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HEADER HYDROLASE 04-SEP-12 4B9E
TITLE STRUCTURE OF A PUTATIVE EPOXIDE HYDROLASE FROM PSEUDOMONAS
TITLE 2 AERUGINOSA, WITH BOUND MFA.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE EPOXIDE HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PA2086;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA PAO1;
SOURCE 3 ORGANISM_TAXID: 208964;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET28
KEYWDS HYDROLASE, MONOFLUOROACETATE, DEFLUORINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.W.SCHMIDBERGER,R.SCHNELL,G.SCHNEIDER
REVDAT 1 06-FEB-13 4B9E 0
JRNL AUTH L.MOYNIE,R.SCHNELL,S.A.MCMAHON,T.SANDALOVA,W.A.BOULKEROU,
JRNL AUTH 2 J.W.SCHMIDBERGER,M.ALPHEY,C.CUKIER,F.DUTHIE,J.KOPEC,H.LIU,
JRNL AUTH 3 A.JACEWICZ,W.N.HUNTER,J.H.NAISMITH,G.SCHNEIDER
JRNL TITL THE AEROPATH PROJECT TARGETING PSEUDOMONAS AERUGINOSA:
JRNL TITL 2 CRYSTALLOGRAPHIC STUDIES FOR ASSESSMENT OF POTENTIAL
JRNL TITL 3 TARGETS IN EARLY-STAGE DRUG DISCOVERY.
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 69 25 2013
JRNL REFN ISSN 1744-3091
JRNL PMID 23295481
JRNL DOI 10.1107/S1744309112044739
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.27
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.68
REMARK 3 NUMBER OF REFLECTIONS : 94130
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) : 0.11165
REMARK 3 R VALUE (WORKING SET) : 0.11040
REMARK 3 FREE R VALUE : 0.13525
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 4952
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) : 1.400
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.436
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6771
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.75
REMARK 3 BIN R VALUE (WORKING SET) : 0.243
REMARK 3 BIN FREE R VALUE SET COUNT : 352
REMARK 3 BIN FREE R VALUE : 0.288
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2417
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 57
REMARK 3 SOLVENT ATOMS : 417
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.7
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.522
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.04
REMARK 3 B22 (A**2) : 0.04
REMARK 3 B33 (A**2) : -0.08
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.032
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.034
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.020
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.143
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.984
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.979
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2540 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2395 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3472 ; 1.720 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5469 ; 0.912 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 320 ; 5.334 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 128 ;30.306 ;22.031
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 388 ;12.136 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;19.155 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 371 ; 0.113 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2909 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 633 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1006 ; 0.279 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2006 ; 0.221 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1158 ; 0.189 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1187 ; 0.107 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 68 ; 0.188 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 4 ; 0.091 ; 0.200
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): 64 ; 0.311 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 52 ; 0.179 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.144 ; 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): 2540 ;10.937 ; 1.529
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2394 ;11.304 ; 1.595
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): 4934 ; 3.690 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 88 ;40.614 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 5198 ;12.522 ; 5.000
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
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 4B9E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-SEP-12.
REMARK 100 THE PDBE ID CODE IS EBI-53963.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-MAY-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0064
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (QUANTUM 315R)
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 99408
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.40
REMARK 200 RESOLUTION RANGE LOW (A) : 36.83
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.2
REMARK 200 R MERGE (I) : 0.09
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.50
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.0
REMARK 200 R MERGE FOR SHELL (I) : 0.69
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.40
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 1Y37
REMARK 200
REMARK 200 REMARK: BEING A SOAK EXPERIMENT, THIS DATA WAS ACTUALLY
REMARK 200 REFINED AGAINST THE NATIVE UNLIGANDED STRUCTURE WITH PDB
REMARK 200 CODE 4B9A.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.5
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M LI2SO4, 1.25 M (NH4)2SO4,
REMARK 280 0.1 M TRIS HCL PH 8.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 70.47500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 41.96000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 41.96000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 35.23750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 41.96000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 41.96000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 105.71250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 41.96000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.96000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 35.23750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 41.96000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.96000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 105.71250
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 70.47500
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: 4770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -133.0 KCAL/MOL
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2238 LIES ON A SPECIAL POSITION.
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 SER A 0
REMARK 465 MET A 1
REMARK 465 ASN A 2
REMARK 465 THR A 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 NE ARG A 234 O2 SO4 A 1305 2.19
REMARK 500 NH2 ARG A 234 O2 SO4 A 1305 2.17
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 PRO A 40 58.07 -100.88
REMARK 500 GLN A 41 -166.66 -116.48
REMARK 500 ASP A 107 -131.36 59.61
REMARK 500 THR A 131 -1.08 80.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAH A1301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAH A1309
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1310
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAH A1311
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4B9A RELATED DB: PDB
REMARK 900 STRUCTURE OF A PUTATIVE EPOXIDE HYDROLASE FROM
REMARK 900 PSEUDOMONAS AERUGINOSA.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CLONING AND CLEAVAGE OF THE HIS TAG LEFT AND EXTRA N-
REMARK 999 TERMINAL SERINE.
