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PDBsum entry 3oe2

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Isomerase PDB id
3oe2
Jmol
Contents
Protein chain
133 a.a.
Ligands
TAR
SRT
Waters ×162
HEADER    ISOMERASE                               12-AUG-10   3OE2
TITLE     1.6 A CRYSTAL STRUCTURE OF PEPTIDYL-PROLYL CIS-TRANS ISOMERASE PPIASE
TITLE    2 FROM PSEUDOMONAS SYRINGAE PV. TOMATO STR. DC3000 (PSPTO DC3000)
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: UNP RESIDUES 26-224;
COMPND   5 EC: 5.2.1.8;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS SYRINGAE PV. TOMATO;
SOURCE   3 ORGANISM_TAXID: 223283;
SOURCE   4 STRAIN: DC3000;
SOURCE   5 GENE: PSPTO0135, PSPTO_0135;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PHAT2
KEYWDS    FKBP, PPIASE, FK506, ISOMERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    H.M.ZHANG,M.LI,W.R.CHANG
REVDAT   2   28-SEP-11 3OE2    1       HETATM
REVDAT   1   21-SEP-11 3OE2    0
JRNL        AUTH   H.M.ZHANG,M.LI,Y.GAO,W.CHANG
JRNL        TITL   CRYSTAL STRUCTURE OF PEPTIDYL-PROLYL CIS-TRANS ISOMERASE
JRNL        TITL 2 PPIASE FROM PSEUDOMONAS SYRINGAE PV. TOMATO STR. DC3000
JRNL        TITL 3 (PSPTO DC3000) AT 1.6 RESOLUTION
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0044
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) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.50
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5
REMARK   3   NUMBER OF REFLECTIONS             : 15209
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) : 0.200
REMARK   3   R VALUE            (WORKING SET) : 0.198
REMARK   3   FREE R VALUE                     : 0.228
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 815
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) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 798
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 70.42
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4100
REMARK   3   BIN FREE R VALUE SET COUNT          : 47
REMARK   3   BIN FREE R VALUE                    : 0.3300
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1007
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 20
REMARK   3   SOLVENT ATOMS            : 162
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.92
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.46000
REMARK   3    B22 (A**2) : 0.48000
REMARK   3    B33 (A**2) : -0.02000
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): 0.105
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.059
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.617
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1048 ; 0.010 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1426 ; 1.313 ; 1.999
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   132 ; 6.700 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    42 ;31.863 ;24.762
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   166 ;12.933 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     6 ;22.365 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   159 ; 0.102 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   807 ; 0.006 ; 0.022
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
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):   662 ; 0.665 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1065 ; 1.297 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   386 ; 2.327 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   361 ; 3.975 ; 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 : 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 RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3OE2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-SEP-10.
REMARK 100 THE RCSB ID CODE IS RCSB060998.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-AUG-09
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.3
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E DW
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16070
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.170
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.5
