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HEADER HYDROLASE 04-APR-06 2CJP
TITLE STRUCTURE OF POTATO (SOLANUM TUBEROSUM) EPOXIDE HYDROLASE I
TITLE 2 (STEH1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPOXIDE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.3.2.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 3 EXPRESSION_SYSTEM_STRAIN: XL1-BLUE;
SOURCE 4 EXPRESSION_SYSTEM_PLASMID: PGTACSTEH1-5H;
SOURCE 5 ORGANISM_SCIENTIFIC: SOLANUM TUBEROSUM;
SOURCE 6 ORGANISM_COMMON: POTATO;
SOURCE 7 STRAIN: LEMHI RUSSET
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.L.MOWBRAY,L.T.ELFSTROM,K.M.AHLGREN,C.E.ANDERSSON,
AUTHOR 2 M.WIDERSTEN
REVDAT 2 15-JUN-06 2CJP 1 JRNL REMARK
REVDAT 1 07-JUN-06 2CJP 0
JRNL AUTH S.L.MOWBRAY,L.T.ELFSTROM,K.M.AHLGREN,
JRNL AUTH 2 C.E.ANDERSSON,M.WIDERSTEN
JRNL TITL X-RAY STRUCTURE OF POTATO EPOXIDE HYDROLASE SHEDS
JRNL TITL 2 LIGHT ON SUBSTRATE SPECIFICITY IN PLANT ENZYMES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.00
REMARK 3 NUMBER OF REFLECTIONS : 47002
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) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 2510
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.950
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.000
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3369
REMARK 3 BIN R VALUE (WORKING SET) : 0.286
REMARK 3 BIN FREE R VALUE SET COUNT : 178
REMARK 3 BIN FREE R VALUE : 0.299
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5115
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 405
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.406
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.803
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.26
REMARK 3 B22 (A**2) : 2.73
REMARK 3 B33 (A**2) : -1.47
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.19
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.16
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.13
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.577
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED (A): 5301 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED (DEGREES): 7202 ; 1.064 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 637 ; 5.248 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 240 ;34.025 ;23.833
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 844 ;12.822 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;17.744 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 764 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED (A): 4068 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED (A): 2384 ; 0.179 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED (A): 3529 ; 0.303 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED (A): 378 ; 0.104 ; 0.200
REMARK 3 SYMMETRY VDW REFINED (A): 37 ; 0.144 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED (A): 14 ; 0.136 ; 0.200
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): 3276 ; 0.475 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): 5142 ; 0.823 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): 2340 ; 0.957 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): 2060 ; 1.512 ; 4.500
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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. RESIDUE 1 OF THE A CHAIN,
REMARK 3 AND 2-3 OF THE B CHAIN WERE OMITTED BECAUSE OF DISORDER.
REMARK 3 THE PROTEIN WAS EXPRESSED WITH AN ADDITIONAL SEQUENCE AT
REMARK 3 THE C-TERMINUS, TSHHHHH, WHICH WAS ALSO NOT VISIBLE IN THE
REMARK 3 ELECTRON DENSITY.
REMARK 4
REMARK 4 2CJP COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 6-APR-2006.
REMARK 100 THE EBI ID CODE IS EBI-28405.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-AUG-2004
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF BEAMLINE ID14-EH2
REMARK 200 BEAMLINE : ID14-EH2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49514
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.95
REMARK 200 RESOLUTION RANGE LOW (A) : 31.60
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 5.1
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.90
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 5.0
REMARK 200 R MERGE FOR SHELL (I) : 0.47
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.10
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 1VJ5
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 UL DROPS OF PROTEIN SOLUTION
REMARK 280 (7.2 MG/ML, I.E. 0.2 MM, IN 30 MM TRIS-HCL, PH 7.4, 5 MM
REMARK 280 VALPROMIDE) WERE MIXED WITH 1 UL DROPS OF RESERVOIR
REMARK 280 SOLUTION (CONTAINING 90 MM NA-HEPES, PH 7.5, 25% PEG 10,
REMARK 280 000), AND EQUILIBRATED BY SITTING-DROP VAPOR DIFFUSION AT
REMARK 280 ROOM TEMPERATURE.
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 27.96300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.01650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.26600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.01650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.96300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.26600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 295
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS
REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.
