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HEADER HYDROLASE 27-JAN-09 3G02
TITLE STRUCTURE OF ENANTIOSELECTIVE MUTANT OF EPOXIDE HYDROLASE
TITLE 2 FROM ASPERGILLUS NIGER GENERATED BY DIRECTED EVOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPOXIDE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 5-398;
COMPND 5 EC: 3.3.2.9;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS NIGER;
SOURCE 3 ORGANISM_TAXID: 5061;
SOURCE 4 STRAIN: LCP521;
SOURCE 5 GENE: HYL1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SG13009;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQEEH_LW202
KEYWDS EPOXIDE HYDROLASE, ALPHA/BETA HYDROLASE FOLD,
KEYWDS 2 ENANTIOSELECTIVE, MUTANT, DIRECTED EVOLUTION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.NAWORYTA,S.L.MOWBRAY
REVDAT 1 09-JUN-09 3G02 0
JRNL AUTH M.T.REETZ,M.BOCOLA,L.-W.WANG,J.SANCHIS,A.CRONIN,
JRNL AUTH 2 M.ARAND,J.ZOU,A.ARCHELAS,A.-L.BOTTALLA,A.NAWORYTA,
JRNL AUTH 3 S.L.MOWBRAY
JRNL TITL DIRECTED EVOLUTION OF AN ENANTIOSELECTIVE EPOXIDE
JRNL TITL 2 HYDROLASE: UNCOVERING THE SOURCE OF
JRNL TITL 3 ENANTIOSELECTIVITY AT EACH EVOLUTIONARY STAGE
JRNL REF J.AM.CHEM.SOC. V. 131 7334 2009
JRNL REFN ISSN 0002-7863
JRNL PMID 19469578
JRNL DOI 10.1021/JA809673D
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.ZOU,B.M.HALLBERG,T.BERGFORS,F.OESCH,M.ARAND,
REMARK 1 AUTH 2 S.L.MOWBRAY,T.A.JONES
REMARK 1 TITL STRUCTURE OF ASPERGILLUS NIGER EPOXIDE HYDROLASE AT
REMARK 1 TITL 2 1.8 A RESOLUTION: IMPLICATIONS FOR THE STRUCTURE
REMARK 1 TITL 3 AND FUNCTION OF THE MAMMALIAN MICROSOMAL CLASS OF
REMARK 1 TITL 4 EPOXIDE HYDROLASES
REMARK 1 REF STRUCTURE V. 8 111 2000
REMARK 1 REFN ISSN 0969-2126
REMARK 1 PMID 10673439
REMARK 2
REMARK 2 RESOLUTION. 1.50 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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.91
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 3 NUMBER OF REFLECTIONS : 120661
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 6102
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8756
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.12
REMARK 3 BIN R VALUE (WORKING SET) : 0.2250
REMARK 3 BIN FREE R VALUE SET COUNT : 435
REMARK 3 BIN FREE R VALUE : 0.2460
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6354
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 715
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 0.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.36000
REMARK 3 B22 (A**2) : 0.95000
REMARK 3 B33 (A**2) : -0.92000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.64000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.081
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.079
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.046
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.201
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6587 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9001 ; 1.007 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 815 ; 5.416 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 290 ;34.027 ;23.310
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1038 ;12.041 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 35 ;13.791 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 957 ; 0.069 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5155 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3503 ; 0.186 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4630 ; 0.308 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 597 ; 0.102 ; 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): 67 ; 0.131 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 58 ; 0.080 ; 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): 4106 ; 0.448 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6542 ; 0.759 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2846 ; 1.143 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2459 ; 1.750 ; 4.500
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 : 1.40
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3G02 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-JAN-09.
