HEADER OXIDOREDUCTASE 28-JAN-02 1KW6
TITLE CRYSTAL STRUCTURE OF 2,3-DIHYDROXYBIPHENYL DIOXYGENASE (BPHC) IN
TITLE 2 COMPLEX WITH 2,3-DIHYDROXYBIPHENYL AT 1.45 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2,3-DIHYDROXYBIPHENYL DIOXYGENASE;
COMPND 3 CHAIN: B;
COMPND 4 SYNONYM: BPHC, BIPHENYL-2,3-DIOL 1,2-DIOXYGENASE;
COMPND 5 EC: 1.13.11.39;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS SP.;
SOURCE 3 ORGANISM_TAXID: 307;
SOURCE 4 STRAIN: KKS102;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FOUR TIME REPETITIONS OF THE BETA-ALPHA-BETA-BETA-BETA MOTIF,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.SATO,Y.URAGAMI,T.NISHIZAKI,Y.TAKAHASHI,G.SAZAKI,K.SUGIMOTO,
AUTHOR 2 T.NONAKA,E.MASAI,M.FUKUDA,T.SENDA
REVDAT 4 13-MAR-24 1KW6 1 REMARK LINK
REVDAT 3 13-JUL-11 1KW6 1 VERSN
REVDAT 2 24-FEB-09 1KW6 1 VERSN
REVDAT 1 28-JAN-03 1KW6 0
JRNL AUTH N.SATO,Y.URAGAMI,T.NISHIZAKI,Y.TAKAHASHI,G.SAZAKI,
JRNL AUTH 2 K.SUGIMOTO,T.NONAKA,E.MASAI,M.FUKUDA,T.SENDA
JRNL TITL CRYSTAL STRUCTURES OF THE REACTION INTERMEDIATE AND ITS
JRNL TITL 2 HOMOLOGUE OF AN EXTRADIOL-CLEAVING CATECHOLIC DIOXYGENASE
JRNL REF J.MOL.BIOL. V. 321 621 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12206778
JRNL DOI 10.1016/S0022-2836(02)00673-3
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
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) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 87.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 68780
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) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.171
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3654
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) : 1.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4978
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2720
REMARK 3 BIN FREE R VALUE SET COUNT : 253
REMARK 3 BIN FREE R VALUE : 0.2900
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2229
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 292
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.050
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.049
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.041
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.076
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.957
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2337 ; 0.009 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2093 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3182 ; 1.400 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4848 ; 2.135 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 295 ; 4.961 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 387 ;17.335 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 342 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2630 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 508 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 451 ; 0.221 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2008 ; 0.198 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 3 ; 0.221 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 249 ; 0.151 ; 0.500
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): 12 ; 0.313 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 56 ; 0.230 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 17 ; 0.654 ; 0.500
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): 1437 ; 0.597 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2304 ; 1.125 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 900 ; 1.696 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 877 ; 2.733 ; 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): 1 ; 1.461 ; 2.000
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 WITH 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 1KW6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-JAN-02.
REMARK 100 THE DEPOSITION ID IS D_1000015397.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-DEC-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72435
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 26.080
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 8.700
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : 0.06300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.37300
REMARK 200 R SYM FOR SHELL (I) : 0.37300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS/HCL, HEXYLENE GLYCOL, AMMONIUM
REMARK 280 SULFATE, PH 7.5, BATCH, TEMPERATURE 285K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 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 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 60.91450
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 60.91450
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 54.67850
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 60.91450
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 60.91450
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 54.67850
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 60.91450
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 60.91450
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 54.67850
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 60.91450
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 60.91450
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 54.67850
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 60.91450
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 60.91450
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 54.67850
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 60.91450
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 60.91450
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 54.67850
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 60.91450
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 60.91450
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 54.67850
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 60.91450
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 60.91450
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 54.67850
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A OCTAMER GENERATED FROM THE
REMARK 300 MONOMER IN THE ASYMMETRIC UNIT BY THE OPERATIONS:
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: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 29160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 73650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -462.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 121.82900
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 121.82900
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 121.82900
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 121.82900
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 5 -1.000000 0.000000 0.000000 121.82900
REMARK 350 BIOMT2 5 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 6 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 6 0.000000 -1.000000 0.000000 121.82900
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 7 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 7 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 8 0.000000 -1.000000 0.000000 121.82900
REMARK 350 BIOMT2 8 -1.000000 0.000000 0.000000 121.82900
REMARK 350 BIOMT3 8 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 ARG B 289
REMARK 465 GLY B 290
REMARK 465 GLN B 291
REMARK 465 ARG B 292
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 NE2 GLN B 244 O HOH B 836 1.45
REMARK 500 OE1 GLN B 244 O HOH B 830 1.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 744 O HOH B 744 15545 0.87
REMARK 500 O HOH B 742 O HOH B 742 6565 0.91
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 ASP B 43 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP B 58 CB - CG - OD2 ANGL. DEV. = 6.2 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 THR B 23 -67.87 -91.61
REMARK 500 ASP B 43 -150.92 -168.25
REMARK 500 PRO B 132 96.81 -64.53
REMARK 500 THR B 138 -104.36 -131.18
REMARK 500 MET B 176 -63.19 -106.68
REMARK 500 CYS B 189 11.00 -143.47
REMARK 500 ASN B 190 -162.33 -168.43
REMARK 500 PRO B 202 48.88 -84.32
REMARK 500 PRO B 204 30.42 -88.19
REMARK 500 MET B 256 -1.79 76.71
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 FE2 B 301 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 145 NE2
REMARK 620 2 HIS B 209 NE2 105.1
REMARK 620 3 GLU B 260 OE2 101.4 94.5
REMARK 620 4 BPY B 401 OK2 144.3 83.4 112.6
REMARK 620 5 BPY B 401 OK1 84.7 158.0 102.9 77.7
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 FE2 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BPY B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EIM RELATED DB: PDB
REMARK 900 1EIM CONTAINS THE SAME PROTEIN COMPLEXED WITH 2,3-DIHYDROXYBIPHENYL
REMARK 900 AT 2.0A RESOLUTION.