REMARK 295
REMARK 295 APPLIED TO TRANSFORMED TO
REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD
REMARK 295 M 1 B 3 .. 321 A 2 .. 321 0.400
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: MONOMERIC
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 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 THR A -6
REMARK 465 SER A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 THR B -6
REMARK 465 SER B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 LYS B 2
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 B 18 CA - CB - CG ANGL. DEV. = 6.8 DEGREES
REMARK 500 PRO B 34 C - N - CA ANGL. DEV. = 8.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 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 129 -53.50 75.91
REMARK 500 SER B 129 -60.28 76.79
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY
REMARK 525 ASSOCIATED WITH:
REMARK 525 PROTEIN CHAIN SOLVENT CHAIN
REMARK 525 A Z
REMARK 525 B Y
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: PG4 BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: VPR BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: EDO BINDING SITE FOR CHAIN B
DBREF 2CJP A -6 0 PDB 2CJP 2CJP -6 0
DBREF 2CJP A 1 321 UNP Q41415 Q41415_SOLTU 1 321
DBREF 2CJP B -6 0 PDB 2CJP 2CJP -6 0
DBREF 2CJP B 1 321 UNP Q41415 Q41415_SOLTU 1 321
SEQADV 2CJP LYS A 2 UNP Q41415 GLU 2 CONFLICT
SEQRES 1 A 328 THR SER HIS HIS HIS HIS HIS MET LYS LYS ILE GLU HIS
SEQRES 2 A 328 LYS MET VAL ALA VAL ASN GLY LEU ASN MET HIS LEU ALA
SEQRES 3 A 328 GLU LEU GLY GLU GLY PRO THR ILE LEU PHE ILE HIS GLY
SEQRES 4 A 328 PHE PRO GLU LEU TRP TYR SER TRP ARG HIS GLN MET VAL
SEQRES 5 A 328 TYR LEU ALA GLU ARG GLY TYR ARG ALA VAL ALA PRO ASP
SEQRES 6 A 328 LEU ARG GLY TYR GLY ASP THR THR GLY ALA PRO LEU ASN
SEQRES 7 A 328 ASP PRO SER LYS PHE SER ILE LEU HIS LEU VAL GLY ASP
SEQRES 8 A 328 VAL VAL ALA LEU LEU GLU ALA ILE ALA PRO ASN GLU GLU
SEQRES 9 A 328 LYS VAL PHE VAL VAL ALA HIS ASP TRP GLY ALA LEU ILE
SEQRES 10 A 328 ALA TRP HIS LEU CYS LEU PHE ARG PRO ASP LYS VAL LYS
SEQRES 11 A 328 ALA LEU VAL ASN LEU SER VAL HIS PHE SER LYS ARG ASN
SEQRES 12 A 328 PRO LYS MET ASN VAL VAL GLU GLY LEU LYS ALA ILE TYR
SEQRES 13 A 328 GLY GLU ASP HIS TYR ILE SER ARG PHE GLN VAL PRO GLY
SEQRES 14 A 328 GLU ILE GLU ALA GLU PHE ALA PRO ILE GLY ALA LYS SER
SEQRES 15 A 328 VAL LEU LYS LYS ILE LEU THR TYR ARG ASP PRO ALA PRO
SEQRES 16 A 328 PHE TYR PHE PRO LYS GLY LYS GLY LEU GLU ALA ILE PRO
SEQRES 17 A 328 ASP ALA PRO VAL ALA LEU SER SER TRP LEU SER GLU GLU
SEQRES 18 A 328 GLU LEU ASP TYR TYR ALA ASN LYS PHE GLU GLN THR GLY
SEQRES 19 A 328 PHE THR GLY ALA VAL ASN TYR TYR ARG ALA LEU PRO ILE
