GenomeNet

Database: PDB
Entry: 4XLL
LinkDB: 4XLL
Original site: 4XLL 
HEADER    UNKNOWN FUNCTION                        13-JAN-15   4XLL              
TITLE     TOXOPLASMA GONDII DJ-1, OXIDIZED                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DJ-1 FAMILY PROTEIN;                                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TOXOPLASMA GONDII;                              
SOURCE   3 ORGANISM_TAXID: 5811;                                                
SOURCE   4 GENE: TGVEG_214290;                                                  
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET15                                     
KEYWDS    OXIDIZED, DJ-1, PSEUDOPROTEASE, PAPAIN-FOLD, UNKNOWN FUNCTION         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.CHILD,M.A.WILSON,M.L.REESE,M.BOGYO                                
REVDAT   2   27-JUL-16 4XLL    1       REMARK                                   
REVDAT   1   11-FEB-15 4XLL    0                                                
JRNL        AUTH   M.A.CHILD,M.GARLAND,P.MADZELAN,M.TREECK,W.VAN DER LINDEN,    
JRNL        AUTH 2 K.ORESIC,E.WEERAPANA,M.A.WILSON,J.C.BOOTHROYD,M.L.REESE,     
JRNL        AUTH 3 M.BOGYO                                                      
JRNL        TITL   TOXOPLASMA DJ-1 REGULATES MICRONEME EXOCYTOSIS THROUGH AN    
JRNL        TITL 2 ASSOCIATION WITH THE PLANT-LIKE KINASE, CDPK1                
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.08 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
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) : 2.08                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.69                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 18630                          
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) : 0.174                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1811                            
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) : 2.08                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.14                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 993                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 80.04                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2260                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 118                          
REMARK   3   BIN FREE R VALUE                    : 0.2470                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2742                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 245                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.53                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.60000                                              
REMARK   3    B22 (A**2) : -2.93000                                             
REMARK   3    B33 (A**2) : -1.84000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.35000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.316         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.208         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.155         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.686        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2780 ; 0.015 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2791 ; 0.004 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3765 ; 1.668 ; 1.985       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6433 ; 1.032 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   368 ; 6.636 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   100 ;34.919 ;24.600       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   495 ;13.265 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;12.574 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   459 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3105 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   547 ; 0.004 ; 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):  1472 ; 1.269 ; 1.761       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1471 ; 1.264 ; 1.759       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1837 ; 2.003 ; 2.632       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
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    185       B     2    185   11647 0.080 0.050     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A   185                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.2264  10.3196  11.2328              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0094 T22:   0.0479                                     
REMARK   3      T33:   0.0302 T12:  -0.0012                                     
REMARK   3      T13:  -0.0060 T23:  -0.0064                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0180 L22:   0.1916                                     
REMARK   3      L33:   0.2286 L12:  -0.0001                                     
REMARK   3      L13:   0.0038 L23:  -0.0437                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0053 S12:  -0.0073 S13:  -0.0015                       
REMARK   3      S21:  -0.0309 S22:   0.0076 S23:   0.0095                       
REMARK   3      S31:   0.0268 S32:  -0.0017 S33:  -0.0023                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     2        B   185                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.8749  32.3746  26.4324              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0101 T22:   0.0485                                     
REMARK   3      T33:   0.0352 T12:   0.0047                                     
