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HEADER HYDROLASE 25-MAR-08 3CN7
TITLE CRYSTAL STRUCTURE ANALYSIS OF THE CARBOXYLESTERASE PA3859
TITLE 2 FROM PSEUDOMONAS AERUGINOSA PAO1- MONOCLINIC CRYSTAL FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLESTERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 STRAIN: PAO1;
SOURCE 5 GENE: PA3859;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: M15 (PREP4);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE-31
KEYWDS ALPHA/BETA HYDROLASE FOLD SUPER-FAMILY
EXPDTA X-RAY DIFFRACTION
AUTHOR A.PESARESI,D.LAMBA
REVDAT 1 10-MAR-09 3CN7 0
JRNL AUTH A.PESARESI,D.LAMBA
JRNL TITL CRYSTAL STRUCTURE ANALYSIS OF THE CARBOXYLESTERASE
JRNL TITL 2 PA3859 FROM PSEUDOMONAS AERUGINOSA PAO1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.PESARESI,G.DEVESCOVI,D.LAMBA,V.VENTURI,G.DEGRASSI
REMARK 1 TITL ISOLATION, CHARACTERIZATION, AND HETEROLOGOUS
REMARK 1 TITL 2 EXPRESSION OF A CARBOXYLESTERASE OF PSEUDOMONAS
REMARK 1 TITL 3 AERUGINOSA PAO1
REMARK 1 REF CURR.MICROBIOL. V. 50 102 2005
REMARK 1 REFN ISSN 0343-8651
REMARK 1 PMID 15717224
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.PESARESI,D.LAMBA
REMARK 1 TITL CRYSTALLIZATION, X-RAY DIFFRACTION ANALYSIS AND
REMARK 1 TITL 2 PHASING OF CARBOXYLESTERASE PA3859 FROM
REMARK 1 TITL 3 PSEUDOMONAS AERUGINOSA
REMARK 1 REF BIOCHEM.BIOPHYS.ACTA V.1752 197 2005
REMARK 1 REF 2 PROTEINS & PROTEOMICS
REMARK 1 REFN ISSN 1570-9639
REMARK 1 PMID 16120484
REMARK 2
REMARK 2 RESOLUTION. 2.99 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.82
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 550394.570
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 18803
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 SET) : 0.204
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1849
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.99
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.18
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2708
REMARK 3 BIN R VALUE (WORKING SET) : 0.2910
REMARK 3 BIN FREE R VALUE : 0.3690
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 285
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6584
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 94
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 56.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.79000
REMARK 3 B22 (A**2) : 1.44000
REMARK 3 B33 (A**2) : 5.35000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.14000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.31
REMARK 3 ESD FROM SIGMAA (A) : 0.42
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.45
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.65
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.50
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.96
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : OVERALL ANISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 5.806 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 8.173 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 8.495 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 10.838; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 21.77
REMARK 3
REMARK 3 NCS MODEL : RESTRAIN
