HEADER OXIDOREDUCTASE 21-OCT-11 3UA5
TITLE CRYSTAL STRUCTURE OF P450 2B6 (Y226H/K262R) IN COMPLEX WITH TWO
TITLE 2 MOLECULES OF AMLODIPINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME P450 2B6;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CYPIIB6, CYTOCHROME P450 IIB1;
COMPND 5 EC: 1.14.14.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CYP2B6;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PKK
KEYWDS P450, HUMAN CYTOCHROME P450 2B6, MONOOXYGENASE, OXIDOREDUCTASE,
KEYWDS 2 MEMBRANE PROTEIN, CYP 2B6
EXPDTA X-RAY DIFFRACTION
AUTHOR M.B.SHAH,C.D.STOUT,J.R.HALPERT
REVDAT 3 13-SEP-23 3UA5 1 REMARK SEQADV LINK
REVDAT 2 03-OCT-12 3UA5 1 JRNL
REVDAT 1 12-SEP-12 3UA5 0
JRNL AUTH M.B.SHAH,P.R.WILDERMAN,J.PASCUAL,Q.ZHANG,C.D.STOUT,
JRNL AUTH 2 J.R.HALPERT
JRNL TITL CONFORMATIONAL ADAPTATION OF HUMAN CYTOCHROME P450 2B6 AND
JRNL TITL 2 RABBIT CYTOCHROME P450 2B4 REVEALED UPON BINDING MULTIPLE
JRNL TITL 3 AMLODIPINE MOLECULES.
JRNL REF BIOCHEMISTRY V. 51 7225 2012
JRNL REFN ISSN 0006-2960
JRNL PMID 22909231
JRNL DOI 10.1021/BI300894Z
REMARK 2
REMARK 2 RESOLUTION. 2.80 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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 82.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.4
REMARK 3 NUMBER OF REFLECTIONS : 24667
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) : 0.245
REMARK 3 R VALUE (WORKING SET) : 0.242
REMARK 3 FREE R VALUE : 0.294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1305
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1627
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.53
REMARK 3 BIN R VALUE (WORKING SET) : 0.3170
REMARK 3 BIN FREE R VALUE SET COUNT : 92
REMARK 3 BIN FREE R VALUE : 0.3590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7379
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 198
REMARK 3 SOLVENT ATOMS : 78
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.88000
REMARK 3 B22 (A**2) : -3.28000
REMARK 3 B33 (A**2) : -3.60000
REMARK 3 B12 (A**2) : 0.00000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.482
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.420
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.595
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.917
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.870
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7775 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10563 ; 1.430 ; 2.016
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 924 ; 5.601 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 351 ;34.053 ;22.934
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1246 ;19.398 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 56 ;18.344 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1125 ; 0.154 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5992 ; 0.007 ; 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): 4630 ; 0.516 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7483 ; 1.007 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3145 ; 1.326 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3080 ; 2.366 ; 4.500
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 28 A 492 1
REMARK 3 1 B 28 B 492 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 3611 ; 0.060 ; 0.050
REMARK 3 TIGHT THERMAL 1 A (A**2): 3611 ; 0.080 ; 0.500
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 3UA5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-NOV-11.
REMARK 100 THE DEPOSITION ID IS D_1000068498.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUL-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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), SIDE SCATTERING I-BEAM
REMARK 200 BENT SINGLE CRYSTAL; ASYMMETRIC
REMARK 200 CUT 4.9650 DEG.