DBREF 4B9E A 1 300 UNP Q9I229 Q9I229_PSEAE 1 300
SEQADV 4B9E SER A 0 UNP Q9I229 EXPRESSION TAG
SEQRES 1 A 301 SER MET ASN THR ASP PRO LEU LEU PRO GLY PHE ASP TYR
SEQRES 2 A 301 LEU THR LEU HIS THR SER ALA ALA ARG LEU ARG VAL ALA
SEQRES 3 A 301 VAL LYS GLY SER GLY PRO PRO LEU LEU LEU LEU HIS GLY
SEQRES 4 A 301 TYR PRO GLN THR HIS LEU ALA TRP HIS ARG ILE ALA PRO
SEQRES 5 A 301 ARG LEU ALA GLU ASP TYR SER VAL VAL LEU ALA ASP LEU
SEQRES 6 A 301 ARG GLY TYR GLY GLU SER ARG ALA LEU ASP GLU GLU GLY
SEQRES 7 A 301 ALA ASP TYR SER LYS ALA ALA LEU ALA ARG ASP GLN LEU
SEQRES 8 A 301 GLU THR MET GLY GLN LEU GLY PHE GLU ARG PHE ALA VAL
SEQRES 9 A 301 ILE GLY HIS ASP ARG GLY ALA ARG VAL GLY TYR ARG LEU
SEQRES 10 A 301 ALA LEU ASP HIS PRO GLN ALA VAL ALA ALA PHE VAL SER
SEQRES 11 A 301 LEU THR VAL VAL PRO ILE LEU ASP ASN TRP ALA ALA VAL
SEQRES 12 A 301 ASN LYS VAL PHE ALA LEU ASN ALA TYR HIS TRP PHE LEU
SEQRES 13 A 301 LEU ALA GLN PRO TYR ASP LEU PRO GLU ARG LEU ILE GLY
SEQRES 14 A 301 ALA ASP PRO GLU HIS PHE LEU ASP TYR THR LEU ARG ARG
SEQRES 15 A 301 MET ALA GLN GLY ARG ASP ILE TYR HIS PRO GLN ALA LEU
SEQRES 16 A 301 GLU SER TYR ARG ARG ALA PHE ARG ASP PRO ALA VAL ARG
SEQRES 17 A 301 HIS ALA MET CYS GLU ASP TYR ARG ALA ALA VAL GLY VAL
SEQRES 18 A 301 ASP ALA ASP ALA ASP GLN ALA ASP ARG ASP ALA GLY ARG
SEQRES 19 A 301 ARG LEU GLN CYS PRO VAL GLN VAL LEU TRP GLN GLU ARG
SEQRES 20 A 301 PRO TYR ALA ALA GLY GLN HIS PRO LEU GLU ILE TRP LYS
SEQRES 21 A 301 THR TRP ALA GLY GLN VAL GLU GLY ALA ALA ILE GLY ALA
SEQRES 22 A 301 SER HIS MET LEU PRO GLU ASP ALA PRO ASP ALA VAL LEU
SEQRES 23 A 301 GLU HIS LEU LEU GLY PHE LEU ALA SER HIS ARG GLU ALA
SEQRES 24 A 301 LEU ARG
HET FAH A1301 5
HET SO4 A1302 5
HET SO4 A1303 5
HET SO4 A1304 5
HET SO4 A1305 5
HET SO4 A1306 5
HET SO4 A1307 5
HET GOL A1308 6
HET FAH A1309 5
HET GOL A1310 6
HET FAH A1311 5
HETNAM FAH FLUOROACETIC ACID
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 FAH 3(C2 H3 F O2)
FORMUL 3 SO4 6(O4 S 2-)
FORMUL 4 GOL 2(C3 H8 O3)
FORMUL 5 HOH *417(H2 O)
HELIX 1 1 THR A 42 HIS A 47 5 6
HELIX 2 2 ILE A 49 GLU A 55 1 7
HELIX 3 3 SER A 81 GLY A 97 1 17
HELIX 4 4 ASP A 107 HIS A 120 1 14
HELIX 5 5 PRO A 134 ALA A 141 1 8
HELIX 6 6 ASN A 143 ALA A 150 1 8
HELIX 7 7 ALA A 150 LEU A 156 1 7
HELIX 8 8 ASP A 161 ALA A 169 1 9
HELIX 9 9 ASP A 170 ALA A 183 1 14
HELIX 10 10 HIS A 190 ARG A 202 1 13
HELIX 11 11 ASP A 203 GLY A 219 1 17
HELIX 12 12 GLY A 219 GLY A 232 1 14
HELIX 13 13 HIS A 253 THR A 260 1 8
HELIX 14 14 MET A 275 ALA A 280 1 6