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : MES.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : MES.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3CN7 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAR-08.
REMARK 100 THE RCSB ID CODE IS RCSB046978.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-JUL-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ELETTRA
REMARK 200 BEAMLINE : 5.2R
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.200
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL (SI111)
REMARK 200 OPTICS : THREE-SEGMENT PT-COATED
REMARK 200 TOROIDAL MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18803
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.980
REMARK 200 RESOLUTION RANGE LOW (A) : 24.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.16000
REMARK 200 R SYM (I) : 0.13000
REMARK 200 FOR THE DATA SET : 3.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.44000
REMARK 200 R SYM FOR SHELL (I) : 0.36000
REMARK 200 FOR SHELL : 1.700
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: PDB ENTRY 1AUO, CHAIN A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.200 M AMS, 0.100 M MES, 30% W/V
REMARK 280 PEGMME-5000, LONG NEEDLES GREW WITHIN 3 DAYS, PH 6.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, 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 25.27400
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 -10
REMARK 465 ARG A -9
REMARK 465 GLY A -8
REMARK 465 SER A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 GLY A 0
REMARK 465 SER A 1
REMARK 465 MET B -10
REMARK 465 ARG B -9
REMARK 465 GLY B -8
REMARK 465 SER B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 GLY B 0
REMARK 465 SER B 1
REMARK 465 MET C -10
REMARK 465 ARG C -9
REMARK 465 GLY C -8
REMARK 465 SER C -7
REMARK 465 HIS C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 HIS C -1
REMARK 465 GLY C 0
REMARK 465 SER C 1
REMARK 465 MET D -10
REMARK 465 ARG D -9
REMARK 465 GLY D -8
REMARK 465 SER D -7
REMARK 465 HIS D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 HIS D -2
REMARK 465 HIS D -1
REMARK 465 GLY D 0
REMARK 465 SER D 1
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 ASN A 58 54.64 -116.74
REMARK 500 ALA A 71 140.67 -177.18
REMARK 500 ALA A 77 47.87 -54.70
REMARK 500 LYS A 100 8.74 -68.52
REMARK 500 GLU A 105 -8.06 -56.57
REMARK 500 SER A 113 -119.67 44.78
REMARK 500 ARG A 125 -42.87 -132.08
REMARK 500 THR A 139 -158.49 -130.73
REMARK 500 PRO A 142 -15.61 -48.76
REMARK 500 ALA A 148 59.80 -148.14
REMARK 500 HIS A 197 81.47 -61.91
REMARK 500 ASP B 13 12.29 -140.38
REMARK 500 ASN B 58 55.13 -114.72
REMARK 500 ALA B 71 140.96 -177.72
REMARK 500 PRO B 74 -156.27 -79.09
REMARK 500 ALA B 77 54.75 -56.61
REMARK 500 LYS B 100 11.78 -69.13
REMARK 500 GLU B 105 -7.10 -55.42
REMARK 500 SER B 113 -116.62 42.79
REMARK 500 ARG B 126 -60.41 -101.04
REMARK 500 THR B 139 -158.45 -134.55
REMARK 500 ALA B 148 59.97 -149.90
REMARK 500 VAL B 168 -34.43 -133.34
REMARK 500 HIS B 197 84.88 -66.49
REMARK 500 ASN C 58 57.46 -117.18
REMARK 500 ALA C 71 139.56 -178.18
REMARK 500 PRO C 74 -160.61 -79.74
REMARK 500 ALA C 77 48.70 -55.35
REMARK 500 LYS C 100 6.69 -68.25
REMARK 500 ALA C 104 -70.65 -45.34
REMARK 500 GLU C 105 -9.19 -53.26
REMARK 500 SER C 113 -118.28 46.88
REMARK 500 ARG C 126 -61.46 -97.58
REMARK 500 VAL C 168 -36.98 -134.12
