HEADER OXIDOREDUCTASE 05-MAR-10 2X80
TITLE P450 BM3 F87A IN COMPLEX WITH DMSO
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIFUNCTIONAL P-450/NADPH-P450 REDUCTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: HEME DOMAIN, RESIDUES 2-456;
COMPND 5 SYNONYM: P450 BM3, CYTOCHROME P450, BM-3, P450BM-3;
COMPND 6 EC: 1.14.14.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS MEGATERIUM;
SOURCE 3 ORGANISM_TAXID: 1404;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PETM11
KEYWDS ELECTRON TRANSPORT, OXIDOREDUCTASE, DMSO-INHIBITION, METAL-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR J.KUPER,T.S.WONG,D.ROCCATANO,M.WILMANNS,U.SCHWANEBERG
REVDAT 5 20-DEC-23 2X80 1 REMARK LINK
REVDAT 4 24-JUL-19 2X80 1 REMARK
REVDAT 3 19-SEP-12 2X80 1 JRNL
REVDAT 2 12-SEP-12 2X80 1 COMPND JRNL REMARK VERSN
REVDAT 1 23-MAR-11 2X80 0
JRNL AUTH J.KUPER,K.L.TEE,M.WILMANNS,D.ROCCATANO,U.SCHWANEBERG,
JRNL AUTH 2 T.S.WONG
JRNL TITL THE ROLE OF ACTIVE-SITE PHE87 IN MODULATING THE ORGANIC
JRNL TITL 2 CO-SOLVENT TOLERANCE OF CYTOCHROME P450 BM3 MONOOXYGENASE.
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 68 1013 2012
JRNL REFN ESSN 1744-3091
JRNL PMID 22949185
JRNL DOI 10.1107/S1744309112031570
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 58625
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) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2979
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 698
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.94
REMARK 3 BIN R VALUE (WORKING SET) : 0.2650
REMARK 3 BIN FREE R VALUE SET COUNT : 33
REMARK 3 BIN FREE R VALUE : 0.2220
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7330
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 97
REMARK 3 SOLVENT ATOMS : 406
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.98
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.17900
REMARK 3 B22 (A**2) : 4.39200
REMARK 3 B33 (A**2) : -2.21300
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): 0.270
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.220
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.166
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.742
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7605 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10310 ; 1.289 ; 2.005
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 908 ; 5.842 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 368 ;36.467 ;24.891
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1356 ;15.176 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;16.590 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1102 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5800 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3429 ; 0.201 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5182 ; 0.299 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 424 ; 0.238 ; 0.200
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): 24 ; 0.170 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.120 ; 0.200
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): 4721 ; 0.697 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7368 ; 1.163 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3278 ; 1.591 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2938 ; 2.500 ; 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 : 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 : BABINET MODEL PLUS 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 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2X80 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-MAR-10.
