HEADER OXIDOREDUCTASE 18-JUL-01 1JME
TITLE CRYSTAL STRUCTURE OF PHE393HIS CYTOCHROME P450 BM3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIFUNCTIONAL P-450:NADPH-P450 REDUCTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CYTOCHROME P450;
COMPND 5 SYNONYM: CYTOCHROME P450 BM3; NADPH--FERRIHEMOPROTEIN REDUCTASE;
COMPND 6 P450BM-3;
COMPND 7 EC: 1.14.14.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS MEGATERIUM;
SOURCE 3 ORGANISM_TAXID: 1404;
SOURCE 4 GENE: CYP102A1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: TG1;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCM81
KEYWDS CYTOCHROME P450, FATTY ACID HYDROXYLASE, MONOOXYGENASE,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.W.B.OST,A.W.MUNRO,C.G.MOWAT,A.PESSEGUIERO,A.J.FULCO,A.K.CHO,
AUTHOR 2 M.A.CHEESMAN,M.D.WALKINSHAW,S.K.CHAPMAN
REVDAT 6 16-AUG-23 1JME 1 REMARK
REVDAT 5 27-OCT-21 1JME 1 REMARK SEQADV LINK
REVDAT 4 04-OCT-17 1JME 1 REMARK
REVDAT 3 24-FEB-09 1JME 1 VERSN
REVDAT 2 01-APR-03 1JME 1 JRNL
REVDAT 1 23-NOV-01 1JME 0
JRNL AUTH T.W.OST,A.W.MUNRO,C.G.MOWAT,P.R.TAYLOR,A.PESSEGUIERO,
JRNL AUTH 2 A.J.FULCO,A.K.CHO,M.A.CHEESMAN,M.D.WALKINSHAW,S.K.CHAPMAN
JRNL TITL STRUCTURAL AND SPECTROSCOPIC ANALYSIS OF THE F393H MUTANT OF
JRNL TITL 2 FLAVOCYTOCHROME P450 BM3.
JRNL REF BIOCHEMISTRY V. 40 13430 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11695889
JRNL DOI 10.1021/BI010717E
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 73016
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 + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3650
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7010
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 86
REMARK 3 SOLVENT ATOMS : 1182
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.50
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.006 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 1.800 ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JME COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUL-01.
REMARK 100 THE DEPOSITION ID IS D_1000013937.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-MAY-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX9.5
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.3
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73016
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 6.580
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
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: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 2HPD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, PIPES, MAGNESIUM SULFATE, PH
