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Database: PDB
Entry: 3ETH
LinkDB: 3ETH
Original site: 3ETH 
HEADER    LYASE                                   08-OCT-08   3ETH              
TITLE     CRYSTAL STRUCTURE OF E. COLI PURK IN COMPLEX WITH MGATP               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE ATPASE SUBUNIT;   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: AIR CARBOXYLASE, AIRC;                                      
COMPND   5 EC: 4.1.1.21;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: B0522, JW0511, PURK, PURK_ECOLI;                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: HMS174(DE3);                               
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET31                                     
KEYWDS    ATP-GRASP, PURINE BIOSYNTHESIS, ANTIMICROBIAL, ATP-BINDING,           
KEYWDS   2 DECARBOXYLASE, LYASE, NUCLEOTIDE-BINDING                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.M.HOLDEN,J.B.THODEN                                                 
REVDAT   5   25-OCT-17 3ETH    1       REMARK                                   
REVDAT   4   09-JUN-09 3ETH    1       REVDAT                                   
REVDAT   3   24-FEB-09 3ETH    1       VERSN                                    
REVDAT   2   30-DEC-08 3ETH    1       JRNL                                     
REVDAT   1   21-OCT-08 3ETH    0                                                
JRNL        AUTH   J.B.THODEN,H.M.HOLDEN,S.M.FIRESTINE                          
JRNL        TITL   STRUCTURAL ANALYSIS OF THE ACTIVE SITE GEOMETRY OF           
JRNL        TITL 2 N(5)-CARBOXYAMINOIMIDAZOLE RIBONUCLEOTIDE SYNTHETASE FROM    
JRNL        TITL 3 ESCHERICHIA COLI.                                            
JRNL        REF    BIOCHEMISTRY                  V.  47 13346 2008              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   19053251                                                     
JRNL        DOI    10.1021/BI801734Z                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT                                                  
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 87820                          
REMARK   3                                                                      
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDON                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.178                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 8777                            
REMARK   3                                                                      
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.1780                 
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 87820                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5572                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 66                                      
REMARK   3   SOLVENT ATOMS            : 690                                     
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : NULL  ; NULL  ; NULL            
REMARK   3   BOND ANGLES            (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL            
REMARK   3   GENERAL PLANES               (A) : NULL  ; NULL  ; NULL            
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL            
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL            
REMARK   3                                                                      
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL                             
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  RESTRAINT LIBRARIES.                                                
REMARK   3   STEREOCHEMISTRY : ENGH & HUBER                                     
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL                         
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3ETH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-OCT-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000049746.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-DEC-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : SBC-3                              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : D*TREK, SCALEPACK                  