REMARK 500 HIS C 197 85.11 -62.65
REMARK 500 ASP D 13 10.07 -141.85
REMARK 500 ASN D 58 51.49 -115.29
REMARK 500 ALA D 71 141.36 -179.34
REMARK 500 ALA D 77 49.40 -56.79
REMARK 500 LYS D 100 9.43 -69.73
REMARK 500 GLU D 105 -7.48 -53.14
REMARK 500 SER D 113 -122.82 45.10
REMARK 500 PRO D 142 -16.46 -47.47
REMARK 500 ALA D 148 57.43 -149.81
REMARK 500 VAL D 168 -35.56 -130.37
REMARK 500 HIS D 197 80.82 -59.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 MES B 216
REMARK 610 MES C 216
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 216
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES C 216
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AUO RELATED DB: PDB
REMARK 900 CARBOXYLESTERASE FROM PSEUDOMONAS FLUORESCENS
REMARK 900 RELATED ID: 1AUR RELATED DB: PDB
REMARK 900 PMSF-INHIBITED CARBOXYLESTERASE FROM PSEUDOMONAS FLUORESCENS
REMARK 900 RELATED ID: 1FJ2 RELATED DB: PDB
REMARK 900 HUMAN ACYL PROTEIN THIOESTERASE 1
REMARK 900 RELATED ID: 3CN9 RELATED DB: PDB
REMARK 900 CARBOXYLESTERASE PA3859 FROM PSEUDOMONAS AERUGINOSA PAO1
REMARK 900 ORTHORHOMBIC CRYSTAL FORM
DBREF 3CN7 A 2 215 UNP Q9HXE7 Q9HXE7_PSEAE 2 215
DBREF 3CN7 B 2 215 UNP Q9HXE7 Q9HXE7_PSEAE 2 215
DBREF 3CN7 C 2 215 UNP Q9HXE7 Q9HXE7_PSEAE 2 215
DBREF 3CN7 D 2 215 UNP Q9HXE7 Q9HXE7_PSEAE 2 215
SEQADV 3CN7 MET A -10 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 ARG A -9 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 GLY A -8 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 SER A -7 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 HIS A -6 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 HIS A -5 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 HIS A -4 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 HIS A -3 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 HIS A -2 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 HIS A -1 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 GLY A 0 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 SER A 1 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 MET B -10 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 ARG B -9 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 GLY B -8 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 SER B -7 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 HIS B -6 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 HIS B -5 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 HIS B -4 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 HIS B -3 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 HIS B -2 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 HIS B -1 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 GLY B 0 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 SER B 1 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 MET C -10 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 ARG C -9 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 GLY C -8 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 SER C -7 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 HIS C -6 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 HIS C -5 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 HIS C -4 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 HIS C -3 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 