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HEADER TRANSFERASE 05-SEP-02 1MNA
TITLE THIOESTERASE DOMAIN OF PICROMYCIN POLYKETIDE SYNTHASE (PICS
TITLE 2 TE), PH 8.0
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYKETIDE SYNTHASE IV;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: THIOESTERASE DOMAIN;
COMPND 5 SYNONYM: PICROMYCIN POLYKETIDE SYNTHASE; PIKAIV; TYPE I
COMPND 6 POLYKETIDE SYNTHASE PIKAIV;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES VENEZUELAE;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 GENE: PICAIV;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS THIOESTERASE, POLYKETIDE SYNTHASE, OPEN SUBSTRATE CHANNEL,
KEYWDS 2 ALPHA-BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.-C.TSAI,H.LU,D.E.CANE,C.KHOSLA,R.M.STROUD
REVDAT 1 04-FEB-03 1MNA 0
JRNL AUTH S.-C.TSAI,H.LU,D.E.CANE,C.KHOSLA,R.M.STROUD
JRNL TITL INSIGHTS INTO CHANNEL ARCHITECTURE AND SUBSTRATE
JRNL TITL 2 SPECIFICITY FROM CRYSTAL STRUCTURES OF TWO
JRNL TITL 3 MACROCYCLE-FORMING THIOESTERASES OF MODULAR
JRNL TITL 4 POLYKETIDE SYNTHASES
JRNL REF BIOCHEMISTRY V. 41 12598 2002
JRNL REFN ASTM BICHAW US ISSN 0006-2960
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 21.28
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.2
REMARK 3 NUMBER OF REFLECTIONS : 70844
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) : 0.236
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3608
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 9747
REMARK 3 BIN R VALUE (WORKING SET) : 0.3220
REMARK 3 BIN FREE R VALUE : 0.3430
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 509
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4193
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 313
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.02000
REMARK 3 B22 (A**2) : -2.85000
REMARK 3 B33 (A**2) : 9.87000
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) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.28
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) : 22.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.85
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 40.34
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MNA COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PRAGUE ON 19-SEP-2002.
REMARK 100 THE RCSB ID CODE IS RCSB017035.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-NOV-2001
REMARK 200 TEMPERATURE (KELVIN) : 190.0
REMARK 200 PH : 8.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : 9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 75591
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.100
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 31.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.58700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.0
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 M LITHIUM SULFATE, 100 MM TRIS, 2
REMARK 280 MM DTT, PH 8.0, VAPOR DIFFUSION, SITTING DROP AT 298K
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 54.02900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 65.29650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 54.02900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 65.29650
