GenomeNet

Database: PDB
Entry: 2JA1
LinkDB: 2JA1
Original site: 2JA1 
HEADER    TRANSFERASE                             17-NOV-06   2JA1              
TITLE     THYMIDINE KINASE FROM B. CEREUS WITH TTP BOUND AS PHOSPHATE           
TITLE    2 DONOR.                                                               
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: BACILLUS CEREUS;                                
SOURCE   3 ORGANISM_TAXID: 1396;                                                
SOURCE   4 STRAIN: DVI;                                                         
SOURCE   5 VARIANT: 98-7869;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: KY895;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PGEX-2T                                    
KEYWDS    TK1, DNK, LASSO, KINASE, TRANSFERASE, PHOSPHATE DONOR,                
KEYWDS   2 DEOXYRIBONUCLEOSIDE KINASE                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    U.KOSINSKA,C.CARNROT,M.P.B.SANDRINI,A.R.CLAUSEN,L.WANG,J.PISKUR,      
AUTHOR   2 S.ERIKSSON,H.EKLUND                                                  
REVDAT   3   13-JUL-11 2JA1    1       VERSN                                    
REVDAT   2   24-FEB-09 2JA1    1       VERSN                                    
REVDAT   1   23-JAN-07 2JA1    0                                                
JRNL        AUTH   U.KOSINSKA,C.CARNROT,M.P.B.SANDRINI,A.R.CLAUSEN,L.WANG,      
JRNL        AUTH 2 J.PISKUR,S.ERIKSSON,H.EKLUND                                 
JRNL        TITL   STRUCTURAL STUDIES OF THYMIDINE KINASES FROM BACILLUS        
JRNL        TITL 2 ANTHRACIS AND BACILLUS CEREUS PROVIDE INSIGHTS INTO          
JRNL        TITL 3 QUATERNARY STRUCTURE AND CONFORMATIONAL CHANGES UPON         
JRNL        TITL 4 SUBSTRATE BINDING                                            
JRNL        REF    FEBS J.                       V. 274   727 2007              
JRNL        REFN                   ISSN 1742-464X                               
JRNL        PMID   17288553                                                     
JRNL        DOI    10.1111/J.1742-4658.2006.05617.X                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.8  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.63                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 11450                          
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) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 574                             
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 795                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3520                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 53                           
REMARK   3   BIN FREE R VALUE                    : 0.3940                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1499                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 38                                      
REMARK   3   SOLVENT ATOMS            : 20                                      
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) : 57.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.34000                                              
REMARK   3    B22 (A**2) : 3.34000                                              
REMARK   3    B33 (A**2) : -6.68000                                             
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): 0.305         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.251         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.178         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.574        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1567 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2130 ; 1.479 ; 1.977       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   192 ; 6.296 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    73 ;36.959 ;23.973       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   258 ;17.675 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;19.696 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   238 ; 0.098 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1179 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   649 ; 0.223 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1046 ; 0.311 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    50 ; 0.159 ; 0.200       
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):    39 ; 0.192 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.180 ; 0.200       
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):   976 ; 0.476 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1557 ; 0.872 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   645 ; 1.330 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   573 ; 2.243 ; 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    -1        A   191                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.0244   8.8685  12.6826              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1380 T22:  -0.0656                                     
REMARK   3      T33:  -0.1998 T12:   0.0397                                     
REMARK   3      T13:  -0.0243 T23:  -0.0526                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9811 L22:   4.9808                                     
REMARK   3      L33:   3.2741 L12:  -1.0101                                     
REMARK   3      L13:  -0.2014 L23:  -0.0342                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0813 S12:  -0.3480 S13:   0.1560                       
REMARK   3      S21:   0.3534 S22:   0.0032 S23:  -0.4679                       
REMARK   3      S31:  -0.3036 S32:   0.6285 S33:  -0.0845                       
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: NULL                                      
REMARK   4                                                                      
REMARK   4 2JA1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-NOV-06.                  
