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HEADER HYDROLASE 29-JUN-09 3I2F
TITLE COCAINE ESTERASE WITH MUTATIONS T172R / G173Q, BOUND TO DTT ADDUCT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COCAINE ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP. MB1 'BRESLER 1999';
SOURCE 3 ORGANISM_TAXID: 104109;
SOURCE 4 STRAIN: MB1;
SOURCE 5 GENE: COCAINE ESTERASE, COCE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL-21 GOLD (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-22B (+)
KEYWDS ALPHA/BETA HYDROLASE, CYTOPLASM, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.J.G.TESMER,M.R.NANCE
REVDAT 1 16-JUN-10 3I2F 0
JRNL AUTH D.NARASIMHAN,M.R.NANCE,D.GAO,M.C.KO,J.MACDONALD,P.TAMBURI,
JRNL AUTH 2 D.YOON,D.M.LANDRY,J.H.WOODS,C.G.ZHAN,J.J.TESMER,
JRNL AUTH 3 R.K.SUNAHARA
JRNL TITL STRUCTURAL ANALYSIS OF THERMOSTABILIZING MUTATIONS OF
JRNL TITL 2 COCAINE ESTERASE.
JRNL REF PROTEIN ENG.DES.SEL. 2010
JRNL REFN ESSN 1741-0134
JRNL PMID 20436035
JRNL DOI 10.1093/PROTEIN/GZQ025
REMARK 2
REMARK 2 RESOLUTION. 2.50 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 25949
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1321
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1833
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.08
REMARK 3 BIN R VALUE (WORKING SET) : 0.2250
REMARK 3 BIN FREE R VALUE SET COUNT : 0
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4383
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 256
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.62000
REMARK 3 B22 (A**2) : -0.62000
REMARK 3 B33 (A**2) : 0.92000
REMARK 3 B12 (A**2) : -0.31000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.389
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.119
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.213
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4822 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6626 ; 1.209 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 634 ; 6.226 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 217 ;34.480 ;23.733
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 719 ;13.716 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 37 ;16.271 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 736 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3820 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2217 ; 0.202 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3279 ; 0.305 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 328 ; 0.131 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.029 ; 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): 48 ; 0.166 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.132 ; 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): 3117 ; 0.587 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4958 ; 1.024 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1941 ; 1.385 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1668 ; 2.254 ; 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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 576
REMARK 3 RESIDUE RANGE : A 584 A 596
REMARK 3 RESIDUE RANGE : A 597 A 882
REMARK 3 ORIGIN FOR THE GROUP (A): 15.8080 64.8460 -0.2540
REMARK 3 T TENSOR
REMARK 3 T11: -0.0642 T22: -0.1064
REMARK 3 T33: 0.0131 T12: 0.0211
REMARK 3 T13: 0.0101 T23: 0.0174
REMARK 3 L TENSOR
REMARK 3 L11: 1.1458 L22: 0.7353
REMARK 3 L33: 0.9694 L12: 0.2971
REMARK 3 L13: 0.2215 L23: 0.0900
REMARK 3 S TENSOR
REMARK 3 S11: 0.0110 S12: -0.1326 S13: 0.0592
REMARK 3 S21: 0.0455 S22: -0.0033 S23: 0.0696
REMARK 3 S31: 0.0425 S32: -0.0562 S33: -0.0077
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3I2F COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUL-09.
