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HEADER HYDROLASE 19-AUG-03 1UKA
TITLE CRYSTAL STRUCTURE OF A META-CLEAVAGE PRODUCT HYDROLASE
TITLE 2 (CUMD) COMPLEXED WITH (S)-2-METHYLBUTYRATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-HYDROXY-6-OXO-7-METHYLOCTA-2,4-DIENOATE
COMPND 3 HYDROLASE;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: META-CLEAVAGE PRODUCT HYDROLASE;
COMPND 6 EC: 3.7.1.9;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS FLUORESCENS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 GENE: CUMD;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: IPI140
KEYWDS AROMATIC COMPOUNDS, CUMENE, ISOPROPYLBENZENE, META-CLEAVAGE
KEYWDS 2 COMPOUND HYDROLASE, POLYCHLORINATED BIPHENYL DEGRADATION,
KEYWDS 3 PSEUDOMONAS FLUORESCENS IP01, ALPHA/BETA-HYDROLASE,
KEYWDS 4 SUBSTRATE SPECIFICITY, CUMENE DEGRADATION, PCB, BETA-
KEYWDS 5 KETOLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.FUSHINOBU,S.-Y.JUN,M.HIDAKA,H.NOJIRI,H.YAMANE,H.SHOUN,
AUTHOR 2 T.OMORI,T.WAKAGI
REVDAT 1 14-SEP-04 1UKA 0
JRNL AUTH S.FUSHINOBU,S.-Y.JUN,M.HIDAKA,H.NOJIRI,H.YAMANE,
JRNL AUTH 2 H.SHOUN,T.OMORI,T.WAKAGI
JRNL TITL A SERIES OF CRYSTAL STRUCTURES OF A META-CLEAVAGE
JRNL TITL 2 PRODUCT HYDROLASE (CUMD) COMPLEXED WITH VARIOUS
JRNL TITL 3 CLEAVAGE PRODUCTS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.38
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1976481.090
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 39076
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1935
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.81
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6098
REMARK 3 BIN R VALUE (WORKING SET) : 0.2160
REMARK 3 BIN FREE R VALUE : 0.2420
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 325
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.013
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2139
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 7
REMARK 3 SOLVENT ATOMS : 366
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.39000
REMARK 3 B22 (A**2) : -0.60000
REMARK 3 B33 (A**2) : -0.78000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.17
REMARK 3 ESD FROM SIGMAA (A) : 0.10
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.14
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.73
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.880 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.540 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.460 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.970 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 44.26
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : SMB.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : SMB.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UKA COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-AUG-2003.
REMARK 100 THE RCSB ID CODE IS RCSB005922.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-2002
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.10
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39097
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 23.390
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07600
REMARK 200 FOR THE DATA SET : 8.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.27600
REMARK 200 FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1IUP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, AMMONIUM (S)-2-
REMARK 280 METHYLBUTYRATE, SODIUM (S)-2-METHYLBUTYRATE, PH 5.1, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 283K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,1/2+Z
REMARK 290 3555 -X,Y,1/2-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 1/2+X,1/2+Y,Z
REMARK 290 6555 1/2-X,1/2-Y,1/2+Z
REMARK 290 7555 1/2-X,1/2+Y,1/2-Z
REMARK 290 8555 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 39.28100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.28100
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 38.50950
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 58.22200
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 38.50950
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 58.22200
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 39.28100
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 38.50950
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 58.22200
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 39.28100
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 38.50950
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 58.22200
REMARK 290 SMTRY3 8 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 1 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
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 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 116.44400
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ASN A 274
REMARK 465 THR A 275
REMARK 465 PRO A 276