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 87837                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.8                               
REMARK 200  DATA REDUNDANCY                : 2.300                              
REMARK 200  R MERGE                    (I) : 0.03300                            
REMARK 200  R SYM                      (I) : 0.03300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 29.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.09800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.09800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1B6S                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-25% MONOMETHYLETHER POLY(ETHYLENE     
REMARK 280  GLYCOL) 5000, 10 MM MGATP, 10 MM AMINOPYRAZOLE RIBONUCLEOTIDE,      
REMARK 280  PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5060 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 A   615     O    HOH A   616              2.19            
REMARK 500   O    HIS A    65     NH2  ARG A    71              2.19            
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    MET A   1   CG  -  SD  -  CE  ANGL. DEV. =   9.6 DEGREES          
REMARK 500    LYS A   2   CB  -  CA  -  C   ANGL. DEV. = -12.7 DEGREES          
REMARK 500    ARG A  14   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG A  14   NE  -  CZ  -  NH2 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ARG A  17   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A 135   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    GLU A 153   CB  -  CA  -  C   ANGL. DEV. = -12.4 DEGREES          
REMARK 500    LEU A 271   CB  -  CG  -  CD2 ANGL. DEV. = -10.8 DEGREES          
REMARK 500    ARG A 327   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG B  17   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    LEU B  92   CB  -  CG  -  CD2 ANGL. DEV. = -12.0 DEGREES          
REMARK 500    ARG B 112   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    LEU B 134   CB  -  CG  -  CD1 ANGL. DEV. =  12.9 DEGREES          
REMARK 500    ARG B 168   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG B 168   NE  -  CZ  -  NH2 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG B 205   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    LEU B 210   CB  -  CG  -  CD1 ANGL. DEV. =  10.6 DEGREES          
REMARK 500    ASP B 306   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    ARG B 313   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ARG B 313   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    LEU B 320   CA  -  CB  -  CG  ANGL. DEV. =  15.5 DEGREES          
REMARK 500    LEU B 320   CB  -  CG  -  CD2 ANGL. DEV. = -13.0 DEGREES          
REMARK 500    ARG B 327   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG B 327   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.5 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    LYS A   2      149.06    -27.92                                   
REMARK 500    ALA A  67       50.44    -96.29                                   
REMARK 500    ASP A 127       28.35     46.43                                   
REMARK 500    ARG A 242     -178.50    172.81                                   
REMARK 500    ARG B  64       14.30     58.22                                   
REMARK 500    ARG B 242      177.83    177.62                                   
REMARK 500    GLU B 342       -9.01    -58.00                                   
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 401  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 226   OE1                                                    
REMARK 620 2 GLU A 226   OE2  58.7                                              
REMARK 620 3 GLU A 238   OE1 101.8  99.0                                        
REMARK 620 4 ATP A 400   O1G 147.0  89.2  90.1                                  
REMARK 620 5 ATP A 400   O2A 100.4 159.1  83.0 111.7                            
REMARK 620 6 HOH A 738   O    91.3  88.3 166.9  79.1  94.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 238   OE1                                                    
REMARK 620 2 GLU A 238   OE2  60.4                                              
REMARK 620 3 ATP A 400   O2G 101.9 162.0                                        
REMARK 620 4 ATP A 400   O2B  95.7  91.0  93.9                                  
