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HEADER HYDROLASE 18-JUN-09 2WKW
TITLE ALCALIGENES ESTERASE COMPLEXED WITH PRODUCT ANALOGUE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ESTERASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ALCALIGENES SP.;
SOURCE 3 ORGANISM_TAXID: 512;
SOURCE 4 EXPRESSION_SYSTEM: AGROBACTERIUM SP.;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 361
KEYWDS HYDROLASE, HYDROLASE(CARBOXYLIC ESTERASE), ESTERASE, ATOMIC
KEYWDS 2 RESOLUTION, ALPHA/BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.C.BOURNE,M.N.ISUPOV,J.A.LITTLECHILD
REVDAT 1 30-JUN-09 2WKW 0
JRNL AUTH P.C.BOURNE,M.N.ISUPOV,J.A.LITTLECHILD
JRNL TITL ALCALIGENES ESTERASE COMPLEXED WITH PRODUCT
JRNL TITL 2 ANALOGUE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.C.BOURNE,M.N.ISUPOV,J.A.LITTLECHILD
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION
REMARK 1 TITL 2 STUDIES OF A NOVEL BACTERIAL ESTERASE
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 55 915 1999
REMARK 1 REFN ISSN 0907-4449
REMARK 1 PMID 10089333
REMARK 1 DOI 10.1107/S0907444998018459
REMARK 1
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.C.BOURNE,M.N.ISUPOV,J.A.LITTLECHILD
REMARK 1 TITL THE ATOMIC-RESOLUTION STRUCTURE OF A NOVEL
REMARK 1 TITL 2 BACTERIAL ESTERASE.
REMARK 1 REF STRUCTURE V. 8 143 2000
REMARK 1 REFN ISSN 0969-2126
REMARK 1 PMID 10673440
REMARK 1 DOI 10.1016/S0969-2126(00)00090-3
REMARK 2
REMARK 2 RESOLUTION. 2.03 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0088
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) : 2.03
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.00
REMARK 3 NUMBER OF REFLECTIONS : 54468
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) : 0.15700
REMARK 3 R VALUE (WORKING SET) : 0.15498
REMARK 3 FREE R VALUE : 0.19430
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 2910
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) : 2.030
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.082
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3942
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.184
REMARK 3 BIN FREE R VALUE SET COUNT : 211
REMARK 3 BIN FREE R VALUE : 0.233
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4932
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 111
REMARK 3 SOLVENT ATOMS : 700
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.0
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.412
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.10
REMARK 3 B22 (A**2) : -2.37
REMARK 3 B33 (A**2) : -1.73
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): 0.137
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.130
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.085
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.060
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5188 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7094 ; 1.242 ; 1.978
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 666 ; 5.700 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 212 ;35.912 ;23.679
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 812 ;12.613 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;11.668 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 768 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3967 ; 0.006 ; 0.022
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 3199 ; 2.021 ; 4.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5185 ; 2.960 ; 6.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1989 ; 4.470 ; 8.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1890 ; 5.424 ;10.000
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 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 : BABINET MODEL WITH 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 3 THE CRYSTALS WERE SOAKED WITH THE PRODUCT ANALOGUE
REMARK 3 IODINATED AT THE PHENOL RING. HOWEVER NO TRACE OF
REMARK 3 IODINATION WAS OBSERVED IN THE STRUCTURE
REMARK 4
REMARK 4 2WKW COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-JUN-09.
