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HEADER HYDROLASE 09-OCT-07 2RHW
TITLE CRYSTAL STRUCTURE OF THE S112A MUTANT OF A C-C HYDROLASE,
TITLE 2 BPHD FROM BURKHOLDERIA XENOVORANS LB400, IN COMPLEX WITH 3,
TITLE 3 10-DI-FLUORO HOPDA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOATE
COMPND 3 HYDROLASE;
COMPND 4 CHAIN: A;
COMPND 5 EC: 3.7.1.-;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA XENOVORANS;
SOURCE 3 STRAIN: LB400
KEYWDS C-C BOND HYDROLASE, HYDROLASE, AROMATIC HYDROCARBONS
KEYWDS 2 CATABOLISM
EXPDTA X-RAY DIFFRACTION
AUTHOR S.BHOWMIK,J.T.BOLIN
REVDAT 1 13-NOV-07 2RHW 0
JRNL AUTH S.BHOWMIK,G.P.HORSMAN,J.T.BOLIN,L.D.ELTIS
JRNL TITL THE MOLECULAR BASIS FOR INHIBITION OF BPHD, A C-C
JRNL TITL 2 BOND HYDROLASE INVOLVED IN POLYCHLORINATED
JRNL TITL 3 BIPHENYLS DEGRADATION: LARGE 3-SUBSTITUENTS
JRNL TITL 4 PREVENT TAUTOMERIZATION.
JRNL REF J.BIOL.CHEM. 2007
JRNL REFN ASTM JBCHA3 US ESSN 1083-351X
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.57 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.57
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 42612
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2151
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.57
REMARK 3 BIN RESOLUTION RANGE LOW : 1.61
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2929
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.01
REMARK 3 BIN R VALUE (WORKING SET) : 0.2080
REMARK 3 BIN FREE R VALUE SET COUNT : 159
REMARK 3 BIN FREE R VALUE : 0.2130
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 2556
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.16
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.52000
REMARK 3 B22 (A**2) : 0.52000
REMARK 3 B33 (A**2) : -1.05000
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): 0.080
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.081
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.050
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.377
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2447 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3333 ; 1.189 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 318 ; 5.104 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 118 ;37.405 ;23.814
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 421 ;13.338 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;19.468 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 348 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1921 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1158 ; 0.205 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1662 ; 0.308 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 143 ; 0.122 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 3 ; 0.145 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 49 ; 0.210 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 24 ; 0.085 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): 1 ; 0.136 ; 0.200
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): 1455 ; 3.854 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2345 ; 6.323 ; 3.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1035 ; 9.228 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 971 ;12.908 ; 3.000
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 : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
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 : 1.20
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2RHW COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB044877.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-2007
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42640
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.570
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 11.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 8.10000
REMARK 200 FOR THE DATA SET : 20.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.57
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 50.20000
REMARK 200 FOR SHELL : 4.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.9 M SODIUM MALONATE, PH 7.0,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,1/2-Y,1/2+Z
REMARK 290 3555 -Y,1/2+X,1/4+Z
REMARK 290 4555 1/2+Y,-X,3/4+Z
REMARK 290 5555 1/2-X,Y,3/4-Z
REMARK 290 6555 X,1/2-Y,1/4-Z
REMARK 290 7555 1/2+Y,1/2+X,1/2-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 1/2+X,1/2+Y,1/2+Z
REMARK 290 10555 1-X,1-Y,1+Z
REMARK 290 11555 1/2-Y,1+X,3/4+Z
REMARK 290 12555 1+Y,1/2-X,5/4+Z
REMARK 290 13555 1-X,1/2+Y,5/4-Z
REMARK 290 14555 1/2+X,1-Y,3/4-Z
REMARK 290 15555 1+Y,1+X,1-Z
REMARK 290 16555 1/2-Y,1/2-X,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 58.97800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 58.97800
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.59650
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 58.97800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 21.79825
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 58.97800
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 65.39475
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 58.97800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 65.39475
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 58.97800
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 21.79825
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 58.97800
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 58.97800
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 43.59650
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 58.97800
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 58.97800
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 43.59650
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 117.95600