HIS C -2 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 HIS C -1 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 GLY C 0 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 SER C 1 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 MET D -10 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 ARG D -9 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 GLY D -8 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 SER D -7 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 HIS D -6 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 HIS D -5 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 HIS D -4 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 HIS D -3 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 HIS D -2 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 HIS D -1 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 GLY D 0 UNP Q9HXE7 EXPRESSION TAG
SEQADV 3CN7 SER D 1 UNP Q9HXE7 EXPRESSION TAG
SEQRES 1 A 226 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER SER
SEQRES 2 A 226 GLU PRO LEU ILE LEU ASP ALA PRO ASN ALA ASP ALA CYS
SEQRES 3 A 226 ILE ILE TRP LEU HIS GLY LEU GLY ALA ASP ARG THR ASP
SEQRES 4 A 226 PHE LYS PRO VAL ALA GLU ALA LEU GLN MET VAL LEU PRO
SEQRES 5 A 226 SER THR ARG PHE ILE LEU PRO GLN ALA PRO SER GLN ALA
SEQRES 6 A 226 VAL THR VAL ASN GLY GLY TRP VAL MET PRO SER TRP TYR
SEQRES 7 A 226 ASP ILE LEU ALA PHE SER PRO ALA ARG ALA ILE ASP GLU
SEQRES 8 A 226 ASP GLN LEU ASN ALA SER ALA ASP GLN VAL ILE ALA LEU
SEQRES 9 A 226 ILE ASP GLU GLN ARG ALA LYS GLY ILE ALA ALA GLU ARG
SEQRES 10 A 226 ILE ILE LEU ALA GLY PHE SER GLN GLY GLY ALA VAL VAL
SEQRES 11 A 226 LEU HIS THR ALA PHE ARG ARG TYR ALA GLN PRO LEU GLY
SEQRES 12 A 226 GLY VAL LEU ALA LEU SER THR TYR ALA PRO THR PHE ASP
SEQRES 13 A 226 ASP LEU ALA LEU ASP GLU ARG HIS LYS ARG ILE PRO VAL
SEQRES 14 A 226 LEU HIS LEU HIS GLY SER GLN ASP ASP VAL VAL ASP PRO
SEQRES 15 A 226 ALA LEU GLY ARG ALA ALA HIS ASP ALA LEU GLN ALA GLN
SEQRES 16 A 226 GLY VAL GLU VAL GLY TRP HIS ASP TYR PRO MET GLY HIS
SEQRES 17 A 226 GLU VAL SER LEU GLU GLU ILE HIS ASP ILE GLY ALA TRP
SEQRES 18 A 226 LEU ARG LYS ARG LEU
SEQRES 1 B 226 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER SER
SEQRES 2 B 226 GLU PRO LEU ILE LEU ASP ALA PRO ASN ALA ASP ALA CYS
SEQRES 3 B 226 ILE ILE TRP LEU HIS GLY LEU GLY ALA ASP ARG THR ASP
SEQRES 4 B 226 PHE LYS PRO VAL ALA GLU ALA LEU GLN MET VAL LEU PRO
SEQRES 5 B 226 SER THR ARG PHE ILE LEU PRO GLN ALA PRO SER GLN ALA
SEQRES 6 B 226 VAL THR VAL ASN GLY GLY TRP VAL MET PRO SER TRP TYR
SEQRES 7 B 226 ASP ILE LEU ALA PHE SER PRO ALA ARG ALA ILE ASP GLU
SEQRES 8 B 226 ASP GLN LEU ASN ALA SER ALA ASP GLN VAL ILE ALA LEU
SEQRES 9 B 226 ILE ASP GLU GLN ARG ALA LYS GLY ILE ALA ALA GLU ARG
SEQRES 10 B 226 ILE ILE LEU ALA GLY PHE SER GLN GLY GLY ALA VAL VAL
SEQRES 11 B 226 LEU HIS THR ALA PHE ARG ARG TYR ALA GLN PRO LEU GLY
SEQRES 12 B 226 GLY VAL LEU ALA LEU SER THR TYR ALA PRO THR PHE ASP
SEQRES 13 B 226 ASP LEU ALA LEU ASP GLU ARG HIS LYS ARG ILE PRO VAL
SEQRES 14 B 226 LEU HIS LEU HIS GLY SER GLN ASP ASP VAL VAL ASP PRO
SEQRES 15 B 226 ALA LEU GLY ARG ALA ALA HIS ASP ALA LEU GLN ALA GLN
SEQRES 16 B 226 GLY VAL GLU VAL GLY TRP HIS ASP TYR PRO MET GLY HIS