REMARK 100 THE RCSB ID CODE IS RCSB053878.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-AUG-06
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26002
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.10700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : 0.55900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE FOURIER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB: 1JU3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10MM TRIS PH 7.5, 25 MM NACL, 1.6 M
REMARK 280 AMMONIUM SULFATE, 10MM DTT, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 146.69400
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 73.34700
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 110.02050
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 36.67350
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 183.36750
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 146.69400
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 73.34700
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 36.67350
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 110.02050
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 183.36750
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: 7190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -155.0 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 0.500000 0.866025 0.000000 -53.12500
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 92.01520
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -36.67350
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 LYS A 575
REMARK 465 LEU A 576
REMARK 465 ALA A 577
REMARK 465 ALA A 578
REMARK 465 ALA A 579
REMARK 465 LEU A 580
REMARK 465 GLU A 581
REMARK 465 HIS A 582
REMARK 465 HIS A 583
REMARK 465 HIS A 584
REMARK 465 HIS A 585
REMARK 465 HIS A 586
REMARK 465 HIS A 587
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 ASP A 32 -78.43 -44.18
REMARK 500 ASP A 45 101.95 73.15
REMARK 500 SER A 56 -91.27 -119.14
REMARK 500 PHE A 78 -114.72 54.44
REMARK 500 HIS A 87 -42.81 72.10
REMARK 500 SER A 117 -115.51 63.62
REMARK 500 MET A 141 56.59 38.62
REMARK 500 TYR A 152 -116.02 -117.30
REMARK 500 SER A 179 -73.03 -56.82
REMARK 500 ASP A 198 70.33 -154.62
REMARK 500 HIS A 228 74.50 -114.23
REMARK 500 PRO A 284 33.00 -85.20
REMARK 500 ASP A 355 9.87 82.85
REMARK 500 THR A 371 169.35 71.15
REMARK 500 ASN A 413 54.44 -149.69
REMARK 500 LEU A 508 -125.25 62.67
REMARK 500 ASN A 528 78.57 -164.77
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 CL A 588
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 589
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 590
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 591
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DBC A 592
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 593
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 594
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 595
