HEADER UNKNOWN FUNCTION 20-APR-04 1T2B
TITLE CRYSTAL STRUCTURE OF CYTOCHROME P450CIN COMPLEXED WITH ITS SUBSTRATE
TITLE 2 1,8-CINEOLE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: P450CIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CITROBACTER BRAAKII;
SOURCE 3 ORGANISM_TAXID: 57706;
SOURCE 4 GENE: CINA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DH5A CELLS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCWORI
KEYWDS B'-HELIX, LOOP, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.T.MEHARENNA,H.LI,D.B.HAWKES,A.G.PEARSON,J.DE VOSS,T.L.POULOS
REVDAT 3 23-AUG-23 1T2B 1 REMARK LINK
REVDAT 2 24-FEB-09 1T2B 1 VERSN
REVDAT 1 26-APR-05 1T2B 0
JRNL AUTH Y.T.MEHARENNA,H.LI,D.B.HAWKES,A.G.PEARSON,J.DE VOSS,
JRNL AUTH 2 T.L.POULOS
JRNL TITL CRYSTAL STRUCTURE OF P450CIN IN A COMPLEX WITH ITS
JRNL TITL 2 SUBSTRATE, 1,8-CINEOLE, A CLOSE STRUCTURAL HOMOLOGUE TO
JRNL TITL 3 D-CAMPHOR, THE SUBSTRATE FOR P450CAM
JRNL REF BIOCHEMISTRY V. 43 9487 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15260491
JRNL DOI 10.1021/BI049293P
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.43
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1564178.950
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 97930
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4915
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 9280
REMARK 3 BIN R VALUE (WORKING SET) : 0.2980
REMARK 3 BIN FREE R VALUE : 0.3260
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 440
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.016
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6298
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 108
REMARK 3 SOLVENT ATOMS : 986
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.55000
REMARK 3 B22 (A**2) : -4.21000
REMARK 3 B33 (A**2) : -0.34000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 6.62000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.19
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.160
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 51.13
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : HETERO.PARAM
REMARK 3 PARAMETER FILE 4 : CIN.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : HETERO.TOP
REMARK 3 TOPOLOGY FILE 4 : CIN.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1T2B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-APR-04.
REMARK 100 THE DEPOSITION ID IS D_1000022222.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-03
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 : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 97930
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 43.430