REMARK 620 5 HOH A 736   O    86.1  85.3  90.8 174.5                            
REMARK 620 6 HOH A 734   O   154.0  94.0 103.3  89.1  87.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 401  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 226   OE1                                                    
REMARK 620 2 GLU B 226   OE2  56.4                                              
REMARK 620 3 GLU B 238   OE2  90.6  91.1                                        
REMARK 620 4 ATP B 400   O1G  86.2 142.4  93.6                                  
REMARK 620 5 ATP B 400   O2A 154.2  97.9  87.7 119.6                            
REMARK 620 6 HOH B 651   O    88.8  88.0 179.1  87.1  92.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 238   OE1                                                    
REMARK 620 2 GLU B 238   OE2  58.2                                              
REMARK 620 3 ATP B 400   O2G 161.1 103.4                                        
REMARK 620 4 ATP B 400   O2B  87.1  91.6  89.7                                  
REMARK 620 5 HOH B 652   O    99.8 156.7  99.0  94.7                            
REMARK 620 6 HOH B 653   O    88.5  84.5  93.9 175.2  87.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 402                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3ETJ   RELATED DB: PDB                                   
DBREF  3ETH A    1   355  UNP    P09029   PURK_ECOLI       1    355             
DBREF  3ETH B    1   355  UNP    P09029   PURK_ECOLI       1    355             
SEQADV 3ETH GLN A   61  UNP  P09029    GLU    61 ENGINEERED                     
SEQADV 3ETH ARG A  205  UNP  P09029    GLN   205 ENGINEERED                     
SEQADV 3ETH GLN B   61  UNP  P09029    GLU    61 ENGINEERED                     
SEQADV 3ETH ARG B  205  UNP  P09029    GLN   205 ENGINEERED                     
SEQRES   1 A  355  MET LYS GLN VAL CYS VAL LEU GLY ASN GLY GLN LEU GLY          
SEQRES   2 A  355  ARG MET LEU ARG GLN ALA GLY GLU PRO LEU GLY ILE ALA          
SEQRES   3 A  355  VAL TRP PRO VAL GLY LEU ASP ALA GLU PRO ALA ALA VAL          
SEQRES   4 A  355  PRO PHE GLN GLN SER VAL ILE THR ALA GLU ILE GLU ARG          
SEQRES   5 A  355  TRP PRO GLU THR ALA LEU THR ARG GLN LEU ALA ARG HIS          
SEQRES   6 A  355  PRO ALA PHE VAL ASN ARG ASP VAL PHE PRO ILE ILE ALA          
SEQRES   7 A  355  ASP ARG LEU THR GLN LYS GLN LEU PHE ASP LYS LEU HIS          
SEQRES   8 A  355  LEU PRO THR ALA PRO TRP GLN LEU LEU ALA GLU ARG SER          
SEQRES   9 A  355  GLU TRP PRO ALA VAL PHE ASP ARG LEU GLY GLU LEU ALA          
SEQRES  10 A  355  ILE VAL LYS ARG ARG THR GLY GLY TYR ASP GLY ARG GLY          
SEQRES  11 A  355  GLN TRP ARG LEU ARG ALA ASN GLU THR GLU GLN LEU PRO          
SEQRES  12 A  355  ALA GLU CYS TYR GLY GLU CYS ILE VAL GLU GLN GLY ILE          
SEQRES  13 A  355  ASN PHE SER GLY GLU VAL SER LEU VAL GLY ALA ARG GLY          
SEQRES  14 A  355  PHE ASP GLY SER THR VAL PHE TYR PRO LEU THR HIS ASN          
SEQRES  15 A  355  LEU HIS GLN ASP GLY ILE LEU ARG THR SER VAL ALA PHE          
SEQRES  16 A  355  PRO GLN ALA ASN ALA GLN GLN GLN ALA ARG ALA GLU GLU          
SEQRES  17 A  355  MET LEU SER ALA ILE MET GLN GLU LEU GLY TYR VAL GLY          
SEQRES  18 A  355  VAL MET ALA MET GLU CYS PHE VAL THR PRO GLN GLY LEU          
SEQRES  19 A  355  LEU ILE ASN GLU LEU ALA PRO ARG VAL HIS ASN SER GLY          
SEQRES  20 A  355  HIS TRP THR GLN ASN GLY ALA SER ILE SER GLN PHE GLU          
SEQRES  21 A  355  LEU HIS LEU ARG ALA ILE THR ASP LEU PRO LEU PRO GLN          
SEQRES  22 A  355  PRO VAL VAL ASN ASN PRO SER VAL MET ILE ASN LEU ILE          
SEQRES  23 A  355  GLY SER ASP VAL ASN TYR ASP TRP LEU LYS LEU PRO LEU          
SEQRES  24 A  355  VAL HIS LEU HIS TRP TYR ASP LYS GLU VAL ARG PRO GLY          
SEQRES  25 A  355  ARG LYS VAL GLY HIS LEU ASN LEU THR ASP SER ASP THR          
SEQRES  26 A  355  SER ARG LEU THR ALA THR LEU GLU ALA LEU ILE PRO LEU          
SEQRES  27 A  355  LEU PRO PRO GLU TYR ALA SER GLY VAL ILE TRP ALA GLN          
SEQRES  28 A  355  SER LYS PHE GLY                                              
SEQRES   1 B  355  MET LYS GLN VAL CYS VAL LEU GLY ASN GLY GLN LEU GLY          
SEQRES   2 B  355  ARG MET LEU ARG GLN ALA GLY GLU PRO LEU GLY ILE ALA          