REMARK 100 THE PDBE ID CODE IS EBI-30518.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12035                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 13.600                             
REMARK 200  R MERGE                    (I) : 0.00000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.00                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.53000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2J9R                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 76.6                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.3                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 60% MPD 0.1M HEPES PH7                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   -X+1/2,Y,-Z+3/4                                         
REMARK 290       6555   X,-Y+1/2,-Z+1/4                                         
REMARK 290       7555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X,-Y,Z                                                 
REMARK 290      11555   -Y+1/2,X,Z+3/4                                          
REMARK 290      12555   Y,-X+1/2,Z+1/4                                          
REMARK 290      13555   -X,Y+1/2,-Z+1/4                                         
REMARK 290      14555   X+1/2,-Y,-Z+3/4                                         
REMARK 290      15555   Y,X,-Z                                                  
REMARK 290      16555   -Y+1/2,-X+1/2,-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       47.69500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       47.69500            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      102.43100            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       47.69500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       51.21550            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       47.69500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      153.64650            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       47.69500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      153.64650            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       47.69500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       51.21550            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000       47.69500            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       47.69500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      102.43100            
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        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       47.69500            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       47.69500            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      102.43100            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       47.69500            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000      153.64650            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       47.69500            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       51.21550            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       47.69500            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       51.21550            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       47.69500            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      153.64650            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       47.69500            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       47.69500            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      102.43100            
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: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  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        0.00000            
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  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  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     ASN A   192                                                      
REMARK 465     LYS A   193                                                      
REMARK 465     ASP A   194                                                      
REMARK 465     LYS A   195                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
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   ATM2   ATM3                                     
REMARK 500    PRO A 190   CA  -  C   -  N   ANGL. DEV. =  13.4 DEGREES          
REMARK 500    PRO A 190   O   -  C   -  N   ANGL. DEV. = -14.1 DEGREES          
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    ASP A  94     -174.24    -62.54                                   
REMARK 500    PHE A 125      -93.60    -78.40                                   
REMARK 500    SER A 153       10.74   -145.89                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL A 173        24.8      L          L   OUTSIDE RANGE           
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 A1192  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 145   SG                                                     
