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Database: PDB
Entry: 2QQ0
LinkDB: 2QQ0
Original site: 2QQ0 
HEADER    TRANSFERASE                             25-JUL-07   2QQ0              
TITLE     THYMIDINE KINASE FROM THERMOTOGA MARITIMA IN COMPLEX WITH             
TITLE    2 THYMIDINE + APPNHP                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THYMIDINE KINASE;                                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 2.7.1.21;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;                            
SOURCE   3 ORGANISM_TAXID: 2336;                                                
SOURCE   4 GENE: TDK;                                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET14B                                    
KEYWDS    THYMIDINE KINASE, TMTK, APPNHP, OPEN-CONFORMATION, ATP-               
KEYWDS   2 BINDING, CYTOPLASM, DNA SYNTHESIS, NUCLEOTIDE-BINDING,               
KEYWDS   3 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.SEGURA-PENA,J.LICHTER,M.TRANI,M.KONRAD,A.LAVIE,S.LUTZ               
REVDAT   2   30-DEC-08 2QQ0    1       JRNL   VERSN                             
REVDAT   1   16-OCT-07 2QQ0    0                                                
JRNL        AUTH   D.SEGURA-PENA,J.LICHTER,M.TRANI,M.KONRAD,A.LAVIE,            
JRNL        AUTH 2 S.LUTZ                                                       
JRNL        TITL   QUATERNARY STRUCTURE CHANGE AS A MECHANISM FOR THE           
JRNL        TITL 2 REGULATION OF THYMIDINE KINASE 1-LIKE ENZYMES.               
JRNL        REF    STRUCTURE                     V.  15  1555 2007              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   18073106                                                     
JRNL        DOI    10.1016/J.STR.2007.09.025                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 49113                          
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) : 0.175                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 5515                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3045                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.71                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2400                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 354                          
REMARK   3   BIN FREE R VALUE                    : 0.3040                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2659                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 100                                     
REMARK   3   SOLVENT ATOMS            : 383                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.03                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.43000                                             
REMARK   3    B22 (A**2) : 0.79000                                              
REMARK   3    B33 (A**2) : -0.31000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.11000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.079         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.086         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.053         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.397         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.967                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2801 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3787 ; 1.686 ; 2.023       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   333 ; 5.491 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   112 ;34.038 ;24.643       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   510 ;13.484 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;15.998 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   439 ; 0.093 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1986 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1476 ; 0.199 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1940 ; 0.312 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   384 ; 0.158 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     3 ; 0.047 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    46 ; 0.191 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    31 ; 0.132 ; 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):  1712 ; 1.096 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2709 ; 1.790 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1219 ; 2.897 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1078 ; 4.608 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2QQ0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JUL-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB043910.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-DEC-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54800                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.45                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.32000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.500                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 60-65% MPD + 0.1 M SODIUM ACETATE,       
REMARK 280  PH 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        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  1.000000  0.000000  0.000000       51.08000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.65500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       51.08000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       29.65500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE TETRAMERIC BIOLOGICAL ASSEMBLY IS GENERATED FROM THE     