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25912
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 247.340
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.7
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.13100
REMARK 200 R SYM (I) : 0.13100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 3.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.60300
REMARK 200 R SYM FOR SHELL (I) : 0.60300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: 3IBD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM ACETATE TRIHYDRATE, 0.1M
REMARK 280 TRIS HCL PH 8.5 AND 30% W/V PEG4000, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 291K
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 29.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 123.67000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.15000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 123.67000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.15000
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, 3
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 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 29.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 39.15000
REMARK 350 BIOMT3 2 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 1
REMARK 465 ALA A 2
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 HIS A 493
REMARK 465 HIS A 494
REMARK 465 HIS A 495
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 LYS B 22
REMARK 465 LYS B 23
REMARK 465 THR B 24
REMARK 465 SER B 25
REMARK 465 SER B 26
REMARK 465 LYS B 27
REMARK 465 GLY B 28
REMARK 465 HIS B 280
REMARK 465 SER B 281
REMARK 465 HIS B 493
REMARK 465 HIS B 494
REMARK 465 HIS B 495
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 LYS A 29 CE NZ
REMARK 470 ARG A 35 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 39 CD1 CD2
REMARK 470 ARG A 85 CZ NH1 NH2
REMARK 470 ARG A 109 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 122 CE NZ
REMARK 470 ARG A 126 CZ NH1 NH2
REMARK 470 GLU A 155 OE1 OE2
REMARK 470 LYS A 159 CG CD CE NZ
REMARK 470 LYS A 161 CG CD CE NZ
REMARK 470 LYS A 197 CE NZ
REMARK 470 PHE A 213 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE A 223 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE A 227 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 273 OE1 OE2
REMARK 470 LYS A 274 CG CD CE NZ
REMARK 470 LYS A 345 CD CE NZ
REMARK 470 LYS A 384 NZ
REMARK 470 HIS A 492 CG ND1 CD2 CE1 NE2
REMARK 470 GLU B 60 CG CD OE1 OE2
REMARK 470 LYS B 61 CE NZ
REMARK 470 LYS B 122 CD CE NZ
REMARK 470 MET B 137 CG SD CE
REMARK 470 LYS B 159 CG CD CE NZ
REMARK 470 PHE B 169 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 186 CD CE NZ
REMARK 470 GLU B 194 CD OE1 OE2
REMARK 470 LYS B 197 CD CE NZ
REMARK 470 LYS B 225 CE NZ
REMARK 470 LYS B 236 NZ
REMARK 470 LYS B 251 NZ
REMARK 470 LYS B 274 CG CD CE NZ
REMARK 470 LYS B 276 CG CD CE NZ
REMARK 470 GLU B 282 CD OE1 OE2
REMARK 470 HIS B 285 O CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 345 CD CE NZ
REMARK 470 HIS B 492 CG ND1 CD2 CE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ALA A 116 NH2 ARG A 434 2.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO A 38 CD PRO A 38 N -0.108
REMARK 500
REMARK 500 REMARK: NULL
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 PRO A 383 C - N - CD ANGL. DEV. = -16.9 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 LEU A 30 136.76 -33.20
REMARK 500 VAL A 89 -60.15 -95.30
REMARK 500 THR A 302 -91.92 -118.70
REMARK 500 ASP A 411 -19.82 -45.16
REMARK 500 SER A 430 -178.66 58.43
REMARK 500 ILE A 435 145.83 -39.77
REMARK 500 VAL B 89 -60.53 -90.77
REMARK 500 THR B 302 -73.70 -121.11
REMARK 500 SER B 430 -172.38 77.27
REMARK 500 ARG B 434 41.19 -75.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 48 0.10 SIDE CHAIN
REMARK 500 ARG A 73 0.29 SIDE CHAIN
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 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 436 SG
REMARK 620 2 HEM A 500 NA 90.8
REMARK 620 3 HEM A 500 NB 81.8 97.3
REMARK 620 4 HEM A 500 NC 85.9 176.5 83.3
REMARK 620 5 HEM A 500 ND 97.0 92.7 169.9 86.6
REMARK 620 6 06X A 501 NAD 174.7 89.7 92.9 93.6 88.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 436 SG
REMARK 620 2 HEM B 500 NA 105.4
REMARK 620 3 HEM B 500 NB 89.1 84.0
REMARK 620 4 HEM B 500 NC 80.4 173.7 93.7
REMARK 620 5 HEM B 500 ND 100.1 93.2 170.8 88.2
REMARK 620 6 06X B 501 NAD 168.9 82.2 83.5 91.8 87.4
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 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 06X A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 06X A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 06X B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 06X B 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3IBD RELATED DB: PDB
REMARK 900 HUMAN CYTOCHROME P450 2B6 (Y226H/K262R) IN COMPLEX WITH 4-(4-
REMARK 900 CHLOROPHENYL)IMIDAZOLE
REMARK 900 RELATED ID: 3QOA RELATED DB: PDB
REMARK 900 HUMAN CYTOCHROME P450 2B6 (Y226H/K262R) IN COMPLEX WITH 4-
REMARK 900 BENZYLPYRIDINE
REMARK 900 RELATED ID: 3QU8 RELATED DB: PDB
REMARK 900 HUMAN CYTOCHROME P450 2B6 (Y226H/K262R) IN COMPLEX WITH 4-(4-
REMARK 900 NITROBENZYL)PYRIDINE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE RESIDUES 3-21 (LSVLLFLALLTGLLLLLVQ) OF CORRESPONDING DATABASE
REMARK 999 REFERENCE SEQUENCE (UNP P20813) IS DELETED IN THIS STRUCTURE.
