321 O ASP B 325
SHEET 3 AA8 4 LYS B 348 LEU B 354 1 O PHE B 352 N PHE B 316
SHEET 4 AA8 4 GLY B 385 GLY B 387 1 O GLY B 385 N GLY B 353
SHEET 1 AA9 3 TYR B 422 VAL B 426 0
SHEET 2 AA9 3 ILE B 522 ASN B 527 -1 O ASN B 526 N GLU B 423
SHEET 3 AA9 3 THR B 542 THR B 543 -1 O THR B 542 N MET B 523
SHEET 1 AB1 6 ARG B 631 SER B 634 0
SHEET 2 AB1 6 HIS B 496 VAL B 499 -1 N VAL B 497 O TYR B 633
SHEET 3 AB1 6 LEU B 685 ARG B 691 -1 O ARG B 691 N HIS B 496
SHEET 4 AB1 6 PHE B 459 LYS B 468 -1 N PHE B 459 O MET B 688
SHEET 5 AB1 6 LEU B 477 ASP B 483 -1 O ASP B 483 N ALA B 462
SHEET 6 AB1 6 SER B 645 VAL B 651 -1 O ALA B 650 N MET B 478
SHEET 1 AB2 2 GLU B 654 GLU B 656 0
SHEET 2 AB2 2 VAL B 662 LYS B 664 -1 O ASN B 663 N TYR B 655
SHEET 1 AB3 5 GLN B 767 PHE B 772 0
SHEET 2 AB3 5 THR B 737 CYS B 743 1 N CYS B 743 O ALA B 771
SHEET 3 AB3 5 VAL B 705 PRO B 710 1 N MET B 707 O LEU B 738
SHEET 4 AB3 5 HIS B 803 ASP B 809 1 O TYR B 805 N ILE B 706
SHEET 5 AB3 5 TYR B 849 TRP B 854 1 O SER B 850 N ILE B 804
LINK NE2 HIS A 25 FE HEM A 901 1555 1555 2.16
LINK NE2 HIS B 25 FE HEM B 901 1555 1555 2.20
CISPEP 1 PRO A 451 PRO A 452 0 2.35
CISPEP 2 CYS A 540 PRO A 541 0 0.67
CISPEP 3 PRO B 451 PRO B 452 0 2.48
CISPEP 4 CYS B 540 PRO B 541 0 0.65
SITE 1 AC1 11 LYS A 18 HIS A 25 GLU A 29 TYR A 134
SITE 2 AC1 11 THR A 135 ARG A 136 GLY A 139 SER A 142
SITE 3 AC1 11 LYS A 179 ARG A 183 PHE A 207
SITE 1 AC2 16 HIS A 496 ARG A 601 ARG A 631 TYR A 632
SITE 2 AC2 16 TYR A 633 SER A 634 CYS A 649 ALA A 650
SITE 3 AC2 16 VAL A 651 VAL A 653 TYR A 655 GLY A 665
SITE 4 AC2 16 VAL A 666 ALA A 667 THR A 668 TRP A 854
SITE 1 AC3 19 SER A 267 GLN A 268 THR A 269 GLY A 270
SITE 2 AC3 19 THR A 271 ALA A 272 ALA A 319 THR A 320
SITE 3 AC3 19 TYR A 321 GLY A 322 LEU A 354 GLY A 355
SITE 4 AC3 19 ASN A 356 TYR A 359 HIS A 361 PHE A 362
SITE 5 AC3 19 ASN A 363 ASP A 389 LEU A 393
SITE 1 AC4 12 LYS B 18 HIS B 25 GLU B 29 GLN B 38
SITE 2 AC4 12 TYR B 134 THR B 135 ARG B 136 GLY B 139
SITE 3 AC4 12 SER B 142 LYS B 179 ARG B 183 PHE B 207
SITE 1 AC5 17 HIS B 496 ARG B 601 ARG B 631 TYR B 632
SITE 2 AC5 17 TYR B 633 SER B 634 CYS B 649 ALA B 650
SITE 3 AC5 17 VAL B 651 VAL B 653 TYR B 655 GLY B 665
SITE 4 AC5 17 VAL B 666 ALA B 667 THR B 668 TRP B 854
SITE 5 AC5 17 SER B 855
SITE 1 AC6 19 SER B 267 GLN B 268 THR B 269 GLY B 270
SITE 2 AC6 19 THR B 271 ALA B 272 ALA B 319 THR B 320
SITE 3 AC6 19 TYR B 321 GLY B 322 LEU B 354 GLY B 355
SITE 4 AC6 19 ASN B 356 TYR B 359 HIS B 361 PHE B 362
SITE 5 AC6 19 ASN B 363 ASP B 389 LEU B 393
CRYST1 82.686 160.191 188.832 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012094 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006243 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005296 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