REMARK 620 2 CYS A 148   SG  100.9                                              
REMARK 620 3 CYS A 183   SG  121.6 118.7                                        
REMARK 620 4 CYS A 186   SG  101.2 116.2  97.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1192                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP A1193                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A1194                 
DBREF  2JA1 A   -1     0  PDB    2JA1     2JA1            -1      0             
DBREF  2JA1 A    1   195  UNP    Q0H9H6   Q0H0H6_BACCE     1    195             
SEQRES   1 A  197  GLY SER MET TYR LEU ILE ASN GLN ASN GLY TRP ILE GLU          
SEQRES   2 A  197  VAL ILE CYS GLY SER MET PHE SER GLY LYS SER GLU GLU          
SEQRES   3 A  197  LEU ILE ARG ARG VAL ARG ARG THR GLN PHE ALA LYS GLN          
SEQRES   4 A  197  HIS ALA ILE VAL PHE LYS PRO CYS ILE ASP ASN ARG TYR          
SEQRES   5 A  197  SER GLU GLU ASP VAL VAL SER HIS ASN GLY LEU LYS VAL          
SEQRES   6 A  197  LYS ALA VAL PRO VAL SER ALA SER LYS ASP ILE PHE GLU          
SEQRES   7 A  197  HIS ILE THR GLU GLU LEU ASP VAL ILE ALA ILE ASP GLU          
SEQRES   8 A  197  VAL GLN PHE PHE ASP GLY ASP ILE VAL GLU VAL VAL GLN          
SEQRES   9 A  197  VAL LEU ALA ASN ARG GLY TYR ARG VAL ILE VAL ALA GLY          
SEQRES  10 A  197  LEU ASP GLN ASP PHE ARG GLY LEU PRO PHE GLY GLN VAL          
SEQRES  11 A  197  PRO GLN LEU MET ALA ILE ALA GLU HIS VAL THR LYS LEU          
SEQRES  12 A  197  GLN ALA VAL CYS SER VAL CYS GLY SER PRO ALA SER ARG          
SEQRES  13 A  197  THR GLN ARG LEU ILE ASP GLY GLU PRO ALA ALA PHE ASP          
SEQRES  14 A  197  ASP PRO ILE ILE LEU VAL GLY ALA SER GLU SER TYR GLU          
SEQRES  15 A  197  PRO ARG CYS ARG HIS CYS HIS ALA VAL PRO ALA ASN LYS          
SEQRES  16 A  197  ASP LYS                                                      
HET     ZN  A1192       1                                                       
HET    TTP  A1193      29                                                       
HET    MPD  A1194       8                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     TTP THYMIDINE-5'-TRIPHOSPHATE                                        
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  TTP    C10 H17 N2 O14 P3                                            
FORMUL   4  MPD    C6 H14 O2                                                    
FORMUL   5  HOH   *20(H2 O)                                                     
HELIX    1   1 GLY A   20  ALA A   35  1                                  16    
HELIX    2   2 ALA A   70  ILE A   78  5                                   9    
HELIX    3   3 GLU A   89  PHE A   93  5                                   5    
HELIX    4   4 ASP A   96  ARG A  107  1                                  12    
HELIX    5   5 GLN A  127  ALA A  135  1                                   9    
SHEET    1  AA 6 VAL A  66  VAL A  68  0                                        
SHEET    2  AA 6 ALA A  39  PRO A  44  1  O  VAL A  41   N  VAL A  66           
SHEET    3  AA 6 VAL A  84  ILE A  87  1  O  VAL A  84   N  ILE A  40           
SHEET    4  AA 6 ARG A 110  LEU A 116  1  O  ARG A 110   N  ILE A  85           
SHEET    5  AA 6 TRP A   9  GLY A  15  1  O  TRP A   9   N  VAL A 111           
SHEET    6  AA 6 HIS A 137  LYS A 140  1  O  HIS A 137   N  VAL A  12           
SHEET    1  AB 2 ASP A  54  VAL A  56  0                                        
SHEET    2  AB 2 LYS A  62  LYS A  64 -1  O  VAL A  63   N  VAL A  55           
SHEET    1  AC 2 ALA A 143  CYS A 145  0                                        
SHEET    2  AC 2 GLY A 149  ALA A 152 -1  O  SER A 150   N  CYS A 145           
SHEET    1  AD 3 GLU A 162  PRO A 163  0                                        
SHEET    2  AD 3 ARG A 154  ILE A 159 -1  O  ILE A 159   N  GLU A 162           
SHEET    3  AD 3 GLU A 177  ARG A 182 -1  O  SER A 178   N  LEU A 158           
LINK        ZN    ZN A1192                 SG  CYS A 145     1555   1555  2.23  
LINK        ZN    ZN A1192                 SG  CYS A 148     1555   1555  2.28  
LINK        ZN    ZN A1192                 SG  CYS A 183     1555   1555  2.35  
LINK        ZN    ZN A1192                 SG  CYS A 186     1555   1555  2.50  
SITE     1 AC1  4 CYS A 145  CYS A 148  CYS A 183  CYS A 186                    
SITE     1 AC2 17 SER A  16  PHE A  18  SER A  19  GLY A  20                    
SITE     2 AC2 17 LYS A  21  SER A  22  GLU A  23  PHE A  34                    
SITE     3 AC2 17 VAL A  56  SER A  57  HIS A  58  ASN A  59                    
SITE     4 AC2 17 ASP A  88  GLU A  89  VAL A 144  HOH A2009                    
SITE     5 AC2 17 HOH A2020                                                     
SITE     1 AC3  7 PHE A  92  LEU A 116  ASP A 119  PHE A 120                    
SITE     2 AC3  7 PHE A 125  ILE A 170  TYR A 179                               
CRYST1   95.390   95.390  204.862  90.00  90.00  90.00 I 41 2 2     16          
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      0.010483  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010483  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004881        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system