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HEADER HYDROLASE 05-JUN-06 2H7X
TITLE PIKROMYCIN THIOESTERASE ADDUCT WITH REDUCED TRIKETIDE
TITLE 2 AFFINITY LABEL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYPE I POLYKETIDE SYNTHASE PIKAIV;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: THIOESTERASE DOMAIN;
COMPND 5 SYNONYM: PIKROMYCIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES VENEZUELAE;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 GENE: PIKAIV;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA
KEYWDS THIOESTERASE, ALPHA-BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.W.GIRALDES,D.L.AKEY,J.D.KITTENDORF,D.H.SHERMAN,J.S.SMITH,
AUTHOR 2 R.A.FECIK
REVDAT 1 19-SEP-06 2H7X 0
JRNL AUTH J.W.GIRALDES,D.L.AKEY,J.D.KITTENDORF,D.H.SHERMAN,
JRNL AUTH 2 J.S.SMITH,R.A.FECIK
JRNL TITL STRUCTURAL AND MECHANISTIC INSIGHTS OF POLYKETIDE
JRNL TITL 2 MACROLACTONIZATION FROM POLYKETIDE-BASED AFFINITY
JRNL TITL 3 LABELS
JRNL REF NAT.CHEM.BIOL. V. 2 531 2006
JRNL REFN US ISSN 1548-7091
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.85 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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 83.33
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 64709
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3333
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4201
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.2640
REMARK 3 BIN FREE R VALUE SET COUNT : 191
REMARK 3 BIN FREE R VALUE : 0.2960
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 4778
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.58
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.72000
REMARK 3 B22 (A**2) : -0.76000
REMARK 3 B33 (A**2) : 2.49000
REMARK 3 B12 (A**2) : 0.00000
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): 0.118
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.119
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.086
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.845
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4383 ; 0.010 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5988 ; 1.235 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 561 ; 5.018 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 204 ;31.909 ;22.748
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 614 ;14.576 ;14.926
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 41 ;13.858 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 642 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3479 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1985 ; 0.199 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2954 ; 0.305 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 415 ; 0.159 ; 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 ; 0.189 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 17 ; 0.120 ; 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): 2859 ; 2.156 ; 3.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4433 ; 3.245 ; 5.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1709 ; 2.187 ; 3.500
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1555 ; 3.322 ; 5.000
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 : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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 4
REMARK 4 2H7X COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-2006.
REMARK 100 THE RCSB ID CODE IS RCSB038041.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-DEC-2005
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.60
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) : 0.97922
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : BLU-ICE
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68102