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 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 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 THR A 109
REMARK 465 GLY A 110
REMARK 465 THR A 111
REMARK 465 GLY A 112
REMARK 465 THR A 113
REMARK 465 ILE A 290
REMARK 465 GLU A 291
REMARK 465 GLY A 292
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 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 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: 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 179 CD PRO A 179 CG 0.034
REMARK 500 PRO B 177 CD PRO B 177 CG 0.035
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 ASP A 98 N - CA - C ANGL. DEV. = -8.3 DEGREES
REMARK 500 ARG A 163 N - CA - C ANGL. DEV. = 8.1 DEGREES
REMARK 500 ALA A 199 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 GLY A 226 N - CA - C ANGL. DEV. = 9.6 DEGREES
REMARK 500 GLU B 85 N - CA - C ANGL. DEV. = 9.4 DEGREES
REMARK 500 ASP B 98 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 GLY B 108 N - CA - C ANGL. DEV. = 7.2 DEGREES
REMARK 500 VAL B 143 N - CA - C ANGL. DEV. = -7.4 DEGREES
REMARK 500 LEU B 233 N - CA - C ANGL. DEV. = -7.5 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 SER A 148 -118.31 54.87
REMARK 500 THR B 115 -72.69 78.81
REMARK 500 SER B 148 -117.66 56.31
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KEZ RELATED DB: PDB
REMARK 900 THIOESTERASE DOMAIN FROM 6-DEOXYERYTHRONOLIDE SYNTHASE
REMARK 900 (DEBS TE), PH 7.2
REMARK 900 RELATED ID: 1MN6 RELATED DB: PDB
REMARK 900 THIOESTERASE DOMAIN FROM PICROMYCIN POLYKETIDE SYNTHASE
REMARK 900 (PICS TE), PH 7.6
REMARK 900 RELATED ID: MNQ RELATED DB: PDB
REMARK 900 THIOESTERASE DOMAIN FROM PICROMYCIN POLYKETIDE SYNTHASE
REMARK 900 (PICS), PH 8.0
REMARK 900 RELATED ID: MO2 RELATED DB: PDB
REMARK 900 THIOESTERASE DOMAIN FROM PICROMYCIN POLYKETIDE SYNTHASE
REMARK 900 (PICS), PH 8.4
DBREF 1MNA A 1 298 PIR T17412 T17412 1049 1346
DBREF 1MNA B 1 298 PIR T17412 T17412 1049 1346
SEQRES 1 A 298 SER GLY ALA ASP THR GLY ALA GLY ALA GLY MET PHE ARG
SEQRES 2 A 298 ALA LEU PHE ARG GLN ALA VAL GLU ASP ASP ARG TYR GLY
SEQRES 3 A 298 GLU PHE LEU ASP VAL LEU ALA GLU ALA SER ALA PHE ARG
SEQRES 4 A 298 PRO GLN PHE ALA SER PRO GLU ALA CYS SER GLU ARG LEU
SEQRES 5 A 298 ASP PRO VAL LEU LEU ALA GLY GLY PRO THR ASP ARG ALA
SEQRES 6 A 298 GLU GLY ARG ALA VAL LEU VAL GLY CYS THR GLY THR ALA
SEQRES 7 A 298 ALA ASN GLY GLY PRO HIS GLU PHE LEU ARG LEU SER THR
SEQRES 8 A 298 SER PHE GLN GLU GLU ARG ASP PHE LEU ALA VAL PRO LEU
SEQRES 9 A 298 PRO GLY TYR GLY THR GLY THR GLY THR GLY THR ALA LEU
SEQRES 10 A 298 LEU PRO ALA ASP LEU ASP THR ALA LEU ASP ALA GLN ALA
SEQRES 11 A 298 ARG ALA ILE LEU ARG ALA ALA GLY ASP ALA PRO VAL VAL
SEQRES 12 A 298 LEU LEU GLY HIS SER GLY GLY ALA LEU LEU ALA HIS GLU
SEQRES 13 A 298 LEU ALA PHE ARG LEU GLU ARG ALA HIS GLY ALA PRO PRO
SEQRES 14 A 298 ALA GLY ILE VAL LEU VAL ASP PRO TYR PRO PRO GLY HIS
SEQRES 15 A 298 GLN GLU PRO ILE GLU VAL TRP SER ARG GLN LEU GLY GLU
SEQRES 16 A 298 GLY LEU PHE ALA GLY GLU LEU GLU PRO MET SER ASP ALA