REMARK 100 THE DEPOSITION ID IS D_1290043069.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-APR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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 : X12
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58691
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 47.620
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.490
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.42
REMARK 200 R MERGE FOR SHELL (I) : 0.49000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.170
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 2J4S
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 41.10500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.09850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.31950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.09850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.10500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.31950
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
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, PHE 88 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, PHE 88 TO ALA
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 148 CA - CB - CG ANGL. DEV. = 15.3 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 -131.15 58.19
REMARK 500 PRO A 45 109.45 -39.49
REMARK 500 ASP A 84 40.46 -95.80
REMARK 500 ASP A 136 -47.95 -26.19
REMARK 500 PHE A 158 34.07 -144.23
REMARK 500 ASP A 232 -176.37 -63.38
REMARK 500 LYS A 349 123.99 -36.12
REMARK 500 ASP A 370 30.46 -93.48
REMARK 500 THR A 436 -126.58 -128.13
REMARK 500 LYS B 15 -126.59 53.70
REMARK 500 ASN B 21 75.27 -101.25
REMARK 500 ASP B 84 40.59 -98.25
REMARK 500 PHE B 158 29.69 -147.90
REMARK 500 PRO B 196 1.08 -63.23
REMARK 500 GLU B 244 -78.63 -67.68
REMARK 500 GLU B 344 -30.37 -133.88
REMARK 500 THR B 436 -129.70 -128.91
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 ZN B1457 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 285 NE2
REMARK 620 2 ASP B 338 OD2 109.2
REMARK 620 3 GLU B 348 OE2 99.1 124.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1457 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 348 OE2
REMARK 620 2 ASP B 23 OD2 105.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A1456 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 400 SG
REMARK 620 2 HEM A1456 NA 98.5
REMARK 620 3 HEM A1456 NB 87.0 92.7
REMARK 620 4 HEM A1456 NC 88.7 172.6 89.4
REMARK 620 5 HEM A1456 ND 101.5 87.1 171.4 89.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1458 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 231 OD2
REMARK 620 2 HIS B 236 NE2 130.1
REMARK 620 3 HIS B 285 NE2 99.6 106.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B1456 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 400 SG
REMARK 620 2 HEM B1456 NA 99.3
REMARK 620 3 HEM B1456 NB 92.4 85.9
REMARK 620 4 HEM B1456 NC 91.3 169.3 92.2
REMARK 620 5 HEM B1456 ND 98.7 91.9 168.9 88.0
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 1456
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1457
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 1458
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 1456
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1457
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1458
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 1459
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1P0V RELATED DB: PDB
REMARK 900 F393A MUTANT HEME DOMAIN OF FLAVOCYTOCHROME P450 BM3
