HEADER OXIDOREDUCTASE 10-SEP-12 4H1N
TITLE CRYSTAL STRUCTURE OF P450 2B4 F297A MUTANT IN COMPLEX WITH ANTI-
TITLE 2 PLATELET DRUG CLOPIDOGREL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME P450 2B4;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CYPIIB4, CYTOCHROME P450 ISOZYME 2, CYTOCHROME P450 LM2,
COMPND 5 CYTOCHROME P450 TYPE B0, CYTOCHROME P450 TYPE B1;
COMPND 6 EC: 1.14.14.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 3 ORGANISM_COMMON: EUROPEAN RABBIT,JAPANESE WHITE RABBIT,DOMESTIC
SOURCE 4 RABBIT,RABBITS;
SOURCE 5 ORGANISM_TAXID: 9986;
SOURCE 6 GENE: CYP2B4, CYP2B6;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: TOPP3;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PKK
KEYWDS P450, CYTOCHROME P450 2B4, MONOOXYGENASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.B.SHAH,H.H.JANG,C.D.STOUT,J.R.HALPERT
REVDAT 4 13-SEP-23 4H1N 1 REMARK SEQADV
REVDAT 3 20-FEB-13 4H1N 1 JRNL
REVDAT 2 23-JAN-13 4H1N 1 JRNL
REVDAT 1 16-JAN-13 4H1N 0
JRNL AUTH M.B.SHAH,H.H.JANG,Q.ZHANG,C.DAVID STOUT,J.R.HALPERT
JRNL TITL X-RAY CRYSTAL STRUCTURE OF THE CYTOCHROME P450 2B4 ACTIVE
JRNL TITL 2 SITE MUTANT F297A IN COMPLEX WITH CLOPIDOGREL: INSIGHTS INTO
JRNL TITL 3 COMPENSATORY REARRANGEMENTS OF THE BINDING POCKET.
JRNL REF ARCH.BIOCHEM.BIOPHYS. V. 530 64 2013
JRNL REFN ISSN 0003-9861
JRNL PMID 23296089
JRNL DOI 10.1016/J.ABB.2012.12.016
REMARK 2
REMARK 2 RESOLUTION. 2.99 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 14553
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) : 0.236
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 774
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.99
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.07
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1019
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.38
REMARK 3 BIN R VALUE (WORKING SET) : 0.3700
REMARK 3 BIN FREE R VALUE SET COUNT : 58
REMARK 3 BIN FREE R VALUE : 0.5060
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3610
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 126
REMARK 3 SOLVENT ATOMS : 19
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 77.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 77.19
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.66000
REMARK 3 B22 (A**2) : -1.66000
REMARK 3 B33 (A**2) : 2.50000
REMARK 3 B12 (A**2) : -0.83000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.753
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.442
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.422
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.678
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.899
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3826 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5207 ; 1.020 ; 2.023
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 456 ; 4.850 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 169 ;32.369 ;22.781
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 586 ;15.257 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;12.837 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 577 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2896 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4H1N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-SEP-12.