REMARK   3      T13:  -0.0101 T23:  -0.0056                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1536 L22:   0.1292                                     
REMARK   3      L33:   0.2310 L12:   0.0439                                     
REMARK   3      L13:  -0.0494 L23:   0.0773                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0137 S12:  -0.0176 S13:  -0.0050                       
REMARK   3      S21:  -0.0102 S22:   0.0132 S23:   0.0103                       
REMARK   3      S31:  -0.0261 S32:   0.0078 S33:   0.0004                       
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 4XLL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JAN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000205903.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-MAY-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL11-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979450                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS VERSION JULY 4, 2012           
REMARK 200  DATA SCALING SOFTWARE          : XSCALE VERSION JULY 4, 2012        
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18638                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.080                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.693                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : 6.840                              
REMARK 200  R MERGE                    (I) : 0.09200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.9600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.08                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.250                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1:1 5MG/ML PROTEIN IN 10 MM HEPES 7.0,   
REMARK 280  100 MM NACL, 10 MM DTT MIXED WITH RESERVOIR: 1.5 M AMMONIUM         
REMARK 280  CITRATE TRIBASIC, PH 7.0, VAPOR DIFFUSION, HANGING DROP,            
REMARK 280  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       27.59050            
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 TOTAL BURIED SURFACE AREA: 2580 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13400 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
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     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
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   SG   CYS A   127     O    HOH A   238              1.84            
REMARK 500   O    HOH B   241     O    HOH B   247              2.08            
REMARK 500   O    HOH A   240     O    HOH A   247              2.10            
REMARK 500   O    HOH B   222     O    HOH B   278              2.16            
REMARK 500   OE1  GLU B   159     O    HOH B   316              2.17            
REMARK 500   O    HOH B   225     O    HOH B   227              2.17            
REMARK 500   O    ARG B    26     O    HOH B   201              2.19            
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    CSD A 104     -118.78     73.97                                   
REMARK 500    ASN A 146     -113.02     52.15                                   
REMARK 500    TYR A 169     -101.95   -113.71                                   
REMARK 500    LEU A 182       33.53     74.22                                   
REMARK 500    CSD B 104     -120.30     72.86                                   
REMARK 500    ASN B 146     -113.58     52.04                                   
REMARK 500    TYR B 169     -101.89   -115.71                                   
REMARK 500    LEU B 182       34.61     72.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  4XLL A    1   185  UNP    B9PZH8   B9PZH8_TOXGO    72    256             
DBREF  4XLL B    1   185  UNP    B9PZH8   B9PZH8_TOXGO    72    256             
SEQADV 4XLL GLY A   -2  UNP  B9PZH8              EXPRESSION TAG                 
SEQADV 4XLL SER A   -1  UNP  B9PZH8              EXPRESSION TAG                 
SEQADV 4XLL HIS A    0  UNP  B9PZH8              EXPRESSION TAG                 
SEQADV 4XLL GLY B   -2  UNP  B9PZH8              EXPRESSION TAG                 
SEQADV 4XLL SER B   -1  UNP  B9PZH8              EXPRESSION TAG                 
SEQADV 4XLL HIS B    0  UNP  B9PZH8              EXPRESSION TAG                 
SEQRES   1 A  188  GLY SER HIS MET ALA VAL LYS VAL LEU VAL PRO VAL ALA          
SEQRES   2 A  188  HIS ASP SER GLU GLU ILE GLU ALA VAL SER ILE ILE ASP          
SEQRES   3 A  188  THR LEU ARG ARG ALA GLY ALA GLU VAL VAL VAL ALA SER          
SEQRES   4 A  188  VAL GLU ASP THR GLU ILE VAL ARG MET SER ARG GLY VAL          
SEQRES   5 A  188  CYS VAL LYS ALA ASP LYS LEU ILE SER ALA VAL GLU ASN          
SEQRES   6 A  188  GLU THR TYR ASP CYS ILE ALA ILE PRO GLY GLY MET PRO          
SEQRES   7 A  188  GLY ALA GLU ARG CYS ARG ASP SER ALA ALA LEU THR ALA          
SEQRES   8 A  188  MET LEU LYS THR HIS LYS ALA GLN GLY LYS LEU ILE ALA          
SEQRES   9 A  188  ALA ILE CSD ALA SER PRO ALA VAL VAL LEU GLN THR HIS          
SEQRES  10 A  188  GLY LEU LEU GLN GLY GLU LYS ALA VAL ALA TYR PRO CYS          
SEQRES  11 A  188  PHE MET ASP GLN PHE PRO ALA ASP MET ARG GLY GLU GLY          
SEQRES  12 A  188  ARG VAL CYS VAL SER ASN LYS ILE VAL THR SER VAL GLY          
SEQRES  13 A  188  PRO SER SER ALA ILE GLU PHE ALA LEU LYS LEU ILE GLU          
SEQRES  14 A  188  VAL LEU TYR ASN LYS GLU GLN ALA LYS LYS ILE ALA ALA          
SEQRES  15 A  188  GLN LEU LEU TYR ALA TYR                                      
SEQRES   1 B  188  GLY SER HIS MET ALA VAL LYS VAL LEU VAL PRO VAL ALA          
SEQRES   2 B  188  HIS ASP SER GLU GLU ILE GLU ALA VAL SER ILE ILE ASP          
