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HEADER HYDROLASE 17-MAR-15 4UFO
TITLE LABORATORY EVOLVED VARIANT R-C1B1D33E6 OF POTATO EPOXIDE
TITLE 2 HYDROLASE 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;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SOLANUM TUBEROSUM;
SOURCE 3 ORGANISM_COMMON: POTATO;
SOURCE 4 ORGANISM_TAXID: 4113;
SOURCE 5 STRAIN: LEMHI RUSSET;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: XL1 BLUE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGTACSTEH1-5H
KEYWDS HYDROLASE, EPOXIDE HYDROLYSIS, ALPHA/BETA-HYDROLASE, DIRECTED
KEYWDS 2 EVOLUTION, ASYMMETRIC SYNTHESES
EXPDTA X-RAY DIFFRACTION
AUTHOR A.J.CARLSSON,P.BAUER,M.NILSSON,D.DOBRITZSCH,S.C.L.KAMERLIN,
AUTHOR 2 M.WIDERSTEN
REVDAT 1 13-APR-16 4UFO 0
JRNL AUTH A.J.CARLSSON,P.BAUER,M.NILSSON,D.DOBRITZSCH,S.C.L.KAMERLIN,
JRNL AUTH 2 M.WIDERSTEN
JRNL TITL PROBING INFLUENCE OF ACTIVE-SITE VOLUME TO CATALYSIS:
JRNL TITL 2 LABORATORY EVOLVED EPOXIDE HYDROLASES AS MODEL ENZYMES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.02 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0069
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,
REMARK 3 STEINER,NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.02
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 76.75
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.95
REMARK 3 NUMBER OF REFLECTIONS : 42775
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) : 0.19115
REMARK 3 R VALUE (WORKING SET) : 0.18907
REMARK 3 FREE R VALUE : 0.23182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.9
REMARK 3 FREE R VALUE TEST SET COUNT : 2208
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) : 2.020
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.072
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3131
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.291
REMARK 3 BIN FREE R VALUE SET COUNT : 153
REMARK 3 BIN FREE R VALUE : 0.298
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5117
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 350
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.1
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.572
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.69
REMARK 3 B22 (A**2) : 1.96
REMARK 3 B33 (A**2) : -1.27
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): 0.199
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.170
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.137
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.134
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5277 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5033 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7173 ; 1.389 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11603 ; 1.055 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 641 ; 5.194 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 238 ;31.097 ;23.866
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 856 ;12.663 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;19.570 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 765 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5918 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1230 ; 0.005 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION 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): 2564 ; 2.201 ; 3.551
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2563 ; 2.199 ; 3.551
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3202 ; 3.098 ; 5.315
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2713 ; 2.680 ; 3.825
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 2 320 B 2 320 19327 0.12 0.05
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 RIDING
REMARK 3 POSITIONS. U VALUES REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4UFO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-MAR-15.