SEQRES 20 A 328 ASN TRP GLU LEU THR ALA PRO TRP THR GLY ALA GLN VAL
SEQRES 21 A 328 LYS VAL PRO THR LYS PHE ILE VAL GLY GLU PHE ASP LEU
SEQRES 22 A 328 VAL TYR HIS ILE PRO GLY ALA LYS GLU TYR ILE HIS ASN
SEQRES 23 A 328 GLY GLY PHE LYS LYS ASP VAL PRO LEU LEU GLU GLU VAL
SEQRES 24 A 328 VAL VAL LEU GLU GLY ALA ALA HIS PHE VAL SER GLN GLU
SEQRES 25 A 328 ARG PRO HIS GLU ILE SER LYS HIS ILE TYR ASP PHE ILE
SEQRES 26 A 328 GLN LYS PHE
SEQRES 1 B 328 THR SER HIS HIS HIS HIS HIS MET LYS LYS ILE GLU HIS
SEQRES 2 B 328 LYS MET VAL ALA VAL ASN GLY LEU ASN MET HIS LEU ALA
SEQRES 3 B 328 GLU LEU GLY GLU GLY PRO THR ILE LEU PHE ILE HIS GLY
SEQRES 4 B 328 PHE PRO GLU LEU TRP TYR SER TRP ARG HIS GLN MET VAL
SEQRES 5 B 328 TYR LEU ALA GLU ARG GLY TYR ARG ALA VAL ALA PRO ASP
SEQRES 6 B 328 LEU ARG GLY TYR GLY ASP THR THR GLY ALA PRO LEU ASN
SEQRES 7 B 328 ASP PRO SER LYS PHE SER ILE LEU HIS LEU VAL GLY ASP
SEQRES 8 B 328 VAL VAL ALA LEU LEU GLU ALA ILE ALA PRO ASN GLU GLU
SEQRES 9 B 328 LYS VAL PHE VAL VAL ALA HIS ASP TRP GLY ALA LEU ILE
SEQRES 10 B 328 ALA TRP HIS LEU CYS LEU PHE ARG PRO ASP LYS VAL LYS
SEQRES 11 B 328 ALA LEU VAL ASN LEU SER VAL HIS PHE SER LYS ARG ASN
SEQRES 12 B 328 PRO LYS MET ASN VAL VAL GLU GLY LEU LYS ALA ILE TYR
SEQRES 13 B 328 GLY GLU ASP HIS TYR ILE SER ARG PHE GLN VAL PRO GLY
SEQRES 14 B 328 GLU ILE GLU ALA GLU PHE ALA PRO ILE GLY ALA LYS SER
SEQRES 15 B 328 VAL LEU LYS LYS ILE LEU THR TYR ARG ASP PRO ALA PRO
SEQRES 16 B 328 PHE TYR PHE PRO LYS GLY LYS GLY LEU GLU ALA ILE PRO
SEQRES 17 B 328 ASP ALA PRO VAL ALA LEU SER SER TRP LEU SER GLU GLU
SEQRES 18 B 328 GLU LEU ASP TYR TYR ALA ASN LYS PHE GLU GLN THR GLY
SEQRES 19 B 328 PHE THR GLY ALA VAL ASN TYR TYR ARG ALA LEU PRO ILE
SEQRES 20 B 328 ASN TRP GLU LEU THR ALA PRO TRP THR GLY ALA GLN VAL
SEQRES 21 B 328 LYS VAL PRO THR LYS PHE ILE VAL GLY GLU PHE ASP LEU
SEQRES 22 B 328 VAL TYR HIS ILE PRO GLY ALA LYS GLU TYR ILE HIS ASN
SEQRES 23 B 328 GLY GLY PHE LYS LYS ASP VAL PRO LEU LEU GLU GLU VAL
SEQRES 24 B 328 VAL VAL LEU GLU GLY ALA ALA HIS PHE VAL SER GLN GLU
SEQRES 25 B 328 ARG PRO HIS GLU ILE SER LYS HIS ILE TYR ASP PHE ILE
SEQRES 26 B 328 GLN LYS PHE
HET PG4 A1322 13
HET VPR B1322 10
HET EDO B1323 4
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
HETNAM PG4 TETRAETHYLENE GLYCOL
HETSYN PG4 POLYETHYLENE GLYCOL PEG400
HETNAM VPR 2-PROPYLPENTANAMIDE
FORMUL 3 EDO C2 H6 O2
FORMUL 4 PG4 C8 H18 O5
FORMUL 5 VPR C8 H17 N1 O1
FORMUL 6 HOH *405(H2 O1)
HELIX 1 1 LEU A 36 SER A 39 5 4
HELIX 2 2 TRP A 40 GLU A 49 1 10
HELIX 3 3 ASP A 72 PHE A 76 5 5
HELIX 4 4 SER A 77 ALA A 93 1 17
HELIX 5 5 ASP A 105 ARG A 118 1 14
HELIX 6 6 ASN A 140 GLY A 150 1 11
HELIX 7 7 HIS A 153 PHE A 158 1 6