REMARK 100 THE DEPOSITION ID IS D_1000074905.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JAN-12
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 : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16796
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.898
REMARK 200 RESOLUTION RANGE LOW (A) : 39.571
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 13.30
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : 0.06800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.2
REMARK 200 DATA REDUNDANCY IN SHELL : 9.30
REMARK 200 R MERGE FOR SHELL (I) : 0.74400
REMARK 200 R SYM FOR SHELL (I) : 0.74400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3MVR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULFATE, 0.1M BIS-TRIS
REMARK 280 PH 6.5, 25% W/V POLYETHYLENE GLYCOL 3350, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.76200
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 101.52400
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 101.52400
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 50.76200
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 20
REMARK 465 ALA A 21
REMARK 465 LYS A 22
REMARK 465 LYS A 23
REMARK 465 THR A 24
REMARK 465 SER A 25
REMARK 465 SER A 26
REMARK 465 LYS A 27
REMARK 465 GLY A 28
REMARK 465 PHE A 135
REMARK 465 GLY A 136
REMARK 465 MET A 137
REMARK 465 ARG A 473
REMARK 465 GLU A 474
REMARK 465 HIS A 493
REMARK 465 HIS A 494
REMARK 465 HIS A 495
REMARK 465 HIS A 496
REMARK 465 HIS A 497
REMARK 465 HIS A 498
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 LEU A 37 CG CD1 CD2
REMARK 470 ARG A 48 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 49 CG CD CE NZ
REMARK 470 ARG A 57 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 61 CG CD CE NZ
REMARK 470 ARG A 126 NE CZ NH1 NH2
REMARK 470 ARG A 140 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 145 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 161 CD CE NZ
REMARK 470 LYS A 191 CG CD CE NZ
REMARK 470 GLN A 239 CD OE1 NE2
REMARK 470 LYS A 251 CD CE NZ
REMARK 470 LYS A 276 CG CD CE NZ
REMARK 470 LYS A 326 CG CD CE NZ
REMARK 470 LYS A 373 CG CD CE NZ
REMARK 470 ILE A 382 CG1 CG2 CD1
REMARK 470 GLU A 466 CG CD OE1 OE2
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 VAL A 39 -54.19 66.43
REMARK 500 SER A 430 -163.15 64.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 CM5 A 502
REMARK 610 CM5 A 503
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 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 436 SG
REMARK 620 2 HEM A 501 NA 94.6
REMARK 620 3 HEM A 501 NB 85.7 88.2
REMARK 620 4 HEM A 501 NC 83.9 178.5 91.3
REMARK 620 5 HEM A 501 ND 91.0 89.8 176.1 90.6
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CM5 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CM5 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CM5 A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CGE A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 506