REMARK 200  DATA REDUNDANCY                : 6.300
REMARK 200  R MERGE                    (I) : 0.05200
REMARK 200  R SYM                      (I) : 0.05200
REMARK 200   FOR THE DATA SET  : 49.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 72.4
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.60
REMARK 200  R MERGE FOR SHELL          (I) : 0.26900
REMARK 200  R SYM FOR SHELL            (I) : 0.25200
REMARK 200   FOR SHELL         : 5.800
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 1FD9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.4M POTASSIUM SODIUM TARTRATE
REMARK 280  TETRAHYDRATE, PH 7.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280  291K
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       16.61100
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       41.15600
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       22.04950
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       41.15600
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       16.61100
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       22.04950
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 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: PISA
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 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     6
REMARK 465     SER A     7
REMARK 465     HIS A     8
REMARK 465     HIS A     9
REMARK 465     HIS A    10
REMARK 465     HIS A    11
REMARK 465     HIS A    12
REMARK 465     HIS A    13
REMARK 465     SER A    14
REMARK 465     MET A    15
REMARK 465     ASP A    16
REMARK 465     ILE A    17
REMARK 465     GLU A    18
REMARK 465     PHE A    19
REMARK 465     VAL A    20
REMARK 465     ASP A    21
REMARK 465     LEU A    22
REMARK 465     GLU A    23
REMARK 465     GLY A    24
REMARK 465     SER A    25
REMARK 465     ASP A    26
REMARK 465     ALA A    27
REMARK 465     HIS A    28
REMARK 465     ASP A    29
REMARK 465     LEU A    30
REMARK 465     ALA A    31
REMARK 465     TYR A    32
REMARK 465     SER A    33
REMARK 465     LEU A    34
REMARK 465     GLY A    35
REMARK 465     ALA A    36
REMARK 465     SER A    37
REMARK 465     LEU A    38
REMARK 465     GLY A    39
REMARK 465     GLU A    40
REMARK 465     ARG A    41
REMARK 465     LEU A    42
REMARK 465     HIS A    43
REMARK 465     GLN A    44
REMARK 465     GLU A    45
REMARK 465     VAL A    46
REMARK 465     PRO A    47
REMARK 465     ASP A    48
REMARK 465     LEU A    49
REMARK 465     ASP A    50
REMARK 465     LEU A    51
REMARK 465     LYS A    52
REMARK 465     ALA A    53
REMARK 465     LEU A    54
REMARK 465     VAL A    55
REMARK 465     ASP A    56
REMARK 465     GLY A    57
REMARK 465     LEU A    58
REMARK 465     LYS A    59
REMARK 465     GLN A    60
REMARK 465     ALA A    61
REMARK 465     TYR A    62
REMARK 465     GLN A    63
REMARK 465     GLY A    64
REMARK 465     LYS A    65
REMARK 465     PRO A    66
REMARK 465     LEU A    67
REMARK 465     ALA A    68
REMARK 465     LEU A    69
REMARK 465     LYS A    70
REMARK 465     GLN A    71
REMARK 465     GLU A    72
REMARK 465     ARG A    73
REMARK 465     ILE A    74
REMARK 465     ASP A    75
REMARK 465     GLN A    76
REMARK 465     ILE A    77
REMARK 465     LEU A    78
REMARK 465     ARG A    79
REMARK 465     GLU A    80
REMARK 465     HIS A    81
REMARK 465     ASP A    82
REMARK 465     ALA A    83
REMARK 465     ALA A    84
REMARK 465     ILE A    85
REMARK 465     ALA A    86
REMARK 465     GLN A    87
REMARK 465     ALA A    88
REMARK 465     GLU A    89
REMARK 465     THR A    90
REMARK 465     ALA A    91
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    ALA A 197     -113.21   -132.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRT A 225
DBREF  3OE2 A   26   224  UNP    Q88B84   Q88B84_PSESM    26    224
SEQADV 3OE2 MET A    6  UNP  Q88B84              EXPRESSION TAG
SEQADV 3OE2 SER A    7  UNP  Q88B84              EXPRESSION TAG
SEQADV 3OE2 HIS A    8  UNP  Q88B84              EXPRESSION TAG
SEQADV 3OE2 HIS A    9  UNP  Q88B84              EXPRESSION TAG