REMARK 900 RELATED ID: 1KW3 RELATED DB: PDB
REMARK 900 1KW3 CONTAINS THE SAME PROTEIN AT 1.45 A RESOLUTION.
REMARK 900 RELATED ID: 1KW8 RELATED DB: PDB
REMARK 900 1KW8 CONTAINS THE SAME PROTEIN COMPLEXED WITH 2,3-DIHYDROXYBIPHENYL-
REMARK 900 NO.
REMARK 900 RELATED ID: 1KW9 RELATED DB: PDB
REMARK 900 1KW9 CONTAINS THE SAME PROTEIN COMPLEXED WITH 2,3-DIHYDROXYBIPHENYL
REMARK 900 AT 2.0 A RESOLUTION.
REMARK 900 RELATED ID: 1KWB RELATED DB: PDB
REMARK 900 1KWB CONTAINS THE SAME PROTEIN, H145A MUTANT.
REMARK 900 RELATED ID: 1KWC RELATED DB: PDB
REMARK 900 1KWC CONTAINS THE SAME PROTEIN, H145A MUTANT COMPLEXED WITH 2,3-
REMARK 900 DIHYDROXYBIPHENYL.
DBREF 1KW6 B 1 292 UNP P17297 BPHC_PSES1 1 292
SEQRES 1 B 292 SER ILE GLU ARG LEU GLY TYR LEU GLY PHE ALA VAL LYS
SEQRES 2 B 292 ASP VAL PRO ALA TRP ASP HIS PHE LEU THR LYS SER VAL
SEQRES 3 B 292 GLY LEU MET ALA ALA GLY SER ALA GLY ASP ALA ALA LEU
SEQRES 4 B 292 TYR ARG ALA ASP GLN ARG ALA TRP ARG ILE ALA VAL GLN
SEQRES 5 B 292 PRO GLY GLU LEU ASP ASP LEU ALA TYR ALA GLY LEU GLU
SEQRES 6 B 292 VAL ASP ASP ALA ALA ALA LEU GLU ARG MET ALA ASP LYS
SEQRES 7 B 292 LEU ARG GLN ALA GLY VAL ALA PHE THR ARG GLY ASP GLU
SEQRES 8 B 292 ALA LEU MET GLN GLN ARG LYS VAL MET GLY LEU LEU CYS
SEQRES 9 B 292 LEU GLN ASP PRO PHE GLY LEU PRO LEU GLU ILE TYR TYR
SEQRES 10 B 292 GLY PRO ALA GLU ILE PHE HIS GLU PRO PHE LEU PRO SER
SEQRES 11 B 292 ALA PRO VAL SER GLY PHE VAL THR GLY ASP GLN GLY ILE
SEQRES 12 B 292 GLY HIS PHE VAL ARG CYS VAL PRO ASP THR ALA LYS ALA
SEQRES 13 B 292 MET ALA PHE TYR THR GLU VAL LEU GLY PHE VAL LEU SER
SEQRES 14 B 292 ASP ILE ILE ASP ILE GLN MET GLY PRO GLU THR SER VAL
SEQRES 15 B 292 PRO ALA HIS PHE LEU HIS CYS ASN GLY ARG HIS HIS THR
SEQRES 16 B 292 ILE ALA LEU ALA ALA PHE PRO ILE PRO LYS ARG ILE HIS
SEQRES 17 B 292 HIS PHE MET LEU GLN ALA ASN THR ILE ASP ASP VAL GLY
SEQRES 18 B 292 TYR ALA PHE ASP ARG LEU ASP ALA ALA GLY ARG ILE THR
SEQRES 19 B 292 SER LEU LEU GLY ARG HIS THR ASN ASP GLN THR LEU SER
SEQRES 20 B 292 PHE TYR ALA ASP THR PRO SER PRO MET ILE GLU VAL GLU
SEQRES 21 B 292 PHE GLY TRP GLY PRO ARG THR VAL ASP SER SER TRP THR
SEQRES 22 B 292 VAL ALA ARG HIS SER ARG THR ALA MET TRP GLY HIS LYS
SEQRES 23 B 292 SER VAL ARG GLY GLN ARG
HET FE2 B 301 1
HET BPY B 401 14
HET MPD B 501 8