REMARK 100 THE PDBE ID CODE IS EBI-63382.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL (PILATUS 6M)
REMARK 200 DETECTOR MANUFACTURER : DECTRIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45055
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.02
REMARK 200 RESOLUTION RANGE LOW (A) : 76.75
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.5
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.10
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.4
REMARK 200 R MERGE FOR SHELL (I) : 0.84
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2CJP
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.3
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% (W/V) PEG5K-MME, 0.1 M TRIS PH 8.5
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 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-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 27.83900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.28550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.22200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.28550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.83900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.22200
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 MET A 1
REMARK 465 SER A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
REMARK 465 HIS A 326
REMARK 465 HIS A 327
REMARK 465 HIS A 328
REMARK 465 MET B 1
REMARK 465 THR B 322
REMARK 465 SER B 323
REMARK 465 HIS B 324
REMARK 465 HIS B 325
REMARK 465 HIS B 326
REMARK 465 HIS B 327
REMARK 465 HIS B 328
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE1 GLU A 309 O HOH A 2177 2.19
REMARK 500 O B HOH A 2003 O HOH A 2010 0.00
REMARK 500 O HOH A 2041 O HOH A 2046 2.09
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
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 -166.95 -121.61
REMARK 500 ASP A 105 -126.41 60.73
REMARK 500 SER A 129 -51.76 77.91
REMARK 500 ALA A 299 -150.19 -99.05
REMARK 500 GLU B 35 -164.76 -121.95
REMARK 500 ASP B 105 -126.22 60.72
REMARK 500 SER B 129 -56.62 75.10
REMARK 500 ALA B 299 -152.04 -98.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UFN RELATED DB: PDB
REMARK 900 LABORATORY EVOLVED VARIANT R-C1B1 OF POTATO EPOXIDE
REMARK 900 HYDROLASE STEH1
REMARK 900 RELATED ID: 4UFP RELATED DB: PDB
REMARK 900 LABORATORY EVOLVED VARIANT R-C1B1D33 OF POTATO EPOXIDE
REMARK 900 HYDROLASE STEH1
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE IS C-TERMINALLY HIS-TAGGED AND IS MUTATED AT
REMARK 999 7 POSITIONS (P84L, W106L, L109Y, V141K, I155V, F189L,
REMARK 999 L266G)
DBREF 4UFO A 1 321 UNP Q41415 Q41415_SOLTU 1 321
DBREF 4UFO B 1 321 UNP Q41415 Q41415_SOLTU 1 321
SEQADV 4UFO LYS A 2 UNP Q41415 GLU 2 CLONING ARTIFACT
SEQADV 4UFO LEU A 94 UNP Q41415 PRO 94 ENGINEERED MUTATION
SEQADV 4UFO LEU A 106 UNP Q41415 TRP 106 ENGINEERED MUTATION