REMARK 100 THE PDBE ID CODE IS EBI-40158.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUL-98
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9076
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57445
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.03
REMARK 200 RESOLUTION RANGE LOW (A) : 20.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.3
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.80
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.03
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.2
REMARK 200 R MERGE FOR SHELL (I) : 0.25
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.80
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 1QLW
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% (NH4)2SO4, 10 MM TRIS HCL,
REMARK 280 PH 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 28.79859
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.57200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.90559
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.57200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.79858
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 57.90550
REMARK 290 SMTRY3 4 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 GENERATING THE BIOMOLECULE
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: 8390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -120.35 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 ALA A 1
REMARK 465 PRO A 2
REMARK 465 PRO A 3
REMARK 465 PRO A 4
REMARK 465 VAL A 5
REMARK 465 PRO A 6
REMARK 465 LYS A 7
REMARK 465 LYS A 323
REMARK 465 PRO A 324
REMARK 465 ALA A 325
REMARK 465 HIS A 326
REMARK 465 GLY A 327
REMARK 465 ARG A 328
REMARK 465 ALA B 1
REMARK 465 PRO B 2
REMARK 465 PRO B 3
REMARK 465 PRO B 4
REMARK 465 VAL B 5
REMARK 465 PRO B 6
REMARK 465 LYS B 7
REMARK 465 LYS B 323
REMARK 465 PRO B 324
REMARK 465 ALA B 325
REMARK 465 HIS B 326
REMARK 465 GLY B 327
REMARK 465 ARG B 328
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 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 ASP A 48 -8.36 80.60
REMARK 500 THR A 74 -166.72 -128.99
REMARK 500 GLU A 79 -153.61 -89.85
REMARK 500 PRO A 152 40.25 -107.26
REMARK 500 SER A 206 -112.04 61.04
REMARK 500 GLU A 230 58.98 38.63
REMARK 500 MET A 299 51.63 -95.94
REMARK 500 PRO B 9 104.10 -58.55
REMARK 500 ASP B 48 -5.99 79.04
REMARK 500 GLU B 79 -155.88 -86.67
REMARK 500 ALA B 125 149.84 -174.45
REMARK 500 SER B 206 -114.96 60.93
REMARK 500 ASN B 219 117.47 -162.54
REMARK 500 GLU B 230 60.95 37.38
REMARK 500 MET B 299 51.60 -90.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ILE A 102 ASP A 103 148.85
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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1323
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1323
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE W22 A 577
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE W22 B 577
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1324
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1325
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1324
