| 3V1K-pdb | HEADER HYDROLASE 09-DEC-11 3V1K
TITLE CRYSTAL STRUCTURE OF THE H265Q MUTANT OF A C-C HYDROLASE, BPHD FROM
TITLE 2 BURKHOLDERIA XENOVORANS LB400.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOATE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HOPDA HYDROLASE, 2,6-DIOXO-6-PHENYLHEXA-3-ENOATE HYDROLASE;
COMPND 5 EC: 3.7.1.8;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA XENOVORANS;
SOURCE 3 ORGANISM_TAXID: 266265;
SOURCE 4 STRAIN: LB400;
SOURCE 5 GENE: BPHD, BXENO_C1120, BXE_C1186;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DH5A;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS C-C BOND HYDROLASE, ALPHA/BETA HYDROLASE FOLD, BPHD, ALPHA/BETA
KEYWDS 2 HYDROLASE, PCB DEGRADATION, META CLEAVAGE PRODUCT HYDROLASE, MCP
KEYWDS 3 HYDROLASE, 2-HYDROXY-6-OXO-6-PHENYL-HEXA-2,4-DIENOATE HYDROLASE,
KEYWDS 4 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.GHOSH,J.T.BOLIN
REVDAT 1 21-MAR-12 3V1K 0
JRNL AUTH A.C.RUZZINI,S.GHOSH,G.P.HORSMAN,L.J.FOSTER,J.T.BOLIN,
JRNL AUTH 2 L.D.ELTIS
JRNL TITL IDENTIFICATION OF AN ACYL-ENZYME INTERMEDIATE IN A
JRNL TITL 2 META-CLEAVAGE PRODUCT HYDROLASE REVEALS THE VERSATILITY OF
JRNL TITL 3 THE CATALYTIC TRIAD.
JRNL REF J.AM.CHEM.SOC. 2012
JRNL REFN ESSN 1520-5126
JRNL PMID 22339283
JRNL DOI 10.1021/JA208544G
REMARK 2
REMARK 2 RESOLUTION. 2.13 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 2.13
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 117.77
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 39106
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1961
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) : 2.12
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.18
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2594
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.13
REMARK 3 BIN R VALUE (WORKING SET) : 0.2640
REMARK 3 BIN FREE R VALUE SET COUNT : 139
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4490
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 7
REMARK 3 SOLVENT ATOMS : 126
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.22000
REMARK 3 B22 (A**2) : 0.22000
REMARK 3 B33 (A**2) : -0.33000
REMARK 3 B12 (A**2) : 0.11000
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): 0.216
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.187
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.129
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.842
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4628 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3166 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6264 ; 1.268 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7685 ; 0.852 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 572 ; 5.746 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 219 ;37.906 ;23.973
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 780 ;15.775 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;18.912 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 660 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5211 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 989 ; 0.001 ; 0.020
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 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS; U VALUES: REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3V1K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-DEC-11.