SEQADV 4UFO TYR A 109 UNP Q41415 LEU 109 ENGINEERED MUTATION
SEQADV 4UFO LYS A 141 UNP Q41415 VAL 141 ENGINEERED MUTATION
SEQADV 4UFO VAL A 155 UNP Q41415 ILE 155 ENGINEERED MUTATION
SEQADV 4UFO LEU A 189 UNP Q41415 PHE 189 ENGINEERED MUTATION
SEQADV 4UFO GLY A 266 UNP Q41415 LEU 266 ENGINEERED MUTATION
SEQADV 4UFO THR A 322 UNP Q41415 EXPRESSION TAG
SEQADV 4UFO SER A 323 UNP Q41415 EXPRESSION TAG
SEQADV 4UFO HIS A 324 UNP Q41415 EXPRESSION TAG
SEQADV 4UFO HIS A 325 UNP Q41415 EXPRESSION TAG
SEQADV 4UFO HIS A 326 UNP Q41415 EXPRESSION TAG
SEQADV 4UFO HIS A 327 UNP Q41415 EXPRESSION TAG
SEQADV 4UFO HIS A 328 UNP Q41415 EXPRESSION TAG
SEQADV 4UFO LYS B 2 UNP Q41415 GLU 2 CLONING ARTIFACT
SEQADV 4UFO LEU B 94 UNP Q41415 PRO 94 ENGINEERED MUTATION
SEQADV 4UFO LEU B 106 UNP Q41415 TRP 106 ENGINEERED MUTATION
SEQADV 4UFO TYR B 109 UNP Q41415 LEU 109 ENGINEERED MUTATION
SEQADV 4UFO LYS B 141 UNP Q41415 VAL 141 ENGINEERED MUTATION
SEQADV 4UFO VAL B 155 UNP Q41415 ILE 155 ENGINEERED MUTATION
SEQADV 4UFO LEU B 189 UNP Q41415 PHE 189 ENGINEERED MUTATION
SEQADV 4UFO GLY B 266 UNP Q41415 LEU 266 ENGINEERED MUTATION
SEQADV 4UFO THR B 322 UNP Q41415 EXPRESSION TAG
SEQADV 4UFO SER B 323 UNP Q41415 EXPRESSION TAG
SEQADV 4UFO HIS B 324 UNP Q41415 EXPRESSION TAG
SEQADV 4UFO HIS B 325 UNP Q41415 EXPRESSION TAG
SEQADV 4UFO HIS B 326 UNP Q41415 EXPRESSION TAG
SEQADV 4UFO HIS B 327 UNP Q41415 EXPRESSION TAG
SEQADV 4UFO HIS B 328 UNP Q41415 EXPRESSION TAG
SEQRES 1 A 328 MET LYS LYS ILE GLU HIS LYS MET VAL ALA VAL ASN GLY
SEQRES 2 A 328 LEU ASN MET HIS LEU ALA GLU LEU GLY GLU GLY PRO THR
SEQRES 3 A 328 ILE LEU PHE ILE HIS GLY PHE PRO GLU LEU TRP TYR SER
SEQRES 4 A 328 TRP ARG HIS GLN MET VAL TYR LEU ALA GLU ARG GLY TYR
SEQRES 5 A 328 ARG ALA VAL ALA PRO ASP LEU ARG GLY TYR GLY ASP THR
SEQRES 6 A 328 THR GLY ALA PRO LEU ASN ASP PRO SER LYS PHE SER ILE
SEQRES 7 A 328 LEU HIS LEU VAL GLY ASP VAL VAL ALA LEU LEU GLU ALA
SEQRES 8 A 328 ILE ALA LEU ASN GLU GLU LYS VAL PHE VAL VAL ALA HIS
SEQRES 9 A 328 ASP LEU GLY ALA TYR ILE ALA TRP HIS LEU CYS LEU PHE
SEQRES 10 A 328 ARG PRO ASP LYS VAL LYS ALA LEU VAL ASN LEU SER VAL
SEQRES 11 A 328 HIS PHE SER LYS ARG ASN PRO LYS MET ASN LYS VAL GLU
SEQRES 12 A 328 GLY LEU LYS ALA ILE TYR GLY GLU ASP HIS TYR VAL SER
SEQRES 13 A 328 ARG PHE GLN VAL PRO GLY GLU ILE GLU ALA GLU PHE ALA
SEQRES 14 A 328 PRO ILE GLY ALA LYS SER VAL LEU LYS LYS ILE LEU THR
SEQRES 15 A 328 TYR ARG ASP PRO ALA PRO LEU TYR PHE PRO LYS GLY LYS
SEQRES 16 A 328 GLY LEU GLU ALA ILE PRO ASP ALA PRO VAL ALA LEU SER
SEQRES 17 A 328 SER TRP LEU SER GLU GLU GLU LEU ASP TYR TYR ALA ASN
SEQRES 18 A 328 LYS PHE GLU GLN THR GLY PHE THR GLY ALA VAL ASN TYR
SEQRES 19 A 328 TYR ARG ALA LEU PRO ILE ASN TRP GLU LEU THR ALA PRO
SEQRES 20 A 328 TRP THR GLY ALA GLN VAL LYS VAL PRO THR LYS PHE ILE
SEQRES 21 A 328 VAL GLY GLU PHE ASP GLY VAL TYR HIS ILE PRO GLY ALA