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1325
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1326
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1326
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1327
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1327
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1328
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1329
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1328
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1330
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QLW RELATED DB: PDB
REMARK 900 THE ATOMIC RESOLUTION STRUCTURE OF A NOVEL
REMARK 900 BACTERIAL ESTERASE
DBREF 2WKW A 1 328 UNP Q7SIA5 Q7SIA5_ALCSP 1 328
DBREF 2WKW B 1 328 UNP Q7SIA5 Q7SIA5_ALCSP 1 328
SEQRES 1 A 328 ALA PRO PRO PRO VAL PRO LYS THR PRO ALA GLY PRO LEU
SEQRES 2 A 328 THR LEU SER GLY GLN GLY SER PHE PHE VAL GLY GLY ARG
SEQRES 3 A 328 ASP VAL THR SER GLU THR LEU SER LEU SER PRO LYS TYR
SEQRES 4 A 328 ASP ALA HIS GLY THR VAL THR VAL ASP GLN MET TYR VAL
SEQRES 5 A 328 ARG TYR GLN ILE PRO GLN ARG ALA LYS ARG TYR PRO ILE
SEQRES 6 A 328 THR LEU ILE HIS GLY CYS CYS LEU THR GLY MET THR TRP
SEQRES 7 A 328 GLU THR THR PRO ASP GLY ARG MET GLY TRP ASP GLU TYR
SEQRES 8 A 328 PHE LEU ARG LYS GLY TYR SER THR TYR VAL ILE ASP GLN
SEQRES 9 A 328 SER GLY ARG GLY ARG SER ALA THR ASP ILE SER ALA ILE
SEQRES 10 A 328 ASN ALA VAL LYS LEU GLY LYS ALA PRO ALA SER SER LEU
SEQRES 11 A 328 PRO ASP LEU PHE ALA ALA GLY HIS GLU ALA ALA TRP ALA
SEQRES 12 A 328 ILE PHE ARG PHE GLY PRO ARG TYR PRO ASP ALA PHE LYS
SEQRES 13 A 328 ASP THR GLN PHE PRO VAL GLN ALA GLN ALA GLU LEU TRP
SEQRES 14 A 328 GLN GLN MET VAL PRO ASP TRP LEU GLY SER MET PRO THR
SEQRES 15 A 328 PRO ASN PRO THR VAL ALA ASN LEU SER LYS LEU ALA ILE
SEQRES 16 A 328 LYS LEU ASP GLY THR VAL LEU LEU SER HIS SER GLN SER
SEQRES 17 A 328 GLY ILE TYR PRO PHE GLN THR ALA ALA MET ASN PRO LYS
SEQRES 18 A 328 GLY ILE THR ALA ILE VAL SER VAL GLU PRO GLY GLU CYS
SEQRES 19 A 328 PRO LYS PRO GLU ASP VAL LYS PRO LEU THR SER ILE PRO
SEQRES 20 A 328 VAL LEU VAL VAL PHE GLY ASP HIS ILE GLU GLU PHE PRO
SEQRES 21 A 328 ARG TRP ALA PRO ARG LEU LYS ALA CYS HIS ALA PHE ILE
SEQRES 22 A 328 ASP ALA LEU ASN ALA ALA GLY GLY LYS GLY GLN LEU MET
SEQRES 23 A 328 SER LEU PRO ALA LEU GLY VAL HIS GLY ASN SER HIS MET
SEQRES 24 A 328 MET MET GLN ASP ARG ASN ASN LEU GLN VAL ALA ASP LEU
SEQRES 25 A 328 ILE LEU ASP TRP ILE GLY ARG ASN THR ALA LYS PRO ALA
SEQRES 26 A 328 HIS GLY ARG
SEQRES 1 B 328 ALA PRO PRO PRO VAL PRO LYS THR PRO ALA GLY PRO LEU
SEQRES 2 B 328 THR LEU SER GLY GLN GLY SER PHE PHE VAL GLY GLY ARG
SEQRES 3 B 328 ASP VAL THR SER GLU THR LEU SER LEU SER PRO LYS TYR
SEQRES 4 B 328 ASP ALA HIS GLY THR VAL THR VAL ASP GLN MET TYR VAL
SEQRES 5 B 328 ARG TYR GLN ILE PRO GLN ARG ALA LYS ARG TYR PRO ILE
SEQRES 6 B 328 THR LEU ILE HIS GLY CYS CYS LEU THR GLY MET THR TRP
SEQRES 7 B 328 GLU THR THR PRO ASP GLY ARG MET GLY TRP ASP GLU TYR
SEQRES 8 B 328 PHE LEU ARG LYS GLY TYR SER THR TYR VAL ILE ASP GLN
SEQRES 9 B 328 SER GLY ARG GLY ARG SER ALA THR ASP ILE SER ALA ILE
