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HEADER HYDROLASE 25-APR-08 3CXU
TITLE STRUCTURE OF A Y149F MUTANT OF EPOXIDE HYDROLASE FROM
TITLE 2 SOLANUM TUBEROSUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPOXIDE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.3.2.10;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SOLANUM TUBEROSUM;
SOURCE 3 ORGANISM_COMMON: POTATO;
SOURCE 4 STRAIN: LEHMI RUSSET;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: XL1-BLUE;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGTACSTEH1-5H-Y149F
KEYWDS EPOXIDE HYDROLASE, ALPHA/BETA HYDROLASE FOLD, Y149F, PROTON
KEYWDS 2 WIRE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.NAWORYTA,S.L.MOWBRAY,M.WIDERSTEN,A.THOMAEUS
REVDAT 1 08-JUL-08 3CXU 0
JRNL AUTH A.THOMAEUS,A.NAWORYTA,S.L.MOWBRAY,M.WIDERSTEN
JRNL TITL REMOVAL OF DISTAL PROTEIN-WATER HYDROGEN BONDS IN
JRNL TITL 2 A PLANT EPOXIDE HYDROLASE INCREASES CATALYTIC
JRNL TITL 3 TURNOVER BUT DECREASES THERMOSTABILITY
JRNL REF PROTEIN SCI. V. 17 1275 2008
JRNL REFN ASTM PRCIEI US ISSN 0961-8368
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.L.MOWBRAY,L.T.ELFSTROM,K.M.AHLGREN,C.E.ANDERSSON,
REMARK 1 AUTH 2 M.WIDERSTEN
REMARK 1 TITL X-RAY STRUCTURE OF POTATO EPOXIDE HYDROLASE SHEDS
REMARK 1 TITL 2 LIGHT ON SUBSTRATE SPECIFICITY IN PLANT ENZYMES
REMARK 1 REF PROTEIN SCI. V. 15 1628 2006
REMARK 1 REFN ASTM PRCIEI US ISSN 0961-8368
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC5
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 45367
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) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.109
REMARK 3 FREE R VALUE TEST SET COUNT : 2318
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5113
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 654
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.65
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.14400
REMARK 3 B22 (A**2) : -0.05700
REMARK 3 B33 (A**2) : -0.08800
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): 0.185
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.152
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.092
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.206
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3CXU COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB047345.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAR-2007
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0723
REMARK 200 MONOCHROMATOR : SINGLE SILICON (111)
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : SINGLE SILICON (111)
REMARK 200 MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45424
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.1000
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) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.15600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 8.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2CJP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 10000, 0.1M HEPES, PH 7.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 27.98450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.10750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.37450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.10750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.98450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.37450
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
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: 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 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 35 -165.89 -120.23
REMARK 500 ASP A 105 -122.16 64.00
REMARK 500 SER A 129 -57.20 76.77