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 596
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 597
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 598
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 599
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 600
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JU3 RELATED DB: PDB
REMARK 900 WILD-TYPE PROTEIN, IN COMPLEX WITH TRANSITION STATE ANALOG.
REMARK 900 RELATED ID: 1JU4 RELATED DB: PDB
REMARK 900 WILD-TYPE PROTEIN, IN COMPLEX WITH PRODUCT.
REMARK 900 RELATED ID: 1L7R RELATED DB: PDB
REMARK 900 COCAINE ESTERASE, WITH MUTATION Y44F.
REMARK 900 RELATED ID: 1L7Q RELATED DB: PDB
REMARK 900 COCAINE ESTERASE, WITH MUTATION S117A.
REMARK 900 RELATED ID: 3I2G RELATED DB: PDB
REMARK 900 RELATED ID: 3I2H RELATED DB: PDB
REMARK 900 RELATED ID: 3I2I RELATED DB: PDB
REMARK 900 RELATED ID: 3I2J RELATED DB: PDB
REMARK 900 RELATED ID: 3I2K RELATED DB: PDB
DBREF 3I2F A 1 574 UNP Q9L9D7 COCE_RHOSM 1 574
SEQADV 3I2F ARG A 172 UNP Q9L9D7 THR 172 ENGINEERED
SEQADV 3I2F GLN A 173 UNP Q9L9D7 GLY 173 ENGINEERED
SEQADV 3I2F LYS A 575 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3I2F LEU A 576 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3I2F ALA A 577 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3I2F ALA A 578 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3I2F ALA A 579 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3I2F LEU A 580 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3I2F GLU A 581 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3I2F HIS A 582 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3I2F HIS A 583 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3I2F HIS A 584 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3I2F HIS A 585 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3I2F HIS A 586 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3I2F HIS A 587 UNP Q9L9D7 EXPRESSION TAG
SEQRES 1 A 587 MET VAL ASP GLY ASN TYR SER VAL ALA SER ASN VAL MET
SEQRES 2 A 587 VAL PRO MET ARG ASP GLY VAL ARG LEU ALA VAL ASP LEU
SEQRES 3 A 587 TYR ARG PRO ASP ALA ASP GLY PRO VAL PRO VAL LEU LEU
SEQRES 4 A 587 VAL ARG ASN PRO TYR ASP LYS PHE ASP VAL PHE ALA TRP
SEQRES 5 A 587 SER THR GLN SER THR ASN TRP LEU GLU PHE VAL ARG ASP
SEQRES 6 A 587 GLY TYR ALA VAL VAL ILE GLN ASP THR ARG GLY LEU PHE
SEQRES 7 A 587 ALA SER GLU GLY GLU PHE VAL PRO HIS VAL ASP ASP GLU
SEQRES 8 A 587 ALA ASP ALA GLU ASP THR LEU SER TRP ILE LEU GLU GLN
SEQRES 9 A 587 ALA TRP CYS ASP GLY ASN VAL GLY MET PHE GLY VAL SER
SEQRES 10 A 587 TYR LEU GLY VAL THR GLN TRP GLN ALA ALA VAL SER GLY
SEQRES 11 A 587 VAL GLY GLY LEU LYS ALA ILE ALA PRO SER MET ALA SER
SEQRES 12 A 587 ALA ASP LEU TYR ARG ALA PRO TRP TYR GLY PRO GLY GLY
SEQRES 13 A 587 ALA LEU SER VAL GLU ALA LEU LEU GLY TRP SER ALA LEU
SEQRES 14 A 587 ILE GLY ARG GLN LEU ILE THR SER ARG SER ASP ALA ARG
SEQRES 15 A 587 PRO GLU ASP ALA ALA ASP PHE VAL GLN LEU ALA ALA ILE