REMARK 300 DIMER IN THE ASSIMETRIC UNIT BY THE OPERATION (-X, Y, -Z)            
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: 11370 ANGSTROM**2                         
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 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ILE A    41                                                      
REMARK 465     ASP A    42                                                      
REMARK 465     SER A    43                                                      
REMARK 465     ARG A    44                                                      
REMARK 465     TYR A    45                                                      
REMARK 465     HIS A    46                                                      
REMARK 465     SER A    47                                                      
REMARK 465     SER A    54                                                      
REMARK 465     GLY A    55                                                      
REMARK 465     ASN A    56                                                      
REMARK 465     GLY A    57                                                      
REMARK 465     LYS A   182                                                      
REMARK 465     ARG A   183                                                      
REMARK 465     VAL A   184                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ILE B    41                                                      
REMARK 465     ASP B    42                                                      
REMARK 465     SER B    43                                                      
REMARK 465     ARG B    44                                                      
REMARK 465     TYR B    45                                                      
REMARK 465     HIS B    46                                                      
REMARK 465     SER B    54                                                      
REMARK 465     GLY B    55                                                      
REMARK 465     ASN B    56                                                      
REMARK 465     GLY B    57                                                      
REMARK 465     LYS B   182                                                      
REMARK 465     ARG B   183                                                      
REMARK 465     VAL B   184                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     MET A  49    CG   SD   CE                                        
REMARK 470     VAL A  51    CG1  CG2                                            
REMARK 470     VAL B  58    CG1  CG2                                            
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   O    HOH B   729     O    HOH B   805              2.02            
REMARK 500   O    HOH A   646     O    HOH A   764              2.03            
REMARK 500   O    HOH A   633     O    HOH A   718              2.13            
REMARK 500   OD1  ASP A    98     O    HOH A   757              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    ASP B  83   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
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    ASN A 147       16.11   -148.72                                   
REMARK 500    ASP A 162      101.30   -163.24                                   
REMARK 500    ASN B 147       17.32   -145.18                                   
REMARK 500    ASP B 162      101.16   -163.44                                   
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                              MG A 450  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  17   OG1                                                    
REMARK 620 2 ANP A 601   O2B  90.5                                              
REMARK 620 3 ANP A 601   O3G 173.9  95.6                                        
REMARK 620 4 HOH A 749   O    88.8  86.6  91.4                                  
REMARK 620 5 HOH A 616   O    80.6  96.1  98.9 169.0                            
REMARK 620 6 HOH A 617   O    86.9 170.1  87.1  83.8  92.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 452  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B  17   OG1                                                    
REMARK 620 2 ADP B 701   O2B  87.0                                              
REMARK 620 3 TMP B 601   O1P 166.4 104.5                                        
REMARK 620 4 HOH B 844   O    92.0  88.8  95.5                                  
REMARK 620 5 HOH B 725   O    80.4  95.1  91.2 171.2                            
REMARK 620 6 HOH B 797   O    83.0 167.6  86.4  84.3  90.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 400  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 140   SG                                                     
REMARK 620 2 CYS A 143   SG  104.3                                              
REMARK 620 3 CYS A 173   SG  116.5 120.6                                        
REMARK 620 4 CYS A 176   SG  102.1 116.1  96.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 402  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 140   SG                                                     
REMARK 620 2 CYS B 143   SG  102.6                                              
REMARK 620 3 CYS B 173   SG  114.6 119.5                                        
REMARK 620 4 CYS B 176   SG  103.6 119.4  96.7                                  
