GenomeNet

Database: PDB
Entry: 3E2I
LinkDB: 3E2I
Original site: 3E2I 
HEADER    TRANSFERASE                             05-AUG-08   3E2I              
TITLE     CRYSTAL STRUCTURE OF THYMIDINE KINASE FROM S. AUREUS                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THYMIDINE KINASE;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 2.7.1.21;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE   3 ORGANISM_TAXID: 1280;                                                
SOURCE   4 GENE: TDK;                                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)CODONPLUS RIPL;                   
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    ZN-BINDING, ATP-BINDING, DNA SYNTHESIS, KINASE, NUCLEOTIDE-BINDING,   
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.LAM,K.JOHNS,K.P.BATTAILE,V.ROMANOV,K.LAM,E.F.PAI,N.Y.CHIRGADZE      
REVDAT   2   13-JUL-11 3E2I    1       VERSN                                    
REVDAT   1   11-AUG-09 3E2I    0                                                
JRNL        AUTH   R.LAM,K.JOHNS,K.P.BATTAILE,V.ROMANOV,K.LAM,E.F.PAI,          
JRNL        AUTH 2 N.Y.CHIRGADZE                                                
JRNL        TITL   CRYSTAL STRUCTURE OF THYMIDINE KINASE FROM S. AUREUS         
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.01 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0043                                      
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) : 2.01                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.81                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 17194                          
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) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 871                             
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) : 2.01                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.07                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1176                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.92                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2020                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 55                           
REMARK   3   BIN FREE R VALUE                    : 0.2790                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1341                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 7                                       
REMARK   3   SOLVENT ATOMS            : 58                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.27                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.03000                                              
REMARK   3    B22 (A**2) : 0.03000                                              
REMARK   3    B33 (A**2) : -0.06000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.151         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.143         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.088         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.633         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1377 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1858 ; 1.228 ; 1.964       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   177 ; 4.989 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    58 ;32.164 ;24.138       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   250 ;14.375 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;14.378 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   213 ; 0.079 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1016 ; 0.005 ; 0.021       
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):   875 ; 0.681 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1419 ; 1.309 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   502 ; 2.255 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   437 ; 3.701 ; 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  : 1                                          
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     7        A   192                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.9370  13.4810  12.5360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1067 T22:   0.0441                                     
REMARK   3      T33:   0.0789 T12:   0.0002                                     
REMARK   3      T13:  -0.0117 T23:  -0.0359                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8770 L22:   0.7463                                     
REMARK   3      L33:   1.8932 L12:  -0.2124                                     
REMARK   3      L13:  -0.0657 L23:  -0.2179                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0030 S12:  -0.0797 S13:   0.1575                       
REMARK   3      S21:   0.1532 S22:  -0.0289 S23:  -0.0553                       
REMARK   3      S31:  -0.3488 S32:  -0.0403 S33:   0.0258                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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:                                           
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS                   
REMARK   3  U VALUES      : RESIDUAL ONLY                                       
REMARK   4                                                                      
REMARK   4 3E2I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-AUG-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB048792.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-MAR-07                          
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               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979331                           
REMARK 200  MONOCHROMATOR                  : SI(111) DOUBLE-CRYSTAL             
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : SI(111) DOUBLE-CRYSTAL             
REMARK 200                                   MONOCHROMATOR                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17226                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.010                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 24.500                             
REMARK 200  R MERGE                    (I) : 0.06400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 22.90                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.18300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SUCCINIC ACID PH 7.0, 15%           
REMARK 280  PEG3350, CRYO-PROTECTED USING 20% GLYCEROL, VAPOR DIFFUSION,        
REMARK 280  SITTING DROP, TEMPERATURE 298.0K                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z+1/2                                              
REMARK 290       4555   Y,-X,Z+1/2                                              
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z                                                 
REMARK 290       7555   Y,X,-Z+1/2                                              
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       48.07200            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       48.07200            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       48.07200            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       48.07200            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL                        
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   BIOMT1   2 -1.000000  0.000000  0.000000       71.62100            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000       71.62100            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 225  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 247  LIES ON A SPECIAL POSITION.                          