SEQRES 17 B 226 GLU VAL SER LEU GLU GLU ILE HIS ASP ILE GLY ALA TRP
SEQRES 18 B 226 LEU ARG LYS ARG LEU
SEQRES 1 C 226 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER SER
SEQRES 2 C 226 GLU PRO LEU ILE LEU ASP ALA PRO ASN ALA ASP ALA CYS
SEQRES 3 C 226 ILE ILE TRP LEU HIS GLY LEU GLY ALA ASP ARG THR ASP
SEQRES 4 C 226 PHE LYS PRO VAL ALA GLU ALA LEU GLN MET VAL LEU PRO
SEQRES 5 C 226 SER THR ARG PHE ILE LEU PRO GLN ALA PRO SER GLN ALA
SEQRES 6 C 226 VAL THR VAL ASN GLY GLY TRP VAL MET PRO SER TRP TYR
SEQRES 7 C 226 ASP ILE LEU ALA PHE SER PRO ALA ARG ALA ILE ASP GLU
SEQRES 8 C 226 ASP GLN LEU ASN ALA SER ALA ASP GLN VAL ILE ALA LEU
SEQRES 9 C 226 ILE ASP GLU GLN ARG ALA LYS GLY ILE ALA ALA GLU ARG
SEQRES 10 C 226 ILE ILE LEU ALA GLY PHE SER GLN GLY GLY ALA VAL VAL
SEQRES 11 C 226 LEU HIS THR ALA PHE ARG ARG TYR ALA GLN PRO LEU GLY
SEQRES 12 C 226 GLY VAL LEU ALA LEU SER THR TYR ALA PRO THR PHE ASP
SEQRES 13 C 226 ASP LEU ALA LEU ASP GLU ARG HIS LYS ARG ILE PRO VAL
SEQRES 14 C 226 LEU HIS LEU HIS GLY SER GLN ASP ASP VAL VAL ASP PRO
SEQRES 15 C 226 ALA LEU GLY ARG ALA ALA HIS ASP ALA LEU GLN ALA GLN
SEQRES 16 C 226 GLY VAL GLU VAL GLY TRP HIS ASP TYR PRO MET GLY HIS
SEQRES 17 C 226 GLU VAL SER LEU GLU GLU ILE HIS ASP ILE GLY ALA TRP
SEQRES 18 C 226 LEU ARG LYS ARG LEU
SEQRES 1 D 226 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER SER
SEQRES 2 D 226 GLU PRO LEU ILE LEU ASP ALA PRO ASN ALA ASP ALA CYS
SEQRES 3 D 226 ILE ILE TRP LEU HIS GLY LEU GLY ALA ASP ARG THR ASP
SEQRES 4 D 226 PHE LYS PRO VAL ALA GLU ALA LEU GLN MET VAL LEU PRO
SEQRES 5 D 226 SER THR ARG PHE ILE LEU PRO GLN ALA PRO SER GLN ALA
SEQRES 6 D 226 VAL THR VAL ASN GLY GLY TRP VAL MET PRO SER TRP TYR
SEQRES 7 D 226 ASP ILE LEU ALA PHE SER PRO ALA ARG ALA ILE ASP GLU
SEQRES 8 D 226 ASP GLN LEU ASN ALA SER ALA ASP GLN VAL ILE ALA LEU
SEQRES 9 D 226 ILE ASP GLU GLN ARG ALA LYS GLY ILE ALA ALA GLU ARG
SEQRES 10 D 226 ILE ILE LEU ALA GLY PHE SER GLN GLY GLY ALA VAL VAL
SEQRES 11 D 226 LEU HIS THR ALA PHE ARG ARG TYR ALA GLN PRO LEU GLY
SEQRES 12 D 226 GLY VAL LEU ALA LEU SER THR TYR ALA PRO THR PHE ASP
SEQRES 13 D 226 ASP LEU ALA LEU ASP GLU ARG HIS LYS ARG ILE PRO VAL
SEQRES 14 D 226 LEU HIS LEU HIS GLY SER GLN ASP ASP VAL VAL ASP PRO
SEQRES 15 D 226 ALA LEU GLY ARG ALA ALA HIS ASP ALA LEU GLN ALA GLN
SEQRES 16 D 226 GLY VAL GLU VAL GLY TRP HIS ASP TYR PRO MET GLY HIS
SEQRES 17 D 226 GLU VAL SER LEU GLU GLU ILE HIS ASP ILE GLY ALA TRP
SEQRES 18 D 226 LEU ARG LYS ARG LEU
HET MES B 216 11
HET MES C 216 11
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
FORMUL 5 MES 2(C6 H13 N O4 S)
FORMUL 7 HOH *94(H2 O)
HELIX 1 1 ASP A 25 ASP A 28 5 4
HELIX 2 2 PHE A 29 LEU A 40 1 12
HELIX 3 3 THR A 56 GLY A 59 5 4
HELIX 4 4 ASP A 79 LYS A 100 1 22
HELIX 5 5 ALA A 103 GLU A 105 5 3
HELIX 6 6 SER A 113 ARG A 125 1 13
HELIX 7 7 ARG A 152 ILE A 156 5 5
HELIX 8 8 ASP A 170 ALA A 183 1 14
HELIX 9 9 SER A 200 LEU A 215 1 16
HELIX 10 10 ASP B 25 ASP B 28 5 4
HELIX 11 11 PHE B 29 LEU B 40 1 12
HELIX 12 12 THR B 56 GLY B 59 5 4
HELIX 13 13 ASP B 79 LYS B 100 1 22
HELIX 14 14 ALA B 103 GLU B 105 5 3
HELIX 15 15 SER B 113 ARG B 125 1 13
HELIX 16 16 ASP B 170 ALA B 183 1 14
HELIX 17 17 SER B 200 LEU B 215 1 16
HELIX 18 18 ASP C 25 ASP C 28 5 4
HELIX 19 19 PHE C 29 LEU C 40 1 12
HELIX 20 20 THR C 56 GLY C 59 5 4
