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Database: PDB
Entry: 2R84
LinkDB: 2R84
Original site: 2R84 
HEADER    UNKNOWN FUNCTION                        10-SEP-07   2R84              
TITLE     CRYSTAL STRUCTURE OF PURP FROM PYROCOCCUS FURIOSUS COMPLEXED WITH AMP 
TITLE    2 AND AICAR                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PURP PROTEIN PF1517;                                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS;                            
SOURCE   3 ORGANISM_TAXID: 2261;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: T7-7                                      
KEYWDS    ATP-GRASP SUPERFAMILY, UNKNOWN FUNCTION                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.ZHANG,R.H.WHITE,S.E.EALICK                                          
REVDAT   5   25-OCT-17 2R84    1       REMARK                                   
REVDAT   4   13-JUL-11 2R84    1       VERSN                                    
REVDAT   3   24-FEB-09 2R84    1       VERSN                                    
REVDAT   2   22-JUL-08 2R84    1       JRNL                                     
REVDAT   1   04-DEC-07 2R84    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.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.3.0037                                      
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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 85981                          
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) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.195                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4365                            
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) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5446                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.05                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2280                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 303                          
REMARK   3   BIN FREE R VALUE                    : 0.2640                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5215                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 118                                     
REMARK   3   SOLVENT ATOMS            : 624                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.78                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.68000                                              
REMARK   3    B22 (A**2) : 0.68000                                              
REMARK   3    B33 (A**2) : -1.02000                                             
REMARK   3    B12 (A**2) : 0.34000                                              
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): 0.113         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.105         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.064         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.012         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5832 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7958 ; 1.072 ; 2.007       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   700 ; 5.334 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   270 ;33.296 ;23.741       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1013 ;12.298 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    44 ;11.573 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   864 ; 0.073 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4448 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2644 ; 0.188 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4014 ; 0.300 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   677 ; 0.091 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     6 ; 0.075 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   160 ; 0.146 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    76 ; 0.093 ; 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):  3443 ; 0.342 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5637 ; 0.667 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2483 ; 0.958 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2321 ; 1.671 ; 4.500       
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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    120       A     128      5                      
REMARK   3           1     B    120       B     128      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):     36 ; 0.120 ; 0.500           
REMARK   3   LOOSE POSITIONAL   1    B    (A):     37 ; 0.520 ; 5.000           
REMARK   3   MEDIUM THERMAL     1    A (A**2):     36 ; 0.780 ; 2.000           
REMARK   3   LOOSE THERMAL      1    B (A**2):     37 ; 0.570 ;10.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   334                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.8759  40.0116  18.0795              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0320 T22:  -0.0006                                     
REMARK   3      T33:  -0.0079 T12:   0.0058                                     
REMARK   3      T13:  -0.0120 T23:   0.0127                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2588 L22:   0.1822                                     
REMARK   3      L33:   0.4254 L12:   0.0217                                     
REMARK   3      L13:  -0.0800 L23:  -0.0764                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0064 S12:   0.0403 S13:   0.0123                       
REMARK   3      S21:  -0.0276 S22:   0.0140 S23:   0.0565                       
REMARK   3      S31:  -0.0015 S32:  -0.0886 S33:  -0.0204                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   334                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.1657  39.5990  75.8350              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0253 T22:   0.0236                                     
REMARK   3      T33:  -0.0386 T12:   0.0022                                     
REMARK   3      T13:   0.0268 T23:  -0.0099                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5397 L22:   0.3750                                     
REMARK   3      L33:   0.7173 L12:  -0.0582                                     
REMARK   3      L13:   0.1939 L23:  -0.1163                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0017 S12:  -0.1075 S13:   0.0189                       
REMARK   3      S21:   0.0861 S22:   0.0024 S23:   0.0653                       
REMARK   3      S31:  -0.0287 S32:  -0.1659 S33:  -0.0007                       
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 2R84 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_1000044543.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-DEC-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 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   : 85981                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
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     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.07400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36500                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2R7K                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% MPD, 200 MM NACL, 100 MM TRIS, PH    