SEQRES 22 A 328 LYS GLU TYR ILE HIS ASN GLY GLY PHE LYS LYS ASP VAL
SEQRES 23 A 328 PRO LEU LEU GLU GLU VAL VAL VAL LEU GLU GLY ALA ALA
SEQRES 24 A 328 HIS PHE VAL SER GLN GLU ARG PRO HIS GLU ILE SER LYS
SEQRES 25 A 328 HIS ILE TYR ASP PHE ILE GLN LYS PHE THR SER HIS HIS
SEQRES 26 A 328 HIS HIS HIS
SEQRES 1 B 328 MET LYS LYS ILE GLU HIS LYS MET VAL ALA VAL ASN GLY
SEQRES 2 B 328 LEU ASN MET HIS LEU ALA GLU LEU GLY GLU GLY PRO THR
SEQRES 3 B 328 ILE LEU PHE ILE HIS GLY PHE PRO GLU LEU TRP TYR SER
SEQRES 4 B 328 TRP ARG HIS GLN MET VAL TYR LEU ALA GLU ARG GLY TYR
SEQRES 5 B 328 ARG ALA VAL ALA PRO ASP LEU ARG GLY TYR GLY ASP THR
SEQRES 6 B 328 THR GLY ALA PRO LEU ASN ASP PRO SER LYS PHE SER ILE
SEQRES 7 B 328 LEU HIS LEU VAL GLY ASP VAL VAL ALA LEU LEU GLU ALA
SEQRES 8 B 328 ILE ALA LEU ASN GLU GLU LYS VAL PHE VAL VAL ALA HIS
SEQRES 9 B 328 ASP LEU GLY ALA TYR ILE ALA TRP HIS LEU CYS LEU PHE
SEQRES 10 B 328 ARG PRO ASP LYS VAL LYS ALA LEU VAL ASN LEU SER VAL
SEQRES 11 B 328 HIS PHE SER LYS ARG ASN PRO LYS MET ASN LYS VAL GLU
SEQRES 12 B 328 GLY LEU LYS ALA ILE TYR GLY GLU ASP HIS TYR VAL SER
SEQRES 13 B 328 ARG PHE GLN VAL PRO GLY GLU ILE GLU ALA GLU PHE ALA
SEQRES 14 B 328 PRO ILE GLY ALA LYS SER VAL LEU LYS LYS ILE LEU THR
SEQRES 15 B 328 TYR ARG ASP PRO ALA PRO LEU TYR PHE PRO LYS GLY LYS
SEQRES 16 B 328 GLY LEU GLU ALA ILE PRO ASP ALA PRO VAL ALA LEU SER
SEQRES 17 B 328 SER TRP LEU SER GLU GLU GLU LEU ASP TYR TYR ALA ASN
SEQRES 18 B 328 LYS PHE GLU GLN THR GLY PHE THR GLY ALA VAL ASN TYR
SEQRES 19 B 328 TYR ARG ALA LEU PRO ILE ASN TRP GLU LEU THR ALA PRO
SEQRES 20 B 328 TRP THR GLY ALA GLN VAL LYS VAL PRO THR LYS PHE ILE
SEQRES 21 B 328 VAL GLY GLU PHE ASP GLY VAL TYR HIS ILE PRO GLY ALA
SEQRES 22 B 328 LYS GLU TYR ILE HIS ASN GLY GLY PHE LYS LYS ASP VAL
SEQRES 23 B 328 PRO LEU LEU GLU GLU VAL VAL VAL LEU GLU GLY ALA ALA
SEQRES 24 B 328 HIS PHE VAL SER GLN GLU ARG PRO HIS GLU ILE SER LYS
SEQRES 25 B 328 HIS ILE TYR ASP PHE ILE GLN LYS PHE THR SER HIS HIS
SEQRES 26 B 328 HIS HIS HIS
FORMUL 3 HOH *350(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 LYS A 320 1 15
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 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 LYS B 320 1 15
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 -8.15
CISPEP 2 PHE B 33 PRO B 34 0 -3.90
CRYST1 55.678 98.444 122.571 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 0.017960 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010158 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008159 0.00000
MTRIX1 1 0.706700 0.688900 0.161300 -73.96000 1
MTRIX2 1 0.662500 -0.564300 -0.492600 116.20000 1
MTRIX3 1 -0.248300 0.455000 -0.855200 18.99000 1
TER 2566 THR A 322
TER 5122 PHE B 321
MASTER 319 0 0 37 16 0 0 9 5471 2 0 52
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