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.570
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.57
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.800
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: 1PHA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.7M SODIUM MALONATE, PH 6.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 34.48000
REMARK 290 SMTRY3 2 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 300 REMARK: DOESN'T FORM A DIMER AT LOWER CONCENTRATIONS
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 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 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 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 MET A 90 -64.63 74.94
REMARK 500 LEU A 144 -61.60 -120.08
REMARK 500 ASP A 241 -73.94 -99.02
REMARK 500 THR A 333 126.78 -170.30
REMARK 500 ARG A 336 53.55 -90.43
REMARK 500 CYS A 347 118.58 -34.35
REMARK 500 MET B 90 -67.04 73.59
REMARK 500 HIS B 176 -54.33 -131.18
REMARK 500 VAL B 177 125.19 -21.10
REMARK 500 ASP B 219 43.59 73.03
REMARK 500 ASP B 241 -74.20 -97.46
REMARK 500 HIS B 342 145.00 -170.05
REMARK 500 CYS B 347 118.75 -38.39
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 450 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 347 SG
REMARK 620 2 HEM A 450 NA 101.3
REMARK 620 3 HEM A 450 NB 93.9 87.2
REMARK 620 4 HEM A 450 NC 92.3 166.2 90.1
REMARK 620 5 HEM A 450 ND 104.0 88.9 162.0 89.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 450 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 347 SG
REMARK 620 2 HEM B 450 NA 102.3
REMARK 620 3 HEM B 450 NB 94.0 87.9
REMARK 620 4 HEM B 450 NC 90.2 167.4 90.2
REMARK 620 5 HEM B 450 ND 102.3 89.7 163.7 88.6
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 450
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CNL A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 450
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CNL B 500
DBREF 1T2B A 8 404 UNP Q8VQF6 Q8VQF6_CITBR 8 404
DBREF 1T2B B 8 404 UNP Q8VQF6 Q8VQF6_CITBR 8 404
SEQRES 1 A 397 THR SER LEU PHE THR THR ALA ASP HIS TYR HIS THR PRO
SEQRES 2 A 397 LEU GLY PRO ASP GLY THR PRO HIS ALA PHE PHE GLU ALA
SEQRES 3 A 397 LEU ARG ASP GLU ALA GLU THR THR PRO ILE GLY TRP SER
SEQRES 4 A 397 GLU ALA TYR GLY GLY HIS TRP VAL VAL ALA GLY TYR LYS
SEQRES 5 A 397 GLU ILE GLN ALA VAL ILE GLN ASN THR LYS ALA PHE SER
SEQRES 6 A 397 ASN LYS GLY VAL THR PHE PRO ARG TYR GLU THR GLY GLU
SEQRES 7 A 397 PHE GLU LEU MET MET ALA GLY GLN ASP ASP PRO VAL HIS
SEQRES 8 A 397 LYS LYS TYR ARG GLN LEU VAL ALA LYS PRO PHE SER PRO
SEQRES 9 A 397 GLU ALA THR ASP LEU PHE THR GLU GLN LEU ARG GLN SER