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PO5 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITHOUT H226Y AND F297A MUTATION IN A LIGAND FREE
REMARK 900 OPEN CONFORMATION
REMARK 900 RELATED ID: 1SUO RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITHOUT F297A MUTATION IN COMPLEX WITH 4-(4-
REMARK 900 CHLOROPHENYL)IMIDAZOLE
REMARK 900 RELATED ID: 2Q6N RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITHOUT F297A MUTATION IN COMPLEX WITH 1-(4-
REMARK 900 CHLOROPHENYL)IMIDAZOLE
REMARK 900 RELATED ID: 2BDM RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITHOUT F297A MUTATION IN COMPLEX WITH BIFONAZOLE
REMARK 900 RELATED ID: 3KW4 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITHOUT F297A MUTATION IN COMPLEX WITH TICLOPIDINE
REMARK 900 RELATED ID: 3ME6 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITHOUT F297A MUTATION IN COMPLEX WITH CLOPIDOGREL
REMARK 900 RELATED ID: 3MVR RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITHOUT F297A MUTATION IN A LIGAND FREE CLOSED
REMARK 900 CONFORMATION
REMARK 900 RELATED ID: 3G5N RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITHOUT F297A MUTATION IN COMPLEX WITH 1-BIPHENYL-
REMARK 900 4-METHYL-1H-IMIDAZOLE (TRIPLE LIGAND OCCUPANCY)
REMARK 900 RELATED ID: 3G93 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITHOUT F297A MUTATION IN COMPLEX WITH 1-BIPHENYL-
REMARK 900 4-METHYL-1H-IMIDAZOLE (SINGLE LIGAND OCCUPANCY)
REMARK 900 RELATED ID: 3R1B RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITHOUT F297A MUTATION IN COMPLEX WITH TERT-
REMARK 900 BUTYLPHENYLACETYLENE (OPEN CONFORMATION)
REMARK 900 RELATED ID: 3R1A RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITHOUT F297A MUTATION IN COMPLEX WITH TERT-
REMARK 900 BUTYLPHENYLACETYLENE (CLOSED CONFORMATION)
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHORS INDICATE THAT THERE IS AN ERROR IN THE SEQUENCE DATABASE
REMARK 999 REFERENCE AT RESIDUE 221
DBREF 4H1N A 20 491 UNP P00178 CP2B4_RABIT 1 491
SEQADV 4H1N ALA A 21 UNP P00178 GLU 2 ENGINEERED MUTATION
SEQADV 4H1N A UNP P00178 PHE 3 DELETION
SEQADV 4H1N A UNP P00178 SER 4 DELETION
SEQADV 4H1N A UNP P00178 LEU 5 DELETION
SEQADV 4H1N A UNP P00178 LEU 6 DELETION
SEQADV 4H1N A UNP P00178 LEU 7 DELETION
SEQADV 4H1N A UNP P00178 LEU 8 DELETION
SEQADV 4H1N A UNP P00178 LEU 9 DELETION
SEQADV 4H1N A UNP P00178 ALA 10 DELETION
SEQADV 4H1N A UNP P00178 PHE 11 DELETION
SEQADV 4H1N A UNP P00178 LEU 12 DELETION
SEQADV 4H1N A UNP P00178 ALA 13 DELETION
SEQADV 4H1N A UNP P00178 GLY 14 DELETION
SEQADV 4H1N A UNP P00178 LEU 15 DELETION
SEQADV 4H1N A UNP P00178 LEU 16 DELETION
SEQADV 4H1N A UNP P00178 LEU 17 DELETION
SEQADV 4H1N A UNP P00178 LEU 18 DELETION
SEQADV 4H1N A UNP P00178 LEU 19 DELETION
SEQADV 4H1N A UNP P00178 PHE 20 DELETION
SEQADV 4H1N A UNP P00178 ARG 21 DELETION
SEQADV 4H1N LYS A 22 UNP P00178 GLY 22 ENGINEERED MUTATION
SEQADV 4H1N LYS A 23 UNP P00178 HIS 23 ENGINEERED MUTATION
SEQADV 4H1N THR A 24 UNP P00178 PRO 24 ENGINEERED MUTATION
SEQADV 4H1N SER A 25 UNP P00178 LYS 25 ENGINEERED MUTATION