REMARK 280 6.5, VAPOR DIFFUSION, HANGING DROP AT 277K
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 76.55100
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 THR A 1
REMARK 465 ILE A 2
REMARK 465 GLN A 189
REMARK 465 ARG A 190
REMARK 465 ALA A 191
REMARK 465 ASN A 192
REMARK 465 PRO A 193
REMARK 465 ASP A 194
REMARK 465 ASP A 195
REMARK 465 PRO A 196
REMARK 465 ALA A 197
REMARK 465 TYR A 198
REMARK 465 ASP A 199
REMARK 465 GLU A 200
REMARK 465 THR B 1
REMARK 465 ILE B 2
REMARK 465 GLN B 189
REMARK 465 ARG B 190
REMARK 465 ALA B 191
REMARK 465 ASN B 192
REMARK 465 PRO B 193
REMARK 465 ASP B 194
REMARK 465 ASP B 195
REMARK 465 PRO B 196
REMARK 465 ALA B 197
REMARK 465 TYR B 198
REMARK 465 ASP B 199
REMARK 465 GLU B 200
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 GLU A 4 CG CD OE1 OE2
REMARK 470 GLU A 13 CG CD OE1 OE2
REMARK 470 LYS A 31 CD CE NZ
REMARK 470 GLU A 35 CD OE1 OE2
REMARK 470 LYS A 41 CG CD CE NZ
REMARK 470 ARG A 47 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 59 CD
REMARK 470 GLN A 128 CD OE1 NE2
REMARK 470 ASP A 136 CG OD1 OD2
REMARK 470 ASP A 182 CG OD1 OD2
REMARK 470 LYS A 210 CD CE NZ
REMARK 470 LYS A 218 CD CE NZ
REMARK 470 GLU A 244 CG CD OE1 OE2
REMARK 470 VAL A 302 CG1 CG2
REMARK 470 LYS A 309 CG CD CE NZ
REMARK 470 GLU A 380 CG CD OE1 OE2
REMARK 470 LYS A 447 CE NZ
REMARK 470 LYS A 449 CG CD CE NZ
REMARK 470 LEU A 455 O
REMARK 470 GLU B 4 CG CD OE1 OE2
REMARK 470 ARG B 47 CB CG CD NE CZ NH1 NH2
REMARK 470 LYS B 59 CD CE NZ
REMARK 470 ASP B 136 CG OD1 OD2
REMARK 470 GLN B 169 CG CD OE1 NE2
REMARK 470 ARG B 203 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 210 CG CD CE NZ
REMARK 470 GLU B 228 CG CD OE1 OE2
REMARK 470 GLU B 430 CD OE1 OE2
REMARK 470 LYS B 449 CG CD CE NZ
REMARK 470 LEU B 455 O
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 A 20 CA - CB - CG ANGL. DEV. = 17.9 DEGREES
REMARK 500 ARG A 50 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 56 CD - NE - CZ ANGL. DEV. = 8.8 DEGREES
REMARK 500 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 161 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 167 CG - CD - NE ANGL. DEV. = 18.2 DEGREES
REMARK 500 ARG A 323 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 323 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 LEU B 148 CA - CB - CG ANGL. DEV. = 17.0 DEGREES
REMARK 500 ARG B 223 CD - NE - CZ ANGL. DEV. = 11.2 DEGREES
REMARK 500 ARG B 223 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ASP B 369 CB - CG - OD2 ANGL. DEV. = 5.7 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 LYS A 15 -131.11 62.13