REMARK 100 THE RCSB ID CODE IS RCSB069478.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-FEB-10
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
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(111)
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-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39177
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.125
REMARK 200 RESOLUTION RANGE LOW (A) : 117.770
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 10.400
REMARK 200 R MERGE (I) : 0.12200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.12
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.20
REMARK 200 R MERGE FOR SHELL (I) : 0.94800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4 M SODIUM MALONATE, 3 % V/V
REMARK 280 ETHYLENE GLYCOL, PH 6.6, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+1/3
REMARK 290 6555 X-Y,X,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 21.92233
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 43.84467
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 21.92233
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 43.84467
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 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 135.99200
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ALA B 3
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ASN A 32 O HOH A 383 2.00
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 18 -111.83 29.37
REMARK 500 ASN A 75 -121.81 47.97
REMARK 500 SER A 112 -112.47 59.32
REMARK 500 TRP A 266 65.11 -115.81
REMARK 500 VAL B 13 126.51 -170.24
REMARK 500 LYS B 18 -112.61 32.76
REMARK 500 ASP B 22 57.07 39.41
REMARK 500 ALA B 62 0.40 -66.23
REMARK 500 PRO B 72 108.83 -55.17
REMARK 500 ASN B 75 -149.63 48.51
REMARK 500 SER B 112 -107.07 65.85
REMARK 500 TYR B 125 59.25 -119.63
REMARK 500 PHE B 145 -45.94 -136.84
REMARK 500 PRO B 163 82.39 -66.45
REMARK 500 TRP B 266 77.71 -100.31
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 370 DISTANCE = 5.23 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLA A 287
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2OG1 RELATED DB: PDB
REMARK 900 BPHD WILD TYPE
REMARK 900 RELATED ID: 2RI6 RELATED DB: PDB
REMARK 900 BPHD S112A MUTANT
REMARK 900 RELATED ID: 2PU7 RELATED DB: PDB
REMARK 900 BPHD S112A/H265A MUTANT
REMARK 900 RELATED ID: 2PUH RELATED DB: PDB
REMARK 900 BPHD S112A MUTANT IN COMPLEX WITH SUBSTRATE HOPDA
REMARK 900 RELATED ID: 2PUJ RELATED DB: PDB
REMARK 900 BPHD S112A/H265Q MUTANT IN COMPLEX WITH SUBSTRATE HOPDA
REMARK 900 RELATED ID: 2RHW RELATED DB: PDB
REMARK 900 BPHD S112A MUTANT IN COMPLEX WITH 3, 10 - DIFLUORO HOPDA
REMARK 900 RELATED ID: 2RHT RELATED DB: PDB
REMARK 900 BPHD S112A MUTANT IN COMPLEX WITH 3-CL HOPDA
REMARK 900 RELATED ID: 3V1L RELATED DB: PDB
REMARK 900 RELATED ID: 3V1M RELATED DB: PDB
REMARK 900 RELATED ID: 3V1N RELATED DB: PDB
DBREF 3V1K A 1 286 UNP P47229 BPHD_BURXL 1 286
