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HEADER TRANSFERASE 05-SEP-02 1MNQ
TITLE THIOESTERASE DOMAIN OF PICROMYCIN POLYKETIDE SYNTHASE (PICS
TITLE 2 TE), PH 8.4
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 1MNQ 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. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 35344
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) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1858
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2570
REMARK 3 BIN R VALUE (WORKING SET) : 0.2550
REMARK 3 BIN FREE R VALUE SET COUNT : 125
REMARK 3 BIN FREE R VALUE : 0.2870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 4523
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.83000
REMARK 3 B22 (A**2) : -0.95000
REMARK 3 B33 (A**2) : 0.11000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.923
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4297 ; 0.017 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5857 ; 1.741 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 548 ; 3.881 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 691 ;21.812 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 625 ; 0.128 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3434 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2400 ; 0.322 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 444 ; 0.289 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 36 ; 0.292 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 10 ; 0.214 ; 0.500
REMARK 3 SYMMETRY H-BOND 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): 2750 ; 0.845 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4353 ; 1.524 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1547 ; 2.829 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1504 ; 4.455 ; 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 : 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 : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MNQ 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 RCSB017038.
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 : 8.40
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 CRYSTALS
REMARK 200 OPTICS : DOUBLE CRYSTALS
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 : 35346
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
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 : 13.800
REMARK 200 R MERGE (I) : 0.10300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.64800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.200
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 (%): 56.2
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000, 100 MM TRIS, 2 MM
REMARK 280 DTT, 100 MM LITHIUM SULFATE, PH 8.4, VAPOR DIFFUSION, SITTING
REMARK 280 DROP AT 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-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 29.50800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 57.17800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.11200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 57.17800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.50800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.11200
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 GLY A 114
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 114
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 MET A 271 SD MET A 271 CG 0.118
REMARK 500 MET A 272 CE MET A 272 SD 0.117
REMARK 500 MET B 11 CE MET B 11 SD -0.225
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 189 CB - CA - C ANGL. DEV. =-12.5 DEGREES
REMARK 500 ASP A 250 N - CA - C ANGL. DEV. =-12.7 DEGREES
REMARK 500 ARG B 51 N - CA - C ANGL. DEV. =-13.6 DEGREES
REMARK 500 ARG B 215 CG - CD - NE ANGL. DEV. =-13.8 DEGREES
REMARK 500 GLN B 245 C - N - CA ANGL. DEV. =-11.2 DEGREES
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: 1MNA RELATED DB: PDB
REMARK 900 THIOESTERASE DOMAIN FROM PICROMYCIN POLYKETIDE SYNTHASE
REMARK 900 (PICS TE), PH 8.0
REMARK 900 RELATED ID: 1MO0 RELATED DB: PDB
REMARK 900 THIOESTERASE DOMAIN FROM 6-DEOXYERYTHRONOLIDE SYNTHASE
REMARK 900 (DEBS TE), PH 8.5
DBREF 1MNQ A 1 298 PIR T17412 T17412 1049 1346
DBREF 1MNQ 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 *340(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 GLU A 184 TRP A 189 1 6
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 PHE A 269 ARG A 273 5 5
HELIX 11 11 HIS A 275 ASP A 288 1 14
HELIX 12 12 GLY B 10 ASP B 22 1 13
HELIX 13 13 ARG B 24 ALA B 37 1 14
HELIX 14 14 SER B 44 CYS B 48 5 5
HELIX 15 15 PHE B 86 THR B 91 1 6
HELIX 16 16 SER B 92 GLN B 94 5 3
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 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 GLY A 73 O LEU A 100
SHEET 4 B 7 VAL A 142 HIS A 147 1 O VAL A 143 N VAL A 70
SHEET 5 B 7 GLY A 171 VAL A 175 1 O VAL A 175 N GLY A 146
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 PHE B 99 N ALA B 58
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 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 ILE B 172
SHEET 7 D 7 THR B 260 VAL B 264 1 O ALA B 262 N LEU B 234
CRYST1 59.016 106.224 114.356 90.00 90.00 90.00 P 21 21 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 0.016945 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009414 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008745 0.00000
TER 2084 ALA A 289
TER 4185 GLU B 291
MASTER 318 0 0 24 18 0 0 6 4523 2 0 46
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