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HEADER HYDROLASE 20-DEC-23 8XIZ
TITLE CRYSTAL STRUCTURE OF AN EPOXIDE HYDROLASE MUTANT A250IC/L344V FROM
TITLE 2 ASPERGILLUS USAMII E001 AT 2.17 ANGSTROMS RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MICROSOMAL EPOXIDE HYDDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.3.2.9;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS USAMII;
SOURCE 3 ORGANISM_TAXID: 186680;
SOURCE 4 GENE: EH2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS ALPHA AND BETA PROTEINS, ALPHA/BETA-HYDROLASES, STYRENE OXIDE,
KEYWDS 2 EPOXIDE HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.C.HU,Z.Y.LU,C.D.TANG,D.HU
REVDAT 1 07-FEB-24 8XIZ 0
JRNL AUTH D.HU,Z.Y.LU
JRNL TITL DIRECTED EVOLUTION OF AN EPOXIDE HYDROLASE AND ITS
JRNL TITL 2 STRUCTURAL MECHANISM FOR THE ENANTIOSELECTIVITY IMPROVEMENT
JRNL TITL 3 TOWARD CHIRAL ORTHO-FLUOROSTYRENE OXIDE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.18 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.18
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.60
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 40335
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.330
REMARK 3 FREE R VALUE TEST SET COUNT : 2148
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 44.6010 - 5.3614 0.98 2655 153 0.1584 0.1828
REMARK 3 2 5.3614 - 4.2565 0.99 2601 146 0.1360 0.1827
REMARK 3 3 4.2565 - 3.7188 0.99 2626 134 0.1426 0.2128
REMARK 3 4 3.7188 - 3.3789 0.99 2580 128 0.1565 0.2161
REMARK 3 5 3.3789 - 3.1368 0.99 2615 119 0.1752 0.2025
REMARK 3 6 3.1368 - 2.9519 0.99 2561 133 0.1814 0.2512
REMARK 3 7 2.9519 - 2.8041 0.99 2581 139 0.1745 0.2371
REMARK 3 8 2.8041 - 2.6820 0.99 2520 154 0.1729 0.2386
REMARK 3 9 2.6820 - 2.5788 0.99 2544 146 0.1756 0.2654
REMARK 3 10 2.5788 - 2.4898 0.98 2561 114 0.1801 0.2727
REMARK 3 11 2.4898 - 2.4120 0.98 2514 156 0.1733 0.2631
REMARK 3 12 2.4120 - 2.3430 0.98 2517 145 0.1771 0.2372
REMARK 3 13 2.3430 - 2.2814 0.98 2517 170 0.1737 0.2471
REMARK 3 14 2.2814 - 2.2257 0.98 2501 147 0.1733 0.2440
REMARK 3 15 2.2257 - 2.1751 0.90 2294 164 0.1745 0.2609
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.850
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 6502
REMARK 3 ANGLE : 0.814 8886
REMARK 3 CHIRALITY : 0.051 948
REMARK 3 PLANARITY : 0.006 1146
REMARK 3 DIHEDRAL : 6.558 3792
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8XIZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-DEC-23.
REMARK 100 THE DEPOSITION ID IS D_1300040916.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JAN-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40335
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.170
REMARK 200 RESOLUTION RANGE LOW (A) : 47.890
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.5500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.17
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : 0.07000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMPLE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: TETRAGONAL CRYSTAL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE TRIBASIC
REMARK 280 DIHYDRATE,PH5.5,18%(W/V) POLYETHYLENE GLYCOL 3,350, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 25.64350
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
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 MET A -35
REMARK 465 GLY A -34
REMARK 465 SER A -33
REMARK 465 SER A -32
REMARK 465 HIS A -31
REMARK 465 HIS A -30
REMARK 465 HIS A -29
REMARK 465 HIS A -28
REMARK 465 HIS A -27
REMARK 465 HIS A -26
REMARK 465 SER A -25
REMARK 465 SER A -24
REMARK 465 GLY A -23
REMARK 465 LEU A -22