REMARK 500 ASP A 84 39.60 -95.98
REMARK 500 PHE A 158 28.92 -146.03
REMARK 500 HIS A 171 139.22 -39.63
REMARK 500 ASP A 370 41.55 -77.97
REMARK 500 HIS A 388 15.83 59.52
REMARK 500 THR A 436 -122.81 -127.78
REMARK 500 LYS B 15 -131.60 58.01
REMARK 500 ASP B 84 43.08 -101.29
REMARK 500 PHE B 158 36.32 -154.28
REMARK 500 ASP B 370 36.98 -80.68
REMARK 500 THR B 436 -126.78 -133.54
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 460 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 400 SG
REMARK 620 2 HEM A 460 NA 102.8
REMARK 620 3 HEM A 460 NB 93.3 90.8
REMARK 620 4 HEM A 460 NC 90.0 167.0 90.6
REMARK 620 5 HEM A 460 ND 99.3 88.0 167.3 87.7
REMARK 620 6 HOH A 469 O 175.1 80.7 83.2 86.6 84.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 460 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 400 SG
REMARK 620 2 HEM B 460 NA 102.4
REMARK 620 3 HEM B 460 NB 94.2 88.8
REMARK 620 4 HEM B 460 NC 90.3 167.3 90.1
REMARK 620 5 HEM B 460 ND 102.2 86.5 163.5 90.9
REMARK 620 6 HOH B 714 O 175.6 80.5 82.4 86.8 81.2
REMARK 620 N 1 2 3 4 5
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 460
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 460
DBREF 1JME A 1 455 UNP P14779 CPXB_BACME 1 455
DBREF 1JME B 1 455 UNP P14779 CPXB_BACME 1 455
SEQADV 1JME HIS A 393 UNP P14779 PHE 393 ENGINEERED MUTATION
SEQADV 1JME HIS B 393 UNP P14779 PHE 393 ENGINEERED MUTATION
SEQRES 1 A 455 THR ILE LYS GLU MET PRO GLN PRO LYS THR PHE GLY GLU
SEQRES 2 A 455 LEU LYS ASN LEU PRO LEU LEU ASN THR ASP LYS PRO VAL
SEQRES 3 A 455 GLN ALA LEU MET LYS ILE ALA ASP GLU LEU GLY GLU ILE
SEQRES 4 A 455 PHE LYS PHE GLU ALA PRO GLY ARG VAL THR ARG TYR LEU
SEQRES 5 A 455 SER SER GLN ARG LEU ILE LYS GLU ALA CYS ASP GLU SER
SEQRES 6 A 455 ARG PHE ASP LYS ASN LEU SER GLN ALA LEU LYS PHE VAL
SEQRES 7 A 455 ARG ASP PHE ALA GLY ASP GLY LEU PHE THR SER TRP THR
SEQRES 8 A 455 HIS GLU LYS ASN TRP LYS LYS ALA HIS ASN ILE LEU LEU
SEQRES 9 A 455 PRO SER PHE SER GLN GLN ALA MET LYS GLY TYR HIS ALA
SEQRES 10 A 455 MET MET VAL ASP ILE ALA VAL GLN LEU VAL GLN LYS TRP
SEQRES 11 A 455 GLU ARG LEU ASN ALA ASP GLU HIS ILE GLU VAL PRO GLU
SEQRES 12 A 455 ASP MET THR ARG LEU THR LEU ASP THR ILE GLY LEU CYS
SEQRES 13 A 455 GLY PHE ASN TYR ARG PHE ASN SER PHE TYR ARG ASP GLN
SEQRES 14 A 455 PRO HIS PRO PHE ILE THR SER MET VAL ARG ALA LEU ASP
SEQRES 15 A 455 GLU ALA MET ASN LYS LEU GLN ARG ALA ASN PRO ASP ASP
SEQRES 16 A 455 PRO ALA TYR ASP GLU ASN LYS ARG GLN PHE GLN GLU ASP
SEQRES 17 A 455 ILE LYS VAL MET ASN ASP LEU VAL ASP LYS ILE ILE ALA