DBREF 3UA5 A 29 491 UNP P20813 CP2B6_HUMAN 29 491
DBREF 3UA5 B 29 491 UNP P20813 CP2B6_HUMAN 29 491
SEQADV 3UA5 ALA A 2 UNP P20813 GLU 2 ENGINEERED MUTATION
SEQADV 3UA5 LYS A 22 UNP P20813 ARG 22 ENGINEERED MUTATION
SEQADV 3UA5 LYS A 23 UNP P20813 HIS 23 ENGINEERED MUTATION
SEQADV 3UA5 THR A 24 UNP P20813 PRO 24 ENGINEERED MUTATION
SEQADV 3UA5 SER A 25 UNP P20813 ASN 25 ENGINEERED MUTATION
SEQADV 3UA5 SER A 26 UNP P20813 THR 26 ENGINEERED MUTATION
SEQADV 3UA5 LYS A 27 UNP P20813 HIS 27 ENGINEERED MUTATION
SEQADV 3UA5 GLY A 28 UNP P20813 ASP 28 ENGINEERED MUTATION
SEQADV 3UA5 LYS A 29 UNP P20813 ARG 29 ENGINEERED MUTATION
SEQADV 3UA5 HIS A 226 UNP P20813 TYR 226 ENGINEERED MUTATION
SEQADV 3UA5 ARG A 262 UNP P20813 LYS 262 ENGINEERED MUTATION
SEQADV 3UA5 HIS A 492 UNP P20813 EXPRESSION TAG
SEQADV 3UA5 HIS A 493 UNP P20813 EXPRESSION TAG
SEQADV 3UA5 HIS A 494 UNP P20813 EXPRESSION TAG
SEQADV 3UA5 HIS A 495 UNP P20813 EXPRESSION TAG
SEQADV 3UA5 ALA B 2 UNP P20813 GLU 2 ENGINEERED MUTATION
SEQADV 3UA5 LYS B 22 UNP P20813 ARG 22 ENGINEERED MUTATION
SEQADV 3UA5 LYS B 23 UNP P20813 HIS 23 ENGINEERED MUTATION
SEQADV 3UA5 THR B 24 UNP P20813 PRO 24 ENGINEERED MUTATION
SEQADV 3UA5 SER B 25 UNP P20813 ASN 25 ENGINEERED MUTATION
SEQADV 3UA5 SER B 26 UNP P20813 THR 26 ENGINEERED MUTATION
SEQADV 3UA5 LYS B 27 UNP P20813 HIS 27 ENGINEERED MUTATION
SEQADV 3UA5 GLY B 28 UNP P20813 ASP 28 ENGINEERED MUTATION
SEQADV 3UA5 LYS B 29 UNP P20813 ARG 29 ENGINEERED MUTATION
SEQADV 3UA5 HIS B 226 UNP P20813 TYR 226 ENGINEERED MUTATION
SEQADV 3UA5 ARG B 262 UNP P20813 LYS 262 ENGINEERED MUTATION
SEQADV 3UA5 HIS B 492 UNP P20813 EXPRESSION TAG
SEQADV 3UA5 HIS B 493 UNP P20813 EXPRESSION TAG
SEQADV 3UA5 HIS B 494 UNP P20813 EXPRESSION TAG
SEQADV 3UA5 HIS B 495 UNP P20813 EXPRESSION TAG
SEQRES 1 A 476 MET ALA LYS LYS THR SER SER LYS GLY LYS LEU PRO PRO
SEQRES 2 A 476 GLY PRO ARG PRO LEU PRO LEU LEU GLY ASN LEU LEU GLN
SEQRES 3 A 476 MET ASP ARG ARG GLY LEU LEU LYS SER PHE LEU ARG PHE
SEQRES 4 A 476 ARG GLU LYS TYR GLY ASP VAL PHE THR VAL HIS LEU GLY
SEQRES 5 A 476 PRO ARG PRO VAL VAL MET LEU CYS GLY VAL GLU ALA ILE
SEQRES 6 A 476 ARG GLU ALA LEU VAL ASP LYS ALA GLU ALA PHE SER GLY
