HEADER OXIDOREDUCTASE 08-OCT-12 4HGF
TITLE CRYSTAL STRUCTURE OF P450 BM3 5F5K HEME DOMAIN VARIANT COMPLEXED WITH
TITLE 2 STYRENE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIFUNCTIONAL P-450/NADPH-P450 REDUCTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: HEME-BINDING DOMAIN;
COMPND 5 SYNONYM: CYTOCHROME P450(BM-3), CYTOCHROME P450BM-3, CYTOCHROME P450
COMPND 6 102, NADPH--CYTOCHROME P450 REDUCTASE;
COMPND 7 EC: 1.14.14.1, 1.6.2.4;
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: CYP102, CYP102A1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PETM11
KEYWDS OXIDOREDUCTASE, P450 BM3, HEMOPROTEIN, STYRENE EPOXIDATION, INVERTED
KEYWDS 2 ENANTIOSELECTIVITY, HEME BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR A.SHEHZAD,S.PANNEERSELVAM,M.BOCOLA,J.MUELLER-DIECKMANN,M.WILMANNS,
AUTHOR 2 U.SCHWANEBERG
REVDAT 3 20-SEP-23 4HGF 1 REMARK SEQADV
REVDAT 2 08-MAY-13 4HGF 1 JRNL
REVDAT 1 01-MAY-13 4HGF 0
JRNL AUTH A.SHEHZAD,S.PANNEERSELVAM,M.LINOW,M.BOCOLA,D.ROCCATANO,
JRNL AUTH 2 J.MUELLER-DIECKMANN,M.WILMANNS,U.SCHWANEBERG
JRNL TITL P450 BM3 CRYSTAL STRUCTURES REVEAL THE ROLE OF THE CHARGED
JRNL TITL 2 SURFACE RESIDUE LYS/ARG184 IN INVERSION OF ENANTIOSELECTIVE
JRNL TITL 3 STYRENE EPOXIDATION.
JRNL REF CHEM.COMMUN.(CAMB.) V. 49 4694 2013
JRNL REFN ISSN 1359-7345
JRNL PMID 23589805
JRNL DOI 10.1039/C3CC39076D
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.L.TEE,U.SCHWANEBERG
REMARK 1 TITL A SCREENING SYSTEM FOR THE DIRECTED EVOLUTION OF
REMARK 1 TITL 2 EPOXYGENASES: IMPORTANCE OF POSITION 184 IN P450 BM3 FOR
REMARK 1 TITL 3 STEREOSELECTIVE STYRENE EPOXIDATION.
REMARK 1 REF ANGEW.CHEM.INT.ED.ENGL. V. 45 5380 2006
REMARK 1 REFN ISSN 1433-7851
REMARK 1 PMID 16847856
REMARK 1 DOI 10.1002/ANIE.200600255
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.51
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 117395
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.700
REMARK 3 FREE R VALUE TEST SET COUNT : 811
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8602
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.27
REMARK 3 BIN R VALUE (WORKING SET) : 0.3500
REMARK 3 BIN FREE R VALUE SET COUNT : 67
REMARK 3 BIN FREE R VALUE : 0.3850
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7117
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 103
REMARK 3 SOLVENT ATOMS : 869
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.49
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.07000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.06000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.04000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.101
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.103
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 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7499 ; 0.026 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10176 ; 2.667 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 913 ; 6.935 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 358 ;34.483 ;24.860
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1370 ;15.858 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 39 ;13.413 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1087 ; 0.156 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5709 ; 0.013 ; 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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4HGF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-OCT-12.