REMARK 465 VAL A -21
REMARK 465 PRO A -20
REMARK 465 ARG A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 MET A -15
REMARK 465 ALA A -14
REMARK 465 SER A -13
REMARK 465 MET A -12
REMARK 465 THR A -11
REMARK 465 GLY A -10
REMARK 465 GLY A -9
REMARK 465 GLN A -8
REMARK 465 GLN A -7
REMARK 465 MET A -6
REMARK 465 GLY A -5
REMARK 465 ARG A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 GLU A -1
REMARK 465 PHE A 0
REMARK 465 PRO A 224
REMARK 465 ASP A 225
REMARK 465 THR A 226
REMARK 465 ALA A 227
REMARK 465 ARG A 394
REMARK 465 LYS A 395
REMARK 465 MET B -35
REMARK 465 GLY B -34
REMARK 465 SER B -33
REMARK 465 SER B -32
REMARK 465 HIS B -31
REMARK 465 HIS B -30
REMARK 465 HIS B -29
REMARK 465 HIS B -28
REMARK 465 HIS B -27
REMARK 465 HIS B -26
REMARK 465 SER B -25
REMARK 465 SER B -24
REMARK 465 GLY B -23
REMARK 465 LEU B -22
REMARK 465 VAL B -21
REMARK 465 PRO B -20
REMARK 465 ARG B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 HIS B -16
REMARK 465 MET B -15
REMARK 465 ALA B -14
REMARK 465 SER B -13
REMARK 465 MET B -12
REMARK 465 THR B -11
REMARK 465 GLY B -10
REMARK 465 GLY B -9
REMARK 465 GLN B -8
REMARK 465 GLN B -7
REMARK 465 MET B -6
REMARK 465 GLY B -5
REMARK 465 ARG B -4
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 GLU B -1
REMARK 465 PHE B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 PRO B 224
REMARK 465 THR B 226
REMARK 465 ALA B 227
REMARK 465 ARG B 394
REMARK 465 LYS B 395
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 PRO A 117 47.39 -93.82
REMARK 500 THR A 152 -116.33 45.36
REMARK 500 ASN A 164 -166.07 -129.29
REMARK 500 ASP A 191 -135.09 51.39
REMARK 500 PRO B 117 48.42 -93.43
REMARK 500 THR B 152 -114.30 42.90
REMARK 500 ASP B 191 -134.18 51.08
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 A 634 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH A 635 DISTANCE = 6.90 ANGSTROMS
REMARK 525 HOH A 636 DISTANCE = 8.63 ANGSTROMS
REMARK 525 HOH B 626 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH B 627 DISTANCE = 6.87 ANGSTROMS
REMARK 525 HOH B 628 DISTANCE = 7.57 ANGSTROMS
REMARK 525 HOH B 629 DISTANCE = 7.60 ANGSTROMS
DBREF 8XIZ A 1 395 UNP T2B4K5 T2B4K5_ASPUS 1 395
DBREF 8XIZ B 1 395 UNP T2B4K5 T2B4K5_ASPUS 1 395
SEQADV 8XIZ MET A -35 UNP T2B4K5 INITIATING METHIONINE
SEQADV 8XIZ GLY A -34 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ SER A -33 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ SER A -32 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ HIS A -31 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ HIS A -30 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ HIS A -29 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ HIS A -28 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ HIS A -27 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ HIS A -26 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ SER A -25 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ SER A -24 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ GLY A -23 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ LEU A -22 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ VAL A -21 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ PRO A -20 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ ARG A -19 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ GLY A -18 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ SER A -17 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ HIS A -16 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ MET A -15 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ ALA A -14 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ SER A -13 