SEQRES 10 B 328 ASN ALA VAL LYS LEU GLY LYS ALA PRO ALA SER SER LEU
SEQRES 11 B 328 PRO ASP LEU PHE ALA ALA GLY HIS GLU ALA ALA TRP ALA
SEQRES 12 B 328 ILE PHE ARG PHE GLY PRO ARG TYR PRO ASP ALA PHE LYS
SEQRES 13 B 328 ASP THR GLN PHE PRO VAL GLN ALA GLN ALA GLU LEU TRP
SEQRES 14 B 328 GLN GLN MET VAL PRO ASP TRP LEU GLY SER MET PRO THR
SEQRES 15 B 328 PRO ASN PRO THR VAL ALA ASN LEU SER LYS LEU ALA ILE
SEQRES 16 B 328 LYS LEU ASP GLY THR VAL LEU LEU SER HIS SER GLN SER
SEQRES 17 B 328 GLY ILE TYR PRO PHE GLN THR ALA ALA MET ASN PRO LYS
SEQRES 18 B 328 GLY ILE THR ALA ILE VAL SER VAL GLU PRO GLY GLU CYS
SEQRES 19 B 328 PRO LYS PRO GLU ASP VAL LYS PRO LEU THR SER ILE PRO
SEQRES 20 B 328 VAL LEU VAL VAL PHE GLY ASP HIS ILE GLU GLU PHE PRO
SEQRES 21 B 328 ARG TRP ALA PRO ARG LEU LYS ALA CYS HIS ALA PHE ILE
SEQRES 22 B 328 ASP ALA LEU ASN ALA ALA GLY GLY LYS GLY GLN LEU MET
SEQRES 23 B 328 SER LEU PRO ALA LEU GLY VAL HIS GLY ASN SER HIS MET
SEQRES 24 B 328 MET MET GLN ASP ARG ASN ASN LEU GLN VAL ALA ASP LEU
SEQRES 25 B 328 ILE LEU ASP TRP ILE GLY ARG ASN THR ALA LYS PRO ALA
SEQRES 26 B 328 HIS GLY ARG
HET SO4 B1323 5
HET SO4 A1323 5
HET W22 A 577 17
HET W22 B 577 17
HET GOL B1324 6
HET GOL B1325 6
HET SO4 A1324 5
HET GOL A1325 6
HET SO4 B1326 5
HET GOL A1326 6
HET GOL A1327 6
HET GOL B1327 6
HET SO4 A1328 5
HET SO4 A1329 5
HET SO4 B1328 5
HET GOL A1330 6
HETNAM SO4 SULFATE ION
HETNAM W22 [(2S)-4-METHYL-3-OXO-2,3,4,5-TETRAHYDRO-1H-1,
HETNAM 2 W22 4-BENZODIAZEPIN-2-YL]ACETIC ACID
HETNAM GOL GLYCEROL
FORMUL 3 SO4 7(O4 S 2-)
FORMUL 4 W22 2(C12 H14 N2 O3)
FORMUL 5 GOL 7(C3 H8 O3)
FORMUL 6 HOH *700(H2 O1)
HELIX 1 1 THR A 74 GLU A 79 5 6
HELIX 2 2 GLY A 87 LYS A 95 1 9
HELIX 3 3 ILE A 114 LEU A 122 1 9
HELIX 4 4 PRO A 126 LEU A 130 5 5
HELIX 5 5 GLY A 137 PHE A 145 1 9
HELIX 6 6 PRO A 161 GLN A 163 5 3
HELIX 7 7 ALA A 164 MET A 172 1 9
HELIX 8 8 TRP A 176 MET A 180 5 5
HELIX 9 9 ASN A 184 ASP A 198 1 15
HELIX 10 10 GLN A 207 GLY A 209 5 3
HELIX 11 11 ILE A 210 ASN A 219 1 10
HELIX 12 12 LYS A 236 VAL A 240 5 5
HELIX 13 13 VAL A 240 THR A 244 5 5
HELIX 14 14 TRP A 262 ALA A 279 1 18
HELIX 15 15 PRO A 289 GLY A 292 5 4
HELIX 16 16 MET A 299 ASP A 303 5 5
HELIX 17 17 ASN A 305 ALA A 322 1 18
HELIX 18 18 THR B 74 GLU B 79 5 6
HELIX 19 19 GLY B 87 LYS B 95 1 9
HELIX 20 20 ILE B 114 GLY B 123 1 10
HELIX 21 21 PRO B 126 LEU B 130 5 5
HELIX 22 22 GLY B 137 PHE B 145 1 9
HELIX 23 23 PRO B 161 GLN B 163 5 3
HELIX 24 24 ALA B 164 GLN B 171 1 8
HELIX 25 25 TRP B 176 MET B 180 5 5
HELIX 26 26 ASN B 184 ASP B 198 1 15
HELIX 27 27 GLN B 207 GLY B 209 5 3
HELIX 28 28 ILE B 210 ASN B 219 1 10
HELIX 29 29 LYS B 236 VAL B 240 5 5
HELIX 30 30 VAL B 240 THR B 244 5 5
HELIX 31 31 TRP B 262 ALA B 279 1 18
HELIX 32 32 PRO B 289 GLY B 292 5 4
HELIX 33 33 MET B 299 ASP B 303 5 5
HELIX 34 34 ASN B 305 THR B 321 1 17
SHEET 1 AA16 GLY A 283 SER A 287 0
SHEET 2 AA16 VAL A 248 PHE A 252 1 O VAL A 248 N GLN A 284
SHEET 3 AA16 ILE A 223 VAL A 229 1 O ILE A 226 N LEU A 249
SHEET 4 AA16 THR A 200 HIS A 205 1 O THR A 200 N THR A 224