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06700
REMARK 200 FOR THE DATA SET : 24.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.52400
REMARK 200 FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1MNA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4 M LI2SO4, 100 MM HEPES 7.6, 80
REMARK 280 MM MGCL2, 2 MM DTT, 5% DMSO, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 1/2-X,1/2+Y,-Z
REMARK 290 4555 1/2+X,1/2-Y,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 53.94900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 65.36400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 53.94900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 65.36400
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 MG MG 507 LIES ON A SPECIAL POSITION.
REMARK 375 HOH 386 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 LEU A -7
REMARK 465 VAL A -6
REMARK 465 PRO A -5
REMARK 465 ARG A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
REMARK 465 SER A 1
REMARK 465 GLY A 2
REMARK 465 ALA A 3
REMARK 465 ASP A 4
REMARK 465 THR A 5
REMARK 465 GLY A 6
REMARK 465 ALA A 7
REMARK 465 GLY A 8
REMARK 465 ARG A 64
REMARK 465 ALA A 65
REMARK 465 THR A 111
REMARK 465 GLY A 112
REMARK 465 THR A 113
REMARK 465 ILE A 293
REMARK 465 GLU A 294
REMARK 465 GLY A 295
REMARK 465 ALA A 296
REMARK 465 GLY A 297
REMARK 465 LYS A 298
REMARK 465 MET B -20
REMARK 465 GLY B -19
REMARK 465 SER B -18
REMARK 465 SER B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 SER B -10
REMARK 465 SER B -9
REMARK 465 GLY B -8
REMARK 465 LEU B -7
REMARK 465 VAL B -6
REMARK 465 PRO B -5
REMARK 465 ARG B -4
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 HIS B -1
REMARK 465 MET B 0
REMARK 465 SER B 1
REMARK 465 GLY B 2
REMARK 465 ALA B 3
REMARK 465 ASP B 4
REMARK 465 THR B 5
REMARK 465 GLY B 6
REMARK 465 ALA B 7
REMARK 465 GLY B 8
REMARK 465 ARG B 64
REMARK 465 ALA B 65
REMARK 465 THR B 109
REMARK 465 GLY B 110
REMARK 465 THR B 111
REMARK 465 GLY B 112
REMARK 465 THR B 113
REMARK 465 GLY B 292
REMARK 465 ILE B 293
REMARK 465 GLU B 294
REMARK 465 GLY B 295
REMARK 465 ALA B 296
REMARK 465 GLY B 297
REMARK 465 LYS B 298
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI
REMARK 500 O GLY B 222 O HOH 306 2.08
REMARK 500 O MET B 272 O HOH 229 2.13
REMARK 500 O GLY A 222 O HOH 329 2.18
REMARK 500 OD1 ASP A 243 O HOH 189 2.18
REMARK 500 O HOH 260 O HOH 310 2.18
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 LEU A 152 CG LEU A 152 CD1 0.072
REMARK 500 PRO B 231 CB PRO B 231 CG -0.066
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 197 CA - CB - CG ANGL. DEV. = 8.2 DEGREES
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MNA RELATED DB: PDB
REMARK 900 PIKROMYCIN THIOESTERASE
REMARK 900 RELATED ID: 2H7Y RELATED DB: PDB
REMARK 900 PIKROMYCIN THIOESTERASE WITH COVALENT AFFINITY LABEL
DBREF 2H7X A 1 298 UNP Q9ZGI2 Q9ZGI2_9ACTO 1049 1346
DBREF 2H7X B 1 298 UNP Q9ZGI2 Q9ZGI2_9ACTO 1049 1346
SEQADV 2H7X MET A -20 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X GLY A -19 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X SER A -18 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X SER A -17 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X HIS A -16 UNP Q9ZGI2 HIS TAG
SEQADV 2H7X HIS A -15 UNP Q9ZGI2 HIS TAG
SEQADV 2H7X HIS A -14 UNP Q9ZGI2 HIS TAG
SEQADV 2H7X HIS A -13 UNP Q9ZGI2 HIS TAG
SEQADV 2H7X HIS A -12 UNP Q9ZGI2 HIS TAG
SEQADV 2H7X HIS A -11 UNP Q9ZGI2 HIS TAG