DBREF 3V1K B 1 286 UNP P47229 BPHD_BURXL 1 286
SEQADV 3V1K GLN A 265 UNP P47229 HIS 265 ENGINEERED MUTATION
SEQADV 3V1K GLN B 265 UNP P47229 HIS 265 ENGINEERED MUTATION
SEQRES 1 A 286 MET THR ALA LEU THR GLU SER SER THR SER LYS PHE VAL
SEQRES 2 A 286 LYS ILE ASN GLU LYS GLY PHE SER ASP PHE ASN ILE HIS
SEQRES 3 A 286 TYR ASN GLU ALA GLY ASN GLY GLU THR VAL ILE MET LEU
SEQRES 4 A 286 HIS GLY GLY GLY PRO GLY ALA GLY GLY TRP SER ASN TYR
SEQRES 5 A 286 TYR ARG ASN VAL GLY PRO PHE VAL ASP ALA GLY TYR ARG
SEQRES 6 A 286 VAL ILE LEU LYS ASP SER PRO GLY PHE ASN LYS SER ASP
SEQRES 7 A 286 ALA VAL VAL MET ASP GLU GLN ARG GLY LEU VAL ASN ALA
SEQRES 8 A 286 ARG ALA VAL LYS GLY LEU MET ASP ALA LEU ASP ILE ASP
SEQRES 9 A 286 ARG ALA HIS LEU VAL GLY ASN SER MET GLY GLY ALA THR
SEQRES 10 A 286 ALA LEU ASN PHE ALA LEU GLU TYR PRO ASP ARG ILE GLY
SEQRES 11 A 286 LYS LEU ILE LEU MET GLY PRO GLY GLY LEU GLY PRO SER
SEQRES 12 A 286 MET PHE ALA PRO MET PRO MET GLU GLY ILE LYS LEU LEU
SEQRES 13 A 286 PHE LYS LEU TYR ALA GLU PRO SER TYR GLU THR LEU LYS
SEQRES 14 A 286 GLN MET LEU GLN VAL PHE LEU TYR ASP GLN SER LEU ILE
SEQRES 15 A 286 THR GLU GLU LEU LEU GLN GLY ARG TRP GLU ALA ILE GLN
SEQRES 16 A 286 ARG GLN PRO GLU HIS LEU LYS ASN PHE LEU ILE SER ALA
SEQRES 17 A 286 GLN LYS ALA PRO LEU SER THR TRP ASP VAL THR ALA ARG
SEQRES 18 A 286 LEU GLY GLU ILE LYS ALA LYS THR PHE ILE THR TRP GLY
SEQRES 19 A 286 ARG ASP ASP ARG PHE VAL PRO LEU ASP HIS GLY LEU LYS
SEQRES 20 A 286 LEU LEU TRP ASN ILE ASP ASP ALA ARG LEU HIS VAL PHE
SEQRES 21 A 286 SER LYS CYS GLY GLN TRP ALA GLN TRP GLU HIS ALA ASP
SEQRES 22 A 286 GLU PHE ASN ARG LEU VAL ILE ASP PHE LEU ARG HIS ALA
SEQRES 1 B 286 MET THR ALA LEU THR GLU SER SER THR SER LYS PHE VAL
SEQRES 2 B 286 LYS ILE ASN GLU LYS GLY PHE SER ASP PHE ASN ILE HIS
SEQRES 3 B 286 TYR ASN GLU ALA GLY ASN GLY GLU THR VAL ILE MET LEU
SEQRES 4 B 286 HIS GLY GLY GLY PRO GLY ALA GLY GLY TRP SER ASN TYR
SEQRES 5 B 286 TYR ARG ASN VAL GLY PRO PHE VAL ASP ALA GLY TYR ARG
SEQRES 6 B 286 VAL ILE LEU LYS ASP SER PRO GLY PHE ASN LYS SER ASP
SEQRES 7 B 286 ALA VAL VAL MET ASP GLU GLN ARG GLY LEU VAL ASN ALA
SEQRES 8 B 286 ARG ALA VAL LYS GLY LEU MET ASP ALA LEU ASP ILE ASP
SEQRES 9 B 286 ARG ALA HIS LEU VAL GLY ASN SER MET GLY GLY ALA THR
SEQRES 10 B 286 ALA LEU ASN PHE ALA LEU GLU TYR PRO ASP ARG ILE GLY
SEQRES 11 B 286 LYS LEU ILE LEU MET GLY PRO GLY GLY LEU GLY PRO SER
SEQRES 12 B 286 MET PHE ALA PRO MET PRO MET GLU GLY ILE LYS LEU LEU
SEQRES 13 B 286 PHE LYS LEU TYR ALA GLU PRO SER TYR GLU THR LEU LYS
SEQRES 14 B 286 GLN MET LEU GLN VAL PHE LEU TYR ASP GLN SER LEU ILE
SEQRES 15 B 286 THR GLU GLU LEU LEU GLN GLY ARG TRP GLU ALA ILE GLN
SEQRES 16 B 286 ARG GLN PRO GLU HIS LEU LYS ASN PHE LEU ILE SER ALA
SEQRES 17 B 286 GLN LYS ALA PRO LEU SER THR TRP ASP VAL THR ALA ARG
SEQRES 18 B 286 LEU GLY GLU ILE LYS ALA LYS THR PHE ILE THR TRP GLY