SEQRES 16 A 587 LEU ASN ASP VAL ALA GLY ALA ALA SER VAL THR PRO LEU
SEQRES 17 A 587 ALA GLU GLN PRO LEU LEU GLY ARG LEU ILE PRO TRP VAL
SEQRES 18 A 587 ILE ASP GLN VAL VAL ASP HIS PRO ASP ASN ASP GLU SER
SEQRES 19 A 587 TRP GLN SER ILE SER LEU PHE GLU ARG LEU GLY GLY LEU
SEQRES 20 A 587 ALA THR PRO ALA LEU ILE THR ALA GLY TRP TYR ASP GLY
SEQRES 21 A 587 PHE VAL GLY GLU SER LEU ARG THR PHE VAL ALA VAL LYS
SEQRES 22 A 587 ASP ASN ALA ASP ALA ARG LEU VAL VAL GLY PRO TRP SER
SEQRES 23 A 587 HIS SER ASN LEU THR GLY ARG ASN ALA ASP ARG LYS PHE
SEQRES 24 A 587 GLY ILE ALA ALA THR TYR PRO ILE GLN GLU ALA THR THR
SEQRES 25 A 587 MET HIS LYS ALA PHE PHE ASP ARG HIS LEU ARG GLY GLU
SEQRES 26 A 587 THR ASP ALA LEU ALA GLY VAL PRO LYS VAL ARG LEU PHE
SEQRES 27 A 587 VAL MET GLY ILE ASP GLU TRP ARG ASP GLU THR ASP TRP
SEQRES 28 A 587 PRO LEU PRO ASP THR ALA TYR THR PRO PHE TYR LEU GLY
SEQRES 29 A 587 GLY SER GLY ALA ALA ASN THR SER THR GLY GLY GLY THR
SEQRES 30 A 587 LEU SER THR SER ILE SER GLY THR GLU SER ALA ASP THR
SEQRES 31 A 587 TYR LEU TYR ASP PRO ALA ASP PRO VAL PRO SER LEU GLY
SEQRES 32 A 587 GLY THR LEU LEU PHE HIS ASN GLY ASP ASN GLY PRO ALA
SEQRES 33 A 587 ASP GLN ARG PRO ILE HIS ASP ARG ASP ASP VAL LEU CYS
SEQRES 34 A 587 TYR SER THR GLU VAL LEU THR ASP PRO VAL GLU VAL THR
SEQRES 35 A 587 GLY THR VAL SER ALA ARG LEU PHE VAL SER SER SER ALA
SEQRES 36 A 587 VAL ASP THR ASP PHE THR ALA LYS LEU VAL ASP VAL PHE
SEQRES 37 A 587 PRO ASP GLY ARG ALA ILE ALA LEU CYS ASP GLY ILE VAL
SEQRES 38 A 587 ARG MET ARG TYR ARG GLU THR LEU VAL ASN PRO THR LEU
SEQRES 39 A 587 ILE GLU ALA GLY GLU ILE TYR GLU VAL ALA ILE ASP MET
SEQRES 40 A 587 LEU ALA THR SER ASN VAL PHE LEU PRO GLY HIS ARG ILE
SEQRES 41 A 587 MET VAL GLN VAL SER SER SER ASN PHE PRO LYS TYR ASP
SEQRES 42 A 587 ARG ASN SER ASN THR GLY GLY VAL ILE ALA ARG GLU GLN
SEQRES 43 A 587 LEU GLU GLU MET CYS THR ALA VAL ASN ARG ILE HIS ARG
SEQRES 44 A 587 GLY PRO GLU HIS PRO SER HIS ILE VAL LEU PRO ILE ILE
SEQRES 45 A 587 LYS ARG LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS
SEQRES 46 A 587 HIS HIS
HET CL A 588 1
HET CL A 589 1
HET CL A 590 1
HET CL A 591 1
HET DBC A 592 10
HET GOL A 593 6
HET GOL A 594 6
HET GOL A 595 6
HET SO4 A 596 5
HET CL A 597 1
HET CL A 598 1
HET CL A 599 1
HET CL A 600 1
HETNAM CL CHLORIDE ION
HETNAM DBC (4S,5S)-4,5-BIS(MERCAPTOMETHYL)-1,3-DIOXOLAN-2-OL
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
FORMUL 2 CL 8(CL 1-)
FORMUL 6 DBC C5 H10 O3 S2
FORMUL 7 GOL 3(C3 H8 O3)
FORMUL 10 SO4 O4 S 2-
FORMUL 15 HOH *256(H2 O)
HELIX 1 1 VAL A 49 THR A 54 1 6
HELIX 2 2 TRP A 59 ASP A 65 1 7
HELIX 3 3 ASP A 89 GLU A 103 1 15
HELIX 4 4 SER A 117 VAL A 128 1 12
HELIX 5 5 SER A 159 SER A 177 1 19
HELIX 6 6 GLU A 184 ASP A 198 1 15
HELIX 7 7 ASP A 198 VAL A 205 1 8
HELIX 8 8 GLN A 211 ILE A 218 1 8
HELIX 9 9 PRO A 219 GLN A 224 1 6
HELIX 10 10 ASP A 232 SER A 237 1 6
HELIX 11 11 LEU A 240 GLY A 245 5 6
HELIX 12 12 PHE A 261 LYS A 273 1 13