REMARK 100 THE RCSB ID CODE IS RCSB051252.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-AUG-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93300
REMARK 200 MONOCHROMATOR : GRAPHITE
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
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 120696
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 30.540
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 200 DATA REDUNDANCY : 1.700
REMARK 200 R MERGE (I) : 0.02700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 1.70
REMARK 200 R MERGE FOR SHELL (I) : 0.12800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 7.200
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 1QO7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 6000, 0.1M MES, PH 6.0,
REMARK 280 0.1M UNBUFFERED SODIUM ACETATE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
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 44.83750
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 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 0
REMARK 465 ASN A 1
REMARK 465 HIS A 2
REMARK 465 ALA A 321
REMARK 465 SER A 322
REMARK 465 ALA A 323
REMARK 465 PRO A 324
REMARK 465 ASN A 325
REMARK 465 GLY A 326
REMARK 465 ALA A 327
REMARK 465 GLN A 397
REMARK 465 LYS A 398
REMARK 465 GLY A 399
REMARK 465 ARG A 400
REMARK 465 SER A 401
REMARK 465 HIS A 402
REMARK 465 HIS A 403
REMARK 465 HIS A 404
REMARK 465 HIS A 405
REMARK 465 HIS A 406
REMARK 465 HIS A 407
REMARK 465 MET B 0
REMARK 465 ASN B 1
REMARK 465 HIS B 2
REMARK 465 GLU B 223
REMARK 465 GLY B 224
REMARK 465 PRO B 225
REMARK 465 SER B 226
REMARK 465 ILE B 227
REMARK 465 GLU B 228
REMARK 465 PRO B 319
REMARK 465 THR B 320
REMARK 465 ALA B 321
REMARK 465 SER B 322
REMARK 465 ALA B 323
REMARK 465 PRO B 324
REMARK 465 ASN B 325
REMARK 465 GLY B 326
REMARK 465 GLN B 397
REMARK 465 LYS B 398
REMARK 465 GLY B 399
REMARK 465 ARG B 400
REMARK 465 SER B 401
REMARK 465 HIS B 402
REMARK 465 HIS B 403
REMARK 465 HIS B 404
REMARK 465 HIS B 405
REMARK 465 HIS B 406
REMARK 465 HIS B 407
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 PRO A 118 41.34 -94.03
REMARK 500 THR A 153 -115.96 44.84
REMARK 500 ASP A 192 -136.50 52.52
REMARK 500 ASP A 286 -78.65 -81.15
REMARK 500 LYS A 332 -99.98 -111.72
REMARK 500 ALA B 4 101.03 63.22
REMARK 500 PRO B 118 45.33 -95.10
REMARK 500 THR B 153 -113.47 43.16
REMARK 500 ASP B 192 -136.93 53.31
REMARK 500 ASP B 286 -80.03 -81.47
REMARK 500 LYS B 332 -104.01 -118.83
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 435 DISTANCE = 8.41 ANGSTROMS
REMARK 525 HOH B 468 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH B 485 DISTANCE = 6.89 ANGSTROMS
REMARK 525 HOH B 535 DISTANCE = 7.12 ANGSTROMS