SEQRES 7 A 476 ARG GLY LYS ILE ALA MET VAL ASP PRO PHE PHE ARG GLY
SEQRES 8 A 476 TYR GLY VAL ILE PHE ALA ASN GLY ASN ARG TRP LYS VAL
SEQRES 9 A 476 LEU ARG ARG PHE SER VAL THR THR MET ARG ASP PHE GLY
SEQRES 10 A 476 MET GLY LYS ARG SER VAL GLU GLU ARG ILE GLN GLU GLU
SEQRES 11 A 476 ALA GLN CYS LEU ILE GLU GLU LEU ARG LYS SER LYS GLY
SEQRES 12 A 476 ALA LEU MET ASP PRO THR PHE LEU PHE GLN SER ILE THR
SEQRES 13 A 476 ALA ASN ILE ILE CYS SER ILE VAL PHE GLY LYS ARG PHE
SEQRES 14 A 476 HIS TYR GLN ASP GLN GLU PHE LEU LYS MET LEU ASN LEU
SEQRES 15 A 476 PHE TYR GLN THR PHE SER LEU ILE SER SER VAL PHE GLY
SEQRES 16 A 476 GLN LEU PHE GLU LEU PHE SER GLY PHE LEU LYS HIS PHE
SEQRES 17 A 476 PRO GLY ALA HIS ARG GLN VAL TYR LYS ASN LEU GLN GLU
SEQRES 18 A 476 ILE ASN ALA TYR ILE GLY HIS SER VAL GLU LYS HIS ARG
SEQRES 19 A 476 GLU THR LEU ASP PRO SER ALA PRO ARG ASP LEU ILE ASP
SEQRES 20 A 476 THR TYR LEU LEU HIS MET GLU LYS GLU LYS SER ASN ALA
SEQRES 21 A 476 HIS SER GLU PHE SER HIS GLN ASN LEU ASN LEU ASN THR
SEQRES 22 A 476 LEU SER LEU PHE PHE ALA GLY THR GLU THR THR SER THR
SEQRES 23 A 476 THR LEU ARG TYR GLY PHE LEU LEU MET LEU LYS TYR PRO
SEQRES 24 A 476 HIS VAL ALA GLU ARG VAL TYR ARG GLU ILE GLU GLN VAL
SEQRES 25 A 476 ILE GLY PRO HIS ARG PRO PRO GLU LEU HIS ASP ARG ALA
SEQRES 26 A 476 LYS MET PRO TYR THR GLU ALA VAL ILE TYR GLU ILE GLN
SEQRES 27 A 476 ARG PHE SER ASP LEU LEU PRO MET GLY VAL PRO HIS ILE
SEQRES 28 A 476 VAL THR GLN HIS THR SER PHE ARG GLY TYR ILE ILE PRO
SEQRES 29 A 476 LYS ASP THR GLU VAL PHE LEU ILE LEU SER THR ALA LEU
SEQRES 30 A 476 HIS ASP PRO HIS TYR PHE GLU LYS PRO ASP ALA PHE ASN
SEQRES 31 A 476 PRO ASP HIS PHE LEU ASP ALA ASN GLY ALA LEU LYS LYS
SEQRES 32 A 476 THR GLU ALA PHE ILE PRO PHE SER LEU GLY LYS ARG ILE
SEQRES 33 A 476 CYS LEU GLY GLU GLY ILE ALA ARG ALA GLU LEU PHE LEU
SEQRES 34 A 476 PHE PHE THR THR ILE LEU GLN ASN PHE SER MET ALA SER
SEQRES 35 A 476 PRO VAL ALA PRO GLU ASP ILE ASP LEU THR PRO GLN GLU
SEQRES 36 A 476 CYS GLY VAL GLY LYS ILE PRO PRO THR TYR GLN ILE ARG
SEQRES 37 A 476 PHE LEU PRO ARG HIS HIS HIS HIS
SEQRES 1 B 476 MET ALA LYS LYS THR SER SER LYS GLY LYS LEU PRO PRO
SEQRES 2 B 476 GLY PRO ARG PRO LEU PRO LEU LEU GLY ASN LEU LEU GLN