SEQRES 18 A 455 ASP ARG LYS ALA SER GLY GLU GLN SER ASP ASP LEU LEU
SEQRES 19 A 455 THR HIS MET LEU ASN GLY LYS ASP PRO GLU THR GLY GLU
SEQRES 20 A 455 PRO LEU ASP ASP GLU ASN ILE ARG TYR GLN ILE ILE THR
SEQRES 21 A 455 PHE LEU ILE ALA GLY HIS GLU THR THR SER GLY LEU LEU
SEQRES 22 A 455 SER PHE ALA LEU TYR PHE LEU VAL LYS ASN PRO HIS VAL
SEQRES 23 A 455 LEU GLN LYS ALA ALA GLU GLU ALA ALA ARG VAL LEU VAL
SEQRES 24 A 455 ASP PRO VAL PRO SER TYR LYS GLN VAL LYS GLN LEU LYS
SEQRES 25 A 455 TYR VAL GLY MET VAL LEU ASN GLU ALA LEU ARG LEU TRP
SEQRES 26 A 455 PRO THR ALA PRO ALA PHE SER LEU TYR ALA LYS GLU ASP
SEQRES 27 A 455 THR VAL LEU GLY GLY GLU TYR PRO LEU GLU LYS GLY ASP
SEQRES 28 A 455 GLU LEU MET VAL LEU ILE PRO GLN LEU HIS ARG ASP LYS
SEQRES 29 A 455 THR ILE TRP GLY ASP ASP VAL GLU GLU PHE ARG PRO GLU
SEQRES 30 A 455 ARG PHE GLU ASN PRO SER ALA ILE PRO GLN HIS ALA PHE
SEQRES 31 A 455 LYS PRO HIS GLY ASN GLY GLN ARG ALA CYS ILE GLY GLN
SEQRES 32 A 455 GLN PHE ALA LEU HIS GLU ALA THR LEU VAL LEU GLY MET
SEQRES 33 A 455 MET LEU LYS HIS PHE ASP PHE GLU ASP HIS THR ASN TYR
SEQRES 34 A 455 GLU LEU ASP ILE LYS GLU THR LEU THR LEU LYS PRO GLU
SEQRES 35 A 455 GLY PHE VAL VAL LYS ALA LYS SER LYS LYS ILE PRO LEU
SEQRES 1 B 455 THR ILE LYS GLU MET PRO GLN PRO LYS THR PHE GLY GLU
SEQRES 2 B 455 LEU LYS ASN LEU PRO LEU LEU ASN THR ASP LYS PRO VAL
SEQRES 3 B 455 GLN ALA LEU MET LYS ILE ALA ASP GLU LEU GLY GLU ILE
SEQRES 4 B 455 PHE LYS PHE GLU ALA PRO GLY ARG VAL THR ARG TYR LEU
SEQRES 5 B 455 SER SER GLN ARG LEU ILE LYS GLU ALA CYS ASP GLU SER
SEQRES 6 B 455 ARG PHE ASP LYS ASN LEU SER GLN ALA LEU LYS PHE VAL
SEQRES 7 B 455 ARG ASP PHE ALA GLY ASP GLY LEU PHE THR SER TRP THR
SEQRES 8 B 455 HIS GLU LYS ASN TRP LYS LYS ALA HIS ASN ILE LEU LEU
SEQRES 9 B 455 PRO SER PHE SER GLN GLN ALA MET LYS GLY TYR HIS ALA
SEQRES 10 B 455 MET MET VAL ASP ILE ALA VAL GLN LEU VAL GLN LYS TRP
SEQRES 11 B 455 GLU ARG LEU ASN ALA ASP GLU HIS ILE GLU VAL PRO GLU
SEQRES 12 B 455 ASP MET THR ARG LEU THR LEU ASP THR ILE GLY LEU CYS
SEQRES 13 B 455 GLY PHE ASN TYR ARG PHE ASN SER PHE TYR ARG ASP GLN
SEQRES 14 B 455 PRO HIS PRO PHE ILE THR SER MET VAL ARG ALA LEU ASP
SEQRES 15 B 455 GLU ALA MET ASN LYS LEU GLN ARG ALA ASN PRO ASP ASP
SEQRES 16 B 455 PRO ALA TYR ASP GLU ASN LYS ARG GLN PHE GLN GLU ASP
SEQRES 17 B 455 ILE LYS VAL MET ASN ASP LEU VAL ASP LYS ILE ILE ALA
SEQRES 18 B 455 ASP ARG LYS ALA SER GLY GLU GLN SER ASP ASP LEU LEU
SEQRES 19 B 455 THR HIS MET LEU ASN GLY LYS ASP PRO GLU THR GLY GLU
SEQRES 20 B 455 PRO LEU ASP ASP GLU ASN ILE ARG TYR GLN ILE ILE THR