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 400                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 402                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 450                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 452                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE THM A 501                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP B 601                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 601                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 701                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2QPO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2QQE   RELATED DB: PDB                                   
DBREF  2QQ0 A    1   184  UNP    Q9WYN2   KITH_THEMA       1    184             
DBREF  2QQ0 B    1   184  UNP    Q9WYN2   KITH_THEMA       1    184             
SEQRES   1 A  184  MET SER GLY LYS LEU THR VAL ILE THR GLY PRO MET TYR          
SEQRES   2 A  184  SER GLY LYS THR THR GLU LEU LEU SER PHE VAL GLU ILE          
SEQRES   3 A  184  TYR LYS LEU GLY LYS LYS LYS VAL ALA VAL PHE LYS PRO          
SEQRES   4 A  184  LYS ILE ASP SER ARG TYR HIS SER THR MET ILE VAL SER          
SEQRES   5 A  184  HIS SER GLY ASN GLY VAL GLU ALA HIS VAL ILE GLU ARG          
SEQRES   6 A  184  PRO GLU GLU MET ARG LYS TYR ILE GLU GLU ASP THR ARG          
SEQRES   7 A  184  GLY VAL PHE ILE ASP GLU VAL GLN PHE PHE ASN PRO SER          
SEQRES   8 A  184  LEU PHE GLU VAL VAL LYS ASP LEU LEU ASP ARG GLY ILE          
SEQRES   9 A  184  ASP VAL PHE CYS ALA GLY LEU ASP LEU THR HIS LYS GLN          
SEQRES  10 A  184  ASN PRO PHE GLU THR THR ALA LEU LEU LEU SER LEU ALA          
SEQRES  11 A  184  ASP THR VAL ILE LYS LYS LYS ALA VAL CYS HIS ARG CYS          
SEQRES  12 A  184  GLY GLU TYR ASN ALA THR LEU THR LEU LYS VAL ALA GLY          
SEQRES  13 A  184  GLY GLU GLU GLU ILE ASP VAL GLY GLY GLN GLU LYS TYR          
SEQRES  14 A  184  ILE ALA VAL CYS ARG ASP CYS TYR ASN THR LEU LYS LYS          
SEQRES  15 A  184  ARG VAL                                                      
SEQRES   1 B  184  MET SER GLY LYS LEU THR VAL ILE THR GLY PRO MET TYR          
SEQRES   2 B  184  SER GLY LYS THR THR GLU LEU LEU SER PHE VAL GLU ILE          
SEQRES   3 B  184  TYR LYS LEU GLY LYS LYS LYS VAL ALA VAL PHE LYS PRO          
SEQRES   4 B  184  LYS ILE ASP SER ARG TYR HIS SER THR MET ILE VAL SER          
SEQRES   5 B  184  HIS SER GLY ASN GLY VAL GLU ALA HIS VAL ILE GLU ARG          
SEQRES   6 B  184  PRO GLU GLU MET ARG LYS TYR ILE GLU GLU ASP THR ARG          
SEQRES   7 B  184  GLY VAL PHE ILE ASP GLU VAL GLN PHE PHE ASN PRO SER          
SEQRES   8 B  184  LEU PHE GLU VAL VAL LYS ASP LEU LEU ASP ARG GLY ILE          
SEQRES   9 B  184  ASP VAL PHE CYS ALA GLY LEU ASP LEU THR HIS LYS GLN          
SEQRES  10 B  184  ASN PRO PHE GLU THR THR ALA LEU LEU LEU SER LEU ALA          
SEQRES  11 B  184  ASP THR VAL ILE LYS LYS LYS ALA VAL CYS HIS ARG CYS          
SEQRES  12 B  184  GLY GLU TYR ASN ALA THR LEU THR LEU LYS VAL ALA GLY          
SEQRES  13 B  184  GLY GLU GLU GLU ILE ASP VAL GLY GLY GLN GLU LYS TYR          
SEQRES  14 B  184  ILE ALA VAL CYS ARG ASP CYS TYR ASN THR LEU LYS LYS          
SEQRES  15 B  184  ARG VAL                                                      
HET     ZN  A 400       1                                                       
HET     ZN  B 402       1                                                       
HET     MG  A 450       1                                                       
HET     MG  B 452       1                                                       
HET    THM  A 501      17                                                       
HET    TMP  B 601      21                                                       
HET    ANP  A 601      31                                                       
HET    ADP  B 701      27                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     THM THYMIDINE                                                        
HETNAM     TMP THYMIDINE-5'-PHOSPHATE                                           
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETSYN     THM DEOXYTHYMIDINE; 2'-DEOXYTHYMIDINE                                
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   5   MG    2(MG 2+)                                                     
FORMUL   7  THM    C10 H14 N2 O5                                                
FORMUL   8  TMP    C10 H15 N2 O8 P                                              
FORMUL   9  ANP    C10 H17 N6 O12 P3                                            
FORMUL  10  ADP    C10 H15 N5 O10 P2                                            
FORMUL  11  HOH   *383(H2 O)                                                    
HELIX    1   1 GLY A   15  GLY A   30  1                                  16    
HELIX    2   2 ARG A   65  ILE A   73  5                                   9    
HELIX    3   3 GLU A   84  PHE A   88  5                                   5    
HELIX    4   4 ASN A   89  PRO A   90  5                                   2    
HELIX    5   5 SER A   91  ARG A  102  1                                  12    
HELIX    6   6 PHE A  120  ALA A  130  1                                  11    
HELIX    7   7 CYS A  173  LYS A  181  1                                   9    
HELIX    8   8 GLY B   15  GLY B   30  1                                  16    
HELIX    9   9 ARG B   65  ILE B   73  5                                   9    
HELIX   10  10 GLU B   84  PHE B   88  5                                   5    
HELIX   11  11 ASN B   89  PRO B   90  5                                   2    
HELIX   12  12 SER B   91  ARG B  102  1                                  12    