SEQRES   3 B  188  THR LEU ARG ARG ALA GLY ALA GLU VAL VAL VAL ALA SER          
SEQRES   4 B  188  VAL GLU ASP THR GLU ILE VAL ARG MET SER ARG GLY VAL          
SEQRES   5 B  188  CYS VAL LYS ALA ASP LYS LEU ILE SER ALA VAL GLU ASN          
SEQRES   6 B  188  GLU THR TYR ASP CYS ILE ALA ILE PRO GLY GLY MET PRO          
SEQRES   7 B  188  GLY ALA GLU ARG CYS ARG ASP SER ALA ALA LEU THR ALA          
SEQRES   8 B  188  MET LEU LYS THR HIS LYS ALA GLN GLY LYS LEU ILE ALA          
SEQRES   9 B  188  ALA ILE CSD ALA SER PRO ALA VAL VAL LEU GLN THR HIS          
SEQRES  10 B  188  GLY LEU LEU GLN GLY GLU LYS ALA VAL ALA TYR PRO CYS          
SEQRES  11 B  188  PHE MET ASP GLN PHE PRO ALA ASP MET ARG GLY GLU GLY          
SEQRES  12 B  188  ARG VAL CYS VAL SER ASN LYS ILE VAL THR SER VAL GLY          
SEQRES  13 B  188  PRO SER SER ALA ILE GLU PHE ALA LEU LYS LEU ILE GLU          
SEQRES  14 B  188  VAL LEU TYR ASN LYS GLU GLN ALA LYS LYS ILE ALA ALA          
SEQRES  15 B  188  GLN LEU LEU TYR ALA TYR                                      
MODRES 4XLL CSD A  104  CYS  MODIFIED RESIDUE                                   
MODRES 4XLL CSD B  104  CYS  MODIFIED RESIDUE                                   
HET    CSD  A 104       8                                                       
HET    CSD  B 104       8                                                       
HETNAM     CSD 3-SULFINOALANINE                                                 
HETSYN     CSD S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE                       
FORMUL   1  CSD    2(C3 H7 N O4 S)                                              
FORMUL   3  HOH   *245(H2 O)                                                    
HELIX    1 AA1 GLU A   14  ALA A   28  1                                  15    
HELIX    2 AA2 SER A   58  GLU A   61  5                                   4    
HELIX    3 AA3 PRO A   75  SER A   83  1                                   9    
HELIX    4 AA4 SER A   83  GLN A   96  1                                  14    
HELIX    5 AA5 ALA A  105  VAL A  110  1                                   6    
HELIX    6 AA6 TYR A  125  PHE A  132  5                                   8    
HELIX    7 AA7 PRO A  133  ARG A  137  5                                   5    
HELIX    8 AA8 GLY A  153  SER A  155  5                                   3    
HELIX    9 AA9 SER A  156  TYR A  169  1                                  14    
HELIX   10 AB1 ASN A  170  LEU A  182  1                                  13    
HELIX   11 AB2 GLU B   14  ALA B   28  1                                  15    
HELIX   12 AB3 SER B   58  GLU B   61  5                                   4    
HELIX   13 AB4 PRO B   75  ASP B   82  1                                   8    
HELIX   14 AB5 SER B   83  GLN B   96  1                                  14    
HELIX   15 AB6 ALA B  105  VAL B  110  1                                   6    
HELIX   16 AB7 TYR B  125  PHE B  132  5                                   8    
HELIX   17 AB8 PRO B  133  ARG B  137  5                                   5    
HELIX   18 AB9 GLY B  153  SER B  155  5                                   3    
HELIX   19 AC1 SER B  156  TYR B  169  1                                  14    
HELIX   20 AC2 ASN B  170  LEU B  182  1                                  13    
SHEET    1 AA1 7 LYS A  55  LEU A  56  0                                        
SHEET    2 AA1 7 GLU A  31  SER A  36  1  N  SER A  36   O  LYS A  55           
SHEET    3 AA1 7 LYS A   4  VAL A   9  1  N  VAL A   5   O  GLU A  31           
SHEET    4 AA1 7 CYS A  67  ILE A  70  1  O  ALA A  69   N  LEU A   6           
SHEET    5 AA1 7 LEU A  99  ILE A 103  1  O  ALA A 101   N  ILE A  68           
SHEET    6 AA1 7 ILE A 148  SER A 151  1  O  VAL A 149   N  ALA A 102           
SHEET    7 AA1 7 VAL A 142  SER A 145 -1  N  SER A 145   O  ILE A 148           
SHEET    1 AA2 4 ILE A  42  ARG A  44  0                                        
SHEET    2 AA2 4 CYS A  50  LYS A  52 -1  O  VAL A  51   N  VAL A  43           
SHEET    3 AA2 4 CYS B  50  LYS B  52 -1  O  CYS B  50   N  LYS A  52           
SHEET    4 AA2 4 ILE B  42  ARG B  44 -1  N  VAL B  43   O  VAL B  51           
SHEET    1 AA3 7 LYS B  55  LEU B  56  0                                        
SHEET    2 AA3 7 GLU B  31  SER B  36  1  N  SER B  36   O  LYS B  55           
SHEET    3 AA3 7 LYS B   4  VAL B   9  1  N  VAL B   5   O  GLU B  31           
SHEET    4 AA3 7 CYS B  67  ILE B  70  1  O  ALA B  69   N  LEU B   6           
SHEET    5 AA3 7 LEU B  99  ILE B 103  1  O  ALA B 101   N  ILE B  70           
SHEET    6 AA3 7 ILE B 148  SER B 151  1  O  VAL B 149   N  ALA B 102           
SHEET    7 AA3 7 VAL B 142  SER B 145 -1  N  SER B 145   O  ILE B 148           
LINK         C   ILE A 103                 N   CSD A 104     1555   1555  1.34  
LINK         C   CSD A 104                 N   ALA A 105     1555   1555  1.33  
LINK         C   ILE B 103                 N   CSD B 104     1555   1555  1.34  
LINK         C   CSD B 104                 N   ALA B 105     1555   1555  1.34  
CISPEP   1 MET A   74    PRO A   75          0         2.23                     
CISPEP   2 MET B   74    PRO B   75          0         2.65                     
CRYST1   38.777   55.181   75.247  90.00  93.92  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      0.025788  0.000000  0.001767        0.00000                         
SCALE2      0.000000  0.018122  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013321        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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