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     MSE A   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MSE A     1                                                      
REMARK 465     TYR A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     TYR A     5                                                      
REMARK 465     HIS A     6                                                      
REMARK 465     ILE A    46                                                      
REMARK 465     ASP A    47                                                      
REMARK 465     ASP A    48                                                      
REMARK 465     ARG A    49                                                      
REMARK 465     TYR A    50                                                      
REMARK 465     HIS A    51                                                      
REMARK 465     LYS A    52                                                      
REMARK 465     GLU A    53                                                      
REMARK 465     LYS A    54                                                      
REMARK 465     VAL A    55                                                      
REMARK 465     VAL A    56                                                      
REMARK 465     ASP A   193                                                      
REMARK 465     ASN A   194                                                      
REMARK 465     ASN A   195                                                      
REMARK 465     LYS A   196                                                      
REMARK 465     GLU A   197                                                      
REMARK 465     GLU A   198                                                      
REMARK 465     LEU A   199                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A  12   CB    CYS A  12   SG     -0.102                       
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    ALA A 143     -160.53   -105.75                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 200  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 145   SG                                                     
REMARK 620 2 CYS A 148   SG  109.5                                              
REMARK 620 3 CYS A 183   SG  113.9 116.6                                        
REMARK 620 4 HIS A 186   ND1 115.9 111.0  88.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 200                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 201                 
DBREF  3E2I A    1   199  UNP    Q0H0G9   Q0H0G9_STAAU     1    199             
SEQADV 3E2I MSE A  -19  UNP  Q0H0G9              EXPRESSION TAG                 
SEQADV 3E2I GLY A  -18  UNP  Q0H0G9              EXPRESSION TAG                 
SEQADV 3E2I SER A  -17  UNP  Q0H0G9              EXPRESSION TAG                 
SEQADV 3E2I SER A  -16  UNP  Q0H0G9              EXPRESSION TAG                 
SEQADV 3E2I HIS A  -15  UNP  Q0H0G9              EXPRESSION TAG                 
SEQADV 3E2I HIS A  -14  UNP  Q0H0G9              EXPRESSION TAG                 
SEQADV 3E2I HIS A  -13  UNP  Q0H0G9              EXPRESSION TAG                 
SEQADV 3E2I HIS A  -12  UNP  Q0H0G9              EXPRESSION TAG                 
SEQADV 3E2I HIS A  -11  UNP  Q0H0G9              EXPRESSION TAG                 
SEQADV 3E2I HIS A  -10  UNP  Q0H0G9              EXPRESSION TAG                 
SEQADV 3E2I SER A   -9  UNP  Q0H0G9              EXPRESSION TAG                 
SEQADV 3E2I SER A   -8  UNP  Q0H0G9              EXPRESSION TAG                 
SEQADV 3E2I GLY A   -7  UNP  Q0H0G9              EXPRESSION TAG                 
SEQADV 3E2I LEU A   -6  UNP  Q0H0G9              EXPRESSION TAG                 
SEQADV 3E2I VAL A   -5  UNP  Q0H0G9              EXPRESSION TAG                 
SEQADV 3E2I PRO A   -4  UNP  Q0H0G9              EXPRESSION TAG                 
SEQADV 3E2I ARG A   -3  UNP  Q0H0G9              EXPRESSION TAG                 
SEQADV 3E2I GLY A   -2  UNP  Q0H0G9              EXPRESSION TAG                 
SEQADV 3E2I SER A   -1  UNP  Q0H0G9              EXPRESSION TAG                 
SEQADV 3E2I HIS A    0  UNP  Q0H0G9              EXPRESSION TAG                 
SEQRES   1 A  219  MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  219  LEU VAL PRO ARG GLY SER HIS MSE TYR GLU THR TYR HIS          
SEQRES   3 A  219  SER GLY TRP ILE GLU CYS ILE THR GLY SER MSE PHE SER          
SEQRES   4 A  219  GLY LYS SER GLU GLU LEU ILE ARG ARG LEU ARG ARG GLY          
SEQRES   5 A  219  ILE TYR ALA LYS GLN LYS VAL VAL VAL PHE LYS PRO ALA          
SEQRES   6 A  219  ILE ASP ASP ARG TYR HIS LYS GLU LYS VAL VAL SER HIS          
SEQRES   7 A  219  ASN GLY ASN ALA ILE GLU ALA ILE ASN ILE SER LYS ALA          
SEQRES   8 A  219  SER GLU ILE MSE THR HIS ASP LEU THR ASN VAL ASP VAL          
SEQRES   9 A  219  ILE GLY ILE ASP GLU VAL GLN PHE PHE ASP ASP GLU ILE          
SEQRES  10 A  219  VAL SER ILE VAL GLU LYS LEU SER ALA ASP GLY HIS ARG          
SEQRES  11 A  219  VAL ILE VAL ALA GLY LEU ASP MSE ASP PHE ARG GLY GLU          
