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Database: PDB
Entry: 2R7L
LinkDB: 2R7L
Original site: 2R7L 
HEADER    LIGASE                                  09-SEP-07   2R7L              
TITLE     CRYSTAL STRUCTURE OF FAICAR SYNTHETASE (PURP) FROM M. JANNASCHII      
TITLE    2 COMPLEXED WITH ATP AND AICAR                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5-FORMAMINOIMIDAZOLE-4-CARBOXAMIDE-1-(BETA)-D-RIBOFURANOSYL
COMPND   3 5'-MONOPHOSPHATE SYNTHETASE;                                         
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: 5-AMINOIMIDAZOLE-4-CARBOXAMIDE-1-BETA-D-RIBOFURANOSYL 5'-   
COMPND   6 MONOPHOSPHATE-FORMATE LIGASE;                                        
COMPND   7 EC: 6.3.4.-;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: METHANOCALDOCOCCUS JANNASCHII;                  
SOURCE   3 ORGANISM_TAXID: 2190;                                                
SOURCE   4 GENE: PURP;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: B834(DE3);                              
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET19                                     
KEYWDS    ATP-GRASP SUPERFAMILY, ATP-BINDING, LIGASE, MAGNESIUM, MANGANESE,     
KEYWDS   2 METAL-BINDING, NUCLEOTIDE-BINDING                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.ZHANG,R.H.WHITE,S.E.EALICK                                          
REVDAT   4   25-OCT-17 2R7L    1       REMARK                                   
REVDAT   3   24-FEB-09 2R7L    1       VERSN                                    
REVDAT   2   22-JUL-08 2R7L    1       JRNL                                     
REVDAT   1   04-DEC-07 2R7L    0                                                
JRNL        AUTH   Y.ZHANG,R.H.WHITE,S.E.EALICK                                 
JRNL        TITL   CRYSTAL STRUCTURE AND FUNCTION OF                            
JRNL        TITL 2 5-FORMAMINOIMIDAZOLE-4-CARBOXAMIDE RIBONUCLEOTIDE SYNTHETASE 
JRNL        TITL 3 FROM METHANOCALDOCOCCUS JANNASCHII.                          
JRNL        REF    BIOCHEMISTRY                  V.  47   205 2008              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   18069798                                                     
JRNL        DOI    10.1021/BI701406G                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.10                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 31507                          
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) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1600                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1437                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 58.96                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2810                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 67                           
REMARK   3   BIN FREE R VALUE                    : 0.4060                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2827                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 60                                      
REMARK   3   SOLVENT ATOMS            : 128                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.12                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.15000                                              
REMARK   3    B22 (A**2) : 3.15000                                              
REMARK   3    B33 (A**2) : -4.73000                                             
REMARK   3    B12 (A**2) : 1.58000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.190         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.183         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.132         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.093         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.931                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2939 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3971 ; 1.004 ; 2.008       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   353 ; 5.134 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   132 ;34.940 ;24.697       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   540 ;13.761 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;19.282 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   439 ; 0.067 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2169 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1258 ; 0.220 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2036 ; 0.324 ; 0.500       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   268 ; 0.195 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   104 ; 0.166 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    39 ; 0.240 ; 0.500       
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):  1814 ; 4.492 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2869 ; 6.073 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1249 ; 4.498 ; 2.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1102 ; 6.163 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2R7L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-SEP-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000044524.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-MAR-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.1                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97918                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31507                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.3                               
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : 0.05400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 61.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.14600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 M (NH4)2SO4, 0.2 M NACL, 0.1 M NA    
REMARK 280  ACETATE, PH 4.1, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3                                      
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3                                   
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3                                  
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3                                      