REMARK 525 HOH B 552 DISTANCE = 8.74 ANGSTROMS
REMARK 525 HOH A 671 DISTANCE = 5.62 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 408
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 409
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 408
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QO7 RELATED DB: PDB
REMARK 900 STRUCTURE OF ASPERGILLUS NIGER EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 3G0I RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, NATIVE FORM
DBREF 3G02 A 5 398 UNP Q9UR30 Q9UR30_ASPNG 5 398
DBREF 3G02 B 5 398 UNP Q9UR30 Q9UR30_ASPNG 5 398
SEQADV 3G02 MET A 0 UNP Q9UR30 INITIATING METHIONINE
SEQADV 3G02 ASN A 1 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G02 HIS A 2 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G02 LYS A 3 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G02 ALA A 4 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G02 PHE A 215 UNP Q9UR30 LEU 215 ENGINEERED
SEQADV 3G02 ASN A 217 UNP Q9UR30 ALA 217 ENGINEERED
SEQADV 3G02 SER A 219 UNP Q9UR30 ARG 219 ENGINEERED
SEQADV 3G02 TYR A 249 UNP Q9UR30 LEU 249 ENGINEERED
SEQADV 3G02 TRP A 317 UNP Q9UR30 THR 317 ENGINEERED
SEQADV 3G02 VAL A 318 UNP Q9UR30 THR 318 ENGINEERED
SEQADV 3G02 PRO A 329 UNP Q9UR30 MET 329 ENGINEERED
SEQADV 3G02 TYR A 330 UNP Q9UR30 LEU 330 ENGINEERED
SEQADV 3G02 VAL A 350 UNP Q9UR30 CYS 350 ENGINEERED
SEQADV 3G02 GLY A 399 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G02 ARG A 400 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G02 SER A 401 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G02 HIS A 402 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G02 HIS A 403 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G02 HIS A 404 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G02 HIS A 405 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G02 HIS A 406 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G02 HIS A 407 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G02 MET B 0 UNP Q9UR30 INITIATING METHIONINE
SEQADV 3G02 ASN B 1 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G02 HIS B 2 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G02 LYS B 3 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G02 ALA B 4 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G02 PHE B 215 UNP Q9UR30 LEU 215 ENGINEERED
SEQADV 3G02 ASN B 217 UNP Q9UR30 ALA 217 ENGINEERED
SEQADV 3G02 SER B 219 UNP Q9UR30 ARG 219 ENGINEERED
SEQADV 3G02 TYR B 249 UNP Q9UR30 LEU 249 ENGINEERED
SEQADV 3G02 TRP B 317 UNP Q9UR30 THR 317 ENGINEERED
SEQADV 3G02 VAL B 318 UNP Q9UR30 THR 318 ENGINEERED
SEQADV 3G02 PRO B 329 UNP Q9UR30 MET 329 ENGINEERED