SEQRES 3 B 476 MET ASP ARG ARG GLY LEU LEU LYS SER PHE LEU ARG PHE
SEQRES 4 B 476 ARG GLU LYS TYR GLY ASP VAL PHE THR VAL HIS LEU GLY
SEQRES 5 B 476 PRO ARG PRO VAL VAL MET LEU CYS GLY VAL GLU ALA ILE
SEQRES 6 B 476 ARG GLU ALA LEU VAL ASP LYS ALA GLU ALA PHE SER GLY
SEQRES 7 B 476 ARG GLY LYS ILE ALA MET VAL ASP PRO PHE PHE ARG GLY
SEQRES 8 B 476 TYR GLY VAL ILE PHE ALA ASN GLY ASN ARG TRP LYS VAL
SEQRES 9 B 476 LEU ARG ARG PHE SER VAL THR THR MET ARG ASP PHE GLY
SEQRES 10 B 476 MET GLY LYS ARG SER VAL GLU GLU ARG ILE GLN GLU GLU
SEQRES 11 B 476 ALA GLN CYS LEU ILE GLU GLU LEU ARG LYS SER LYS GLY
SEQRES 12 B 476 ALA LEU MET ASP PRO THR PHE LEU PHE GLN SER ILE THR
SEQRES 13 B 476 ALA ASN ILE ILE CYS SER ILE VAL PHE GLY LYS ARG PHE
SEQRES 14 B 476 HIS TYR GLN ASP GLN GLU PHE LEU LYS MET LEU ASN LEU
SEQRES 15 B 476 PHE TYR GLN THR PHE SER LEU ILE SER SER VAL PHE GLY
SEQRES 16 B 476 GLN LEU PHE GLU LEU PHE SER GLY PHE LEU LYS HIS PHE
SEQRES 17 B 476 PRO GLY ALA HIS ARG GLN VAL TYR LYS ASN LEU GLN GLU
SEQRES 18 B 476 ILE ASN ALA TYR ILE GLY HIS SER VAL GLU LYS HIS ARG
SEQRES 19 B 476 GLU THR LEU ASP PRO SER ALA PRO ARG ASP LEU ILE ASP
SEQRES 20 B 476 THR TYR LEU LEU HIS MET GLU LYS GLU LYS SER ASN ALA
SEQRES 21 B 476 HIS SER GLU PHE SER HIS GLN ASN LEU ASN LEU ASN THR
SEQRES 22 B 476 LEU SER LEU PHE PHE ALA GLY THR GLU THR THR SER THR
SEQRES 23 B 476 THR LEU ARG TYR GLY PHE LEU LEU MET LEU LYS TYR PRO
SEQRES 24 B 476 HIS VAL ALA GLU ARG VAL TYR ARG GLU ILE GLU GLN VAL
SEQRES 25 B 476 ILE GLY PRO HIS ARG PRO PRO GLU LEU HIS ASP ARG ALA
SEQRES 26 B 476 LYS MET PRO TYR THR GLU ALA VAL ILE TYR GLU ILE GLN
SEQRES 27 B 476 ARG PHE SER ASP LEU LEU PRO MET GLY VAL PRO HIS ILE
SEQRES 28 B 476 VAL THR GLN HIS THR SER PHE ARG GLY TYR ILE ILE PRO
SEQRES 29 B 476 LYS ASP THR GLU VAL PHE LEU ILE LEU SER THR ALA LEU
SEQRES 30 B 476 HIS ASP PRO HIS TYR PHE GLU LYS PRO ASP ALA PHE ASN
SEQRES 31 B 476 PRO ASP HIS PHE LEU ASP ALA ASN GLY ALA LEU LYS LYS
SEQRES 32 B 476 THR GLU ALA PHE ILE PRO PHE SER LEU GLY LYS ARG ILE
SEQRES 33 B 476 CYS LEU GLY GLU GLY ILE ALA ARG ALA GLU LEU PHE LEU
SEQRES 34 B 476 PHE PHE THR THR ILE LEU GLN ASN PHE SER MET ALA SER