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3                                   
REMARK 290      18555   -X+1/3,-X+Y+2/3,-Z+2/3                                  
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000       54.77700            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       31.62552            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       85.26900            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       54.77700            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       31.62552            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       85.26900            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       54.77700            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       31.62552            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       85.26900            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       54.77700            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       31.62552            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       85.26900            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       54.77700            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       31.62552            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       85.26900            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       54.77700            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       31.62552            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       85.26900            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       63.25103            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000      170.53800            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       63.25103            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000      170.53800            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       63.25103            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      170.53800            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       63.25103            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      170.53800            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       63.25103            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000      170.53800            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       63.25103            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000      170.53800            
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: BIOLOGICAL UNIT IS A HEXAMER FROM THE MONOMER IN THE         
REMARK 300 ASYMMETRIC UNIT BY THE OPERATIONS: (X,Y,Z), (-Y,X-Y,Z), (-X+Y,-X,Z), 
REMARK 300 (Y,X,-Z), (X-Y,-Y,-Z), (-X,-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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 42070 ANGSTROM**2                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 707  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO A   158                                                      
REMARK 465     GLY A   159                                                      
REMARK 465     ALA A   160                                                      
REMARK 465     ARG A   161                                                      
REMARK 465     GLY A   162                                                      
REMARK 465     GLY A   163                                                      
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     ARG A 164    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   720     O    HOH A   722     3555     2.15            
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    ILE A   2      121.85    -36.34                                   
REMARK 500    HIS A  27      -79.33     67.92                                   
REMARK 500    ASN A 106       13.18   -153.01                                   
REMARK 500    PHE A 322       52.03   -119.81                                   
REMARK 500    MET A 355       34.65   -141.39                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMZ A 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2R7K   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN COMPLEXED WITH AMPPCP AND AICAR                         
REMARK 900 RELATED ID: 2R7M   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN COMPLEXED WITH AMP                                      
REMARK 900 RELATED ID: 2R7N   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN COMPLEXED WITH ADP AND FAICAR                           
DBREF  2R7L A    1   361  UNP    Q57600   PURP_METJA       1    361             
SEQRES   1 A  361  MET ILE SER LYS ASP GLU ILE LEU GLU ILE PHE ASP LYS          
SEQRES   2 A  361  TYR ASN LYS ASP GLU ILE THR ILE ALA THR LEU GLY SER          
SEQRES   3 A  361  HIS THR SER LEU HIS ILE LEU LYS GLY ALA LYS LEU GLU          
SEQRES   4 A  361  GLY PHE SER THR VAL CYS ILE THR MET LYS GLY ARG ASP          
SEQRES   5 A  361  VAL PRO TYR LYS ARG PHE LYS VAL ALA ASP LYS PHE ILE          
SEQRES   6 A  361  TYR VAL ASP ASN PHE SER ASP ILE LYS ASN GLU GLU ILE          
SEQRES   7 A  361  GLN GLU LYS LEU ARG GLU LEU ASN SER ILE VAL VAL PRO          
SEQRES   8 A  361  HIS GLY SER PHE ILE ALA TYR CYS GLY LEU ASP ASN VAL          
SEQRES   9 A  361  GLU ASN SER PHE LEU VAL PRO MET PHE GLY ASN ARG ARG          
SEQRES  10 A  361  ILE LEU ARG TRP GLU SER GLU ARG SER LEU GLU GLY LYS          
SEQRES  11 A  361  LEU LEU ARG GLU ALA GLY LEU ARG VAL PRO LYS LYS TYR          
SEQRES  12 A  361  GLU SER PRO GLU ASP ILE ASP GLY THR VAL ILE VAL LYS          
SEQRES  13 A  361  PHE PRO GLY ALA ARG GLY GLY ARG GLY TYR PHE ILE ALA          
SEQRES  14 A  361  SER SER THR GLU GLU PHE TYR LYS LYS ALA GLU ASP LEU          
SEQRES  15 A  361  LYS LYS ARG GLY ILE LEU THR ASP GLU ASP ILE ALA ASN          
SEQRES  16 A  361  ALA HIS ILE GLU GLU TYR VAL VAL GLY THR ASN PHE CYS          
SEQRES  17 A  361  ILE HIS TYR PHE TYR SER PRO LEU LYS ASP GLU VAL GLU          
SEQRES  18 A  361  LEU LEU GLY MET ASP LYS ARG TYR GLU SER ASN ILE ASP          