SEQADV 3G02 TYR B 330 UNP Q9UR30 LEU 330 ENGINEERED
SEQADV 3G02 VAL B 350 UNP Q9UR30 CYS 350 ENGINEERED
SEQADV 3G02 GLY B 399 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G02 ARG B 400 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G02 SER B 401 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G02 HIS B 402 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G02 HIS B 403 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G02 HIS B 404 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G02 HIS B 405 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G02 HIS B 406 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G02 HIS B 407 UNP Q9UR30 EXPRESSION TAG
SEQRES 1 A 408 MET ASN HIS LYS ALA PHE ALA LYS PHE PRO SER SER ALA
SEQRES 2 A 408 SER ILE SER PRO ASN PRO PHE THR VAL SER ILE PRO ASP
SEQRES 3 A 408 GLU GLN LEU ASP ASP LEU LYS THR LEU VAL ARG LEU SER
SEQRES 4 A 408 LYS ILE ALA PRO PRO THR TYR GLU SER LEU GLN ALA ASP
SEQRES 5 A 408 GLY ARG PHE GLY ILE THR SER GLU TRP LEU THR THR MET
SEQRES 6 A 408 ARG GLU LYS TRP LEU SER GLU PHE ASP TRP ARG PRO PHE
SEQRES 7 A 408 GLU ALA ARG LEU ASN SER PHE PRO GLN PHE THR THR GLU
SEQRES 8 A 408 ILE GLU GLY LEU THR ILE HIS PHE ALA ALA LEU PHE SER
SEQRES 9 A 408 GLU ARG GLU ASP ALA VAL PRO ILE ALA LEU LEU HIS GLY
SEQRES 10 A 408 TRP PRO GLY SER PHE VAL GLU PHE TYR PRO ILE LEU GLN
SEQRES 11 A 408 LEU PHE ARG GLU GLU TYR THR PRO GLU THR LEU PRO PHE
SEQRES 12 A 408 HIS LEU VAL VAL PRO SER LEU PRO GLY TYR THR PHE SER
SEQRES 13 A 408 SER GLY PRO PRO LEU ASP LYS ASP PHE GLY LEU MET ASP
SEQRES 14 A 408 ASN ALA ARG VAL VAL ASP GLN LEU MET LYS ASP LEU GLY
SEQRES 15 A 408 PHE GLY SER GLY TYR ILE ILE GLN GLY GLY ASP ILE GLY
SEQRES 16 A 408 SER PHE VAL GLY ARG LEU LEU GLY VAL GLY PHE ASP ALA
SEQRES 17 A 408 CYS LYS ALA VAL HIS LEU ASN PHE CYS ASN MET SER ALA
SEQRES 18 A 408 PRO PRO GLU GLY PRO SER ILE GLU SER LEU SER ALA ALA
SEQRES 19 A 408 GLU LYS GLU GLY ILE ALA ARG MET GLU LYS PHE MET THR
SEQRES 20 A 408 ASP GLY TYR ALA TYR ALA MET GLU HIS SER THR ARG PRO
SEQRES 21 A 408 SER THR ILE GLY HIS VAL LEU SER SER SER PRO ILE ALA
SEQRES 22 A 408 LEU LEU ALA TRP ILE GLY GLU LYS TYR LEU GLN TRP VAL
SEQRES 23 A 408 ASP LYS PRO LEU PRO SER GLU THR ILE LEU GLU MET VAL
SEQRES 24 A 408 SER LEU TYR TRP LEU THR GLU SER PHE PRO ARG ALA ILE
SEQRES 25 A 408 HIS THR TYR ARG GLU TRP VAL PRO THR ALA SER ALA PRO
SEQRES 26 A 408 ASN GLY ALA THR PRO TYR GLN LYS GLU LEU TYR ILE HIS
SEQRES 27 A 408 LYS PRO PHE GLY PHE SER PHE PHE PRO LYS ASP LEU VAL
SEQRES 28 A 408 PRO VAL PRO ARG SER TRP ILE ALA THR THR GLY ASN LEU
SEQRES 29 A 408 VAL PHE PHE ARG ASP HIS ALA GLU GLY GLY HIS PHE ALA
SEQRES 30 A 408 ALA LEU GLU ARG PRO ARG GLU LEU LYS THR ASP LEU THR