REMARK 100 THE DEPOSITION ID IS D_1000075434.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-MAY-10
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 : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X13
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.81
REMARK 200 MONOCHROMATOR : SI 111 HORIZONTALLY FOCUSSING
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 117395
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 19.510
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.9900
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) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
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: AUTO-RICKSHAW
REMARK 200 STARTING MODEL: PDB ENTRY 2J4S
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 300 MM MAGNESIUM FORMATE, 100 MM
REMARK 280 TRIS(HYDROXYMETHYL)AMINOMETHANE (PH 8.5), 200 MM SODIUM MALONATE/
REMARK 280 110 MM POTASSIUM CHLORIDE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 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 74.06250
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASN A 186
REMARK 465 LYS A 187
REMARK 465 LEU A 188
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 THR B 1
REMARK 465 ASN B 186
REMARK 465 LYS B 187
REMARK 465 LEU B 188
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 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 OD2 ASP A 370 NH1 ARG A 375 1.91
REMARK 500 NE2 GLN B 128 O HOH B 1003 1.92
REMARK 500 OD2 ASP B 222 O HOH B 885 2.05
REMARK 500 O HOH A 794 O HOH A 1012 2.06
REMARK 500 O HOH B 948 O HOH B 965 2.09
REMARK 500 O HOH A 922 O HOH A 931 2.13
REMARK 500 O HOH A 943 O HOH A 999 2.13
REMARK 500 O HOH B 736 O HOH B 802 2.17
REMARK 500 OE1 GLN B 109 OH TYR B 305 2.18
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 -130.86 54.89
REMARK 500 ASP A 84 37.01 -98.20
REMARK 500 ASP A 136 -3.26 75.72
REMARK 500 GLU A 183 37.02 -61.53
REMARK 500 LYS A 184 65.24 -169.48
REMARK 500 HIS A 266 -30.48 -140.91
REMARK 500 ASP A 370 35.10 -69.79
REMARK 500 THR A 436 -132.61 -124.93
REMARK 500 LYS B 15 -127.73 56.90
REMARK 500 ASP B 136 17.05 59.50
REMARK 500 GLU B 183 30.96 -62.80
REMARK 500 LYS B 184 -52.94 -145.38
REMARK 500 GLU B 200 35.91 -85.06
REMARK 500 HIS B 266 -37.91 -138.46
REMARK 500 LYS B 349 124.35 -34.55
REMARK 500 ASP B 370 40.12 -81.06
REMARK 500 THR B 436 -132.41 -126.59
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 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 400 SG
REMARK 620 2 HEM A 501 NA 98.9
REMARK 620 3 HEM A 501 NB 88.8 87.5
REMARK 620 4 HEM A 501 NC 86.6 173.5 89.3
REMARK 620 5 HEM A 501 ND 97.4 90.9 173.8 91.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 400 SG
REMARK 620 2 HEM B 501 NA 98.4
REMARK 620 3 HEM B 501 NB 89.5 90.8
REMARK 620 4 HEM B 501 NC 88.7 172.9 89.6
REMARK 620 5 HEM B 501 ND 96.8 88.6 173.7 90.3
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 SYN A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SYN B 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BU7 RELATED DB: PDB
REMARK 900 CRYOGENIC STRUCTURE OF CYTOCHROME P450BM-3 HEME DOMAIN
REMARK 900 RELATED ID: 1JPZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A COMPLEX OF THE HEME DOMAIN OF P450BM-3 WITH
REMARK 900 N-PALMITOYLGLYCINE
DBREF 4HGF A 1 455 UNP P14779 CPXB_BACME 2 456
DBREF 4HGF B 1 455 UNP P14779 CPXB_BACME 2 456
SEQADV 4HGF ALA A 87 UNP P14779 PHE 88 ENGINEERED MUTATION
SEQADV 4HGF LYS A 184 UNP P14779 ALA 185 ENGINEERED MUTATION
SEQADV 4HGF ALA A 235 UNP P14779 THR 236 ENGINEERED MUTATION
SEQADV 4HGF ALA B 87 UNP P14779 PHE 88 ENGINEERED MUTATION
SEQADV 4HGF LYS B 184 UNP P14779 ALA 185 ENGINEERED MUTATION
SEQADV 4HGF ALA B 235 UNP P14779 THR 236 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 ALA 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 LYS 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 ALA 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 PHE 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 ALA 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 LYS 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 ALA 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 PHE 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 501 43