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ MET A -12 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ THR A -11 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ GLY A -10 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ GLY A -9 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ GLN A -8 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ GLN A -7 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ MET A -6 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ GLY A -5 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ ARG A -4 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ GLY A -3 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ SER A -2 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ GLU A -1 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ PHE A 0 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ ILE A 250 UNP T2B4K5 ALA 250 ENGINEERED MUTATION
SEQADV 8XIZ VAL A 344 UNP T2B4K5 LEU 344 ENGINEERED MUTATION
SEQADV 8XIZ MET B -35 UNP T2B4K5 INITIATING METHIONINE
SEQADV 8XIZ GLY B -34 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ SER B -33 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ SER B -32 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ HIS B -31 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ HIS B -30 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ HIS B -29 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ HIS B -28 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ HIS B -27 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ HIS B -26 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ SER B -25 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ SER B -24 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ GLY B -23 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ LEU B -22 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ VAL B -21 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ PRO B -20 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ ARG B -19 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ GLY B -18 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ SER B -17 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ HIS B -16 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ MET B -15 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ ALA B -14 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ SER B -13 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ MET B -12 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ THR B -11 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ GLY B -10 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ GLY B -9 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ GLN B -8 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ GLN B -7 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ MET B -6 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ GLY B -5 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ ARG B -4 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ GLY B -3 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ SER B -2 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ GLU B -1 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ PHE B 0 UNP T2B4K5 EXPRESSION TAG
SEQADV 8XIZ ILE B 250 UNP T2B4K5 ALA 250 ENGINEERED MUTATION
SEQADV 8XIZ VAL B 344 UNP T2B4K5 LEU 344 ENGINEERED MUTATION
SEQRES 1 A 431 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 431 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 A 431 GLY GLN GLN MET GLY ARG GLY SER GLU PHE MET ALA LEU
SEQRES 4 A 431 ALA TYR SER ASN ILE PRO LEU GLY ALA THR VAL ILE PRO