SEQADV 2H7X SER A -10 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X SER A -9 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X GLY A -8 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X LEU A -7 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X VAL A -6 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X PRO A -5 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X ARG A -4 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X GLY A -3 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X SER A -2 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X HIS A -1 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X MET A 0 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X MET B -20 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X GLY B -19 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X SER B -18 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X SER B -17 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X HIS B -16 UNP Q9ZGI2 HIS TAG
SEQADV 2H7X HIS B -15 UNP Q9ZGI2 HIS TAG
SEQADV 2H7X HIS B -14 UNP Q9ZGI2 HIS TAG
SEQADV 2H7X HIS B -13 UNP Q9ZGI2 HIS TAG
SEQADV 2H7X HIS B -12 UNP Q9ZGI2 HIS TAG
SEQADV 2H7X HIS B -11 UNP Q9ZGI2 HIS TAG
SEQADV 2H7X SER B -10 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X SER B -9 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X GLY B -8 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X LEU B -7 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X VAL B -6 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X PRO B -5 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X ARG B -4 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X GLY B -3 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X SER B -2 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X HIS B -1 UNP Q9ZGI2 CLONING ARTIFACT
SEQADV 2H7X MET B 0 UNP Q9ZGI2 CLONING ARTIFACT
SEQRES 1 A 319 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 319 LEU VAL PRO ARG GLY SER HIS MET SER GLY ALA ASP THR
SEQRES 3 A 319 GLY ALA GLY ALA GLY MET PHE ARG ALA LEU PHE ARG GLN
SEQRES 4 A 319 ALA VAL GLU ASP ASP ARG TYR GLY GLU PHE LEU ASP VAL
SEQRES 5 A 319 LEU ALA GLU ALA SER ALA PHE ARG PRO GLN PHE ALA SER
SEQRES 6 A 319 PRO GLU ALA CYS SER GLU ARG LEU ASP PRO VAL LEU LEU
SEQRES 7 A 319 ALA GLY GLY PRO THR ASP ARG ALA GLU GLY ARG ALA VAL
SEQRES 8 A 319 LEU VAL GLY CYS THR GLY THR ALA ALA ASN GLY GLY PRO
SEQRES 9 A 319 HIS GLU PHE LEU ARG LEU SER THR SER PHE GLN GLU GLU
SEQRES 10 A 319 ARG ASP PHE LEU ALA VAL PRO LEU PRO GLY TYR GLY THR
SEQRES 11 A 319 GLY THR GLY THR GLY THR ALA LEU LEU PRO ALA ASP LEU
SEQRES 12 A 319 ASP THR ALA LEU ASP ALA GLN ALA ARG ALA ILE LEU ARG
SEQRES 13 A 319 ALA ALA GLY ASP ALA PRO VAL VAL LEU LEU GLY HIS SER
SEQRES 14 A 319 GLY GLY ALA LEU LEU ALA HIS GLU LEU ALA PHE ARG LEU
SEQRES 15 A 319 GLU ARG ALA HIS GLY ALA PRO PRO ALA GLY ILE VAL LEU
SEQRES 16 A 319 VAL ASP PRO TYR PRO PRO GLY HIS GLN GLU PRO ILE GLU
SEQRES 17 A 319 VAL TRP SER ARG GLN LEU GLY GLU GLY LEU PHE ALA GLY
SEQRES 18 A 319 GLU LEU GLU PRO MET SER ASP ALA ARG LEU LEU ALA MET
SEQRES 19 A 319 GLY ARG TYR ALA ARG PHE LEU ALA GLY PRO ARG PRO GLY
SEQRES 20 A 319 ARG SER SER ALA PRO VAL LEU LEU VAL ARG ALA SER GLU
SEQRES 21 A 319 PRO LEU GLY ASP TRP GLN GLU GLU ARG GLY ASP TRP ARG
SEQRES 22 A 319 ALA HIS TRP ASP LEU PRO HIS THR VAL ALA ASP VAL PRO
SEQRES 23 A 319 GLY ASP HIS PHE THR MET MET ARG ASP HIS ALA PRO ALA
SEQRES 24 A 319 VAL ALA GLU ALA VAL LEU SER TRP LEU ASP ALA ILE GLU
SEQRES 25 A 319 GLY ILE GLU GLY ALA GLY LYS
SEQRES 1 B 319 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 319 LEU VAL PRO ARG GLY SER HIS MET SER GLY ALA ASP THR
SEQRES 3 B 319 GLY ALA GLY ALA GLY MET PHE ARG ALA LEU PHE ARG GLN
SEQRES 4 B 319 ALA VAL GLU ASP ASP ARG TYR GLY GLU PHE LEU ASP VAL
SEQRES 5 B 319 LEU ALA GLU ALA SER ALA PHE ARG PRO GLN PHE ALA SER
SEQRES 6 B 319 PRO GLU ALA CYS SER GLU ARG LEU ASP PRO VAL LEU LEU
SEQRES 7 B 319 ALA GLY GLY PRO THR ASP ARG ALA GLU GLY ARG ALA VAL
SEQRES 8 B 319 LEU VAL GLY CYS THR GLY THR ALA ALA ASN GLY GLY PRO