SEQRES  19 A  361  GLY LEU VAL ARG ILE PRO ALA LYS ASP GLN LEU GLU MET          
SEQRES  20 A  361  ASN ILE ASN PRO SER TYR VAL ILE THR GLY ASN ILE PRO          
SEQRES  21 A  361  VAL VAL ILE ARG GLU SER LEU LEU PRO GLN VAL PHE GLU          
SEQRES  22 A  361  MET GLY ASP LYS LEU VAL ALA LYS ALA LYS GLU LEU VAL          
SEQRES  23 A  361  PRO PRO GLY MET ILE GLY PRO PHE CYS LEU GLN SER LEU          
SEQRES  24 A  361  CYS ASN GLU ASN LEU GLU LEU VAL VAL PHE GLU MET SER          
SEQRES  25 A  361  ALA ARG VAL ASP GLY GLY THR ASN SER PHE MET ASN GLY          
SEQRES  26 A  361  GLY PRO TYR SER PHE LEU TYR ASN GLY GLU PRO LEU SER          
SEQRES  27 A  361  MET GLY GLN ARG ILE ALA ARG GLU ILE LYS MET ALA LEU          
SEQRES  28 A  361  GLN LEU ASP MET ILE ASP LYS ILE ILE SER                      
HET    SO4  A 500       5                                                       
HET     CL  A 601       1                                                       
HET     CL  A 602       1                                                       
HET    ATP  A 400      31                                                       
HET    AMZ  A 401      22                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM     AMZ AMINOIMIDAZOLE 4-CARBOXAMIDE RIBONUCLEOTIDE                      
HETSYN     AMZ AICAR                                                            
FORMUL   2  SO4    O4 S 2-                                                      
FORMUL   3   CL    2(CL 1-)                                                     
FORMUL   5  ATP    C10 H16 N5 O13 P3                                            
FORMUL   6  AMZ    C9 H15 N4 O8 P                                               
FORMUL   7  HOH   *128(H2 O)                                                    
HELIX    1   1 SER A    3  ASP A   12  1                                  10    
HELIX    2   2 THR A   28  GLU A   39  1                                  12    
HELIX    3   3 ASP A   52  PHE A   58  1                                   7    
HELIX    4   4 ASN A   69  LYS A   74  5                                   6    
HELIX    5   5 ASN A   75  LEU A   85  1                                  11    
HELIX    6   6 HIS A   92  GLY A  100  1                                   9    
HELIX    7   7 GLY A  100  SER A  107  1                                   8    
HELIX    8   8 ASN A  115  ARG A  120  5                                   6    
HELIX    9   9 GLU A  124  GLY A  136  1                                  13    
HELIX   10  10 SER A  145  ILE A  149  5                                   5    
HELIX   11  11 SER A  171  ARG A  185  1                                  15    
HELIX   12  12 THR A  189  ASN A  195  1                                   7    
HELIX   13  13 ILE A  233  VAL A  237  1                                   5    
HELIX   14  14 PRO A  240  GLU A  246  1                                   7    
HELIX   15  15 ARG A  264  SER A  266  5                                   3    
HELIX   16  16 LEU A  267  VAL A  286  1                                  20    
HELIX   17  17 ASP A  316  MET A  323  5                                   8    
HELIX   18  18 GLY A  326  TYR A  332  1                                   7    
HELIX   19  19 SER A  338  ASP A  354  1                                  17    
HELIX   20  20 MET A  355  LYS A  358  5                                   4    
SHEET    1   A 4 LYS A  63  TYR A  66  0                                        
SHEET    2   A 4 THR A  43  THR A  47  1  N  CYS A  45   O  LYS A  63           
SHEET    3   A 4 THR A  20  LEU A  24  1  N  ILE A  21   O  VAL A  44           
SHEET    4   A 4 SER A  87  VAL A  89  1  O  ILE A  88   N  THR A  20           
SHEET    1   B 2 MET A 112  PHE A 113  0                                        
SHEET    2   B 2 ILE A 360  SER A 361 -1  O  SER A 361   N  MET A 112           
SHEET    1   C 4 LYS A 142  TYR A 143  0                                        
SHEET    2   C 4 HIS A 197  GLU A 200 -1  O  ILE A 198   N  TYR A 143           
SHEET    3   C 4 VAL A 153  LYS A 156 -1  N  LYS A 156   O  HIS A 197           
SHEET    4   C 4 PHE A 167  ALA A 169 -1  O  ALA A 169   N  VAL A 153           
SHEET    1   D 5 TYR A 253  PRO A 260  0                                        
SHEET    2   D 5 GLU A 219  ASN A 232 -1  N  LYS A 227   O  ILE A 259           
SHEET    3   D 5 THR A 205  SER A 214 -1  N  PHE A 212   O  GLU A 221           
SHEET    4   D 5 GLY A 292  CYS A 300 -1  O  PHE A 294   N  TYR A 211           
SHEET    5   D 5 LEU A 306  SER A 312 -1  O  VAL A 307   N  LEU A 299           
CISPEP   1 SER A  231    ASN A  232          0        10.66                     
CISPEP   2 PRO A  287    PRO A  288          0         0.93                     
SITE     1 AC1  2 LYS A  56  ARG A  57                                          
SITE     1 AC2  4 HIS A  27  ARG A 314  ASP A 316  GLY A 317                    
SITE     1 AC3  3 HIS A 210  ASP A 316  THR A 319                               
SITE     1 AC4 22 PRO A 140  ILE A 154  LYS A 156  TYR A 166                    
SITE     2 AC4 22 GLU A 199  GLU A 200  TYR A 201  ARG A 228                    
SITE     3 AC4 22 GLU A 230  ARG A 238  TYR A 253  ILE A 255                    
SITE     4 AC4 22 GLN A 297  LEU A 299  PHE A 309  GLU A 310                    
SITE     5 AC4 22 HOH A 608  HOH A 611  HOH A 612  HOH A 613                    
SITE     6 AC4 22 HOH A 689  HOH A 726                                          
SITE     1 AC5 14 HIS A  27  SER A  94  ARG A 228  ILE A 255                    
SITE     2 AC5 14 ASN A 258  ARG A 264  SER A 266  GLY A 317                    
SITE     3 AC5 14 GLY A 318  HOH A 603  HOH A 604  HOH A 605                    
SITE     4 AC5 14 HOH A 645  HOH A 724                                          
CRYST1  109.554  109.554  255.807  90.00  90.00 120.00 H 3 2        18          
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      0.009128  0.005270  0.000000        0.00000                         
SCALE2      0.000000  0.010540  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003909        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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