SEQRES 21 B 455 PHE LEU ILE ALA GLY HIS GLU THR THR SER GLY LEU LEU
SEQRES 22 B 455 SER PHE ALA LEU TYR PHE LEU VAL LYS ASN PRO HIS VAL
SEQRES 23 B 455 LEU GLN LYS ALA ALA GLU GLU ALA ALA ARG VAL LEU VAL
SEQRES 24 B 455 ASP PRO VAL PRO SER TYR LYS GLN VAL LYS GLN LEU LYS
SEQRES 25 B 455 TYR VAL GLY MET VAL LEU ASN GLU ALA LEU ARG LEU TRP
SEQRES 26 B 455 PRO THR ALA PRO ALA PHE SER LEU TYR ALA LYS GLU ASP
SEQRES 27 B 455 THR VAL LEU GLY GLY GLU TYR PRO LEU GLU LYS GLY ASP
SEQRES 28 B 455 GLU LEU MET VAL LEU ILE PRO GLN LEU HIS ARG ASP LYS
SEQRES 29 B 455 THR ILE TRP GLY ASP ASP VAL GLU GLU PHE ARG PRO GLU
SEQRES 30 B 455 ARG PHE GLU ASN PRO SER ALA ILE PRO GLN HIS ALA PHE
SEQRES 31 B 455 LYS PRO HIS GLY ASN GLY GLN ARG ALA CYS ILE GLY GLN
SEQRES 32 B 455 GLN PHE ALA LEU HIS GLU ALA THR LEU VAL LEU GLY MET
SEQRES 33 B 455 MET LEU LYS HIS PHE ASP PHE GLU ASP HIS THR ASN TYR
SEQRES 34 B 455 GLU LEU ASP ILE LYS GLU THR LEU THR LEU LYS PRO GLU
SEQRES 35 B 455 GLY PHE VAL VAL LYS ALA LYS SER LYS LYS ILE PRO LEU
HET HEM A 460 43
HET HEM B 460 43
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 5 HOH *1182(H2 O)
HELIX 1 1 PHE A 11 LYS A 15 5 5
HELIX 2 2 ASN A 16 ASN A 21 5 6
HELIX 3 3 LYS A 24 GLY A 37 1 14
HELIX 4 4 SER A 54 CYS A 62 1 9
HELIX 5 5 SER A 72 GLY A 83 1 12
HELIX 6 6 GLU A 93 LEU A 104 1 12
HELIX 7 7 PRO A 105 PHE A 107 5 3
HELIX 8 8 SER A 108 ARG A 132 1 25
HELIX 9 9 VAL A 141 ASN A 159 1 19
HELIX 10 10 ASN A 163 ARG A 167 5 5
HELIX 11 11 HIS A 171 LYS A 187 1 17
HELIX 12 12 ASN A 201 GLY A 227 1 27
HELIX 13 13 ASP A 232 GLY A 240 1 9
HELIX 14 14 ASP A 250 LYS A 282 1 33
HELIX 15 15 ASN A 283 LEU A 298 1 16
HELIX 16 16 SER A 304 LEU A 311 1 8
HELIX 17 17 LEU A 311 TRP A 325 1 15
HELIX 18 18 ILE A 357 HIS A 361 1 5
HELIX 19 19 ASP A 363 GLY A 368 1 6
HELIX 20 20 ARG A 375 GLU A 380 5 6
HELIX 21 21 ASN A 381 ILE A 385 5 5
HELIX 22 22 ASN A 395 ALA A 399 5 5
HELIX 23 23 GLY A 402 HIS A 420 1 19
HELIX 24 24 PHE B 11 LYS B 15 5 5
HELIX 25 25 ASN B 16 ASN B 21 5 6
HELIX 26 26 LYS B 24 GLY B 37 1 14
HELIX 27 27 SER B 54 CYS B 62 1 9
HELIX 28 28 SER B 72 GLY B 83 1 12
HELIX 29 29 GLU B 93 LEU B 104 1 12
HELIX 30 30 PRO B 105 SER B 108 5 4
HELIX 31 31 GLN B 109 GLN B 110 5 2
HELIX 32 32 ALA B 111 ARG B 132 1 22
HELIX 33 33 VAL B 141 ASN B 159 1 19
HELIX 34 34 ASN B 163 ARG B 167 5 5
HELIX 35 35 HIS B 171 LEU B 188 1 18
HELIX 36 36 ASN B 201 ALA B 225 1 25
HELIX 37 37 ASP B 232 GLY B 240 1 9
HELIX 38 38 ASP B 250 ASN B 283 1 34
HELIX 39 39 ASN B 283 LEU B 298 1 16
HELIX 40 40 SER B 304 GLN B 310 1 7
HELIX 41 41 LEU B 311 TRP B 325 1 15