SEQRES 9 B 319 HIS GLU PHE LEU ARG LEU SER THR SER PHE GLN GLU GLU
SEQRES 10 B 319 ARG ASP PHE LEU ALA VAL PRO LEU PRO GLY TYR GLY THR
SEQRES 11 B 319 GLY THR GLY THR GLY THR ALA LEU LEU PRO ALA ASP LEU
SEQRES 12 B 319 ASP THR ALA LEU ASP ALA GLN ALA ARG ALA ILE LEU ARG
SEQRES 13 B 319 ALA ALA GLY ASP ALA PRO VAL VAL LEU LEU GLY HIS SER
SEQRES 14 B 319 GLY GLY ALA LEU LEU ALA HIS GLU LEU ALA PHE ARG LEU
SEQRES 15 B 319 GLU ARG ALA HIS GLY ALA PRO PRO ALA GLY ILE VAL LEU
SEQRES 16 B 319 VAL ASP PRO TYR PRO PRO GLY HIS GLN GLU PRO ILE GLU
SEQRES 17 B 319 VAL TRP SER ARG GLN LEU GLY GLU GLY LEU PHE ALA GLY
SEQRES 18 B 319 GLU LEU GLU PRO MET SER ASP ALA ARG LEU LEU ALA MET
SEQRES 19 B 319 GLY ARG TYR ALA ARG PHE LEU ALA GLY PRO ARG PRO GLY
SEQRES 20 B 319 ARG SER SER ALA PRO VAL LEU LEU VAL ARG ALA SER GLU
SEQRES 21 B 319 PRO LEU GLY ASP TRP GLN GLU GLU ARG GLY ASP TRP ARG
SEQRES 22 B 319 ALA HIS TRP ASP LEU PRO HIS THR VAL ALA ASP VAL PRO
SEQRES 23 B 319 GLY ASP HIS PHE THR MET MET ARG ASP HIS ALA PRO ALA
SEQRES 24 B 319 VAL ALA GLU ALA VAL LEU SER TRP LEU ASP ALA ILE GLU
SEQRES 25 B 319 GLY ILE GLU GLY ALA GLY LYS
HET SO4 503 5
HET SO4 504 5
HET MG 507 1
HET SO4 505 5
HET PSX A 548 12
HET PSX B 548 12
HET DMS 501 4
HET DMS 502 4
HETNAM SO4 SULFATE ION
HETNAM MG MAGNESIUM ION
HETNAM PSX [(2S,3R,4S)-2,4-DIHYDROXY-3-METHYLHEXYL]PHOSPHONIC
HETNAM 2 PSX ACID
HETNAM DMS DIMETHYL SULFOXIDE
FORMUL 3 SO4 3(O4 S1 2-)
FORMUL 5 MG MG1 2+
FORMUL 7 PSX 2(C7 H17 O5 P1)
FORMUL 9 DMS 2(C2 H6 O1 S1)
FORMUL 11 HOH *485(H2 O1)
HELIX 1 1 GLY A 10 ASP A 22 1 13
HELIX 2 2 ARG A 24 ALA A 37 1 14
HELIX 3 3 SER A 44 CYS A 48 5 5
HELIX 4 4 PHE A 86 SER A 92 1 7
HELIX 5 5 ASP A 121 GLY A 138 1 18
HELIX 6 6 SER A 148 GLY A 166 1 19
HELIX 7 7 GLN A 183 TRP A 189 1 7
HELIX 8 8 TRP A 189 GLY A 200 1 12
HELIX 9 9 SER A 206 GLY A 222 1 17
HELIX 10 10 GLN A 245 GLY A 249 5 5
HELIX 11 11 PHE A 269 ASP A 274 1 6
HELIX 12 12 HIS A 275 GLY A 292 1 18
HELIX 13 13 GLY B 10 ASP B 22 1 13
HELIX 14 14 ARG B 24 ALA B 37 1 14
HELIX 15 15 SER B 44 CYS B 48 5 5
HELIX 16 16 PHE B 86 SER B 92 1 7
HELIX 17 17 ASP B 121 GLY B 138 1 18
HELIX 18 18 SER B 148 GLY B 166 1 19
HELIX 19 19 GLN B 183 TRP B 189 1 7
HELIX 20 20 TRP B 189 GLY B 200 1 12
HELIX 21 21 SER B 206 GLY B 222 1 17
HELIX 22 22 GLN B 245 GLY B 249 5 5
HELIX 23 23 PHE B 269 ASP B 274 1 6
HELIX 24 24 HIS B 275 GLU B 291 1 17
SHEET 1 A 2 GLN A 41 PHE A 42 0
SHEET 2 A 2 LEU A 118 PRO A 119 1 O LEU A 118 N PHE A 42
SHEET 1 B 7 VAL A 55 ALA A 58 0
SHEET 2 B 7 PHE A 99 VAL A 102 -1 O PHE A 99 N LEU A 57
SHEET 3 B 7 VAL A 70 CYS A 74 1 N LEU A 71 O LEU A 100
SHEET 4 B 7 VAL A 142 HIS A 147 1 O LEU A 145 N CYS A 74
SHEET 5 B 7 GLY A 171 VAL A 175 1 O VAL A 173 N LEU A 144
SHEET 6 B 7 VAL A 232 ALA A 237 1 O LEU A 233 N LEU A 174
SHEET 7 B 7 THR A 260 VAL A 264 1 O ALA A 262 N LEU A 234
SHEET 1 C 2 GLN B 41 PHE B 42 0
SHEET 2 C 2 LEU B 118 PRO B 119 1 O LEU B 118 N PHE B 42
SHEET 1 D 7 VAL B 55 ALA B 58 0
SHEET 2 D 7 PHE B 99 VAL B 102 -1 O ALA B 101 N VAL B 55
SHEET 3 D 7 VAL B 70 CYS B 74 1 N GLY B 73 O LEU B 100
SHEET 4 D 7 VAL B 142 HIS B 147 1 O LEU B 145 N CYS B 74
SHEET 5 D 7 GLY B 171 VAL B 175 1 O VAL B 173 N LEU B 144
SHEET 6 D 7 VAL B 232 ALA B 237 1 O LEU B 233 N LEU B 174
SHEET 7 D 7 THR B 260 VAL B 264 1 O ALA B 262 N ARG B 236
LINK OG SER A 148 P1 PSX A 548
LINK OG SER B 148 P1 PSX B 548
CRYST1 107.898 130.728 56.484 90.00 90.00 90.00 P 21 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009268 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007649 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017704 0.00000
TER 2143 GLY A 292
TER 4247 GLU B 291
MASTER 375 0 8 24 18 0 0 6 4778 2 49 50
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