SEQADV 4H1N SER A 26 UNP P00178 ALA 26 ENGINEERED MUTATION
SEQADV 4H1N LYS A 27 UNP P00178 HIS 27 ENGINEERED MUTATION
SEQADV 4H1N LYS A 29 UNP P00178 ARG 29 ENGINEERED MUTATION
SEQADV 4H1N SER A 221 UNP P00178 PRO 221 SEE REMARK 999
SEQADV 4H1N TYR A 226 UNP P00178 HIS 226 ENGINEERED MUTATION
SEQADV 4H1N ALA A 297 UNP P00178 PHE 297 ENGINEERED MUTATION
SEQADV 4H1N HIS A 492 UNP P00178 EXPRESSION TAG
SEQADV 4H1N HIS A 493 UNP P00178 EXPRESSION TAG
SEQADV 4H1N HIS A 494 UNP P00178 EXPRESSION TAG
SEQADV 4H1N HIS A 495 UNP P00178 EXPRESSION TAG
SEQADV 4H1N HIS A 496 UNP P00178 EXPRESSION TAG
SEQADV 4H1N HIS A 497 UNP P00178 EXPRESSION TAG
SEQADV 4H1N HIS A 498 UNP P00178 EXPRESSION TAG
SEQRES 1 A 479 MET ALA LYS LYS THR SER SER LYS GLY LYS LEU PRO PRO
SEQRES 2 A 479 GLY PRO SER PRO LEU PRO VAL LEU GLY ASN LEU LEU GLN
SEQRES 3 A 479 MET ASP ARG LYS GLY LEU LEU ARG SER PHE LEU ARG LEU
SEQRES 4 A 479 ARG GLU LYS TYR GLY ASP VAL PHE THR VAL TYR LEU GLY
SEQRES 5 A 479 SER ARG PRO VAL VAL VAL LEU CYS GLY THR ASP ALA ILE
SEQRES 6 A 479 ARG GLU ALA LEU VAL ASP GLN ALA GLU ALA PHE SER GLY
SEQRES 7 A 479 ARG GLY LYS ILE ALA VAL VAL ASP PRO ILE PHE GLN GLY
SEQRES 8 A 479 TYR GLY VAL ILE PHE ALA ASN GLY GLU ARG TRP ARG ALA
SEQRES 9 A 479 LEU ARG ARG PHE SER LEU ALA THR MET ARG ASP PHE GLY
SEQRES 10 A 479 MET GLY LYS ARG SER VAL GLU GLU ARG ILE GLN GLU GLU
SEQRES 11 A 479 ALA ARG CYS LEU VAL GLU GLU LEU ARG LYS SER LYS GLY
SEQRES 12 A 479 ALA LEU LEU ASP ASN THR LEU LEU PHE HIS SER ILE THR
SEQRES 13 A 479 SER ASN ILE ILE CYS SER ILE VAL PHE GLY LYS ARG PHE
SEQRES 14 A 479 ASP TYR LYS ASP PRO VAL PHE LEU ARG LEU LEU ASP LEU
SEQRES 15 A 479 PHE PHE GLN SER PHE SER LEU ILE SER SER PHE SER SER
SEQRES 16 A 479 GLN VAL PHE GLU LEU PHE SER GLY PHE LEU LYS TYR PHE
SEQRES 17 A 479 PRO GLY THR HIS ARG GLN ILE TYR ARG ASN LEU GLN GLU
SEQRES 18 A 479 ILE ASN THR PHE ILE GLY GLN SER VAL GLU LYS HIS ARG
SEQRES 19 A 479 ALA THR LEU ASP PRO SER ASN PRO ARG ASP PHE ILE ASP
SEQRES 20 A 479 VAL TYR LEU LEU ARG MET GLU LYS ASP LYS SER ASP PRO
SEQRES 21 A 479 SER SER GLU PHE HIS HIS GLN ASN LEU ILE LEU THR VAL
SEQRES 22 A 479 LEU SER LEU PHE ALA ALA GLY THR GLU THR THR SER THR
SEQRES 23 A 479 THR LEU ARG TYR GLY PHE LEU LEU MET LEU LYS TYR PRO
SEQRES 24 A 479 HIS VAL THR GLU ARG VAL GLN LYS GLU ILE GLU GLN VAL
SEQRES 25 A 479 ILE GLY SER HIS ARG PRO PRO ALA LEU ASP ASP ARG ALA
SEQRES 26 A 479 LYS MET PRO TYR THR ASP ALA VAL ILE HIS GLU ILE GLN
SEQRES 27 A 479 ARG LEU GLY ASP LEU ILE PRO PHE GLY VAL PRO HIS THR
SEQRES 28 A 479 VAL THR LYS ASP THR GLN PHE ARG GLY TYR VAL ILE PRO
SEQRES 29 A 479 LYS ASN THR GLU VAL PHE PRO VAL LEU SER SER ALA LEU
SEQRES 30 A 479 HIS ASP PRO ARG TYR PHE GLU THR PRO ASN THR PHE ASN
SEQRES 31 A 479 PRO GLY HIS PHE LEU ASP ALA ASN GLY ALA LEU LYS ARG
SEQRES 32 A 479 ASN GLU GLY PHE MET PRO PHE SER LEU GLY LYS ARG ILE
SEQRES 33 A 479 CYS LEU GLY GLU GLY ILE ALA ARG THR GLU LEU PHE LEU
SEQRES 34 A 479 PHE PHE THR THR ILE LEU GLN ASN PHE SER ILE ALA SER