SEQRES  12 A  219  PRO PHE GLU PRO MSE PRO LYS LEU MSE ALA VAL SER GLU          
SEQRES  13 A  219  GLN VAL THR LYS LEU GLN ALA VAL CYS ALA VAL CYS GLY          
SEQRES  14 A  219  SER SER SER SER ARG THR GLN ARG LEU ILE ASN GLY LYS          
SEQRES  15 A  219  PRO ALA LYS ILE ASP ASP PRO ILE ILE LEU VAL GLY ALA          
SEQRES  16 A  219  ASN GLU SER TYR GLU PRO ARG CYS ARG ALA HIS HIS ILE          
SEQRES  17 A  219  VAL ALA PRO SER ASP ASN ASN LYS GLU GLU LEU                  
MODRES 3E2I MSE A   17  MET  SELENOMETHIONINE                                   
MODRES 3E2I MSE A   75  MET  SELENOMETHIONINE                                   
MODRES 3E2I MSE A  118  MET  SELENOMETHIONINE                                   
MODRES 3E2I MSE A  128  MET  SELENOMETHIONINE                                   
MODRES 3E2I MSE A  132  MET  SELENOMETHIONINE                                   
HET    MSE  A  17       8                                                       
HET    MSE  A  75       8                                                       
HET    MSE  A 118       8                                                       
HET    MSE  A 128      13                                                       
HET    MSE  A 132       8                                                       
HET     ZN  A 200       1                                                       
HET    GOL  A 201       6                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      ZN ZINC ION                                                         
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  MSE    5(C5 H11 N O2 SE)                                            
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  GOL    C3 H8 O3                                                     
FORMUL   4  HOH   *58(H2 O)                                                     
HELIX    1   1 GLY A   20  ALA A   35  1                                  16    
HELIX    2   2 LYS A   70  HIS A   77  5                                   8    
HELIX    3   3 GLU A   89  ASP A   94  5                                   6    
HELIX    4   4 ASP A   95  ASP A  107  1                                  13    
HELIX    5   5 PRO A  127  SER A  135  1                                   9    
HELIX    6   6 CYS A  183  HIS A  187  5                                   5    
SHEET    1   A 6 GLU A  64  ILE A  68  0                                        
SHEET    2   A 6 VAL A  39  PRO A  44  1  N  VAL A  41   O  ILE A  66           
SHEET    3   A 6 VAL A  84  ILE A  87  1  O  GLY A  86   N  VAL A  40           
SHEET    4   A 6 ARG A 110  LEU A 116  1  O  ARG A 110   N  ILE A  85           
SHEET    5   A 6 TRP A   9  GLY A  15  1  N  ILE A  13   O  VAL A 113           
SHEET    6   A 6 GLN A 137  LEU A 141  1  O  LEU A 141   N  THR A  14           
SHEET    1   B 2 ALA A 143  VAL A 144  0                                        
SHEET    2   B 2 SER A 151  SER A 152 -1  O  SER A 152   N  ALA A 143           
SHEET    1   C 3 LYS A 162  PRO A 163  0                                        
SHEET    2   C 3 ARG A 154  ILE A 159 -1  N  ILE A 159   O  LYS A 162           
SHEET    3   C 3 GLU A 177  ARG A 182 -1  O  SER A 178   N  LEU A 158           
LINK         C   SER A  16                 N   MSE A  17     1555   1555  1.33  
LINK         C   MSE A  17                 N   PHE A  18     1555   1555  1.33  
LINK         C   ILE A  74                 N   MSE A  75     1555   1555  1.32  
LINK         C   MSE A  75                 N   THR A  76     1555   1555  1.34  
LINK         C   ASP A 117                 N   MSE A 118     1555   1555  1.33  
LINK         C   MSE A 118                 N   ASP A 119     1555   1555  1.33  
LINK         C   PRO A 127                 N   MSE A 128     1555   1555  1.33  
LINK         C   MSE A 128                 N   PRO A 129     1555   1555  1.35  
LINK         C   LEU A 131                 N   MSE A 132     1555   1555  1.33  
LINK         C   MSE A 132                 N   ALA A 133     1555   1555  1.33  
LINK         SG  CYS A 145                ZN    ZN A 200     1555   1555  2.36  
LINK         SG  CYS A 148                ZN    ZN A 200     1555   1555  2.31  
LINK         SG  CYS A 183                ZN    ZN A 200     1555   1555  2.22  
LINK         ND1 HIS A 186                ZN    ZN A 200     1555   1555  2.25  
CISPEP   1 GLU A  126    PRO A  127          0        -0.30                     
SITE     1 AC1  4 CYS A 145  CYS A 148  CYS A 183  HIS A 186                    
SITE     1 AC2  9 SER A  16  MSE A  17  PHE A  18  SER A  19                    
SITE     2 AC2  9 GLY A  20  LYS A  21  SER A  22  ARG A  31                    
SITE     3 AC2  9 HOH A 227                                                     
CRYST1   71.621   71.621   96.144  90.00  90.00  90.00 P 42 2 2      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      0.013962  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013962  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010401        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system