SEQRES 35 B 476 PRO VAL ALA PRO GLU ASP ILE ASP LEU THR PRO GLN GLU
SEQRES 36 B 476 CYS GLY VAL GLY LYS ILE PRO PRO THR TYR GLN ILE ARG
SEQRES 37 B 476 PHE LEU PRO ARG HIS HIS HIS HIS
HET HEM A 500 43
HET 06X A 501 28
HET 06X A 502 28
HET HEM B 500 43
HET 06X B 501 28
HET 06X B 502 28
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM 06X AMLODIPINE
HETSYN HEM HEME
HETSYN 06X O3-ETHYL O5-METHYL 2-(2-AZANYLETHOXYMETHYL)-4-(2-
HETSYN 2 06X CHLOROPHENYL)-6-METHYL-1,4-DIHYDROPYRIDINE-3,5-
HETSYN 3 06X DICARBOXYLATE
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 06X 4(C20 H25 CL N2 O5)
FORMUL 9 HOH *78(H2 O)
HELIX 1 1 GLY A 50 GLY A 63 1 14
HELIX 2 2 CYS A 79 VAL A 89 1 11
HELIX 3 3 LYS A 91 SER A 96 1 6
HELIX 4 4 VAL A 104 ARG A 109 1 6
HELIX 5 5 ASN A 117 PHE A 135 1 19
HELIX 6 6 SER A 141 SER A 160 1 20
HELIX 7 7 PRO A 167 GLY A 185 1 19
HELIX 8 8 ASP A 192 SER A 210 1 19
HELIX 9 9 SER A 211 LYS A 225 1 15
HELIX 10 10 GLY A 229 GLU A 254 1 26
HELIX 11 11 ASP A 263 SER A 277 1 15
HELIX 12 12 ASN A 287 THR A 300 1 14
HELIX 13 13 THR A 302 TYR A 317 1 16
HELIX 14 14 TYR A 317 ILE A 332 1 16
HELIX 15 15 GLU A 339 LYS A 345 5 7
HELIX 16 16 MET A 346 ASP A 361 1 16
HELIX 17 17 ILE A 391 HIS A 397 1 7
HELIX 18 18 ASN A 409 LEU A 414 5 6
HELIX 19 19 GLY A 438 PHE A 457 1 20
HELIX 20 20 ALA A 464 ILE A 468 5 5
HELIX 21 21 ASN B 42 MET B 46 5 5
HELIX 22 22 GLY B 50 GLY B 63 1 14
HELIX 23 23 CYS B 79 VAL B 89 1 11
HELIX 24 24 LYS B 91 SER B 96 1 6
HELIX 25 25 VAL B 104 ARG B 109 1 6
HELIX 26 26 ASN B 117 PHE B 135 1 19
HELIX 27 27 SER B 141 SER B 160 1 20
HELIX 28 28 PRO B 167 GLY B 185 1 19
HELIX 29 29 ASP B 192 SER B 210 1 19
HELIX 30 30 SER B 211 PHE B 220 1 10
HELIX 31 31 PHE B 220 LYS B 225 1 6
HELIX 32 32 GLY B 229 THR B 255 1 27
HELIX 33 33 ASP B 263 SER B 277 1 15
HELIX 34 34 ASN B 287 THR B 300 1 14
HELIX 35 35 THR B 302 TYR B 317 1 16
HELIX 36 36 TYR B 317 ILE B 332 1 16
HELIX 37 37 GLU B 339 LYS B 345 5 7
HELIX 38 38 MET B 346 ASP B 361 1 16
HELIX 39 39 LEU B 392 HIS B 397 1 6
HELIX 40 40 ASN B 409 LEU B 414 5 6
HELIX 41 41 GLY B 438 PHE B 457 1 20
HELIX 42 42 ALA B 464 ILE B 468 5 5
SHEET 1 A 4 VAL A 65 LEU A 70 0