SEQRES 31 A 408 ALA PHE VAL GLU GLN VAL TRP GLN LYS GLY ARG SER HIS
SEQRES 32 A 408 HIS HIS HIS HIS HIS
SEQRES 1 B 408 MET ASN HIS LYS ALA PHE ALA LYS PHE PRO SER SER ALA
SEQRES 2 B 408 SER ILE SER PRO ASN PRO PHE THR VAL SER ILE PRO ASP
SEQRES 3 B 408 GLU GLN LEU ASP ASP LEU LYS THR LEU VAL ARG LEU SER
SEQRES 4 B 408 LYS ILE ALA PRO PRO THR TYR GLU SER LEU GLN ALA ASP
SEQRES 5 B 408 GLY ARG PHE GLY ILE THR SER GLU TRP LEU THR THR MET
SEQRES 6 B 408 ARG GLU LYS TRP LEU SER GLU PHE ASP TRP ARG PRO PHE
SEQRES 7 B 408 GLU ALA ARG LEU ASN SER PHE PRO GLN PHE THR THR GLU
SEQRES 8 B 408 ILE GLU GLY LEU THR ILE HIS PHE ALA ALA LEU PHE SER
SEQRES 9 B 408 GLU ARG GLU ASP ALA VAL PRO ILE ALA LEU LEU HIS GLY
SEQRES 10 B 408 TRP PRO GLY SER PHE VAL GLU PHE TYR PRO ILE LEU GLN
SEQRES 11 B 408 LEU PHE ARG GLU GLU TYR THR PRO GLU THR LEU PRO PHE
SEQRES 12 B 408 HIS LEU VAL VAL PRO SER LEU PRO GLY TYR THR PHE SER
SEQRES 13 B 408 SER GLY PRO PRO LEU ASP LYS ASP PHE GLY LEU MET ASP
SEQRES 14 B 408 ASN ALA ARG VAL VAL ASP GLN LEU MET LYS ASP LEU GLY
SEQRES 15 B 408 PHE GLY SER GLY TYR ILE ILE GLN GLY GLY ASP ILE GLY
SEQRES 16 B 408 SER PHE VAL GLY ARG LEU LEU GLY VAL GLY PHE ASP ALA
SEQRES 17 B 408 CYS LYS ALA VAL HIS LEU ASN PHE CYS ASN MET SER ALA
SEQRES 18 B 408 PRO PRO GLU GLY PRO SER ILE GLU SER LEU SER ALA ALA
SEQRES 19 B 408 GLU LYS GLU GLY ILE ALA ARG MET GLU LYS PHE MET THR
SEQRES 20 B 408 ASP GLY TYR ALA TYR ALA MET GLU HIS SER THR ARG PRO
SEQRES 21 B 408 SER THR ILE GLY HIS VAL LEU SER SER SER PRO ILE ALA
SEQRES 22 B 408 LEU LEU ALA TRP ILE GLY GLU LYS TYR LEU GLN TRP VAL
SEQRES 23 B 408 ASP LYS PRO LEU PRO SER GLU THR ILE LEU GLU MET VAL
SEQRES 24 B 408 SER LEU TYR TRP LEU THR GLU SER PHE PRO ARG ALA ILE
SEQRES 25 B 408 HIS THR TYR ARG GLU TRP VAL PRO THR ALA SER ALA PRO
SEQRES 26 B 408 ASN GLY ALA THR PRO TYR GLN LYS GLU LEU TYR ILE HIS
SEQRES 27 B 408 LYS PRO PHE GLY PHE SER PHE PHE PRO LYS ASP LEU VAL
SEQRES 28 B 408 PRO VAL PRO ARG SER TRP ILE ALA THR THR GLY ASN LEU
SEQRES 29 B 408 VAL PHE PHE ARG ASP HIS ALA GLU GLY GLY HIS PHE ALA
SEQRES 30 B 408 ALA LEU GLU ARG PRO ARG GLU LEU LYS THR ASP LEU THR
SEQRES 31 B 408 ALA PHE VAL GLU GLN VAL TRP GLN LYS GLY ARG SER HIS
SEQRES 32 B 408 HIS HIS HIS HIS HIS
HET FMT A 408 3
HET FMT A 409 3
HET FMT B 408 3
HETNAM FMT FORMIC ACID
FORMUL 3 FMT 3(C H2 O2)
FORMUL 6 HOH *706(H2 O)
HELIX 1 1 PRO A 24 SER A 38 1 15
HELIX 2 2 TYR A 45 GLN A 49 5 5
HELIX 3 3 THR A 57 GLU A 71 1 15
HELIX 4 4 ASP A 73 ASN A 82 1 10
HELIX 5 5 SER A 120 GLU A 123 5 4
HELIX 6 6 PHE A 124 TYR A 135 1 12
HELIX 7 7 GLY A 165 LEU A 180 1 16
HELIX 8 8 ASP A 192 PHE A 205 1 14
HELIX 9 9 SER A 226 LEU A 230 5 5
HELIX 10 10 SER A 231 GLY A 248 1 18