SEQRES 5 A 431 SER PRO PHE GLN VAL HIS ILE SER ASP GLU GLN ILE GLU
SEQRES 6 A 431 GLU LEU GLN LEU LEU VAL LYS LEU SER LYS LEU ALA PRO
SEQRES 7 A 431 PRO THR TYR GLU GLY LEU GLN GLN ASP ARG ARG TYR GLY
SEQRES 8 A 431 ILE THR ASN GLU TRP LEU ALA ASN ALA LYS GLU ALA TRP
SEQRES 9 A 431 LYS SER PHE ASP TRP ARG PRO ALA GLU SER ARG ILE ASN
SEQRES 10 A 431 SER PHE PRO GLN PHE THR TYR ASP ILE GLU GLY LEU THR
SEQRES 11 A 431 ILE HIS PHE VAL ALA LEU PHE SER GLU LYS LYS ASP ALA
SEQRES 12 A 431 ILE PRO ILE VAL LEU LEU HIS GLY TRP PRO GLY SER PHE
SEQRES 13 A 431 LEU GLU PHE LEU PRO VAL LEU THR SER ILE ARG ASP LYS
SEQRES 14 A 431 TYR SER PRO GLU THR LEU PRO TYR HIS ILE VAL VAL PRO
SEQRES 15 A 431 SER LEU PRO GLY TYR THR PHE SER SER GLY PRO PRO LEU
SEQRES 16 A 431 ASP VAL ASN PHE ASN GLY GLU ASP THR ALA ARG VAL ILE
SEQRES 17 A 431 ASN LYS VAL MET LEU ASN LEU GLY PHE GLU ASP GLY TYR
SEQRES 18 A 431 VAL ALA GLN GLY GLY ASP ILE GLY SER LYS ILE GLY ARG
SEQRES 19 A 431 ILE LEU ALA VAL ASP HIS ASP ALA CYS LYS ALA VAL HIS
SEQRES 20 A 431 LEU ASN ALA CYS TYR MET GLY LYS PRO SER SER ILE PRO
SEQRES 21 A 431 ASP THR ALA ILE THR GLU GLU ASP LYS ARG ALA LEU ALA
SEQRES 22 A 431 ARG ALA GLN TRP PHE ALA THR PHE GLY SER GLY TYR ILE
SEQRES 23 A 431 VAL GLU HIS GLY THR ARG PRO SER THR ILE GLY ASN ALA
SEQRES 24 A 431 LEU SER THR SER PRO VAL ALA LEU LEU SER TRP ILE GLY
SEQRES 25 A 431 GLU LYS PHE LEU ASP TRP ALA GLY GLU THR ILE PRO LEU
SEQRES 26 A 431 GLU THR ILE LEU GLU SER VAL THR LEU TYR TRP PHE THR
SEQRES 27 A 431 GLU THR PHE PRO ARG SER ILE TYR HIS TYR ARG GLU ASN
SEQRES 28 A 431 PHE PRO PRO PRO LYS LEU ARG HIS THR GLU ASP PRO ARG
SEQRES 29 A 431 TRP TYR ILE ARG LYS PRO PHE GLY PHE SER TYR TYR PRO
SEQRES 30 A 431 MET GLU VAL VAL PRO THR PRO ARG ALA TRP VAL GLU THR
SEQRES 31 A 431 THR GLY ASN LEU VAL PHE TRP GLN ALA HIS GLU LYS GLY
SEQRES 32 A 431 GLY HIS PHE ALA ALA LEU GLU ARG PRO GLN ASP TYR LEU
SEQRES 33 A 431 ASP ASP LEU THR ALA PHE CYS GLU GLN VAL TRP ALA GLY
SEQRES 34 A 431 ARG LYS
SEQRES 1 B 431 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 431 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 B 431 GLY GLN GLN MET GLY ARG GLY SER GLU PHE MET ALA LEU
SEQRES 4 B 431 ALA TYR SER ASN ILE PRO LEU GLY ALA THR VAL ILE PRO
SEQRES 5 B 431 SER PRO PHE GLN VAL HIS ILE SER ASP GLU GLN ILE GLU
SEQRES 6 B 431 GLU LEU GLN LEU LEU VAL LYS LEU SER LYS LEU ALA PRO
SEQRES 7 B 431 PRO THR TYR GLU GLY LEU GLN GLN ASP ARG ARG TYR GLY
SEQRES 8 B 431 ILE THR ASN GLU TRP LEU ALA ASN ALA LYS GLU ALA TRP
SEQRES 9 B 431 LYS SER PHE ASP TRP ARG PRO ALA GLU SER ARG ILE ASN
SEQRES 10 B 431 SER PHE PRO GLN PHE THR TYR ASP ILE GLU GLY LEU THR
SEQRES 11 B 431 ILE HIS PHE VAL ALA LEU PHE SER GLU LYS LYS ASP ALA
SEQRES 12 B 431 ILE PRO ILE VAL LEU LEU HIS GLY TRP PRO GLY SER PHE
SEQRES 13 B 431 LEU GLU PHE LEU PRO VAL LEU THR SER ILE ARG ASP LYS
SEQRES 14 B 431 TYR SER PRO GLU THR LEU PRO TYR HIS ILE VAL VAL PRO
SEQRES 15 B 431 SER LEU PRO GLY TYR THR PHE SER SER GLY PRO PRO LEU
SEQRES 16 B 431 ASP VAL ASN PHE ASN GLY GLU ASP THR ALA ARG VAL ILE
SEQRES 17 B 431 ASN LYS VAL MET LEU ASN LEU GLY PHE GLU ASP GLY TYR
SEQRES 18 B 431 VAL ALA GLN GLY GLY ASP ILE GLY SER LYS ILE GLY ARG
SEQRES 19 B 431 ILE LEU ALA VAL ASP HIS ASP ALA CYS LYS ALA VAL HIS
SEQRES 20 B 431 LEU ASN ALA CYS TYR MET GLY LYS PRO SER SER ILE PRO
SEQRES 21 B 431 ASP THR ALA ILE THR GLU GLU ASP LYS ARG ALA LEU ALA
SEQRES 22 B 431 ARG ALA GLN TRP PHE ALA THR PHE GLY SER GLY TYR ILE
SEQRES 23 B 431 VAL GLU HIS GLY THR ARG PRO SER THR ILE GLY ASN ALA
SEQRES 24 B 431 LEU SER THR SER PRO VAL ALA LEU LEU SER TRP ILE GLY
SEQRES 25 B 431 GLU LYS PHE LEU ASP TRP ALA GLY GLU THR ILE PRO LEU