SEQADV 3OE2 HIS A   10  UNP  Q88B84              EXPRESSION TAG
SEQADV 3OE2 HIS A   11  UNP  Q88B84              EXPRESSION TAG
SEQADV 3OE2 HIS A   12  UNP  Q88B84              EXPRESSION TAG
SEQADV 3OE2 HIS A   13  UNP  Q88B84              EXPRESSION TAG
SEQADV 3OE2 SER A   14  UNP  Q88B84              EXPRESSION TAG
SEQADV 3OE2 MET A   15  UNP  Q88B84              EXPRESSION TAG
SEQADV 3OE2 ASP A   16  UNP  Q88B84              EXPRESSION TAG
SEQADV 3OE2 ILE A   17  UNP  Q88B84              EXPRESSION TAG
SEQADV 3OE2 GLU A   18  UNP  Q88B84              EXPRESSION TAG
SEQADV 3OE2 PHE A   19  UNP  Q88B84              EXPRESSION TAG
SEQADV 3OE2 VAL A   20  UNP  Q88B84              EXPRESSION TAG
SEQADV 3OE2 ASP A   21  UNP  Q88B84              EXPRESSION TAG
SEQADV 3OE2 LEU A   22  UNP  Q88B84              EXPRESSION TAG
SEQADV 3OE2 GLU A   23  UNP  Q88B84              EXPRESSION TAG
SEQADV 3OE2 GLY A   24  UNP  Q88B84              EXPRESSION TAG
SEQADV 3OE2 SER A   25  UNP  Q88B84              EXPRESSION TAG
SEQRES   1 A  219  MET SER HIS HIS HIS HIS HIS HIS SER MET ASP ILE GLU
SEQRES   2 A  219  PHE VAL ASP LEU GLU GLY SER ASP ALA HIS ASP LEU ALA
SEQRES   3 A  219  TYR SER LEU GLY ALA SER LEU GLY GLU ARG LEU HIS GLN
SEQRES   4 A  219  GLU VAL PRO ASP LEU ASP LEU LYS ALA LEU VAL ASP GLY
SEQRES   5 A  219  LEU LYS GLN ALA TYR GLN GLY LYS PRO LEU ALA LEU LYS
SEQRES   6 A  219  GLN GLU ARG ILE ASP GLN ILE LEU ARG GLU HIS ASP ALA
SEQRES   7 A  219  ALA ILE ALA GLN ALA GLU THR ALA GLY THR ASP ALA PRO
SEQRES   8 A  219  THR GLU ALA ALA LEU LYS ALA GLU ARG THR PHE MET ALA
SEQRES   9 A  219  GLY GLU LYS ALA LYS PRO GLY VAL LYS GLU LEU ALA ASP
SEQRES  10 A  219  GLY ILE LEU MET THR GLU LEU THR PRO GLY THR GLY PRO
SEQRES  11 A  219  LYS PRO ASP ALA ASN GLY ARG VAL GLU VAL ARG TYR VAL
SEQRES  12 A  219  GLY ARG LEU PRO ASP GLY LYS ILE PHE ASP GLN SER THR
SEQRES  13 A  219  GLN PRO GLN TRP PHE ARG LEU ASP SER VAL ILE SER GLY
SEQRES  14 A  219  TRP THR SER ALA LEU GLN ASN MET PRO THR GLY ALA LYS
SEQRES  15 A  219  TRP ARG LEU VAL ILE PRO SER ASP GLN ALA TYR GLY ALA
SEQRES  16 A  219  GLU GLY ALA GLY ASP LEU ILE ASP PRO PHE THR PRO LEU
SEQRES  17 A  219  VAL PHE GLU ILE GLU LEU ILE ALA VAL SER GLN
HET    TAR  A   1      10
HET    SRT  A 225      14
HETNAM     TAR D(-)-TARTARIC ACID
HETNAM     SRT S,R MESO-TARTARIC ACID
FORMUL   2  TAR    C4 H6 O6
FORMUL   3  SRT    C4 H6 O6
FORMUL   4  HOH   *162(H2 O)
HELIX    1   1 PRO A   96  ALA A  113  1                                  18
HELIX    2   2 ALA A  121  GLY A  123  5                                   3
HELIX    3   3 ASP A  169  VAL A  171  5                                   3
HELIX    4   4 ILE A  172  GLN A  180  1                                   9
HELIX    5   5 PRO A  193  ALA A  197  5                                   5
SHEET    1   A 6 LYS A 118  GLU A 119  0
SHEET    2   A 6 LEU A 125  THR A 130 -1  O  MET A 126   N  LYS A 118
SHEET    3   A 6 LYS A 187  ILE A 192 -1  O  ARG A 189   N  THR A 127
SHEET    4   A 6 LEU A 213  SER A 223 -1  O  PHE A 215   N  LEU A 190
SHEET    5   A 6 ARG A 142  ARG A 150 -1  N  ARG A 150   O  VAL A 214
SHEET    6   A 6 ILE A 156  GLN A 159 -1  O  ASP A 158   N  GLY A 149
SHEET    1   B 6 LYS A 118  GLU A 119  0
SHEET    2   B 6 LEU A 125  THR A 130 -1  O  MET A 126   N  LYS A 118
SHEET    3   B 6 LYS A 187  ILE A 192 -1  O  ARG A 189   N  THR A 127
SHEET    4   B 6 LEU A 213  SER A 223 -1  O  PHE A 215   N  LEU A 190
SHEET    5   B 6 ARG A 142  ARG A 150 -1  N  ARG A 150   O  VAL A 214
SHEET    6   B 6 GLN A 164  ARG A 167 -1  O  GLN A 164   N  VAL A 145
SITE     1 AC1  6 TYR A 147  ASP A 158  VAL A 171  ILE A 172
SITE     2 AC1  6 TRP A 175  PHE A 215
SITE     1 AC2  4 PHE A 157  ARG A 189  HOH A 239  HOH A 334
CRYST1   33.222   44.099   82.312  90.00  90.00  90.00 P 21 21 21    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      0.030101  0.000000  0.000000        0.00000
SCALE2      0.000000  0.022676  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012149        0.00000
      
PROCHECK
Go to PROCHECK summary
 References