SEQRES 35 A 479 PRO VAL PRO PRO GLU ASP ILE ASP LEU THR PRO ARG GLU
SEQRES 36 A 479 SER GLY VAL GLY ASN VAL PRO PRO SER TYR GLN ILE ARG
SEQRES 37 A 479 PHE LEU ALA ARG HIS HIS HIS HIS HIS HIS HIS
HET HEM A 501 43
HET CM5 A 502 11
HET CM5 A 503 12
HET CM5 A 504 34
HET CGE A 505 21
HET SO4 A 506 5
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM CM5 5-CYCLOHEXYL-1-PENTYL-BETA-D-MALTOSIDE
HETNAM CGE CLOPIDOGREL
HETNAM SO4 SULFATE ION
HETSYN HEM HEME
HETSYN CM5 5-CYCLOHEXYLPENTYL 4-O-ALPHA-D-GLUCOPYRANOSYL-BETA-D-
HETSYN 2 CM5 GLUCOPYRANOSIDE; CYMAL-5
HETSYN CGE METHYL (2S)-(2-CHLOROPHENYL)(6,7-DIHYDROTHIENO[3,2-
HETSYN 2 CGE C]PYRIDIN-5(4H)-YL)ETHANOATE
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 CM5 3(C23 H42 O11)
FORMUL 6 CGE C16 H16 CL N O2 S
FORMUL 7 SO4 O4 S 2-
FORMUL 8 HOH *19(H2 O)
HELIX 1 1 ASN A 42 MET A 46 5 5
HELIX 2 2 GLY A 50 GLY A 63 1 14
HELIX 3 3 GLY A 80 VAL A 89 1 10
HELIX 4 4 ALA A 92 SER A 96 5 5
HELIX 5 5 VAL A 104 GLN A 109 1 6
HELIX 6 6 ASN A 117 ARG A 133 1 17
HELIX 7 7 SER A 141 SER A 160 1 20
HELIX 8 8 ASN A 167 PHE A 184 1 18
HELIX 9 9 ASP A 192 SER A 210 1 19
HELIX 10 10 SER A 211 LYS A 225 1 15
HELIX 11 11 GLY A 229 LEU A 256 1 28
HELIX 12 12 ASP A 263 ASP A 275 1 13
HELIX 13 13 HIS A 284 THR A 300 1 17
HELIX 14 14 THR A 300 TYR A 317 1 18
HELIX 15 15 TYR A 317 ILE A 332 1 16
HELIX 16 16 ALA A 339 ALA A 344 5 6
HELIX 17 17 MET A 346 ASP A 361 1 16
HELIX 18 18 VAL A 391 HIS A 397 1 7
HELIX 19 19 ASN A 409 LEU A 414 5 6
HELIX 20 20 LEU A 431 ILE A 435 5 5
HELIX 21 21 GLY A 438 ASN A 456 1 19
HELIX 22 22 PRO A 464 ILE A 468 5 5
SHEET 1 A 5 VAL A 65 LEU A 70 0
SHEET 2 A 5 ARG A 73 LEU A 78 -1 O VAL A 77 N PHE A 66
SHEET 3 A 5 GLU A 387 PRO A 390 1 O PHE A 389 N VAL A 76
SHEET 4 A 5 HIS A 369 THR A 370 -1 N HIS A 369 O VAL A 388
SHEET 5 A 5 GLY A 97 ARG A 98 -1 N GLY A 97 O THR A 370
SHEET 1 B 3 LEU A 164 LEU A 165 0
SHEET 2 B 3 ILE A 486 ALA A 490 -1 O ILE A 486 N LEU A 165
SHEET 3 B 3 PHE A 457 ALA A 460 -1 N ALA A 460 O ARG A 487
SHEET 1 C 2 THR A 375 PHE A 377 0
SHEET 2 C 2 TYR A 380 ILE A 382 -1 O TYR A 380 N PHE A 377
LINK SG CYS A 436 FE HEM A 501 1555 1555 2.54
SITE 1 AC1 20 ARG A 98 ILE A 114 TRP A 121 ARG A 125
SITE 2 AC1 20 ILE A 179 ALA A 298 GLY A 299 THR A 303
SITE 3 AC1 20 ILE A 363 VAL A 367 HIS A 369 LEU A 392
SITE 4 AC1 20 PRO A 428 PHE A 429 SER A 430 ARG A 434
SITE 5 AC1 20 CYS A 436 GLY A 438 ALA A 442 CGE A 505
SITE 1 AC2 2 GLU A 250 GLU A 322
SITE 1 AC3 3 LEU A 43 MET A 46 ASP A 47
SITE 1 AC4 6 LYS A 186 PHE A 188 PHE A 195 LEU A 198
SITE 2 AC4 6 PHE A 244 PHE A 296
SITE 1 AC5 8 ILE A 101 ILE A 114 ILE A 209 ALA A 297
SITE 2 AC5 8 ALA A 298 VAL A 367 VAL A 477 HEM A 501
SITE 1 AC6 4 THR A 404 PRO A 405 ASN A 406 THR A 407
CRYST1 91.385 91.385 152.286 90.00 90.00 120.00 P 31 2 1 6
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 0.010943 0.006318 0.000000 0.00000
SCALE2 0.000000 0.012636 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006567 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