HELIX   13  13 PHE B  120  ALA B  130  1                                  11    
HELIX   14  14 CYS B  173  LYS B  181  1                                   9    
SHEET    1   A 6 HIS A  61  ILE A  63  0                                        
SHEET    2   A 6 LYS A  33  PRO A  39  1  N  VAL A  36   O  HIS A  61           
SHEET    3   A 6 THR A  77  ILE A  82  1  O  ARG A  78   N  LYS A  33           
SHEET    4   A 6 ASP A 105  LEU A 111  1  O  PHE A 107   N  ILE A  82           
SHEET    5   A 6 LEU A   5  GLY A  10  1  N  ILE A   8   O  CYS A 108           
SHEET    6   A 6 THR A 132  LYS A 135  1  O  ILE A 134   N  THR A   9           
SHEET    1   B 2 LEU A 150  LYS A 153  0                                        
SHEET    2   B 2 TYR A 169  VAL A 172 -1  O  ILE A 170   N  LEU A 152           
SHEET    1   C 6 HIS B  61  ILE B  63  0                                        
SHEET    2   C 6 LYS B  33  PRO B  39  1  N  VAL B  36   O  HIS B  61           
SHEET    3   C 6 THR B  77  ILE B  82  1  O  PHE B  81   N  PHE B  37           
SHEET    4   C 6 ASP B 105  GLY B 110  1  O  PHE B 107   N  ILE B  82           
SHEET    5   C 6 LEU B   5  THR B   9  1  N  ILE B   8   O  CYS B 108           
SHEET    6   C 6 THR B 132  LYS B 135  1  O  ILE B 134   N  VAL B   7           
SHEET    1   D 2 LEU B 150  LYS B 153  0                                        
SHEET    2   D 2 TYR B 169  VAL B 172 -1  O  ILE B 170   N  LEU B 152           
LINK         OG1 THR A  17                MG    MG A 450     1555   1555  2.15  
LINK         OG1 THR B  17                MG    MG B 452     1555   1555  2.15  
LINK        MG    MG A 450                 O2B ANP A 601     1555   1555  2.02  
LINK        MG    MG A 450                 O3G ANP A 601     1555   1555  1.98  
LINK        MG    MG B 452                 O2B ADP B 701     1555   1555  1.92  
LINK        MG    MG B 452                 O1P TMP B 601     1555   1555  1.96  
LINK        MG    MG A 450                 O   HOH A 749     1555   1555  2.12  
LINK        MG    MG A 450                 O   HOH A 616     1555   1555  2.22  
LINK        MG    MG A 450                 O   HOH A 617     1555   1555  2.17  
LINK        MG    MG B 452                 O   HOH B 844     1555   1555  2.11  
LINK        MG    MG B 452                 O   HOH B 725     1555   1555  2.22  
LINK        MG    MG B 452                 O   HOH B 797     1555   1555  2.11  
LINK         SG  CYS A 140                ZN    ZN A 400     1555   1555  2.31  
LINK         SG  CYS A 143                ZN    ZN A 400     1555   1555  2.39  
LINK         SG  CYS A 173                ZN    ZN A 400     1555   1555  2.34  
LINK         SG  CYS A 176                ZN    ZN A 400     1555   1555  2.50  
LINK         SG  CYS B 140                ZN    ZN B 402     1555   1555  2.37  
LINK         SG  CYS B 143                ZN    ZN B 402     1555   1555  2.35  
LINK         SG  CYS B 173                ZN    ZN B 402     1555   1555  2.39  
LINK         SG  CYS B 176                ZN    ZN B 402     1555   1555  2.32  
SITE     1 AC1  4 CYS A 140  CYS A 143  CYS A 173  CYS A 176                    
SITE     1 AC2  4 CYS B 140  CYS B 143  CYS B 173  CYS B 176                    
SITE     1 AC3  5 THR A  17  ANP A 601  HOH A 616  HOH A 617                    
SITE     2 AC3  5 HOH A 749                                                     
SITE     1 AC4  6 THR B  17  TMP B 601  ADP B 701  HOH B 725                    
SITE     2 AC4  6 HOH B 797  HOH B 844                                          
SITE     1 AC5 16 GLU A  84  GLN A  86  PHE A  87  LEU A 111                    
SITE     2 AC5 16 THR A 114  HIS A 115  THR A 151  GLU A 160                    
SITE     3 AC5 16 ILE A 161  ASP A 162  VAL A 163  GLY A 164                    
SITE     4 AC5 16 TYR A 169  ANP A 601  HOH A 675  HOH A 767                    
SITE     1 AC6 24 MET B  12  LYS B  16  HIS B  53  GLU B  84                    
SITE     2 AC6 24 GLN B  86  PHE B  87  LEU B 111  THR B 114                    
SITE     3 AC6 24 HIS B 115  THR B 151  GLU B 160  ILE B 161                    
SITE     4 AC6 24 ASP B 162  VAL B 163  GLY B 164  TYR B 169                    
SITE     5 AC6 24  MG B 452  ADP B 701  HOH B 717  HOH B 725                    
SITE     6 AC6 24 HOH B 774  HOH B 797  HOH B 798  HOH B 844                    
SITE     1 AC7 23 MET A  12  TYR A  13  SER A  14  GLY A  15                    
SITE     2 AC7 23 LYS A  16  THR A  17  THR A  18  SER A  52                    
SITE     3 AC7 23 HIS A  53  GLU A  84  ALA A 138  VAL A 139                    
SITE     4 AC7 23 GLN A 166   MG A 450  THM A 501  HOH A 617                    
SITE     5 AC7 23 HOH A 640  HOH A 643  HOH A 675  HOH A 708                    
SITE     6 AC7 23 HOH A 749  GLU B  25  LEU B  29                               
SITE     1 AC8 20 GLU A  25  LEU A  29  TYR B  13  SER B  14                    
SITE     2 AC8 20 GLY B  15  LYS B  16  THR B  17  THR B  18                    
SITE     3 AC8 20 SER B  52  HIS B  53  ALA B 138  VAL B 139                    
SITE     4 AC8 20  MG B 452  TMP B 601  HOH B 725  HOH B 811                    
SITE     5 AC8 20 HOH B 828  HOH B 843  HOH B 844  HOH B 882                    
CRYST1  102.160   59.310   61.300  90.00 103.02  90.00 C 1 2 1       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      0.009789  0.000000  0.002264        0.00000                         
SCALE2      0.000000  0.016861  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016744        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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