SEQRES   3 B  355  VAL TRP PRO VAL GLY LEU ASP ALA GLU PRO ALA ALA VAL          
SEQRES   4 B  355  PRO PHE GLN GLN SER VAL ILE THR ALA GLU ILE GLU ARG          
SEQRES   5 B  355  TRP PRO GLU THR ALA LEU THR ARG GLN LEU ALA ARG HIS          
SEQRES   6 B  355  PRO ALA PHE VAL ASN ARG ASP VAL PHE PRO ILE ILE ALA          
SEQRES   7 B  355  ASP ARG LEU THR GLN LYS GLN LEU PHE ASP LYS LEU HIS          
SEQRES   8 B  355  LEU PRO THR ALA PRO TRP GLN LEU LEU ALA GLU ARG SER          
SEQRES   9 B  355  GLU TRP PRO ALA VAL PHE ASP ARG LEU GLY GLU LEU ALA          
SEQRES  10 B  355  ILE VAL LYS ARG ARG THR GLY GLY TYR ASP GLY ARG GLY          
SEQRES  11 B  355  GLN TRP ARG LEU ARG ALA ASN GLU THR GLU GLN LEU PRO          
SEQRES  12 B  355  ALA GLU CYS TYR GLY GLU CYS ILE VAL GLU GLN GLY ILE          
SEQRES  13 B  355  ASN PHE SER GLY GLU VAL SER LEU VAL GLY ALA ARG GLY          
SEQRES  14 B  355  PHE ASP GLY SER THR VAL PHE TYR PRO LEU THR HIS ASN          
SEQRES  15 B  355  LEU HIS GLN ASP GLY ILE LEU ARG THR SER VAL ALA PHE          
SEQRES  16 B  355  PRO GLN ALA ASN ALA GLN GLN GLN ALA ARG ALA GLU GLU          
SEQRES  17 B  355  MET LEU SER ALA ILE MET GLN GLU LEU GLY TYR VAL GLY          
SEQRES  18 B  355  VAL MET ALA MET GLU CYS PHE VAL THR PRO GLN GLY LEU          
SEQRES  19 B  355  LEU ILE ASN GLU LEU ALA PRO ARG VAL HIS ASN SER GLY          
SEQRES  20 B  355  HIS TRP THR GLN ASN GLY ALA SER ILE SER GLN PHE GLU          
SEQRES  21 B  355  LEU HIS LEU ARG ALA ILE THR ASP LEU PRO LEU PRO GLN          
SEQRES  22 B  355  PRO VAL VAL ASN ASN PRO SER VAL MET ILE ASN LEU ILE          
SEQRES  23 B  355  GLY SER ASP VAL ASN TYR ASP TRP LEU LYS LEU PRO LEU          
SEQRES  24 B  355  VAL HIS LEU HIS TRP TYR ASP LYS GLU VAL ARG PRO GLY          
SEQRES  25 B  355  ARG LYS VAL GLY HIS LEU ASN LEU THR ASP SER ASP THR          
SEQRES  26 B  355  SER ARG LEU THR ALA THR LEU GLU ALA LEU ILE PRO LEU          
SEQRES  27 B  355  LEU PRO PRO GLU TYR ALA SER GLY VAL ILE TRP ALA GLN          
SEQRES  28 B  355  SER LYS PHE GLY                                              
HET    ATP  A 400      31                                                       
HET     MG  A 401       1                                                       
HET     MG  A 402       1                                                       
HET    ATP  B 400      31                                                       
HET     MG  B 401       1                                                       
HET     MG  B 402       1                                                       
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   3  ATP    2(C10 H16 N5 O13 P3)                                         
FORMUL   4   MG    4(MG 2+)                                                     
FORMUL   9  HOH   *690(H2 O)                                                    
HELIX    1   1 GLY A   10  GLU A   21  1                                  12    
HELIX    2   2 PRO A   22  GLY A   24  5                                   3    
HELIX    3   3 GLU A   35  VAL A   39  5                                   5    
HELIX    4   4 THR A   56  ARG A   64  1                                   9    
HELIX    5   5 ASP A   72  ASP A   79  1                                   8    
HELIX    6   6 ASP A   79  LEU A   90  1                                  12    
HELIX    7   7 GLU A  102  SER A  104  5                                   3    
HELIX    8   8 GLU A  105  GLY A  114  1                                  10    
HELIX    9   9 GLU A  138  LEU A  142  5                                   5    
HELIX   10  10 PRO A  143  TYR A  147  5                                   5    
HELIX   11  11 ASN A  199  GLY A  218  1                                  20    
HELIX   12  12 HIS A  244  HIS A  248  5                                   5    
HELIX   13  13 TRP A  249  ALA A  254  1                                   6    
HELIX   14  14 SER A  257  THR A  267  1                                  11    
HELIX   15  15 ASN A  291  LEU A  297  5                                   7    
HELIX   16  16 ASP A  324  ILE A  336  1                                  13    
HELIX   17  17 PRO A  337  LEU A  339  5                                   3    
HELIX   18  18 PRO A  340  GLU A  342  5                                   3    