HELIX 13 13 GLY A 300 THR A 304 5 5
HELIX 14 14 PRO A 306 ARG A 323 1 18
HELIX 15 15 GLN A 418 HIS A 422 5 5
HELIX 16 16 ARG A 484 ARG A 486 5 3
HELIX 17 17 VAL A 541 GLU A 545 5 5
HELIX 18 18 GLN A 546 MET A 550 5 5
SHEET 1 A 6 TYR A 6 PRO A 15 0
SHEET 2 A 6 ARG A 21 PRO A 29 -1 O LEU A 22 N VAL A 14
SHEET 3 A 6 ALA A 68 ASP A 73 -1 O VAL A 69 N TYR A 27
SHEET 4 A 6 VAL A 35 ASN A 42 1 N LEU A 38 O VAL A 70
SHEET 5 A 6 CYS A 107 MET A 113 1 O GLY A 112 N VAL A 37
SHEET 6 A 6 LEU A 134 ALA A 136 1 O LYS A 135 N VAL A 111
SHEET 1 B 2 GLY A 115 VAL A 116 0
SHEET 2 B 2 PRO A 139 SER A 140 1 O SER A 140 N GLY A 115
SHEET 1 C 4 ALA A 251 TYR A 258 0
SHEET 2 C 4 ALA A 278 SER A 286 1 O ARG A 279 N ILE A 253
SHEET 3 C 4 VAL A 335 VAL A 339 1 O PHE A 338 N VAL A 282
SHEET 4 C 4 GLU A 344 GLU A 348 -1 O GLU A 344 N VAL A 339
SHEET 1 D 2 ARG A 293 ASN A 294 0
SHEET 2 D 2 ARG A 297 LYS A 298 -1 O ARG A 297 N ASN A 294
SHEET 1 E 6 THR A 377 SER A 379 0
SHEET 2 E 6 ALA A 357 GLY A 364 -1 N TYR A 362 O SER A 379
SHEET 3 E 6 HIS A 566 ILE A 572 -1 O LEU A 569 N THR A 359
SHEET 4 E 6 VAL A 439 SER A 453 -1 N SER A 446 O VAL A 568
SHEET 5 E 6 ALA A 553 ARG A 559 -1 O HIS A 558 N PHE A 450
SHEET 6 E 6 SER A 387 TYR A 393 -1 N TYR A 393 O ALA A 553
SHEET 1 F 5 THR A 377 SER A 379 0
SHEET 2 F 5 ALA A 357 GLY A 364 -1 N TYR A 362 O SER A 379
SHEET 3 F 5 HIS A 566 ILE A 572 -1 O LEU A 569 N THR A 359
SHEET 4 F 5 VAL A 439 SER A 453 -1 N SER A 446 O VAL A 568
SHEET 5 F 5 TYR A 501 PHE A 514 -1 O TYR A 501 N VAL A 451
SHEET 1 G 4 CYS A 429 SER A 431 0
SHEET 2 G 4 ARG A 519 SER A 525 -1 O VAL A 522 N TYR A 430
SHEET 3 G 4 ASP A 459 VAL A 467 -1 N THR A 461 O SER A 525
SHEET 4 G 4 ALA A 473 ARG A 482 -1 O CYS A 477 N LEU A 464
LINK OG SER A 117 C5 DBC A 592 1555 1555 1.57
CISPEP 1 ALA A 149 PRO A 150 0 3.73
CISPEP 2 THR A 206 PRO A 207 0 2.01
CISPEP 3 TRP A 351 PRO A 352 0 -4.44
CISPEP 4 PHE A 529 PRO A 530 0 5.32
SITE 1 AC1 3 LYS A 298 ARG A 472 GLU A 549
SITE 1 AC2 3 ARG A 75 GLY A 82 GLU A 83
SITE 1 AC3 2 PRO A 354 ASP A 355
SITE 1 AC4 1 TRP A 345
SITE 1 AC5 7 TYR A 44 SER A 117 TYR A 118 HIS A 287
SITE 2 AC5 7 PHE A 408 HOH A 662 HOH A 776
SITE 1 AC6 8 LEU A 196 ASN A 197 ASP A 198 VAL A 199
SITE 2 AC6 8 ARG A 293 PHE A 408 HIS A 409 ASN A 410
SITE 1 AC7 5 ASP A 394 ALA A 396 LEU A 547 MET A 550
SITE 2 AC7 5 THR A 552
SITE 1 AC8 4 PRO A 306 GLU A 309 ARG A 336 HOH A 769
SITE 1 AC9 5 GLY A 364 GLY A 365 SER A 383 GLY A 384
SITE 2 AC9 5 THR A 385
SITE 1 BC1 1 ARG A 556
SITE 1 BC2 1 HIS A 563
SITE 1 BC3 2 ARG A 28 HOH A 839
SITE 1 BC4 2 ARG A 519 HOH A 806
CRYST1 106.250 106.250 220.041 90.00 90.00 120.00 P 65 2 2 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009412 0.005434 0.000000 0.00000
SCALE2 0.000000 0.010868 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004545 0.00000
TER 4657 ARG A 574
MASTER 412 0 13 18 29 0 17 6 4680 1 34 46
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