HELIX 21 21 ASP C 79 LYS C 100 1 22
HELIX 22 22 ALA C 103 GLU C 105 5 3
HELIX 23 23 SER C 113 ARG C 125 1 13
HELIX 24 24 ARG C 152 ILE C 156 5 5
HELIX 25 25 ASP C 170 ALA C 183 1 14
HELIX 26 26 SER C 200 LEU C 215 1 16
HELIX 27 27 ASP D 25 ASP D 28 5 4
HELIX 28 28 PHE D 29 LEU D 40 1 12
HELIX 29 29 THR D 56 GLY D 59 5 4
HELIX 30 30 ASP D 79 LYS D 100 1 22
HELIX 31 31 ALA D 103 GLU D 105 5 3
HELIX 32 32 SER D 113 ARG D 125 1 13
HELIX 33 33 ARG D 152 ILE D 156 5 5
HELIX 34 34 ASP D 170 GLN D 184 1 15
HELIX 35 35 SER D 200 LEU D 215 1 16
SHEET 1 A 7 LEU A 5 LEU A 7 0
SHEET 2 A 7 THR A 43 LEU A 47 -1 O PHE A 45 N LEU A 7
SHEET 3 A 7 ALA A 14 LEU A 19 1 N ILE A 16 O ILE A 46
SHEET 4 A 7 ILE A 107 PHE A 112 1 O ALA A 110 N LEU A 19
SHEET 5 A 7 GLY A 133 LEU A 137 1 O LEU A 137 N GLY A 111
SHEET 6 A 7 VAL A 158 GLY A 163 1 O LEU A 159 N ALA A 136
SHEET 7 A 7 VAL A 188 TYR A 193 1 O GLY A 189 N HIS A 160
SHEET 1 B 2 SER A 52 ALA A 54 0
SHEET 2 B 2 VAL A 62 PRO A 64 -1 O MET A 63 N GLN A 53
SHEET 1 C 7 LEU B 5 LEU B 7 0
SHEET 2 C 7 THR B 43 LEU B 47 -1 O PHE B 45 N LEU B 7
SHEET 3 C 7 ALA B 14 LEU B 19 1 N ALA B 14 O ARG B 44
SHEET 4 C 7 ILE B 107 PHE B 112 1 O ALA B 110 N ILE B 17
SHEET 5 C 7 GLY B 133 LEU B 137 1 O LEU B 137 N GLY B 111
SHEET 6 C 7 VAL B 158 GLY B 163 1 O LEU B 159 N ALA B 136
SHEET 7 C 7 VAL B 188 TYR B 193 1 O GLY B 189 N HIS B 160
SHEET 1 D 2 SER B 52 ALA B 54 0
SHEET 2 D 2 VAL B 62 PRO B 64 -1 O MET B 63 N GLN B 53
SHEET 1 E 7 LEU C 5 LEU C 7 0
SHEET 2 E 7 THR C 43 LEU C 47 -1 O PHE C 45 N LEU C 7
SHEET 3 E 7 ALA C 14 LEU C 19 1 N ALA C 14 O ARG C 44
SHEET 4 E 7 ILE C 107 PHE C 112 1 O ALA C 110 N ILE C 17
SHEET 5 E 7 GLY C 133 LEU C 137 1 O LEU C 137 N GLY C 111
SHEET 6 E 7 VAL C 158 GLY C 163 1 O LEU C 161 N ALA C 136
SHEET 7 E 7 VAL C 188 TYR C 193 1 O GLY C 189 N HIS C 160
SHEET 1 F 2 SER C 52 ALA C 54 0
SHEET 2 F 2 VAL C 62 PRO C 64 -1 O MET C 63 N GLN C 53
SHEET 1 G 7 LEU D 5 LEU D 7 0
SHEET 2 G 7 THR D 43 LEU D 47 -1 O PHE D 45 N LEU D 7
SHEET 3 G 7 ALA D 14 LEU D 19 1 N ALA D 14 O ARG D 44
SHEET 4 G 7 ILE D 107 PHE D 112 1 O ALA D 110 N ILE D 17
SHEET 5 G 7 GLY D 133 LEU D 137 1 O LEU D 137 N GLY D 111
SHEET 6 G 7 VAL D 158 GLY D 163 1 O LEU D 161 N ALA D 136
SHEET 7 G 7 VAL D 188 TYR D 193 1 O GLY D 189 N HIS D 160
SHEET 1 H 2 SER D 52 ALA D 54 0
SHEET 2 H 2 VAL D 62 PRO D 64 -1 O MET D 63 N GLN D 53
LINK OG SER B 113 S MES B 216 1555 1555 1.42
LINK OG SER C 113 S MES C 216 1555 1555 1.42
CISPEP 1 SER A 73 PRO A 74 0 -0.09
CISPEP 2 SER B 73 PRO B 74 0 -0.06
CISPEP 3 SER C 73 PRO C 74 0 0.00
CISPEP 4 SER D 73 PRO D 74 0 0.08
SITE 1 AC1 9 GLY B 21 LEU B 22 ILE B 69 SER B 113
SITE 2 AC1 9 GLN B 114 TYR B 140 VAL B 168 HIS B 197
SITE 3 AC1 9 HOH B 237
SITE 1 AC2 11 GLY C 21 LEU C 22 TYR C 67 ILE C 69
SITE 2 AC2 11 PHE C 112 SER C 113 GLN C 114 TYR C 140
SITE 3 AC2 11 HIS C 197 HOH C 223 HOH C 239
CRYST1 65.649 50.548 142.548 90.00 92.94 90.00 P 1 21 1 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 0.015233 0.000000 0.000782 0.00000
SCALE2 0.000000 0.019783 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007024 0.00000
TER 1647 LEU A 215
TER 3294 LEU B 215
TER 4941 LEU C 215
TER 6588 LEU D 215
MASTER 404 0 2 35 36 0 6 6 6700 4 24 72
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