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HEADER HYDROLASE 20-JUL-09 3IDA
TITLE THERMOSTABLE COCAINE ESTERASE WITH MUTATIONS L169K AND
TITLE 2 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;
SOURCE 3 ORGANISM_TAXID: 51612;
SOURCE 4 STRAIN: MB1;
SOURCE 5 GENE: COCE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL-21 GOLD;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-22 (B) +
KEYWDS ALPHA/BETA HYDROLASE, ESTERASE, CYTOPLASM, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.J.G.TESMER,M.R.NANCE
REVDAT 1 02-MAR-10 3IDA 0
JRNL AUTH R.L.BRIM,M.R.NANCE,D.W.YOUNGSTROM,D.NARASIMHAN,
JRNL AUTH 2 C.G.ZHAN,J.J.TESMER,R.K.SUNAHARA,J.H.WOODS
JRNL TITL A THERMALLY STABLE FORM OF BACTERIAL COCAINE
JRNL TITL 2 ESTERASE: A POTENTIAL THERAPEUTIC AGENT FOR
JRNL TITL 3 TREATMENT OF COCAINE ABUSE.
JRNL REF MOL.PHARMACOL. 2010
JRNL REFN ESSN 1521-0111
JRNL PMID 20086035
JRNL DOI 10.1124/MOL.109.060806
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.59
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 102995
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.195
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 6117
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7431
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.36
REMARK 3 BIN R VALUE (WORKING SET) : 0.2240
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 : 4799
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 67
REMARK 3 SOLVENT ATOMS : 694
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.58000
REMARK 3 B22 (A**2) : 0.58000
REMARK 3 B33 (A**2) : -0.87000
REMARK 3 B12 (A**2) : 0.29000
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): 0.074
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.041
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.149
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
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): 5003 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6881 ; 1.193 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 666 ; 5.729 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 224 ;32.060 ;23.839
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 759 ;11.240 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 38 ;13.806 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 753 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3981 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1627 ; 0.192 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3311 ; 0.289 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 252 ; 0.073 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 35 ; 0.139 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 36 ; 0.092 ; 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): 3259 ; 0.409 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5141 ; 0.679 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2026 ; 0.969 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1740 ; 1.495 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 3IDA COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUL-09.
REMARK 100 THE RCSB ID CODE IS RCSB054267.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-FEB-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.02
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 103956
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09400
REMARK 200 FOR THE DATA SET : 22.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: 1JU3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.7 M AMMONIUM SULFATE, 25 MM NACL,
REMARK 280 10 MM TRIS PH 7.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 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 151.47467
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 75.73733
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 113.60600
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 37.86867
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 189.34333
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 151.47467
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 75.73733
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 37.86867
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 113.60600
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 189.34333
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: 8600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 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 -54.14000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 93.77323
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -37.86867
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 VAL A 2
REMARK 465 ASP A 3
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 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 THR A 385 N CA C O CB OG1 CG2
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 45 107.91 79.05
REMARK 500 SER A 56 -87.83 -131.15
REMARK 500 PHE A 78 -114.44 49.51
REMARK 500 HIS A 87 -38.72 74.34
REMARK 500 SER A 117 -119.57 64.26
REMARK 500 TYR A 152 -121.18 -116.36
REMARK 500 ASP A 198 66.21 -156.29