SEQRES 10 A 397 THR ASN ASP LEU ILE ASP ALA ARG ILE GLU LEU GLY GLU
SEQRES 11 A 397 GLY ASP ALA ALA THR TRP LEU ALA ASN GLU ILE PRO ALA
SEQRES 12 A 397 ARG LEU THR ALA ILE LEU LEU GLY LEU PRO PRO GLU ASP
SEQRES 13 A 397 GLY ASP THR TYR ARG ARG TRP VAL TRP ALA ILE THR HIS
SEQRES 14 A 397 VAL GLU ASN PRO GLU GLU GLY ALA GLU ILE PHE ALA GLU
SEQRES 15 A 397 LEU VAL ALA HIS ALA ARG THR LEU ILE ALA GLU ARG ARG
SEQRES 16 A 397 THR ASN PRO GLY ASN ASP ILE MET SER ARG VAL ILE MET
SEQRES 17 A 397 SER LYS ILE ASP GLY GLU SER LEU SER GLU ASP ASP LEU
SEQRES 18 A 397 ILE GLY PHE PHE THR ILE LEU LEU LEU GLY GLY ILE ASP
SEQRES 19 A 397 ASN THR ALA ARG PHE LEU SER SER VAL PHE TRP ARG LEU
SEQRES 20 A 397 ALA TRP ASP ILE GLU LEU ARG ARG ARG LEU ILE ALA HIS
SEQRES 21 A 397 PRO GLU LEU ILE PRO ASN ALA VAL ASP GLU LEU LEU ARG
SEQRES 22 A 397 PHE TYR GLY PRO ALA MET VAL GLY ARG LEU VAL THR GLN
SEQRES 23 A 397 GLU VAL THR VAL GLY ASP ILE THR MET LYS PRO GLY GLN
SEQRES 24 A 397 THR ALA MET LEU TRP PHE PRO ILE ALA SER ARG ASP ARG
SEQRES 25 A 397 SER ALA PHE ASP SER PRO ASP ASN ILE VAL ILE GLU ARG
SEQRES 26 A 397 THR PRO ASN ARG HIS LEU SER LEU GLY HIS GLY ILE HIS
SEQRES 27 A 397 ARG CYS LEU GLY ALA HIS LEU ILE ARG VAL GLU ALA ARG
SEQRES 28 A 397 VAL ALA ILE THR GLU PHE LEU LYS ARG ILE PRO GLU PHE
SEQRES 29 A 397 SER LEU ASP PRO ASN LYS GLU CYS GLU TRP LEU MET GLY
SEQRES 30 A 397 GLN VAL ALA GLY MET LEU HIS VAL PRO ILE ILE PHE PRO
SEQRES 31 A 397 LYS GLY LYS ARG LEU SER GLU
SEQRES 1 B 397 THR SER LEU PHE THR THR ALA ASP HIS TYR HIS THR PRO
SEQRES 2 B 397 LEU GLY PRO ASP GLY THR PRO HIS ALA PHE PHE GLU ALA
SEQRES 3 B 397 LEU ARG ASP GLU ALA GLU THR THR PRO ILE GLY TRP SER
SEQRES 4 B 397 GLU ALA TYR GLY GLY HIS TRP VAL VAL ALA GLY TYR LYS
SEQRES 5 B 397 GLU ILE GLN ALA VAL ILE GLN ASN THR LYS ALA PHE SER
SEQRES 6 B 397 ASN LYS GLY VAL THR PHE PRO ARG TYR GLU THR GLY GLU
SEQRES 7 B 397 PHE GLU LEU MET MET ALA GLY GLN ASP ASP PRO VAL HIS
SEQRES 8 B 397 LYS LYS TYR ARG GLN LEU VAL ALA LYS PRO PHE SER PRO
SEQRES 9 B 397 GLU ALA THR ASP LEU PHE THR GLU GLN LEU ARG GLN SER
SEQRES 10 B 397 THR ASN ASP LEU ILE ASP ALA ARG ILE GLU LEU GLY GLU
SEQRES 11 B 397 GLY ASP ALA ALA THR TRP LEU ALA ASN GLU ILE PRO ALA
SEQRES 12 B 397 ARG LEU THR ALA ILE LEU LEU GLY LEU PRO PRO GLU ASP
SEQRES 13 B 397 GLY ASP THR TYR ARG ARG TRP VAL TRP ALA ILE THR HIS
SEQRES 14 B 397 VAL GLU ASN PRO GLU GLU GLY ALA GLU ILE PHE ALA GLU
SEQRES 15 B 397 LEU VAL ALA HIS ALA ARG THR LEU ILE ALA GLU ARG ARG
SEQRES 16 B 397 THR ASN PRO GLY ASN ASP ILE MET SER ARG VAL ILE MET
SEQRES 17 B 397 SER LYS ILE ASP GLY GLU SER LEU SER GLU ASP ASP LEU
SEQRES 18 B 397 ILE GLY PHE PHE THR ILE LEU LEU LEU GLY GLY ILE ASP