HELIX   19  19 TYR A  343  PHE A  354  1                                  12    
HELIX   20  20 GLY B   10  GLU B   21  1                                  12    
HELIX   21  21 PRO B   22  GLY B   24  5                                   3    
HELIX   22  22 GLU B   35  VAL B   39  5                                   5    
HELIX   23  23 THR B   56  ALA B   63  1                                   8    
HELIX   24  24 VAL B   73  ASP B   79  1                                   7    
HELIX   25  25 ASP B   79  LEU B   90  1                                  12    
HELIX   26  26 GLU B  102  SER B  104  5                                   3    
HELIX   27  27 GLU B  105  GLY B  114  1                                  10    
HELIX   28  28 GLU B  138  LEU B  142  5                                   5    
HELIX   29  29 PRO B  143  TYR B  147  5                                   5    
HELIX   30  30 ASN B  199  GLY B  218  1                                  20    
HELIX   31  31 HIS B  244  HIS B  248  5                                   5    
HELIX   32  32 TRP B  249  ALA B  254  1                                   6    
HELIX   33  33 SER B  257  THR B  267  1                                  11    
HELIX   34  34 ASN B  291  LEU B  297  5                                   7    
HELIX   35  35 ASP B  324  ILE B  336  1                                  13    
HELIX   36  36 PRO B  337  LEU B  339  5                                   3    
HELIX   37  37 PRO B  340  GLU B  342  5                                   3    
HELIX   38  38 TYR B  343  PHE B  354  1                                  12    
SHEET    1   A 3 ALA A  26  VAL A  30  0                                        
SHEET    2   A 3 GLN A   3  LEU A   7  1  N  VAL A   6   O  VAL A  30           
SHEET    3   A 3 VAL A  45  ALA A  48  1  O  THR A  47   N  LEU A   7           
SHEET    1   B 4 TRP A  97  LEU A 100  0                                        
SHEET    2   B 4 CYS A 150  GLN A 154 -1  O  CYS A 150   N  LEU A 100           
SHEET    3   B 4 LEU A 116  ARG A 121 -1  N  ILE A 118   O  GLU A 153           
SHEET    4   B 4 GLN A 131  ARG A 135 -1  O  LEU A 134   N  ALA A 117           
SHEET    1   C 4 THR A 174  PHE A 176  0                                        
SHEET    2   C 4 GLY A 160  ARG A 168 -1  N  ALA A 167   O  VAL A 175           
SHEET    3   C 4 GLY A 221  THR A 230 -1  O  MET A 225   N  LEU A 164           
SHEET    4   C 4 GLY A 233  ALA A 240 -1  O  ASN A 237   N  GLU A 226           
SHEET    1   D 7 THR A 174  PHE A 176  0                                        
SHEET    2   D 7 GLY A 160  ARG A 168 -1  N  ALA A 167   O  VAL A 175           
SHEET    3   D 7 THR A 180  GLN A 185 -1  O  THR A 180   N  SER A 163           
SHEET    4   D 7 ILE A 188  ALA A 194 -1  O  ARG A 190   N  LEU A 183           
SHEET    5   D 7 SER A 280  ILE A 286 -1  O  SER A 280   N  ALA A 194           
SHEET    6   D 7 LYS A 314  THR A 321 -1  O  GLY A 316   N  LEU A 285           
SHEET    7   D 7 HIS A 301  TRP A 304 -1  N  HIS A 301   O  ASN A 319           
SHEET    1   E 3 ALA B  26  VAL B  30  0                                        
SHEET    2   E 3 GLN B   3  LEU B   7  1  N  VAL B   4   O  ALA B  26           
SHEET    3   E 3 VAL B  45  ALA B  48  1  O  THR B  47   N  LEU B   7           
SHEET    1   F 4 TRP B  97  LEU B 100  0                                        
SHEET    2   F 4 CYS B 150  GLN B 154 -1  O  VAL B 152   N  GLN B  98           
SHEET    3   F 4 ALA B 117  ARG B 121 -1  N  ILE B 118   O  GLU B 153           
SHEET    4   F 4 GLN B 131  LEU B 134 -1  O  TRP B 132   N  VAL B 119           
SHEET    1   G 4 THR B 174  PHE B 176  0                                        
SHEET    2   G 4 GLY B 160  ARG B 168 -1  N  ALA B 167   O  VAL B 175           
SHEET    3   G 4 GLY B 221  THR B 230 -1  O  CYS B 227   N  VAL B 162           
SHEET    4   G 4 GLY B 233  ALA B 240 -1  O  LEU B 235   N  PHE B 228           
SHEET    1   H 7 THR B 174  PHE B 176  0                                        
SHEET    2   H 7 GLY B 160  ARG B 168 -1  N  ALA B 167   O  VAL B 175           
SHEET    3   H 7 THR B 180  GLN B 185 -1  O  THR B 180   N  SER B 163           
SHEET    4   H 7 ILE B 188  ALA B 194 -1  O  ARG B 190   N  LEU B 183           