HET MPD B 601 8
HETNAM FE2 FE (II) ION
HETNAM BPY BIPHENYL-2,3-DIOL
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
FORMUL 2 FE2 FE 2+
FORMUL 3 BPY C12 H10 O2
FORMUL 4 MPD 2(C6 H14 O2)
FORMUL 6 HOH *292(H2 O)
HELIX 1 1 ASP B 14 SER B 25 1 12
HELIX 2 2 ASP B 68 GLY B 83 1 16
HELIX 3 3 ASP B 90 LYS B 98 1 9
HELIX 4 4 THR B 138 GLY B 142 5 5
HELIX 5 5 ASP B 152 VAL B 163 1 12
HELIX 6 6 THR B 216 ALA B 230 1 15
SHEET 1 A 8 MET B 29 ALA B 34 0
SHEET 2 A 8 ALA B 37 ARG B 41 -1 O ARG B 41 N MET B 29
SHEET 3 A 8 ILE B 49 PRO B 53 -1 O VAL B 51 N ALA B 38
SHEET 4 A 8 ARG B 4 VAL B 12 1 N PHE B 10 O ALA B 50
SHEET 5 A 8 ASP B 58 GLU B 65 -1 O GLY B 63 N TYR B 7
SHEET 6 A 8 PRO B 112 TYR B 117 1 O GLU B 114 N LEU B 64
SHEET 7 A 8 GLY B 101 GLN B 106 -1 N LEU B 105 O LEU B 113
SHEET 8 A 8 THR B 87 ARG B 88 -1 N THR B 87 O CYS B 104
SHEET 1 B10 ARG B 276 HIS B 277 0
SHEET 2 B10 VAL B 167 GLN B 175 1 N ILE B 171 O HIS B 277
SHEET 3 B10 SER B 181 HIS B 188 -1 O HIS B 188 N VAL B 167
SHEET 4 B10 ILE B 196 ALA B 199 -1 O ILE B 196 N LEU B 187
SHEET 5 B10 HIS B 145 CYS B 149 1 N ARG B 148 O ALA B 197
SHEET 6 B10 ILE B 207 GLN B 213 -1 O MET B 211 N HIS B 145
SHEET 7 B10 GLU B 258 TRP B 263 1 O GLU B 260 N LEU B 212
SHEET 8 B10 LEU B 246 ASP B 251 -1 N LEU B 246 O TRP B 263
SHEET 9 B10 GLY B 238 HIS B 240 -1 N GLY B 238 O SER B 247
SHEET 10 B10 ALA B 281 GLY B 284 -1 O TRP B 283 N ARG B 239
LINK NE2 HIS B 145 FE FE2 B 301 1555 1555 2.12
LINK NE2 HIS B 209 FE FE2 B 301 1555 1555 2.17
LINK OE2 GLU B 260 FE FE2 B 301 1555 1555 1.99
LINK FE FE2 B 301 OK2 BPY B 401 1555 1555 1.98
LINK FE FE2 B 301 OK1 BPY B 401 1555 1555 2.30
SITE 1 AC1 4 HIS B 145 HIS B 209 GLU B 260 BPY B 401
SITE 1 AC2 12 HIS B 145 PHE B 186 HIS B 194 HIS B 208
SITE 2 AC2 12 HIS B 209 HIS B 240 ASN B 242 TYR B 249
SITE 3 AC2 12 GLU B 260 THR B 280 FE2 B 301 HOH B 741
SITE 1 AC3 8 PRO B 126 PHE B 127 PRO B 132 VAL B 133
SITE 2 AC3 8 SER B 134 HOH B 767 HOH B 771 HOH B 873
SITE 1 AC4 2 ASP B 228 LYS B 286
CRYST1 121.829 121.829 109.357 90.00 90.00 90.00 I 4 2 2 16
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 0.008208 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008208 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009144 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