REMARK 465 LYS A 277
REMARK 465 LEU A 278
REMARK 465 VAL A 279
REMARK 465 GLY A 280
REMARK 465 ARG A 281
REMARK 465 PRO A 282
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH 168 O HOH 168 3554 2.09
REMARK 500 OE1 GLU A 268 OE1 GLU A 268 4565 2.15
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 MET A 126 SD MET A 126 CE 0.068
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 TRP A 44 N - CA - C ANGL. DEV. = 8.9 DEGREES
REMARK 500 ARG A 56 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 ASP A 61 N - CA - C ANGL. DEV. = -8.6 DEGREES
REMARK 500 HIS A 98 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 VAL A 124 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 ALA A 128 N - CA - C ANGL. DEV. = 10.8 DEGREES
REMARK 500 ALA A 129 N - CA - C ANGL. DEV. =-13.3 DEGREES
REMARK 500 THR A 146 N - CA - C ANGL. DEV. =-12.0 DEGREES
REMARK 500 PRO A 147 N - CA - C ANGL. DEV. = 10.1 DEGREES
REMARK 500 GLU A 215 N - CA - C ANGL. DEV. =-11.2 DEGREES
REMARK 500 GLN A 243 N - CA - C ANGL. DEV. = -8.8 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 ALA A 103 -109.39 51.90
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IUN RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH A HEXAGONAL SPACE GROUP
REMARK 900 RELATED ID: 1IUO RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH ACETATE
REMARK 900 RELATED ID: 1IUP RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH ISOBUTYRATE
REMARK 900 RELATED ID: 1UK6 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH PROPIONATE
REMARK 900 RELATED ID: 1UK7 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH N-BUTYRATE
REMARK 900 RELATED ID: 1UK8 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH N-VALERATE
REMARK 900 RELATED ID: 1UK9 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH ISOVALERATE
REMARK 900 RELATED ID: 1UKB RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH BENZOATE
DBREF 1UKA A 1 282 GB 1871461 BAA12150 1 282
SEQADV 1UKA ALA A 103 GB 1871461 SER 103 ENGINEERED
SEQRES 1 A 282 MET ALA ASN LEU GLU ILE GLY LYS SER ILE LEU ALA ALA
SEQRES 2 A 282 GLY VAL LEU THR ASN TYR HIS ASP VAL GLY GLU GLY GLN
SEQRES 3 A 282 PRO VAL ILE LEU ILE HIS GLY SER GLY PRO GLY VAL SER
SEQRES 4 A 282 ALA TYR ALA ASN TRP ARG LEU THR ILE PRO ALA LEU SER
SEQRES 5 A 282 LYS PHE TYR ARG VAL ILE ALA PRO ASP MET VAL GLY PHE
SEQRES 6 A 282 GLY PHE THR ASP ARG PRO GLU ASN TYR ASN TYR SER LYS
SEQRES 7 A 282 ASP SER TRP VAL ASP HIS ILE ILE GLY ILE MET ASP ALA
SEQRES 8 A 282 LEU GLU ILE GLU LYS ALA HIS ILE VAL GLY ASN ALA PHE
SEQRES 9 A 282 GLY GLY GLY LEU ALA ILE ALA THR ALA LEU ARG TYR SER
SEQRES 10 A 282 GLU ARG VAL ASP ARG MET VAL LEU MET GLY ALA ALA GLY
SEQRES 11 A 282 THR ARG PHE ASP VAL THR GLU GLY LEU ASN ALA VAL TRP
SEQRES 12 A 282 GLY TYR THR PRO SER ILE GLU ASN MET ARG ASN LEU LEU
SEQRES 13 A 282 ASP ILE PHE ALA TYR ASP ARG SER LEU VAL THR ASP GLU
SEQRES 14 A 282 LEU ALA ARG LEU ARG TYR GLU ALA SER ILE GLN PRO GLY
SEQRES 15 A 282 PHE GLN GLU SER PHE SER SER MET PHE PRO GLU PRO ARG
SEQRES 16 A 282 GLN ARG TRP ILE ASP ALA LEU ALA SER SER ASP GLU ASP
SEQRES 17 A 282 ILE LYS THR LEU PRO ASN GLU THR LEU ILE ILE HIS GLY
SEQRES 18 A 282 ARG GLU ASP GLN VAL VAL PRO LEU SER SER SER LEU ARG
SEQRES 19 A 282 LEU GLY GLU LEU ILE ASP ARG ALA GLN LEU HIS VAL PHE
SEQRES 20 A 282 GLY ARG CYS GLY HIS TRP THR GLN ILE GLU GLN THR ASP
SEQRES 21 A 282 ARG PHE ASN ARG LEU VAL VAL GLU PHE PHE ASN GLU ALA
SEQRES 22 A 282 ASN THR PRO LYS LEU VAL GLY ARG PRO
HET SMB 1300 7
HETNAM SMB 2-METHYLBUTANOIC ACID
FORMUL 2 SMB C5 H10 O2
FORMUL 3 HOH *366(H2 O1)
HELIX 1 1 SER A 39 ARG A 45 1 7
HELIX 2 2 THR A 47 SER A 52 1 6
HELIX 3 3 SER A 77 LEU A 92 1 16
HELIX 4 4 ALA A 103 TYR A 116 1 14
HELIX 5 5 THR A 136 GLY A 144 1 9
HELIX 6 6 SER A 148 ALA A 160 1 13
HELIX 7 7 ASP A 162 VAL A 166 5 5
HELIX 8 8 THR A 167 ILE A 179 1 13
HELIX 9 9 GLY A 182 PHE A 191 1 10
HELIX 10 10 ARG A 195 ALA A 203 1 9
HELIX 11 11 SER A 205 LYS A 210 1 6
HELIX 12 12 PRO A 228 ILE A 239 1 12
HELIX 13 13 TRP A 253 GLN A 258 1 6
HELIX 14 14 GLN A 258 ALA A 273 1 16
SHEET 1 A 8 LYS A 8 ALA A 12 0
SHEET 2 A 8 VAL A 15 VAL A 22 -1 O TYR A 19 N LYS A 8
SHEET 3 A 8 ARG A 56 PRO A 60 -1 O VAL A 57 N VAL A 22
SHEET 4 A 8 PRO A 27 ILE A 31 1 N VAL A 28 O ILE A 58
SHEET 5 A 8 ALA A 97 ASN A 102 1 O VAL A 100 N ILE A 31
SHEET 6 A 8 VAL A 120 MET A 126 1 O VAL A 124 N GLY A 101
SHEET 7 A 8 THR A 216 GLY A 221 1 O ILE A 219 N LEU A 125
SHEET 8 A 8 ALA A 242 PHE A 247 1 O GLN A 243 N ILE A 218
CISPEP 1 GLU A 193 PRO A 194 0 -0.36
CRYST1 77.019 116.444 78.562 90.00 90.00 90.00 C 2 2 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 0.012984 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008588 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012729 0.00000
TER 2140 ALA A 273
MASTER 342 0 1 14 8 0 0 6 2512 1 7 22
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