HELIX 42 42 GLY B 342 GLU B 344 5 3
HELIX 43 43 ILE B 357 HIS B 361 1 5
HELIX 44 44 ASP B 363 GLY B 368 1 6
HELIX 45 45 ARG B 375 GLU B 380 5 6
HELIX 46 46 ASN B 381 ILE B 385 5 5
HELIX 47 47 ASN B 395 ALA B 399 5 5
HELIX 48 48 GLY B 402 HIS B 420 1 19
SHEET 1 A 5 ILE A 39 ALA A 44 0
SHEET 2 A 5 ARG A 47 LEU A 52 -1 O ARG A 47 N ALA A 44
SHEET 3 A 5 GLU A 352 LEU A 356 1 O GLU A 352 N ARG A 50
SHEET 4 A 5 ALA A 330 ALA A 335 -1 O PHE A 331 N VAL A 355
SHEET 5 A 5 PHE A 67 LYS A 69 -1 O ASP A 68 N TYR A 334
SHEET 1 B 3 ILE A 139 GLU A 140 0
SHEET 2 B 3 VAL A 445 SER A 450 -1 O VAL A 446 N ILE A 139
SHEET 3 B 3 PHE A 421 GLU A 424 -1 N ASP A 422 O LYS A 449
SHEET 1 C 2 THR A 339 LEU A 341 0
SHEET 2 C 2 TYR A 345 LEU A 347 -1 O TYR A 345 N LEU A 341
SHEET 1 D 2 ILE A 433 GLU A 435 0
SHEET 2 D 2 LEU A 439 PRO A 441 -1 O LYS A 440 N LYS A 434
SHEET 1 E 5 ILE B 39 GLU B 43 0
SHEET 2 E 5 VAL B 48 LEU B 52 -1 O THR B 49 N PHE B 42
SHEET 3 E 5 GLU B 352 LEU B 356 1 O GLU B 352 N ARG B 50
SHEET 4 E 5 ALA B 330 ALA B 335 -1 O PHE B 331 N VAL B 355
SHEET 5 E 5 PHE B 67 LYS B 69 -1 O ASP B 68 N TYR B 334
SHEET 1 F 3 ILE B 139 GLU B 140 0
SHEET 2 F 3 VAL B 445 SER B 450 -1 O VAL B 446 N ILE B 139
SHEET 3 F 3 PHE B 421 GLU B 424 -1 O ASP B 422 N LYS B 449
SHEET 1 G 2 THR B 339 LEU B 341 0
SHEET 2 G 2 TYR B 345 LEU B 347 -1 O TYR B 345 N LEU B 341
SHEET 1 H 2 ILE B 433 GLU B 435 0
SHEET 2 H 2 LEU B 439 PRO B 441 -1 O LYS B 440 N LYS B 434
LINK SG CYS A 400 FE HEM A 460 1555 1555 2.14
LINK FE HEM A 460 O HOH A 469 1555 1555 1.82
LINK SG CYS B 400 FE HEM B 460 1555 1555 2.10
LINK FE HEM B 460 O HOH B 714 1555 1555 1.78
SITE 1 AC1 26 LYS A 69 LEU A 86 TRP A 96 PHE A 107
SITE 2 AC1 26 ALA A 264 GLY A 265 THR A 268 THR A 269
SITE 3 AC1 26 THR A 327 PHE A 331 PRO A 392 HIS A 393
SITE 4 AC1 26 GLY A 394 ARG A 398 ALA A 399 CYS A 400
SITE 5 AC1 26 ILE A 401 GLY A 402 ALA A 406 HOH A 463
SITE 6 AC1 26 HOH A 469 HOH A 486 HOH A 515 HOH A 526
SITE 7 AC1 26 HOH A 536 HOH A 686
SITE 1 AC2 23 LYS B 69 LEU B 86 TRP B 96 ALA B 264
SITE 2 AC2 23 GLY B 265 THR B 268 THR B 269 THR B 327
SITE 3 AC2 23 PHE B 331 PRO B 392 HIS B 393 GLY B 394
SITE 4 AC2 23 ARG B 398 ALA B 399 CYS B 400 ALA B 406
SITE 5 AC2 23 HOH B 461 HOH B 465 HOH B 503 HOH B 507
SITE 6 AC2 23 HOH B 517 HOH B 710 HOH B 714
CRYST1 58.842 153.102 61.479 90.00 94.67 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 0.016995 0.000000 0.001388 0.00000
SCALE2 0.000000 0.006532 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016320 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