SHEET    5   H 7 SER B 280  ILE B 286 -1  O  ASN B 284   N  ARG B 190           
SHEET    6   H 7 LYS B 314  THR B 321 -1  O  GLY B 316   N  LEU B 285           
SHEET    7   H 7 HIS B 301  TRP B 304 -1  N  HIS B 301   O  ASN B 319           
LINK         OE1 GLU A 226                MG    MG A 401     1555   1555  2.12  
LINK         OE2 GLU A 226                MG    MG A 401     1555   1555  2.30  
LINK         OE1 GLU A 238                MG    MG A 402     1555   1555  2.11  
LINK         OE1 GLU A 238                MG    MG A 401     1555   1555  1.97  
LINK         OE2 GLU A 238                MG    MG A 402     1555   1555  2.21  
LINK         OE1 GLU B 226                MG    MG B 401     1555   1555  2.46  
LINK         OE2 GLU B 226                MG    MG B 401     1555   1555  2.12  
LINK         OE1 GLU B 238                MG    MG B 402     1555   1555  2.20  
LINK         OE2 GLU B 238                MG    MG B 402     1555   1555  2.28  
LINK         OE2 GLU B 238                MG    MG B 401     1555   1555  2.11  
LINK         O1G ATP A 400                MG    MG A 401     1555   1555  2.03  
LINK         O2G ATP A 400                MG    MG A 402     1555   1555  1.85  
LINK         O2B ATP A 400                MG    MG A 402     1555   1555  1.86  
LINK         O2A ATP A 400                MG    MG A 401     1555   1555  2.04  
LINK        MG    MG A 401                 O   HOH A 738     1555   1555  2.10  
LINK        MG    MG A 402                 O   HOH A 736     1555   1555  2.14  
LINK        MG    MG A 402                 O   HOH A 734     1555   1555  2.12  
LINK         O1G ATP B 400                MG    MG B 401     1555   1555  2.02  
LINK         O2G ATP B 400                MG    MG B 402     1555   1555  2.01  
LINK         O2B ATP B 400                MG    MG B 402     1555   1555  1.94  
LINK         O2A ATP B 400                MG    MG B 401     1555   1555  1.94  
LINK        MG    MG B 401                 O   HOH B 651     1555   1555  2.05  
LINK        MG    MG B 402                 O   HOH B 652     1555   1555  1.98  
LINK        MG    MG B 402                 O   HOH B 653     1555   1555  2.02  
SITE     1 AC1 29 ARG A  80  ILE A 118  LYS A 120  GLY A 125                    
SITE     2 AC1 29 TYR A 126  ASP A 127  GLY A 128  GLN A 131                    
SITE     3 AC1 29 GLU A 153  GLN A 154  ILE A 156  PHE A 158                    
SITE     4 AC1 29 GLU A 161  HIS A 184  GLU A 226  PHE A 228                    
SITE     5 AC1 29 ASN A 237  GLU A 238   MG A 401   MG A 402                    
SITE     6 AC1 29 HOH A 664  HOH A 733  HOH A 734  HOH A 735                    
SITE     7 AC1 29 HOH A 736  HOH A 737  HOH A 738  HOH A 739                    
SITE     8 AC1 29 HOH A 740                                                     
SITE     1 AC2  5 GLU A 226  GLU A 238  ATP A 400   MG A 402                    
SITE     2 AC2  5 HOH A 738                                                     
SITE     1 AC3  5 GLU A 238  ATP A 400   MG A 401  HOH A 734                    
SITE     2 AC3  5 HOH A 736                                                     
SITE     1 AC4 30 ARG B  80  ILE B 118  LYS B 120  GLY B 125                    
SITE     2 AC4 30 TYR B 126  ASP B 127  GLY B 128  GLN B 131                    
SITE     3 AC4 30 GLU B 153  GLN B 154  GLY B 155  ILE B 156                    
SITE     4 AC4 30 PHE B 158  GLU B 161  HIS B 184  GLU B 226                    
SITE     5 AC4 30 PHE B 228  ASN B 237  GLU B 238   MG B 401                    
SITE     6 AC4 30  MG B 402  HOH B 524  HOH B 525  HOH B 528                    
SITE     7 AC4 30 HOH B 649  HOH B 651  HOH B 652  HOH B 653                    
SITE     8 AC4 30 HOH B 658  HOH B 685                                          
SITE     1 AC5  4 GLU B 226  GLU B 238  ATP B 400  HOH B 651                    
SITE     1 AC6  4 GLU B 238  ATP B 400  HOH B 652  HOH B 653                    
CRYST1   57.101   57.109   59.215  77.46  82.39  77.26 P 1           2          
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      0.017513 -0.003958 -0.001602        0.00000                         
SCALE2      0.000000  0.017952 -0.003556        0.00000                         
SCALE3      0.000000  0.000000  0.017369        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system