HELIX 11 11 TYR A 249 ARG A 258 1 10
HELIX 12 12 ARG A 258 SER A 268 1 11
HELIX 13 13 SER A 269 TRP A 284 1 16
HELIX 14 14 PRO A 290 THR A 304 1 15
HELIX 15 15 GLU A 305 ILE A 311 1 7
HELIX 16 16 THR A 313 VAL A 318 1 6
HELIX 17 17 PRO A 353 ALA A 358 1 6
HELIX 18 18 PHE A 375 ARG A 380 1 6
HELIX 19 19 ARG A 380 TRP A 396 1 17
HELIX 20 20 PRO B 24 SER B 38 1 15
HELIX 21 21 TYR B 45 GLN B 49 5 5
HELIX 22 22 THR B 57 GLU B 71 1 15
HELIX 23 23 ASP B 73 ASN B 82 1 10
HELIX 24 24 SER B 120 GLU B 123 5 4
HELIX 25 25 PHE B 124 TYR B 135 1 12
HELIX 26 26 GLY B 165 LEU B 180 1 16
HELIX 27 27 ASP B 192 PHE B 205 1 14
HELIX 28 28 SER B 231 GLY B 248 1 18
HELIX 29 29 TYR B 249 ARG B 258 1 10
HELIX 30 30 ARG B 258 SER B 268 1 11
HELIX 31 31 SER B 269 TRP B 284 1 16
HELIX 32 32 PRO B 290 THR B 304 1 15
HELIX 33 33 GLU B 305 ILE B 311 1 7
HELIX 34 34 THR B 313 VAL B 318 1 6
HELIX 35 35 THR B 328 LYS B 332 5 5
HELIX 36 36 PRO B 353 ALA B 358 1 6
HELIX 37 37 PHE B 375 ARG B 380 1 6
HELIX 38 38 ARG B 380 TRP B 396 1 17
SHEET 1 A 8 GLN A 86 ILE A 91 0
SHEET 2 A 8 LEU A 94 LEU A 101 -1 O ILE A 96 N THR A 89
SHEET 3 A 8 PHE A 142 PRO A 147 -1 O VAL A 146 N ALA A 99
SHEET 4 A 8 VAL A 109 LEU A 114 1 N ILE A 111 O VAL A 145
SHEET 5 A 8 TYR A 186 GLY A 190 1 O GLN A 189 N LEU A 114
SHEET 6 A 8 CYS A 208 LEU A 213 1 O HIS A 212 N ILE A 188
SHEET 7 A 8 ILE A 336 PHE A 344 1 O GLY A 341 N LEU A 213
SHEET 8 A 8 GLY A 361 ASP A 368 1 O ARG A 367 N PHE A 344
SHEET 1 B 8 GLN B 86 ILE B 91 0
SHEET 2 B 8 LEU B 94 LEU B 101 -1 O ILE B 96 N THR B 89
SHEET 3 B 8 PHE B 142 PRO B 147 -1 O VAL B 146 N ALA B 99
SHEET 4 B 8 VAL B 109 LEU B 114 1 N ILE B 111 O VAL B 145
SHEET 5 B 8 TYR B 186 GLY B 190 1 O GLN B 189 N LEU B 114
SHEET 6 B 8 CYS B 208 LEU B 213 1 O HIS B 212 N ILE B 188
SHEET 7 B 8 ILE B 336 PHE B 344 1 O GLY B 341 N LEU B 213
SHEET 8 B 8 GLY B 361 ASP B 368 1 O ARG B 367 N PHE B 344
CISPEP 1 TRP A 117 PRO A 118 0 2.09
CISPEP 2 GLY A 157 PRO A 158 0 -2.54
CISPEP 3 GLY A 224 PRO A 225 0 -1.69
CISPEP 4 TRP B 117 PRO B 118 0 1.28
CISPEP 5 GLY B 157 PRO B 158 0 -1.39
SITE 1 AC1 7 TRP A 117 ASP A 192 TYR A 251 TRP A 284
SITE 2 AC1 7 TYR A 314 TRP A 317 HOH A 495
SITE 1 AC2 6 SER A 195 ARG A 199 CYS A 216 ASN A 217
SITE 2 AC2 6 TYR A 330 HOH A 496
SITE 1 AC3 6 TRP B 117 ASP B 192 TYR B 251 TRP B 284
SITE 2 AC3 6 TYR B 314 TRP B 317
CRYST1 61.866 89.675 75.344 90.00 104.79 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 0.016164 0.000000 0.004268 0.00000
SCALE2 0.000000 0.011151 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013727 0.00000
TER 3199 TRP A 396
TER 6356 TRP B 396
MASTER 356 0 3 38 16 0 6 6 7069 2 9 64
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