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HEADER HYDROLASE 06-MAR-02 1IUO
TITLE META-CLEAVAGE PRODUCT HYDROLASE FROM PSEUDOMONAS
TITLE 2 FLUORESCENS IP01 (CUMD) S103A MUTANT COMPLEXED WITH
TITLE 3 ACETATES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: META-CLEAVAGE PRODUCT HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 2-HYDROXY-6-OXO-7-METHYLOCTA-2,4-DIENOATE
COMPND 5 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 STRAIN: IP01;
SOURCE 5 GENE: CUMD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PIP140
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,T.SAKU,M.HIDAKA,S.-Y.JUN,H.NOJIRI,H.YAMANE,
AUTHOR 2 H.SHOUN,T.OMORI,T.WAKAGI
REVDAT 1 18-SEP-02 1IUO 0
JRNL AUTH S.FUSHINOBU,T.SAKU,M.HIDAKA,S.-Y.JUN,H.NOJIRI,
JRNL AUTH 2 H.YAMANE,H.SHOUN,T.OMORI,T.WAKAGI
JRNL TITL CRYSTAL STRUCTURES OF A META-CLEAVAGE PRODUCT
JRNL TITL 2 HYDROLASE FROM PSEUDOMONAS FLUORESCENS IP01 (CUMD)
JRNL TITL 3 COMPLEXED WITH CLEAVAGE PRODUCTS
JRNL REF PROTEIN SCI. V. 11 2184 2002
JRNL REFN ASTM PRCIEI US ISSN 0961-8368
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.SAKU,S.FUSHINOBU,S.-Y.JUN,N.IKEDA,H.NOJIRI,
REMARK 1 AUTH 2 H.YAMANE,T.OMORI,T.WAKAGI
REMARK 1 TITL PURIFICATION, CHARACTERIZATION, AND STEADY-STATE
REMARK 1 TITL 2 KINETICS OF A META-CLEAVAGE COMPOUND HYDROLASE
REMARK 1 TITL 3 FROM PSEUDOMONAS FLUORESCENS IP01
REMARK 1 REF J.BIOSCI.BIOENG. V. 93 568 2002
REMARK 1 REFN JA ISSN 1389-1723
REMARK 1 REFERENCE 2
REMARK 1 AUTH H.HABE,K.KASUGA,H.NOJIRI,H.YAMANE,T.OMORI
REMARK 1 TITL ANALYSIS OF CUMENE (ISOPROPYLBENZENE) DEGRADATION
REMARK 1 TITL 2 GENES FROM PSEUDOMONAS FLUORESCENS IP01
REMARK 1 REF APPL.ENVIRON.MICROBIOL. V. 62 4471 1996
REMARK 1 REFN US ISSN 1098-5336
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 23950
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) : 0.174
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1203
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3742
REMARK 3 BIN R VALUE (WORKING SET) : 0.1790
REMARK 3 BIN FREE R VALUE : 0.2360
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 180
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2147
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 238
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 8.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.63000
REMARK 3 B22 (A**2) : -0.63000
REMARK 3 B33 (A**2) : -1.00000
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.13
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.71
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) : 1.600 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.130 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.850 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.110 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 64.01
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 : ACETATEION.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 : ACETATEION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1IUO COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-MAR-2002.
REMARK 100 THE RCSB ID CODE IS RCSB005296.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-FEB-2001
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 3.80
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) : 1.0
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 : 23969
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 29.617
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : 0.09600
REMARK 200 FOR THE DATA SET : 7.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 0.29200
REMARK 200 R SYM FOR SHELL (I) : 0.29200
REMARK 200 FOR SHELL : 2.500
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 1C4X
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, AMMONIUM ACETATE, SODIUM
REMARK 280 ACETATE
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 39.01850
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 39.01850
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 38.27150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 58.30950
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 38.27150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 58.30950
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 39.01850
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 38.27150
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 58.30950
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 39.01850
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 38.27150
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 58.30950
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 116.61900
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 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: 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 PRO A 60 CD PRO A 60 CG 0.033
REMARK 500 MET A 190 CE MET A 190 SD 0.033
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. = 8.8 DEGREES
REMARK 500 ARG A 56 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 HIS A 98 N - CA - C ANGL. DEV. = -9.5 DEGREES
REMARK 500 VAL A 124 N - CA - C ANGL. DEV. = -7.6 DEGREES
REMARK 500 THR A 146 N - CA - C ANGL. DEV. =-10.9 DEGREES
REMARK 500 PRO A 147 N - CA - C ANGL. DEV. = 9.7 DEGREES
REMARK 500 GLU A 215 N - CA - C ANGL. DEV. =-10.7 DEGREES
REMARK 500 GLN A 243 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 GLY A 248 N - CA - C ANGL. DEV. = -7.7 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 -105.17 46.90
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IUN RELATED DB: PDB
REMARK 900 1IUN CONTAINS THE SAME PROTEIN LIGAND FREE
REMARK 900 RELATED ID: 1IUP RELATED DB: PDB
REMARK 900 1IUP CONTAINS THE SAME PROTEIN COMPLEXED WITH ISOBUTYRATES
DBREF 1IUO A 1 282 GB 1871461 BAA12150 1 282
SEQADV 1IUO 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 ACT 300 4
HET ACT 301 4
HETNAM ACT ACETATE ION
FORMUL 2 ACT 2(C2 H3 O2 1-)
FORMUL 4 HOH *238(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 GLU A 272 1 15
SHEET 1 A 8 LYS A 8 ALA A 12 0
SHEET 2 A 8 VAL A 15 VAL A 22 -1 O THR A 17 N ILE A 10
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 -0.41
CRYST1 76.543 116.619 78.037 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 0.013065 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008575 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012814 0.00000
TER 2148 ASN A 274
MASTER 323 0 2 14 8 0 0 6 2393 1 8 22
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