HELIX 8 8 GLY A 162 GLY A 172 1 11
HELIX 9 9 GLY A 172 THR A 182 1 11
HELIX 10 10 PRO A 204 SER A 209 5 6
HELIX 11 11 SER A 212 GLY A 227 1 16
HELIX 12 12 PHE A 228 ALA A 237 1 10
HELIX 13 13 ALA A 237 THR A 245 1 9
HELIX 14 14 ALA A 246 THR A 249 5 4
HELIX 15 15 ASP A 265 ILE A 270 5 6
HELIX 16 16 GLY A 272 GLY A 280 1 9
HELIX 17 17 GLY A 280 VAL A 286 1 7
HELIX 18 18 PHE A 301 ARG A 306 1 6
HELIX 19 19 ARG A 306 GLN A 319 1 14
HELIX 20 20 LEU B 36 SER B 39 5 4
HELIX 21 21 TRP B 40 ARG B 50 1 11
HELIX 22 22 ASP B 72 PHE B 76 5 5
HELIX 23 23 SER B 77 ALA B 93 1 17
HELIX 24 24 ASP B 105 ARG B 118 1 14
HELIX 25 25 ASN B 140 GLY B 150 1 11
HELIX 26 26 HIS B 153 PHE B 158 1 6
HELIX 27 27 GLY B 162 ALA B 169 1 8
HELIX 28 28 GLY B 172 THR B 182 1 11
HELIX 29 29 PRO B 204 SER B 209 5 6
HELIX 30 30 SER B 212 GLY B 227 1 16
HELIX 31 31 PHE B 228 THR B 245 1 18
HELIX 32 32 ALA B 246 THR B 249 5 4
HELIX 33 33 ASP B 265 ILE B 270 5 6
HELIX 34 34 GLY B 272 ASN B 279 1 8
HELIX 35 35 GLY B 280 VAL B 286 1 7
HELIX 36 36 PHE B 301 ARG B 306 1 6
HELIX 37 37 ARG B 306 GLN B 319 1 14
SHEET 1 AA 8 GLU A 5 VAL A 11 0
SHEET 2 AA 8 LEU A 14 LEU A 21 -1 O LEU A 14 N VAL A 11
SHEET 3 AA 8 ARG A 53 PRO A 57 -1 O ALA A 54 N LEU A 21
SHEET 4 AA 8 THR A 26 ILE A 30 1 O ILE A 27 N VAL A 55
SHEET 5 AA 8 VAL A 99 HIS A 104 1 O PHE A 100 N LEU A 28
SHEET 6 AA 8 VAL A 122 LEU A 128 1 N LYS A 123 O VAL A 99
SHEET 7 AA 8 THR A 257 GLY A 262 1 O LYS A 258 N ASN A 127
SHEET 8 AA 8 VAL A 293 LEU A 295 1 O VAL A 293 N VAL A 261
SHEET 1 BA 8 GLU B 5 VAL B 11 0
SHEET 2 BA 8 LEU B 14 LEU B 21 -1 O LEU B 14 N VAL B 11
SHEET 3 BA 8 ARG B 53 PRO B 57 -1 O ALA B 54 N LEU B 21
SHEET 4 BA 8 THR B 26 ILE B 30 1 O ILE B 27 N VAL B 55
SHEET 5 BA 8 VAL B 99 HIS B 104 1 O PHE B 100 N LEU B 28
SHEET 6 BA 8 VAL B 122 LEU B 128 1 N LYS B 123 O VAL B 99
SHEET 7 BA 8 THR B 257 GLY B 262 1 O LYS B 258 N ASN B 127
SHEET 8 BA 8 VAL B 293 LEU B 295 1 O VAL B 293 N VAL B 261
CISPEP 1 PHE A 33 PRO A 34 0 -7.95
CISPEP 2 PHE B 33 PRO B 34 0 -11.24
SITE 1 AC1 4 ASP A 105 TRP A 106 LEU A 109 HOH Z 202
SITE 1 AC2 9 PHE B 33 ASP B 105 TYR B 154 ILE B 180
SITE 2 AC2 9 PHE B 189 LEU B 266 HIS B 300 PHE B 301
SITE 3 AC2 9 HOH Y 203
SITE 1 AC3 3 ASP B 105 TRP B 106 HOH Y 203
CRYST1 55.926 98.532 122.033 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 0.017881 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010149 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008195 0.00000
MTRIX1 1 0.703500 0.665300 -0.250100 -19.89670 1
MTRIX2 1 0.691000 -0.557800 0.459800 106.97270 1
MTRIX3 1 0.166400 -0.496300 -0.852100 85.47320 1
TER 2563 PHE A 321
TER 5117 PHE B 321
MASTER 317 0 3 37 16 0 5 9 5547 2 27 52
END |