SEQRES 19 B 286 ARG ASP ASP ARG PHE VAL PRO LEU ASP HIS GLY LEU LYS
SEQRES 20 B 286 LEU LEU TRP ASN ILE ASP ASP ALA ARG LEU HIS VAL PHE
SEQRES 21 B 286 SER LYS CYS GLY GLN TRP ALA GLN TRP GLU HIS ALA ASP
SEQRES 22 B 286 GLU PHE ASN ARG LEU VAL ILE ASP PHE LEU ARG HIS ALA
HET MLA A 287 7
HETNAM MLA MALONIC ACID
HETSYN MLA DICARBOXYLIC ACID C3; PROPANEDIOLIC ACID;
HETSYN 2 MLA METAHNEDICARBOXYLIC ACID
FORMUL 3 MLA C3 H4 O4
FORMUL 4 HOH *126(H2 O)
HELIX 1 1 GLY A 47 TYR A 53 1 7
HELIX 2 2 ASN A 55 ALA A 62 1 8
HELIX 3 3 GLN A 85 ASP A 102 1 18
HELIX 4 4 SER A 112 TYR A 125 1 14
HELIX 5 5 MET A 150 GLU A 162 1 13
HELIX 6 6 SER A 164 LEU A 176 1 13
HELIX 7 7 ASP A 178 ILE A 182 5 5
HELIX 8 8 THR A 183 GLN A 197 1 15
HELIX 9 9 GLN A 197 ALA A 211 1 15
HELIX 10 10 PRO A 212 ASP A 217 5 6
HELIX 11 11 VAL A 218 ILE A 225 5 8
HELIX 12 12 LEU A 242 ILE A 252 1 11
HELIX 13 13 TRP A 266 HIS A 271 1 6
HELIX 14 14 HIS A 271 ALA A 286 1 16
HELIX 15 15 THR B 5 THR B 9 1 5
HELIX 16 16 GLY B 47 TYR B 53 1 7
HELIX 17 17 ASN B 55 ALA B 62 1 8
HELIX 18 18 GLN B 85 LEU B 101 1 17
HELIX 19 19 SER B 112 TYR B 125 1 14
HELIX 20 20 MET B 150 GLU B 162 1 13
HELIX 21 21 SER B 164 LEU B 176 1 13
HELIX 22 22 ASP B 178 ILE B 182 5 5
HELIX 23 23 THR B 183 GLN B 197 1 15
HELIX 24 24 PRO B 198 ALA B 211 1 14
HELIX 25 25 PRO B 212 ASP B 217 5 6
HELIX 26 26 VAL B 218 ILE B 225 5 8
HELIX 27 27 LEU B 242 ILE B 252 1 11
HELIX 28 28 TRP B 266 HIS B 271 1 6
HELIX 29 29 HIS B 271 ALA B 286 1 16
SHEET 1 A16 SER A 10 GLU A 17 0
SHEET 2 A16 PHE A 20 ALA A 30 -1 O TYR A 27 N LYS A 11
SHEET 3 A16 ARG A 65 LYS A 69 -1 O LEU A 68 N ASN A 28
SHEET 4 A16 THR A 35 LEU A 39 1 N MET A 38 O ILE A 67
SHEET 5 A16 ALA A 106 ASN A 111 1 O HIS A 107 N THR A 35
SHEET 6 A16 ILE A 129 MET A 135 1 O MET A 135 N GLY A 110
SHEET 7 A16 THR A 229 GLY A 234 1 O THR A 232 N LEU A 134
SHEET 8 A16 ALA A 255 PHE A 260 1 O ARG A 256 N ILE A 231
SHEET 9 A16 ALA B 255 PHE B 260 -1 O VAL B 259 N LEU A 257
SHEET 10 A16 LYS B 228 GLY B 234 1 N ILE B 231 O ARG B 256
SHEET 11 A16 ILE B 129 MET B 135 1 N LEU B 134 O THR B 232
SHEET 12 A16 ALA B 106 ASN B 111 1 N ALA B 106 O GLY B 130
SHEET 13 A16 THR B 35 LEU B 39 1 N ILE B 37 O HIS B 107
SHEET 14 A16 ARG B 65 LYS B 69 1 O ARG B 65 N VAL B 36
SHEET 15 A16 PHE B 23 ALA B 30 -1 N ASN B 28 O LEU B 68
SHEET 16 A16 SER B 10 ILE B 15 -1 N LYS B 11 O TYR B 27
CISPEP 1 MET A 148 PRO A 149 0 3.12
CISPEP 2 MET B 148 PRO B 149 0 2.13
SITE 1 AC1 10 GLY A 41 GLY A 43 ALA A 46 ASN A 51
SITE 2 AC1 10 ASN A 111 SER A 112 PHE A 175 ARG A 190
SITE 3 AC1 10 GLN A 265 TRP A 266
CRYST1 135.992 135.992 65.767 90.00 90.00 120.00 P 64 12
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 0.007353 0.004245 0.000000 0.00000
SCALE2 0.000000 0.008491 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015205 0.00000
TER 2263 ALA A 286
TER 4509 ALA B 286
MASTER 335 0 1 29 16 0 3 6 4623 2 7 44
END
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