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 117.95600
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 87.19300
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 58.97800
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 117.95600
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 65.39475
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 117.95600
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 58.97800
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 108.99125
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 117.95600
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 58.97800
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 108.99125
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 58.97800
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 117.95600
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 65.39475
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 117.95600
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 117.95600
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 87.19300
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 58.97800
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 58.97800
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 43.59650
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND 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: TETRAMER
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 AVERAGE BURIED SURFACE AREA: 9090 ANGSTROM**2
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 BIOMT1 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 -1.000000 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 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
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 18 80.63 13.26
REMARK 500 ASN A 75 -121.41 44.95
REMARK 500 ALA A 112 -117.18 57.51
REMARK 500 LEU A 140 32.66 -90.09
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 NA A 1 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MLI A 287 O9
REMARK 620 2 MLI A 287 O7 82.3
REMARK 620 3 HOH A 343 O 101.4 169.7
REMARK 620 4 HOH A 452 O 117.8 97.6 89.3
REMARK 620 N 1 2 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2PUH RELATED DB: PDB
REMARK 900 RELATED ID: 2PUJ RELATED DB: PDB
REMARK 900 RELATED ID: 2RHT RELATED DB: PDB
DBREF 2RHW A 4 286 UNP P47229 BPHD_BURXL 4 286
SEQADV 2RHW ALA A 112 UNP P47229 SER 112 ENGINEERED
SEQRES 1 A 283 LEU THR GLU SER SER THR SER LYS PHE VAL LYS ILE ASN
SEQRES 2 A 283 GLU LYS GLY PHE SER ASP PHE ASN ILE HIS TYR ASN GLU
SEQRES 3 A 283 ALA GLY ASN GLY GLU THR VAL ILE MET LEU HIS GLY GLY
SEQRES 4 A 283 GLY PRO GLY ALA GLY GLY TRP SER ASN TYR TYR ARG ASN
SEQRES 5 A 283 VAL GLY PRO PHE VAL ASP ALA GLY TYR ARG VAL ILE LEU
SEQRES 6 A 283 LYS ASP SER PRO GLY PHE ASN LYS SER ASP ALA VAL VAL
SEQRES 7 A 283 MET ASP GLU GLN ARG GLY LEU VAL ASN ALA ARG ALA VAL
SEQRES 8 A 283 LYS GLY LEU MET ASP ALA LEU ASP ILE ASP ARG ALA HIS
SEQRES 9 A 283 LEU VAL GLY ASN ALA MET GLY GLY ALA THR ALA LEU ASN
SEQRES 10 A 283 PHE ALA LEU GLU TYR PRO ASP ARG ILE GLY LYS LEU ILE
SEQRES 11 A 283 LEU MET GLY PRO GLY GLY LEU GLY PRO SER MET PHE ALA
SEQRES 12 A 283 PRO MET PRO MET GLU GLY ILE LYS LEU LEU PHE LYS LEU
SEQRES 13 A 283 TYR ALA GLU PRO SER TYR GLU THR LEU LYS GLN MET LEU
SEQRES 14 A 283 GLN VAL PHE LEU TYR ASP GLN SER LEU ILE THR GLU GLU
SEQRES 15 A 283 LEU LEU GLN GLY ARG TRP GLU ALA ILE GLN ARG GLN PRO
SEQRES 16 A 283 GLU HIS LEU LYS ASN PHE LEU ILE SER ALA GLN LYS ALA
SEQRES 17 A 283 PRO LEU SER THR TRP ASP VAL THR ALA ARG LEU GLY GLU
SEQRES 18 A 283 ILE LYS ALA LYS THR PHE ILE THR TRP GLY ARG ASP ASP
SEQRES 19 A 283 ARG PHE VAL PRO LEU ASP HIS GLY LEU LYS LEU LEU TRP
SEQRES 20 A 283 ASN ILE ASP ASP ALA ARG LEU HIS VAL PHE SER LYS CYS
SEQRES 21 A 283 GLY HIS TRP ALA GLN TRP GLU HIS ALA ASP GLU PHE ASN
SEQRES 22 A 283 ARG LEU VAL ILE ASP PHE LEU ARG HIS ALA
HET NA A 1 1
HET MLI A 287 7
HET MLI A 2 7
HET C0E A 288 18
HETNAM NA SODIUM ION
HETNAM MLI MALONATE ION
HETNAM C0E 3-FLUORO-6-(4-FLUOROPHENYL)-2-HYDROXY-6-OXOHEXA-2,4-
HETNAM 2 C0E DIENOIC ACID
FORMUL 2 NA NA 1+
FORMUL 3 MLI 2(C3 H2 O4 2-)
FORMUL 5 C0E C12 H8 F2 O4
FORMUL 6 HOH *183(H2 O)
HELIX 1 1 THR A 5 THR A 9 1 5
HELIX 2 2 GLY A 47 TYR A 53 1 7
HELIX 3 3 ASN A 55 ALA A 62 1 8
HELIX 4 4 GLN A 85 ASP A 102 1 18
HELIX 5 5 ALA A 112 TYR A 125 1 14
HELIX 6 6 MET A 150 GLU A 162 1 13
HELIX 7 7 SER A 164 LEU A 176 1 13
HELIX 8 8 ASP A 178 ILE A 182 5 5
HELIX 9 9 THR A 183 GLN A 197 1 15
HELIX 10 10 GLN A 197 ALA A 211 1 15
HELIX 11 11 PRO A 212 ASP A 217 5 6
HELIX 12 12 VAL A 218 ILE A 225 5 8
HELIX 13 13 LEU A 242 ILE A 252 1 11
HELIX 14 14 TRP A 266 HIS A 271 1 6
HELIX 15 15 HIS A 271 ALA A 286 1 16
SHEET 1 A 8 SER A 10 GLU A 17 0
SHEET 2 A 8 PHE A 20 ALA A 30 -1 O PHE A 20 N GLU A 17
SHEET 3 A 8 ARG A 65 LYS A 69 -1 O LEU A 68 N ASN A 28
SHEET 4 A 8 THR A 35 LEU A 39 1 N MET A 38 O ILE A 67
SHEET 5 A 8 ALA A 106 ASN A 111 1 O VAL A 109 N LEU A 39
SHEET 6 A 8 ILE A 129 MET A 135 1 O MET A 135 N GLY A 110
SHEET 7 A 8 THR A 229 GLY A 234 1 O THR A 232 N LEU A 134
SHEET 8 A 8 ALA A 255 PHE A 260 1 O ARG A 256 N ILE A 231
LINK NA NA A 1 O9 MLI A 287 1555 1555 2.30
LINK NA NA A 1 O7 MLI A 287 1555 1555 2.47
LINK NA NA A 1 O HOH A 343 1555 1555 2.32
LINK NA NA A 1 O HOH A 452 1555 1555 2.20
CISPEP 1 MET A 148 PRO A 149 0 2.88
CISPEP 2 MET A 148 PRO A 149 0 -0.19
CRYST1 117.956 117.956 87.193 90.00 90.00 90.00 I 41 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 0.008478 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008478 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011469 0.00000
TER 2341 ALA A 286
MASTER 325 0 4 15 8 0 0 6 2556 1 35 22
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