SEQRES 19 B 397 ASN THR ALA ARG PHE LEU SER SER VAL PHE TRP ARG LEU
SEQRES 20 B 397 ALA TRP ASP ILE GLU LEU ARG ARG ARG LEU ILE ALA HIS
SEQRES 21 B 397 PRO GLU LEU ILE PRO ASN ALA VAL ASP GLU LEU LEU ARG
SEQRES 22 B 397 PHE TYR GLY PRO ALA MET VAL GLY ARG LEU VAL THR GLN
SEQRES 23 B 397 GLU VAL THR VAL GLY ASP ILE THR MET LYS PRO GLY GLN
SEQRES 24 B 397 THR ALA MET LEU TRP PHE PRO ILE ALA SER ARG ASP ARG
SEQRES 25 B 397 SER ALA PHE ASP SER PRO ASP ASN ILE VAL ILE GLU ARG
SEQRES 26 B 397 THR PRO ASN ARG HIS LEU SER LEU GLY HIS GLY ILE HIS
SEQRES 27 B 397 ARG CYS LEU GLY ALA HIS LEU ILE ARG VAL GLU ALA ARG
SEQRES 28 B 397 VAL ALA ILE THR GLU PHE LEU LYS ARG ILE PRO GLU PHE
SEQRES 29 B 397 SER LEU ASP PRO ASN LYS GLU CYS GLU TRP LEU MET GLY
SEQRES 30 B 397 GLN VAL ALA GLY MET LEU HIS VAL PRO ILE ILE PHE PRO
SEQRES 31 B 397 LYS GLY LYS ARG LEU SER GLU
HET HEM A 450 43
HET CNL A 500 11
HET HEM B 450 43
HET CNL B 500 11
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM CNL 1,3,3-TRIMETHYL-2-OXABICYCLO[2.2.2]OCTANE
HETSYN HEM HEME
HETSYN CNL 1,8-CINEOLE
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 CNL 2(C10 H18 O)
FORMUL 7 HOH *986(H2 O)
HELIX 1 1 SER A 9 ALA A 14 5 6
HELIX 2 2 PRO A 27 GLU A 39 1 13
HELIX 3 3 GLU A 47 GLY A 51 5 5
HELIX 4 4 GLY A 57 ASN A 67 1 11
HELIX 5 5 ASN A 73 VAL A 76 5 4
HELIX 6 6 PRO A 96 LEU A 104 1 9
HELIX 7 7 VAL A 105 PHE A 109 5 5
HELIX 8 8 SER A 110 ASP A 115 1 6
HELIX 9 9 PHE A 117 GLU A 134 1 18
HELIX 10 10 ALA A 140 LEU A 144 1 5
HELIX 11 11 ASN A 146 GLY A 158 1 13
HELIX 12 12 PRO A 160 GLU A 162 5 3
HELIX 13 13 ASP A 163 HIS A 176 1 14
HELIX 14 14 ASN A 179 ASN A 204 1 26
HELIX 15 15 ASP A 208 MET A 215 1 8
HELIX 16 16 SER A 224 ASP A 241 1 18
HELIX 17 17 ASP A 241 ASP A 257 1 17
HELIX 18 18 ASP A 257 HIS A 267 1 11
HELIX 19 19 LEU A 270 GLY A 283 1 14
HELIX 20 20 TRP A 311 SER A 316 1 6
HELIX 21 21 HIS A 342 ARG A 346 5 5
HELIX 22 22 GLY A 349 ILE A 368 1 20
HELIX 23 23 PRO B 27 GLU B 39 1 13
HELIX 24 24 GLU B 47 GLY B 51 5 5
HELIX 25 25 GLY B 57 ASN B 67 1 11
HELIX 26 26 ASN B 73 VAL B 76 5 4
HELIX 27 27 PRO B 96 ALA B 106 1 11
HELIX 28 28 LYS B 107 PHE B 109 5 3
HELIX 29 29 SER B 110 LEU B 116 1 7
HELIX 30 30 PHE B 117 GLU B 134 1 18
HELIX 31 31 ALA B 140 LEU B 144 1 5
HELIX 32 32 ASN B 146 GLY B 158 1 13
HELIX 33 33 PRO B 160 GLU B 162 5 3
HELIX 34 34 ASP B 163 HIS B 176 1 14
HELIX 35 35 ASN B 179 ASN B 204 1 26
HELIX 36 36 ASP B 208 SER B 216 1 9
HELIX 37 37 SER B 224 ASP B 241 1 18
HELIX 38 38 ASP B 241 ASP B 257 1 17
HELIX 39 39 ASP B 257 HIS B 267 1 11
HELIX 40 40 LEU B 270 GLY B 283 1 14
HELIX 41 41 TRP B 311 SER B 316 1 6