SEQRES 26 B 431 GLU THR ILE LEU GLU SER VAL THR LEU TYR TRP PHE THR
SEQRES 27 B 431 GLU THR PHE PRO ARG SER ILE TYR HIS TYR ARG GLU ASN
SEQRES 28 B 431 PHE PRO PRO PRO LYS LEU ARG HIS THR GLU ASP PRO ARG
SEQRES 29 B 431 TRP TYR ILE ARG LYS PRO PHE GLY PHE SER TYR TYR PRO
SEQRES 30 B 431 MET GLU VAL VAL PRO THR PRO ARG ALA TRP VAL GLU THR
SEQRES 31 B 431 THR GLY ASN LEU VAL PHE TRP GLN ALA HIS GLU LYS GLY
SEQRES 32 B 431 GLY HIS PHE ALA ALA LEU GLU ARG PRO GLN ASP TYR LEU
SEQRES 33 B 431 ASP ASP LEU THR ALA PHE CYS GLU GLN VAL TRP ALA GLY
SEQRES 34 B 431 ARG LYS
FORMUL 3 HOH *465(H2 O)
HELIX 1 AA1 SER A 24 SER A 38 1 15
HELIX 2 AA2 TYR A 45 GLN A 49 5 5
HELIX 3 AA3 THR A 57 SER A 70 1 14
HELIX 4 AA4 ASP A 72 SER A 82 1 11
HELIX 5 AA5 SER A 119 GLU A 122 5 4
HELIX 6 AA6 PHE A 123 TYR A 134 1 12
HELIX 7 AA7 ASN A 164 LEU A 179 1 16
HELIX 8 AA8 ASP A 191 HIS A 204 1 14
HELIX 9 AA9 THR A 229 GLY A 246 1 18
HELIX 10 AB1 SER A 247 ARG A 256 1 10
HELIX 11 AB2 ARG A 256 THR A 266 1 11
HELIX 12 AB3 SER A 267 ALA A 283 1 17
HELIX 13 AB4 PRO A 288 THR A 302 1 15
HELIX 14 AB5 GLU A 303 SER A 308 1 6
HELIX 15 AB6 ILE A 309 PHE A 316 5 8
HELIX 16 AB7 ARG A 322 TYR A 330 5 9
HELIX 17 AB8 PRO A 348 THR A 354 1 7
HELIX 18 AB9 PHE A 370 ARG A 375 1 6
HELIX 19 AC1 ARG A 375 TRP A 391 1 17
HELIX 20 AC2 SER B 24 SER B 38 1 15
HELIX 21 AC3 TYR B 45 GLN B 49 5 5
HELIX 22 AC4 THR B 57 SER B 70 1 14
HELIX 23 AC5 ASP B 72 SER B 82 1 11
HELIX 24 AC6 SER B 119 GLU B 122 5 4
HELIX 25 AC7 PHE B 123 TYR B 134 1 12
HELIX 26 AC8 ASN B 164 LEU B 179 1 16
HELIX 27 AC9 ASP B 191 HIS B 204 1 14
HELIX 28 AD1 THR B 229 GLY B 246 1 18
HELIX 29 AD2 SER B 247 ARG B 256 1 10
HELIX 30 AD3 ARG B 256 THR B 266 1 11
HELIX 31 AD4 SER B 267 ALA B 283 1 17
HELIX 32 AD5 PRO B 288 THR B 302 1 15
HELIX 33 AD6 GLU B 303 ILE B 309 1 7
HELIX 34 AD7 TYR B 310 PHE B 316 5 7
HELIX 35 AD8 ARG B 322 TYR B 330 5 9
HELIX 36 AD9 PRO B 348 GLU B 353 1 6
HELIX 37 AE1 PHE B 370 ARG B 375 1 6
HELIX 38 AE2 ARG B 375 TRP B 391 1 17
SHEET 1 AA1 9 SER A 17 PRO A 18 0
SHEET 2 AA1 9 GLN A 85 ILE A 90 -1 O THR A 87 N SER A 17
SHEET 3 AA1 9 LEU A 93 LEU A 100 -1 O ILE A 95 N TYR A 88
SHEET 4 AA1 9 TYR A 141 PRO A 146 -1 O VAL A 145 N VAL A 98
SHEET 5 AA1 9 ILE A 108 LEU A 113 1 N ILE A 110 O VAL A 144
SHEET 6 AA1 9 TYR A 185 GLY A 189 1 O VAL A 186 N VAL A 111
SHEET 7 AA1 9 CYS A 207 LEU A 212 1 O LYS A 208 N TYR A 185
SHEET 8 AA1 9 ILE A 331 TYR A 339 1 O GLY A 336 N LEU A 212
SHEET 9 AA1 9 GLY A 356 ALA A 363 1 O ASN A 357 N ILE A 331
SHEET 1 AA2 9 SER B 17 PRO B 18 0
SHEET 2 AA2 9 GLN B 85 ILE B 90 -1 O THR B 87 N SER B 17
SHEET 3 AA2 9 LEU B 93 LEU B 100 -1 O ILE B 95 N TYR B 88
SHEET 4 AA2 9 TYR B 141 PRO B 146 -1 O VAL B 145 N VAL B 98
SHEET 5 AA2 9 ILE B 108 LEU B 113 1 N ILE B 110 O HIS B 142
SHEET 6 AA2 9 TYR B 185 GLY B 189 1 O GLN B 188 N LEU B 113
SHEET 7 AA2 9 CYS B 207 LEU B 212 1 O HIS B 211 N ALA B 187
SHEET 8 AA2 9 ILE B 331 TYR B 339 1 O GLY B 336 N LEU B 212
SHEET 9 AA2 9 GLY B 356 ALA B 363 1 O GLN B 362 N TYR B 339
CISPEP 1 TRP A 116 PRO A 117 0 1.71
CISPEP 2 GLY A 156 PRO A 157 0 -0.85
CISPEP 3 PHE A 316 PRO A 317 0 -2.39
CISPEP 4 TRP B 116 PRO B 117 0 2.13
CISPEP 5 GLY B 156 PRO B 157 0 -1.32
CISPEP 6 PHE B 316 PRO B 317 0 0.24
CRYST1 57.049 51.287 133.812 90.00 90.52 90.00 P 1 21 1 4
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 0.017529 0.000000 0.000160 0.00000
SCALE2 0.000000 0.019498 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007473 0.00000
TER 3120 GLY A 393
TER 6235 GLY B 393
MASTER 331 0 0 38 18 0 0 6 6698 2 0 68
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