SHEET 5 AA16 ILE A 65 ILE A 68 1 O THR A 66 N LEU A 203
SHEET 6 AA16 THR A 99 ASP A 103 1 O TYR A 100 N LEU A 67
SHEET 7 AA16 MET A 50 PRO A 57 -1 O TYR A 51 N ASP A 103
SHEET 8 AA16 LEU A 13 VAL A 23 -1 N SER A 16 O ILE A 56
SHEET 9 AA16 LEU B 13 VAL B 23 -1 O LEU B 13 N LEU A 15
SHEET 10 AA16 MET B 50 PRO B 57 -1 O MET B 50 N VAL B 23
SHEET 11 AA16 THR B 99 ASP B 103 -1 O THR B 99 N GLN B 55
SHEET 12 AA16 ILE B 65 ILE B 68 1 O ILE B 65 N TYR B 100
SHEET 13 AA16 THR B 200 HIS B 205 1 O VAL B 201 N THR B 66
SHEET 14 AA16 ILE B 223 VAL B 229 1 N THR B 224 O THR B 200
SHEET 15 AA16 VAL B 248 PHE B 252 1 O LEU B 249 N SER B 228
SHEET 16 AA16 GLY B 283 SER B 287 1 O GLN B 284 N VAL B 250
SHEET 1 AB 2 ARG A 26 SER A 30 0
SHEET 2 AB 2 GLY A 43 VAL A 47 -1 O GLY A 43 N SER A 30
SHEET 1 BA 2 ARG B 26 SER B 30 0
SHEET 2 BA 2 GLY B 43 VAL B 47 -1 O GLY B 43 N SER B 30
SSBOND 1 CYS A 71 CYS A 72 1555 1555 2.05
SSBOND 2 CYS A 234 CYS A 269 1555 1555 2.02
SSBOND 3 CYS B 71 CYS B 72 1555 1555 2.06
SSBOND 4 CYS B 234 CYS B 269 1555 1555 2.05
CISPEP 1 TYR A 151 PRO A 152 0 -1.49
CISPEP 2 THR A 182 PRO A 183 0 -1.10
CISPEP 3 TYR B 151 PRO B 152 0 -3.35
CISPEP 4 THR B 182 PRO B 183 0 -0.10
SITE 1 AC1 5 SER B 16 GLN B 58 ARG B 59 HOH B2077
SITE 2 AC1 5 HOH B2330
SITE 1 AC2 4 SER A 16 ARG A 59 HOH A2352 HOH A2353
SITE 1 AC3 10 CYS A 71 ALA A 136 ILE A 144 PHE A 145
SITE 2 AC3 10 SER A 206 GLN A 207 ARG A 261 ARG A 265
SITE 3 AC3 10 HIS A 298 HOH A2351
SITE 1 AC4 10 CYS B 71 ALA B 136 ILE B 144 PHE B 145
SITE 2 AC4 10 SER B 206 GLN B 207 ARG B 261 ARG B 265
SITE 3 AC4 10 HIS B 298 HOH B2328
SITE 1 AC5 6 ASP B 254 HIS B 255 ILE B 256 GLU B 257
SITE 2 AC5 6 GLU B 258 HOH B2331
SITE 1 AC6 4 PHE B 155 LYS B 156 ASP B 157 HIS B 255
SITE 1 AC7 5 TYR A 54 HOH A2354 HOH A2356 THR B 80
SITE 2 AC7 5 GLY B 84
SITE 1 AC8 8 ASP A 254 HIS A 255 ILE A 256 GLU A 257
SITE 2 AC8 8 GLU A 258 HOH A2357 HOH A2358 HOH A2359
SITE 1 AC9 4 THR A 80 GLY A 84 TYR B 54 HOH B2333
SITE 1 BC1 5 PRO A 82 ASP A 83 GLU A 167 HOH A2360
SITE 2 BC1 5 HOH B2333
SITE 1 BC2 6 THR A 80 GLU A 90 HOH A2123 HOH A2125
SITE 2 BC2 6 GLN B 18 GLY B 19
SITE 1 BC3 7 GLN A 18 GLY A 19 HOH A2011 THR B 80
SITE 2 BC3 7 GLU B 90 HOH B2126 HOH B2335
SITE 1 BC4 10 ILE A 210 PHE A 213 GLN A 214 PRO A 235
SITE 2 BC4 10 ASP A 239 HOH A2264 HOH A2284 HOH A2361
SITE 3 BC4 10 PRO B 126 SER B 128
SITE 1 BC5 7 ARG A 319 HOH A2362 HOH A2363 GLN B 284
SITE 2 BC5 7 LEU B 285 HOH B2286 HOH B2288
SITE 1 BC6 8 ILE A 273 GLN A 284 LEU A 285 HOH A2312
SITE 2 BC6 8 HOH A2316 ARG B 319 HOH B2336 HOH B2337
SITE 1 BC7 5 GLY A 123 ALA A 125 PRO A 126 GLN A 163
SITE 2 BC7 5 GLN A 165
CRYST1 57.597 115.811 131.144 90.00 90.00 90.00 P 21 21 21 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 0.017362 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008635 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007625 0.00000
MTRIX1 1 -0.972180 -0.010390 -0.234000 8.01847 1
MTRIX2 1 0.003150 -0.999500 0.031310 73.07857 1
MTRIX3 1 -0.234210 0.029700 0.971730 -0.18449 1
TER 2465 ALA A 322
TER 4934 ALA B 322
MASTER 411 0 16 34 20 0 32 9 5743 2 119 52
END |