REMARK 500 GLN A 224 -60.39 -97.31
REMARK 500 PRO A 284 30.31 -87.94
REMARK 500 ASP A 355 36.51 -94.93
REMARK 500 THR A 371 164.49 69.30
REMARK 500 ASN A 413 52.24 -145.91
REMARK 500 LEU A 508 -123.70 61.46
REMARK 500 ASN A 528 80.65 -164.51
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 DBC A 589
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 590
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 591
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL 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 CL A 595
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 596
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3287
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 597
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 598
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3I2K RELATED DB: PDB
REMARK 900 WILD-TYPE, ALSO BOUND TO DTT-ADDUCT
REMARK 900 RELATED ID: 3I2J RELATED DB: PDB
REMARK 900 WILD-TYPE, NO LIGAND BOUND
REMARK 900 RELATED ID: 3I2I RELATED DB: PDB
REMARK 900 COCE, MUTATION T172R, ALSO BOUND TO DTT-ADDUCT
REMARK 900 RELATED ID: 3I2G RELATED DB: PDB
REMARK 900 COCE, MUTATION G173Q, ALSO BOUND TO DTT-ADDUCT
DBREF 3IDA A 1 574 UNP Q9L9D7 COCE_RHOSM 1 574
SEQADV 3IDA LYS A 169 UNP Q9L9D7 LEU 169 ENGINEERED
SEQADV 3IDA GLN A 173 UNP Q9L9D7 GLY 173 ENGINEERED
SEQADV 3IDA LYS A 575 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3IDA LEU A 576 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3IDA ALA A 577 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3IDA ALA A 578 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3IDA ALA A 579 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3IDA LEU A 580 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3IDA GLU A 581 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3IDA HIS A 582 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3IDA HIS A 583 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3IDA HIS A 584 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3IDA HIS A 585 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3IDA HIS A 586 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3IDA 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 LYS
SEQRES 14 A 587 ILE GLY THR 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 DBC A 589 10
HET GOL A 590 6
HET GOL A 591 6
HET GOL A 592 6
HET GOL A 593 6
HET GOL A 594 6
HET CL A 595 1
HET CL A 596 1
HET GOL A3287 12
HET GOL A 597 6
HET GOL A 598 6
HETNAM CL CHLORIDE ION
HETNAM DBC (4S,5S)-4,5-BIS(MERCAPTOMETHYL)-1,3-DIOXOLAN-2-OL
HETNAM GOL GLYCEROL
FORMUL 2 CL 3(CL 1-)
FORMUL 3 DBC C5 H10 O3 S2
FORMUL 4 GOL 8(C3 H8 O3)
FORMUL 14 HOH *694(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 GLN A 104 1 16
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 ASN A 197 1 14
HELIX 7 7 ASP A 198 SER A 204 1 7
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 239 1 8
HELIX 11 11 LEU A 240 LEU A 247 5 8
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 LEU A 39
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 GLY A 256 0
SHEET 2 C 4 ALA A 278 GLY A 283 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 348 N VAL A 335
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 ILE A 567 N PHE A 361
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 ILE A 567 N PHE A 361
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 ASN A 512 N VAL A 441
SHEET 1 G 4 LEU A 428 SER A 431 0
SHEET 2 G 4 ARG A 519 SER A 525 -1 O VAL A 524 N LEU A 428
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 589 1555 1555 1.56
CISPEP 1 ALA A 149 PRO A 150 0 6.28
CISPEP 2 THR A 206 PRO A 207 0 -4.08
CISPEP 3 TRP A 351 PRO A 352 0 -5.14
CISPEP 4 PHE A 529 PRO A 530 0 4.53
SITE 1 AC1 2 LYS A 298 ARG A 472
SITE 1 AC2 7 TYR A 44 SER A 117 TYR A 118 TRP A 166
SITE 2 AC2 7 HIS A 287 GOL A 593 HOH A 853
SITE 1 AC3 6 GLU A 309 ALA A 310 ARG A 336 TRP A 345
SITE 2 AC3 6 HOH A 806 HOH A1008
SITE 1 AC4 8 LEU A 515 PRO A 516 HIS A 518 GLY A 540
SITE 2 AC4 8 GLU A 545 HOH A 857 HOH A1265 HOH A1280
SITE 1 AC5 9 LEU A 196 ASN A 197 VAL A 199 ARG A 293
SITE 2 AC5 9 PHE A 408 HIS A 409 ASN A 410 GOL A 597
SITE 3 AC5 9 HOH A 672
SITE 1 AC6 7 TYR A 44 SER A 117 LYS A 169 DBC A 589
SITE 2 AC6 7 HOH A 842 HOH A 856 HOH A1074
SITE 1 AC7 3 LYS A 573 HOH A 816 HOH A1027
SITE 1 AC8 2 TRP A 345 HOH A 878
SITE 1 AC9 2 GLY A 365 SER A 383
SITE 1 BC1 13 ARG A 148 ALA A 149 PRO A 150 TYR A 152
SITE 2 BC1 13 PRO A 154 SER A 159 GLY A 260 THR A 405
SITE 3 BC1 13 LEU A 508 LYS A 531 TYR A 532 HOH A 931
SITE 4 BC1 13 HOH A1210
SITE 1 BC2 8 SER A 288 LEU A 407 PHE A 408 ASN A 410
SITE 2 BC2 8 GLY A 411 ASP A 412 GOL A 592 HOH A 807
SITE 1 BC3 6 SER A 372 SER A 431 ARG A 519 HOH A 744
SITE 2 BC3 6 HOH A 820 HOH A 870
CRYST1 108.280 108.280 227.212 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 0.009235 0.005332 0.000000 0.00000
SCALE2 0.000000 0.010664 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004401 0.00000
TER 4800 LYS A 575
MASTER 389 0 12 18 29 0 23 6 5560 1 65 46
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