HELIX 15 15 ALA A 280 HIS A 295 1 16
HELIX 16 16 HIS A 295 ARG A 300 1 6
SHEET 1 AA 2 ASP A 11 HIS A 16 0
SHEET 2 AA 2 ALA A 20 LYS A 27 -1 O LEU A 22 N LEU A 15
SHEET 1 AB 2 ARG A 71 ALA A 72 0
SHEET 2 AB 2 ALA A 20 LYS A 27 1 O ARG A 21 N ARG A 71
SHEET 1 AC 8 VAL A 265 ILE A 270 0
SHEET 2 AC 8 VAL A 239 GLN A 244 1 O VAL A 239 N GLU A 266
SHEET 3 AC 8 VAL A 124 LEU A 130 1 O PHE A 127 N GLN A 240
SHEET 4 AC 8 PHE A 101 HIS A 106 1 O PHE A 101 N ALA A 125
SHEET 5 AC 8 PRO A 32 LEU A 36 1 O PRO A 32 N ALA A 102
SHEET 6 AC 8 SER A 58 ALA A 62 1 O SER A 58 N LEU A 33
SHEET 7 AC 8 ALA A 20 LYS A 27 -1 O ALA A 25 N LEU A 61
SHEET 8 AC 8 ARG A 71 ALA A 72 1 O ARG A 71 N ARG A 21
SHEET 1 AD 8 VAL A 265 ILE A 270 0
SHEET 2 AD 8 VAL A 239 GLN A 244 1 O VAL A 239 N GLU A 266
SHEET 3 AD 8 VAL A 124 LEU A 130 1 O PHE A 127 N GLN A 240
SHEET 4 AD 8 PHE A 101 HIS A 106 1 O PHE A 101 N ALA A 125
SHEET 5 AD 8 PRO A 32 LEU A 36 1 O PRO A 32 N ALA A 102
SHEET 6 AD 8 SER A 58 ALA A 62 1 O SER A 58 N LEU A 33
SHEET 7 AD 8 ALA A 20 LYS A 27 -1 O ALA A 25 N LEU A 61
SHEET 8 AD 8 ASP A 11 HIS A 16 -1 O ASP A 11 N VAL A 26
CISPEP 1 TYR A 39 PRO A 40 0 -5.30
CISPEP 2 TYR A 160 ASP A 161 0 5.68
SITE 1 AC1 9 ASP A 107 HIS A 152 TRP A 153 MET A 182
SITE 2 AC1 9 TYR A 214 HIS A 274 HOH A2189 HOH A2240
SITE 3 AC1 9 HOH A2406
SITE 1 AC2 7 HIS A 47 ARG A 48 HIS A 190 HOH A2001
SITE 2 AC2 7 HOH A2003 HOH A2407 HOH A2408
SITE 1 AC3 5 ARG A 199 GLN A 226 ARG A 229 HOH A2126
SITE 2 AC3 5 HOH A2319
SITE 1 AC4 3 ARG A 52 HOH A2409 HOH A2410
SITE 1 AC5 4 ARG A 234 GLN A 236 HOH A2326 HOH A2332
SITE 1 AC6 7 ASP A 279 ALA A 280 PRO A 281 ASP A 282
SITE 2 AC6 7 ALA A 283 HOH A2391 HOH A2412
SITE 1 AC7 2 ARG A 198 HOH A2413
SITE 1 AC8 7 LEU A 6 LEU A 7 PHE A 10 TYR A 12
SITE 2 AC8 7 LYS A 144 HOH A2019 HOH A2311
SITE 1 AC9 10 GLY A 68 GLU A 69 SER A 70 ARG A 71
SITE 2 AC9 10 ARG A 199 ASP A 203 VAL A 206 HOH A2123
SITE 3 AC9 10 HOH A2414 HOH A2415
SITE 1 BC1 8 ASP A 176 ARG A 180 TYR A 189 LEU A 194
SITE 2 BC1 8 ARG A 198 HOH A2270 HOH A2282 HOH A2286
SITE 1 BC2 7 GLU A 212 ARG A 215 HOH A2109 HOH A2307
SITE 2 BC2 7 HOH A2310 HOH A2313 HOH A2417
CRYST1 83.920 83.920 140.950 90.00 90.00 90.00 P 41 21 2 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 0.011916 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011916 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007095 0.00000
TER 2418 ARG A 300
MASTER 359 0 11 16 20 0 21 6 2891 1 57 24
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