HELIX 42 42 HIS B 342 ARG B 346 5 5
HELIX 43 43 GLY B 349 ILE B 368 1 20
SHEET 1 A 5 ILE A 43 SER A 46 0
SHEET 2 A 5 HIS A 52 VAL A 55 -1 O VAL A 54 N GLY A 44
SHEET 3 A 5 THR A 307 LEU A 310 1 O MET A 309 N TRP A 53
SHEET 4 A 5 VAL A 287 VAL A 291 -1 N VAL A 287 O LEU A 310
SHEET 5 A 5 PHE A 71 SER A 72 -1 N SER A 72 O LEU A 290
SHEET 1 B 3 GLU A 137 ASP A 139 0
SHEET 2 B 3 PRO A 393 ILE A 395 -1 O ILE A 394 N GLY A 138
SHEET 3 B 3 SER A 372 LEU A 373 -1 N SER A 372 O ILE A 395
SHEET 1 C 2 VAL A 295 VAL A 297 0
SHEET 2 C 2 ILE A 300 MET A 302 -1 O MET A 302 N VAL A 295
SHEET 1 D 2 GLU A 380 LEU A 382 0
SHEET 2 D 2 GLY A 388 HIS A 391 -1 O LEU A 390 N GLU A 380
SHEET 1 E 5 ILE B 43 SER B 46 0
SHEET 2 E 5 HIS B 52 VAL B 55 -1 O HIS B 52 N SER B 46
SHEET 3 E 5 THR B 307 LEU B 310 1 O MET B 309 N TRP B 53
SHEET 4 E 5 VAL B 287 VAL B 291 -1 N VAL B 287 O LEU B 310
SHEET 5 E 5 PHE B 71 SER B 72 -1 N SER B 72 O LEU B 290
SHEET 1 F 3 GLU B 137 ASP B 139 0
SHEET 2 F 3 PRO B 393 ILE B 395 -1 O ILE B 394 N GLY B 138
SHEET 3 F 3 SER B 372 LEU B 373 -1 N SER B 372 O ILE B 395
SHEET 1 G 2 VAL B 295 VAL B 297 0
SHEET 2 G 2 ILE B 300 MET B 302 -1 O MET B 302 N VAL B 295
SHEET 1 H 2 GLU B 380 LEU B 382 0
SHEET 2 H 2 GLY B 388 HIS B 391 -1 O LEU B 390 N GLU B 380
LINK SG CYS A 347 FE HEM A 450 1555 1555 2.27
LINK SG CYS B 347 FE HEM B 450 1555 1555 2.28
CISPEP 1 PHE A 78 PRO A 79 0 0.04
CISPEP 2 ASP A 95 PRO A 96 0 0.32
CISPEP 3 THR A 333 PRO A 334 0 0.23
CISPEP 4 PHE B 78 PRO B 79 0 -0.38
CISPEP 5 ASP B 95 PRO B 96 0 0.64
CISPEP 6 THR B 333 PRO B 334 0 0.16
SITE 1 AC1 24 ASN A 73 VAL A 76 MET A 90 ALA A 91
SITE 2 AC1 24 HIS A 98 ARG A 102 PHE A 109 ILE A 234
SITE 3 AC1 24 GLY A 238 ASN A 242 THR A 243 PRO A 284
SITE 4 AC1 24 ARG A 289 PHE A 312 SER A 339 LEU A 340
SITE 5 AC1 24 GLY A 341 ILE A 344 HIS A 345 CYS A 347
SITE 6 AC1 24 LEU A 348 ILE A 353 CNL A 500 HOH A 528
SITE 1 AC2 6 THR A 77 GLY A 238 ASN A 242 VAL A 287
SITE 2 AC2 6 VAL A 386 HEM A 450
SITE 1 AC3 24 ASN B 73 VAL B 76 MET B 90 ALA B 91
SITE 2 AC3 24 HIS B 98 ARG B 102 PHE B 109 ILE B 234
SITE 3 AC3 24 GLY B 238 ASN B 242 THR B 243 PRO B 284
SITE 4 AC3 24 ARG B 289 PHE B 312 SER B 339 LEU B 340
SITE 5 AC3 24 GLY B 341 ILE B 344 HIS B 345 CYS B 347
SITE 6 AC3 24 ILE B 353 CNL B 500 HOH B 513 HOH B 850
SITE 1 AC4 7 THR B 77 GLY B 238 ASN B 242 ALA B 285
SITE 2 AC4 7 VAL B 287 VAL B 386 HEM B 450
CRYST1 62.400 68.960 105.550 90.00 95.61 90.00 P 1 21 1 4
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 0.016026 0.000000 0.001574 0.00000
SCALE2 0.000000 0.014501 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009520 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