REMARK 900 RELATED ID: 1FAG RELATED DB: PDB
REMARK 900 STRUCTURE OF CYTOCHROME P450
REMARK 900 RELATED ID: 1SMI RELATED DB: PDB
REMARK 900 A SINGLE MUTATION OF P450 BM3 INDUCES THE
REMARK 900 CONFORMATIONALREARRANGEMENT SEEN UPON SUBSTRATE-BINDING IN WILD-
REMARK 900 TYPEENZYME
REMARK 900 RELATED ID: 2J1M RELATED DB: PDB
REMARK 900 BM3 P450 IN COMPLEX WITH DMSO
REMARK 900 RELATED ID: 1JME RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PHE393HIS CYTOCHROME P450 BM3
REMARK 900 RELATED ID: 2X7Y RELATED DB: PDB
REMARK 900 P450 BM3 F87A IN COMPLEX WITH DMSO
REMARK 900 RELATED ID: 1SMJ RELATED DB: PDB
REMARK 900 STRUCTURE OF THE A264E MUTANT OF CYTOCHROME P450 BM3COMPLEXED WITH
REMARK 900 PALMITOLEATE
REMARK 900 RELATED ID: 2J4S RELATED DB: PDB
REMARK 900 P450 BM3 HEME DOMAIN IN COMPLEX WITH DMSO
REMARK 900 RELATED ID: 2HPD RELATED DB: PDB
REMARK 900 RELATED ID: 1BVY RELATED DB: PDB
REMARK 900 COMPLEX OF THE HEME AND FMN-BINDING DOMAINS OF THE CYTOCHROME
REMARK 900 P450(BM-3)
REMARK 900 RELATED ID: 1BU7 RELATED DB: PDB
REMARK 900 CRYOGENIC STRUCTURE OF CYTOCHROME P450BM-3 HEME DOMAIN
REMARK 900 RELATED ID: 1YQP RELATED DB: PDB
REMARK 900 T268N MUTANT CYTOCHROME DOMAIN OF FLAVOCYTOCHROME P450 BM3
REMARK 900 RELATED ID: 2UWH RELATED DB: PDB
REMARK 900 CYTOCHROME P450 BM3 MUTANT IN COMPLEX WITH PALMITIC ACID
REMARK 900 RELATED ID: 2BMH RELATED DB: PDB
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
REMARK 900 RELATED ID: 1YQO RELATED DB: PDB
REMARK 900 T268A MUTANT HEME DOMAIN OF FLAVOCYTOCHROME P450 BM3
REMARK 900 RELATED ID: 1P0X RELATED DB: PDB
REMARK 900 F393Y MUTANT HEME DOMAIN OF FLAVOCYTOCHROME P450 BM3
REMARK 900 RELATED ID: 1FAH RELATED DB: PDB
REMARK 900 STRUCTURE OF CYTOCHROME P450
REMARK 900 RELATED ID: 1P0W RELATED DB: PDB
REMARK 900 F393W MUTANT HEME DOMAIN OF FLAVOCYTOCHROME P450 BM3
DBREF 2X80 A 1 455 UNP P14779 CPXB_BACME 2 456
DBREF 2X80 B 1 455 UNP P14779 CPXB_BACME 2 456
SEQADV 2X80 ALA A 87 UNP P14779 PHE 88 ENGINEERED MUTATION
SEQADV 2X80 ALA B 87 UNP P14779 PHE 88 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 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 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 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 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 A1456 43
HET ZN A1457 1
HET DMS A1458 4
HET HEM B1456 43
HET ZN B1457 1
HET ZN B1458 1
HET DMS B1459 4
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM ZN ZINC ION
HETNAM DMS DIMETHYL SULFOXIDE
HETSYN HEM HEME
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 ZN 3(ZN 2+)
FORMUL 5 DMS 2(C2 H6 O S)
FORMUL 10 HOH *406(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 SER A 108 5 4
HELIX 8 8 ALA A 111 ARG A 132 1 22
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 ASP A 195 ALA A 197 5 3
HELIX 13 13 TYR A 198 GLY A 227 1 30
HELIX 14 14 ASP A 232 GLY A 240 1 9
HELIX 15 15 ASP A 250 ASN A 283 1 34
HELIX 16 16 ASN A 283 LEU A 298 1 16
HELIX 17 17 SER A 304 LYS A 309 1 6
HELIX 18 18 LEU A 311 TRP A 325 1 15
HELIX 19 19 ILE A 357 HIS A 361 1 5
HELIX 20 20 ASP A 363 GLY A 368 1 6
HELIX 21 21 ARG A 375 GLU A 380 5 6
HELIX 22 22 ASN A 381 ILE A 385 5 5
HELIX 23 23 ASN A 395 ALA A 399 5 5
HELIX 24 24 GLY A 402 HIS A 420 1 19
HELIX 25 25 PHE B 11 LYS B 15 5 5
HELIX 26 26 ASN B 16 LEU B 20 5 5
HELIX 27 27 LYS B 24 GLY B 37 1 14
HELIX 28 28 SER B 54 CYS B 62 1 9
HELIX 29 29 SER B 72 GLY B 83 1 12
HELIX 30 30 GLY B 85 SER B 89 5 5
HELIX 31 31 GLU B 93 LEU B 104 1 12
HELIX 32 32 PRO B 105 SER B 108 5 4
HELIX 33 33 ALA B 111 LEU B 133 1 23
HELIX 34 34 VAL B 141 ASN B 159 1 19