SEQRES 17 A 298 ARG LEU LEU ALA MET GLY ARG TYR ALA ARG PHE LEU ALA
SEQRES 18 A 298 GLY PRO ARG PRO GLY ARG SER SER ALA PRO VAL LEU LEU
SEQRES 19 A 298 VAL ARG ALA SER GLU PRO LEU GLY ASP TRP GLN GLU GLU
SEQRES 20 A 298 ARG GLY ASP TRP ARG ALA HIS TRP ASP LEU PRO HIS THR
SEQRES 21 A 298 VAL ALA ASP VAL PRO GLY ASP HIS PHE THR MET MET ARG
SEQRES 22 A 298 ASP HIS ALA PRO ALA VAL ALA GLU ALA VAL LEU SER TRP
SEQRES 23 A 298 LEU ASP ALA ILE GLU GLY ILE GLU GLY ALA GLY LYS
SEQRES 1 B 298 SER GLY ALA ASP THR GLY ALA GLY ALA GLY MET PHE ARG
SEQRES 2 B 298 ALA LEU PHE ARG GLN ALA VAL GLU ASP ASP ARG TYR GLY
SEQRES 3 B 298 GLU PHE LEU ASP VAL LEU ALA GLU ALA SER ALA PHE ARG
SEQRES 4 B 298 PRO GLN PHE ALA SER PRO GLU ALA CYS SER GLU ARG LEU
SEQRES 5 B 298 ASP PRO VAL LEU LEU ALA GLY GLY PRO THR ASP ARG ALA
SEQRES 6 B 298 GLU GLY ARG ALA VAL LEU VAL GLY CYS THR GLY THR ALA
SEQRES 7 B 298 ALA ASN GLY GLY PRO HIS GLU PHE LEU ARG LEU SER THR
SEQRES 8 B 298 SER PHE GLN GLU GLU ARG ASP PHE LEU ALA VAL PRO LEU
SEQRES 9 B 298 PRO GLY TYR GLY THR GLY THR GLY THR GLY THR ALA LEU
SEQRES 10 B 298 LEU PRO ALA ASP LEU ASP THR ALA LEU ASP ALA GLN ALA
SEQRES 11 B 298 ARG ALA ILE LEU ARG ALA ALA GLY ASP ALA PRO VAL VAL
SEQRES 12 B 298 LEU LEU GLY HIS SER GLY GLY ALA LEU LEU ALA HIS GLU
SEQRES 13 B 298 LEU ALA PHE ARG LEU GLU ARG ALA HIS GLY ALA PRO PRO
SEQRES 14 B 298 ALA GLY ILE VAL LEU VAL ASP PRO TYR PRO PRO GLY HIS
SEQRES 15 B 298 GLN GLU PRO ILE GLU VAL TRP SER ARG GLN LEU GLY GLU
SEQRES 16 B 298 GLY LEU PHE ALA GLY GLU LEU GLU PRO MET SER ASP ALA
SEQRES 17 B 298 ARG LEU LEU ALA MET GLY ARG TYR ALA ARG PHE LEU ALA
SEQRES 18 B 298 GLY PRO ARG PRO GLY ARG SER SER ALA PRO VAL LEU LEU
SEQRES 19 B 298 VAL ARG ALA SER GLU PRO LEU GLY ASP TRP GLN GLU GLU
SEQRES 20 B 298 ARG GLY ASP TRP ARG ALA HIS TRP ASP LEU PRO HIS THR
SEQRES 21 B 298 VAL ALA ASP VAL PRO GLY ASP HIS PHE THR MET MET ARG
SEQRES 22 B 298 ASP HIS ALA PRO ALA VAL ALA GLU ALA VAL LEU SER TRP
SEQRES 23 B 298 LEU ASP ALA ILE GLU GLY ILE GLU GLY ALA GLY LYS
FORMUL 3 HOH *313(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 HIS A 165 1 18
HELIX 7 7 GLN A 183 TRP A 189 1 7
HELIX 8 8 TRP A 189 ALA A 199 1 11
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 ALA A 289 1 15
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 HIS B 165 1 18
HELIX 19 19 GLN B 183 TRP B 189 1 7
HELIX 20 20 TRP B 189 ALA B 199 1 11
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 ARG B 273 5 5
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 ALA A 101 N VAL A 55
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 VAL A 72
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 ILE A 172
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 VAL B 143 N VAL B 72
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 THR B 260 N LEU B 234
CRYST1 108.058 130.593 56.750 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 0.009254 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007657 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017621 0.00000
TER 2088 ALA A 289
TER 4193 GLU B 291
MASTER 329 0 0 24 18 0 0 6 4504 2 0 46
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