SHEET 2 A 4 ARG A 73 LEU A 78 -1 O MET A 77 N PHE A 66
SHEET 3 A 4 GLU A 387 LEU A 390 1 O PHE A 389 N VAL A 76
SHEET 4 A 4 HIS A 369 ILE A 370 -1 N HIS A 369 O VAL A 388
SHEET 1 B 2 THR A 375 SER A 376 0
SHEET 2 B 2 ILE A 381 ILE A 382 -1 O ILE A 382 N THR A 375
SHEET 1 C 2 SER A 458 ALA A 460 0
SHEET 2 C 2 ARG A 487 LEU A 489 -1 O LEU A 489 N SER A 458
SHEET 1 D 4 VAL B 65 LEU B 70 0
SHEET 2 D 4 ARG B 73 LEU B 78 -1 O VAL B 75 N VAL B 68
SHEET 3 D 4 GLU B 387 LEU B 390 1 O GLU B 387 N VAL B 76
SHEET 4 D 4 HIS B 369 ILE B 370 -1 N HIS B 369 O VAL B 388
SHEET 1 E 2 THR B 375 SER B 376 0
SHEET 2 E 2 ILE B 381 ILE B 382 -1 O ILE B 382 N THR B 375
SHEET 1 F 2 SER B 458 ALA B 460 0
SHEET 2 F 2 ARG B 487 LEU B 489 -1 O LEU B 489 N SER B 458
LINK SG CYS A 436 FE HEM A 500 1555 1555 2.60
LINK FE HEM A 500 NAD 06X A 501 1555 1555 2.21
LINK SG CYS B 436 FE HEM B 500 1555 1555 2.39
LINK FE HEM B 500 NAD 06X B 501 1555 1555 2.21
CISPEP 1 ARG A 48 ARG A 49 0 -6.25
CISPEP 2 ARG B 48 ARG B 49 0 5.97
SITE 1 AC1 16 ARG A 98 VAL A 113 TRP A 121 ARG A 125
SITE 2 AC1 16 ALA A 298 GLY A 299 THR A 302 HIS A 369
SITE 3 AC1 16 PRO A 428 PHE A 429 SER A 430 ARG A 434
SITE 4 AC1 16 CYS A 436 LEU A 437 GLY A 438 06X A 501
SITE 1 AC2 7 ILE A 101 PHE A 115 ALA A 298 THR A 300
SITE 2 AC2 7 THR A 302 VAL A 477 HEM A 500
SITE 1 AC3 10 ARG A 49 LEU A 51 ARG A 73 GLN A 215
SITE 2 AC3 10 GLU A 218 LEU A 219 MET A 365 PHE A 389
SITE 3 AC3 10 GLY A 476 VAL A 477
SITE 1 AC4 16 ARG B 98 VAL B 113 TRP B 121 ARG B 125
SITE 2 AC4 16 THR B 302 THR B 306 LEU B 362 HIS B 369
SITE 3 AC4 16 PRO B 428 PHE B 429 SER B 430 ARG B 434
SITE 4 AC4 16 CYS B 436 LEU B 437 GLY B 438 06X B 501
SITE 1 AC5 11 ILE B 101 PHE B 115 PHE B 206 SER B 210
SITE 2 AC5 11 PHE B 297 ALA B 298 THR B 300 GLU B 301
SITE 3 AC5 11 THR B 302 VAL B 477 HEM B 500
SITE 1 AC6 9 LEU B 51 ARG B 73 GLN B 215 GLU B 218
SITE 2 AC6 9 LEU B 219 PRO B 368 PHE B 389 GLY B 476
SITE 3 AC6 9 VAL B 477
CRYST1 58.000 78.300 247.340 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 0.017241 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012771 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004043 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