HELIX 35 35 ASN B 163 ARG B 167 5 5
HELIX 36 36 HIS B 171 LYS B 187 1 17
HELIX 37 37 LEU B 188 ARG B 190 5 3
HELIX 38 38 ASP B 195 ALA B 197 5 3
HELIX 39 39 TYR B 198 GLY B 227 1 30
HELIX 40 40 ASP B 232 GLY B 240 1 9
HELIX 41 41 ASP B 250 ASN B 283 1 34
HELIX 42 42 ASN B 283 LEU B 298 1 16
HELIX 43 43 SER B 304 LYS B 309 1 6
HELIX 44 44 LEU B 311 TRP B 325 1 15
HELIX 45 45 ILE B 357 HIS B 361 1 5
HELIX 46 46 ASP B 363 GLY B 368 1 6
HELIX 47 47 ARG B 375 GLU B 380 5 6
HELIX 48 48 ASN B 381 ILE B 385 5 5
HELIX 49 49 ASN B 395 ALA B 399 5 5
HELIX 50 50 GLY B 402 HIS B 420 1 19
SHEET 1 AA 5 ILE A 39 ALA A 44 0
SHEET 2 AA 5 ARG A 47 LEU A 52 -1 O ARG A 47 N ALA A 44
SHEET 3 AA 5 GLU A 352 LEU A 356 1 O GLU A 352 N ARG A 50
SHEET 4 AA 5 ALA A 330 ALA A 335 -1 O PHE A 331 N VAL A 355
SHEET 5 AA 5 PHE A 67 LYS A 69 -1 O ASP A 68 N TYR A 334
SHEET 1 AB 3 ILE A 139 GLU A 140 0
SHEET 2 AB 3 VAL A 445 SER A 450 -1 O VAL A 446 N ILE A 139
SHEET 3 AB 3 PHE A 421 GLU A 424 -1 O ASP A 422 N LYS A 449
SHEET 1 AC 2 THR A 339 LEU A 341 0
SHEET 2 AC 2 TYR A 345 LEU A 347 -1 O TYR A 345 N LEU A 341
SHEET 1 AD 2 ILE A 433 GLU A 435 0
SHEET 2 AD 2 LEU A 439 PRO A 441 -1 O LYS A 440 N LYS A 434
SHEET 1 BA 5 ILE B 39 ALA B 44 0
SHEET 2 BA 5 ARG B 47 LEU B 52 -1 O ARG B 47 N ALA B 44
SHEET 3 BA 5 GLU B 352 LEU B 356 1 O GLU B 352 N ARG B 50
SHEET 4 BA 5 ALA B 330 ALA B 335 -1 O PHE B 331 N VAL B 355
SHEET 5 BA 5 PHE B 67 LYS B 69 -1 O ASP B 68 N TYR B 334
SHEET 1 BB 3 ILE B 139 GLU B 140 0
SHEET 2 BB 3 VAL B 445 SER B 450 -1 O VAL B 446 N ILE B 139
SHEET 3 BB 3 PHE B 421 GLU B 424 -1 O ASP B 422 N LYS B 449
SHEET 1 BC 2 THR B 339 LEU B 341 0
SHEET 2 BC 2 TYR B 345 LEU B 347 -1 O TYR B 345 N LEU B 341
SHEET 1 BD 2 ILE B 433 GLU B 435 0
SHEET 2 BD 2 LEU B 439 PRO B 441 -1 O LYS B 440 N LYS B 434
LINK NE2 HIS A 285 ZN ZN B1457 1655 1555 2.00
LINK OE2 GLU A 348 ZN ZN A1457 1555 1555 1.99
LINK SG CYS A 400 FE HEM A1456 1555 1555 2.29
LINK ZN ZN A1457 OD2 ASP B 23 1555 1555 2.07
LINK OD2 ASP B 231 ZN ZN B1458 4446 1555 2.45
LINK NE2 HIS B 236 ZN ZN B1458 4446 1555 2.03
LINK NE2 HIS B 285 ZN ZN B1458 1555 1555 2.03
LINK OD2 ASP B 338 ZN ZN B1457 1555 1555 2.04
LINK OE2 GLU B 348 ZN ZN B1457 1555 1555 2.21
LINK SG CYS B 400 FE HEM B1456 1555 1555 2.29
SITE 1 AC1 25 LYS A 69 LEU A 86 ALA A 87 TRP A 96
SITE 2 AC1 25 PHE A 107 PHE A 261 ALA A 264 GLY A 265
SITE 3 AC1 25 THR A 268 LEU A 272 THR A 327 PHE A 331
SITE 4 AC1 25 PRO A 392 PHE A 393 GLY A 394 ARG A 398
SITE 5 AC1 25 ALA A 399 CYS A 400 ILE A 401 ALA A 406
SITE 6 AC1 25 DMS A1458 HOH A2029 HOH A2149 HOH A2176
SITE 7 AC1 25 HOH A2177
SITE 1 AC2 4 ASP A 338 GLU A 348 HOH A2178 ASP B 23
SITE 1 AC3 2 ALA A 264 HEM A1456
SITE 1 AC4 25 LYS B 69 LEU B 86 ALA B 87 TRP B 96
SITE 2 AC4 25 PHE B 261 ALA B 264 GLY B 265 THR B 268
SITE 3 AC4 25 THR B 269 PHE B 331 PRO B 392 PHE B 393
SITE 4 AC4 25 GLY B 394 ARG B 398 ALA B 399 CYS B 400
SITE 5 AC4 25 ILE B 401 GLY B 402 ALA B 406 DMS B1459
SITE 6 AC4 25 HOH B2161 HOH B2225 HOH B2226 HOH B2227
SITE 7 AC4 25 HOH B2228
SITE 1 AC5 3 HIS A 285 ASP B 338 GLU B 348
SITE 1 AC6 3 ASP B 231 HIS B 236 HIS B 285
SITE 1 AC7 2 ALA B 264 HEM B1456
CRYST1 82.210 96.639 164.197 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 0.012164 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010348 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006090 0.00000
MTRIX1 1 0.530900 0.846900 -0.031830 -6.30600 1
MTRIX2 1 0.803000 -0.490700 0.338200 -59.01000 1
MTRIX3 1 0.270800 -0.205100 -0.940500 102.80000 1
(ATOM LINES ARE NOT SHOWN.)
END