REMARK 500 ALA A 299 -145.11 -107.54
REMARK 500 GLU B 35 -164.70 -117.01
REMARK 500 ALA B 93 55.93 -140.31
REMARK 500 ASP B 105 -122.61 61.18
REMARK 500 SER B 129 -58.92 77.69
REMARK 500 ALA B 299 -141.67 -111.11
REMARK 500 PHE B 301 58.25 -90.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M=MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 520 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH A 992 DISTANCE = 6.68 ANGSTROMS
REMARK 525 HOH A 995 DISTANCE = 8.76 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: PG4 BINDING SITE FOR RESIDUE A 656
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2CJP RELATED DB: PDB
REMARK 900 STRUCTURE OF POTATO (SOLANUM TUBEROSUM) EPOXIDE HYDROLASE I
REMARK 900 (STEH1)
DBREF 3CXU A 1 321 UNP Q41415 Q41415_SOLTU 1 321
DBREF 3CXU B 1 321 UNP Q41415 Q41415_SOLTU 1 321
SEQADV 3CXU THR A -6 UNP Q41415 EXPRESSION TAG
SEQADV 3CXU SER A -5 UNP Q41415 EXPRESSION TAG
SEQADV 3CXU HIS A -4 UNP Q41415 EXPRESSION TAG
SEQADV 3CXU HIS A -3 UNP Q41415 EXPRESSION TAG
SEQADV 3CXU HIS A -2 UNP Q41415 EXPRESSION TAG
SEQADV 3CXU HIS A -1 UNP Q41415 EXPRESSION TAG
SEQADV 3CXU HIS A 0 UNP Q41415 EXPRESSION TAG
SEQADV 3CXU LYS A 2 UNP Q41415 GLU 2 CONFLICT
SEQADV 3CXU PHE A 149 UNP Q41415 TYR 149 ENGINEERED
SEQADV 3CXU THR B -6 UNP Q41415 EXPRESSION TAG
SEQADV 3CXU SER B -5 UNP Q41415 EXPRESSION TAG
SEQADV 3CXU HIS B -4 UNP Q41415 EXPRESSION TAG
SEQADV 3CXU HIS B -3 UNP Q41415 EXPRESSION TAG
SEQADV 3CXU HIS B -2 UNP Q41415 EXPRESSION TAG
SEQADV 3CXU HIS B -1 UNP Q41415 EXPRESSION TAG
SEQADV 3CXU HIS B 0 UNP Q41415 EXPRESSION TAG
SEQADV 3CXU LYS B 2 UNP Q41415 GLU 2 CONFLICT
SEQADV 3CXU PHE B 149 UNP Q41415 TYR 149 ENGINEERED
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 PHE
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 PHE
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 A 656 13
HETNAM PG4 TETRAETHYLENE GLYCOL
FORMUL 3 PG4 C8 H18 O5
FORMUL 4 HOH *654(H2 O)
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 ALA A 169 1 8
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 ASN A 279 1 8
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 GLU B 49 1 10
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 ALA B 237 1 10
HELIX 32 32 ALA B 237 THR B 245 1 9
HELIX 33 33 ALA B 246 THR B 249 5 4
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 A 8 GLU A 5 VAL A 11 0
SHEET 2 A 8 LEU A 14 LEU A 21 -1 O LEU A 18 N LYS A 7
SHEET 3 A 8 ARG A 53 PRO A 57 -1 O ALA A 56 N ALA A 19
SHEET 4 A 8 THR A 26 ILE A 30 1 N PHE A 29 O VAL A 55
SHEET 5 A 8 VAL A 99 HIS A 104 1 O VAL A 102 N LEU A 28
SHEET 6 A 8 VAL A 122 LEU A 128 1 O VAL A 126 N VAL A 101
SHEET 7 A 8 THR A 257 GLY A 262 1 O LYS A 258 N LEU A 125
SHEET 8 A 8 VAL A 293 LEU A 295 1 O VAL A 293 N PHE A 259
SHEET 1 B 8 GLU B 5 VAL B 11 0
SHEET 2 B 8 LEU B 14 LEU B 21 -1 O LEU B 18 N LYS B 7
SHEET 3 B 8 ARG B 53 PRO B 57 -1 O ALA B 56 N ALA B 19
SHEET 4 B 8 THR B 26 ILE B 30 1 N PHE B 29 O VAL B 55
SHEET 5 B 8 VAL B 99 HIS B 104 1 O VAL B 102 N LEU B 28
SHEET 6 B 8 VAL B 122 LEU B 128 1 O LYS B 123 N VAL B 99
SHEET 7 B 8 THR B 257 GLY B 262 1 O LYS B 258 N LEU B 125
SHEET 8 B 8 VAL B 293 LEU B 295 1 O LEU B 295 N VAL B 261
CISPEP 1 PHE A 33 PRO A 34 0 -10.72
CISPEP 2 PHE B 33 PRO B 34 0 -8.49
SITE 1 AC1 5 ASP A 105 TRP A 106 HIS A 131 PHE A 132
SITE 2 AC1 5 SER A 133
CRYST1 55.969 96.749 122.215 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 0.017867 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010336 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008182 0.00000
TER 2562 PHE A 321
TER 5115 PHE B 321
MASTER 279 0 1 37 16 0 2 6 5780 2 13 52
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