HET SYN A 502 8
HET CL A 503 1
HET HEM B 501 43
HET SYN B 502 8
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM SYN ETHENYLBENZENE
HETNAM CL CHLORIDE ION
HETSYN HEM HEME
HETSYN SYN STYRENE
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 SYN 2(C8 H8)
FORMUL 5 CL CL 1-
FORMUL 8 HOH *869(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 GLY A 85 SER A 89 5 5
HELIX 7 7 GLU A 93 LEU A 104 1 12
HELIX 8 8 PRO A 105 PHE A 107 5 3
HELIX 9 9 SER A 108 ARG A 132 1 25
HELIX 10 10 VAL A 141 ASN A 159 1 19
HELIX 11 11 ASN A 163 ARG A 167 5 5
HELIX 12 12 HIS A 171 GLU A 183 1 13
HELIX 13 13 GLN A 204 SER A 226 1 23
HELIX 14 14 ASP A 232 GLY A 240 1 9
HELIX 15 15 ASP A 250 GLY A 265 1 16
HELIX 16 16 HIS A 266 ASN A 283 1 18
HELIX 17 17 ASN A 283 LEU A 298 1 16
HELIX 18 18 SER A 304 GLN A 310 1 7
HELIX 19 19 LEU A 311 TRP A 325 1 15
HELIX 20 20 GLY A 342 GLU A 344 5 3
HELIX 21 21 ILE A 357 HIS A 361 1 5
HELIX 22 22 ASP A 363 GLY A 368 1 6
HELIX 23 23 ARG A 375 GLU A 380 5 6
HELIX 24 24 ASN A 381 ILE A 385 5 5
HELIX 25 25 ASN A 395 ALA A 399 5 5
HELIX 26 26 GLY A 402 HIS A 420 1 19
HELIX 27 27 PHE B 11 LYS B 15 5 5
HELIX 28 28 ASN B 16 ASN B 21 5 6
HELIX 29 29 LYS B 24 GLY B 37 1 14
HELIX 30 30 SER B 54 CYS B 62 1 9
HELIX 31 31 SER B 72 GLY B 83 1 12
HELIX 32 32 GLU B 93 LEU B 104 1 12
HELIX 33 33 PRO B 105 PHE B 107 5 3
HELIX 34 34 SER B 108 ARG B 132 1 25
HELIX 35 35 VAL B 141 ASN B 159 1 19
HELIX 36 36 ASN B 163 ARG B 167 5 5
HELIX 37 37 HIS B 171 GLU B 183 1 13
HELIX 38 38 GLU B 200 ALA B 225 1 26
HELIX 39 39 ASP B 232 GLY B 240 1 9
HELIX 40 40 ASP B 250 GLY B 265 1 16
HELIX 41 41 HIS B 266 ASN B 283 1 18
HELIX 42 42 ASN B 283 LEU B 298 1 16
HELIX 43 43 SER B 304 GLN B 310 1 7
HELIX 44 44 LEU B 311 TRP B 325 1 15
HELIX 45 45 GLY B 342 GLU B 344 5 3
HELIX 46 46 ILE B 357 HIS B 361 1 5
HELIX 47 47 ASP B 363 GLY B 368 1 6
HELIX 48 48 ARG B 375 GLU B 380 5 6
HELIX 49 49 ASN B 381 ILE B 385 5 5
HELIX 50 50 ASN B 395 ALA B 399 5 5
HELIX 51 51 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 MET A 354 N LEU A 52
SHEET 4 A 5 ALA A 330 ALA A 335 -1 N PHE A 331 O VAL A 355
SHEET 5 A 5 PHE A 67 ASN A 70 -1 N ASP A 68 O 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 GLU A 424 O LYS A 447
SHEET 1 C 2 THR A 339 LEU A 341 0
SHEET 2 C 2 TYR A 345 LEU A 347 -1 O LEU A 347 N THR A 339
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 ALA B 44 0
SHEET 2 E 5 ARG B 47 LEU B 52 -1 O THR B 49 N PHE B 42
SHEET 3 E 5 GLU B 352 LEU B 356 1 O MET B 354 N LEU B 52
SHEET 4 E 5 ALA B 330 ALA B 335 -1 N PHE B 331 O VAL B 355
SHEET 5 E 5 PHE B 67 ASN B 70 -1 N ASN B 70 O SER B 332
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 N GLU B 424 O LYS B 447
SHEET 1 G 2 THR B 339 LEU B 341 0
SHEET 2 G 2 TYR B 345 LEU B 347 -1 O LEU B 347 N THR B 339
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 501 1555 1555 2.26
LINK SG CYS B 400 FE HEM B 501 1555 1555 2.29
SITE 1 AC1 26 LYS A 69 LEU A 86 ALA A 87 TRP A 96
SITE 2 AC1 26 PHE A 261 ALA A 264 GLY A 265 THR A 268
SITE 3 AC1 26 THR A 269 THR A 327 PHE A 331 PRO A 392
SITE 4 AC1 26 PHE A 393 GLY A 394 ARG A 398 ALA A 399
SITE 5 AC1 26 CYS A 400 ILE A 401 GLY A 402 SYN A 502
SITE 6 AC1 26 HOH A 602 HOH A 627 HOH A 647 HOH A 665
SITE 7 AC1 26 HOH A 690 HOH A 961
SITE 1 AC2 4 ALA A 264 THR A 268 HEM A 501 HOH A 874
SITE 1 AC3 1 ARG A 375
SITE 1 AC4 28 LYS B 69 LEU B 86 ALA B 87 TRP B 96
SITE 2 AC4 28 PHE B 107 PHE B 261 ALA B 264 GLY B 265
SITE 3 AC4 28 THR B 268 THR B 269 THR B 327 PHE B 331
SITE 4 AC4 28 PRO B 392 PHE B 393 GLY B 394 ARG B 398
SITE 5 AC4 28 ALA B 399 CYS B 400 ILE B 401 GLY B 402
SITE 6 AC4 28 ALA B 406 SYN B 502 HOH B 614 HOH B 615
SITE 7 AC4 28 HOH B 624 HOH B 632 HOH B 652 HOH B 983
SITE 1 AC5 6 ALA B 87 ALA B 264 THR B 268 HEM B 501
SITE 2 AC5 6 HOH B 821 HOH B1046
CRYST1 59.138 148.125 64.066 90.00 98.16 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 0.016910 0.000000 0.002425 0.00000
SCALE2 0.000000 0.006751 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015769 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