REMARK 280  7.0, 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       61.83550            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       35.70074            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000      125.11967            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       61.83550            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       35.70074            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000      125.11967            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       61.83550            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       35.70074            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      125.11967            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       61.83550            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       35.70074            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      125.11967            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       61.83550            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       35.70074            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      125.11967            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       61.83550            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       35.70074            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      125.11967            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       71.40149            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000      250.23933            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       71.40149            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000      250.23933            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       71.40149            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      250.23933            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       71.40149            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      250.23933            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       71.40149            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000      250.23933            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       71.40149            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000      250.23933            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 ASSEMBLY IS A HEXAMER OR A TRIMER FROM THE        
REMARK 300 ASYMMETRIC UNIT BY THE OPERATIONS: (X,Y,Z), (-Y,X-Y,Z +(1 1 0)), (-  
REMARK 300 X+Y,-X,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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 20210 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      123.67100            
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       61.83550            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      107.10223            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 18770 ANGSTROM**2                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 -0.500000 -0.866025  0.000000      123.67100            
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       61.83550            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      107.10223            
REMARK 350   BIOMT3   3  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 662  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 694  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 879  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 652  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 704  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 823  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     HIS A   134                                                      
REMARK 465     GLY A   135                                                      
REMARK 465     ALA A   136                                                      
REMARK 465     LYS A   137                                                      
REMARK 465     GLY A   138                                                      
REMARK 465     PRO B   133                                                      
REMARK 465     HIS B   134                                                      
REMARK 465     GLY B   135                                                      
REMARK 465     ALA B   136                                                      
REMARK 465     LYS B   137                                                      
REMARK 465     GLY B   138                                                      
REMARK 465     GLY B   139                                                      
REMARK 465     LYS B   140                                                      
REMARK 465     LYS B   157                                                      
REMARK 465     PHE B   158                                                      
REMARK 465     LEU B   159                                                      
REMARK 465     GLY B   160                                                      
REMARK 465     ILE B   161                                                      
REMARK 465     LYS B   162                                                      
REMARK 465     ARG B   163                                                      
REMARK 465     LYS B   164                                                      
REMARK 465     GLU B   165                                                      
REMARK 465     ASP B   166                                                      
REMARK 465     LEU B   167                                                      
REMARK 465     LYS B   168                                                      
REMARK 465     ASN B   169                                                      
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    HIS A  11      -68.41     74.58                                   
REMARK 500    SER A  12       20.36   -155.65                                   
REMARK 500    LYS A  41      -63.50   -120.30                                   
REMARK 500    PRO A  44       88.49    -69.43                                   
REMARK 500    TYR A  54       89.04   -152.72                                   
REMARK 500    SER A  71      -60.25    -94.13                                   
REMARK 500    SER A 198      170.89    173.89                                   
REMARK 500    MET A 260       13.60   -141.16                                   
REMARK 500    ALA A 286       48.88    -93.28                                   
REMARK 500    ASN A 297       34.48    -95.41                                   
REMARK 500    MET A 328       30.79   -140.66                                   
REMARK 500    HIS B  11      -66.60     72.17                                   
REMARK 500    SER B  12       20.76   -155.51                                   
REMARK 500    SER B 198      171.36    175.00                                   
REMARK 500    MET B 260       12.36   -140.85                                   
REMARK 500    ALA B 286       48.11    -96.23                                   
REMARK 500    ARG B 287     -174.84   -170.54                                   
REMARK 500    ASN B 297       32.39    -94.69                                   
REMARK 500    MET B 328       29.40   -142.78                                   
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                              NA A 600  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  98   O                                                      
REMARK 620 2 GLU A 104   OE2  85.4                                              
REMARK 620 3 ILE A 284   O   119.0  88.2                                        
REMARK 620 4 HOH A 602   O    93.6  93.7 147.3                                  
REMARK 620 5 HOH A 621   O    85.9 164.3  84.6  99.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 600  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  98   O                                                      
REMARK 620 2 GLU B 104   OE2  82.2                                              
REMARK 620 3 ILE B 284   O   101.2  79.1                                        
REMARK 620 4 HOH B 842   O    88.5  82.9 158.2                                  
REMARK 620 5 HOH B 795   O   158.9 118.8  85.9  92.0                            
REMARK 620 6 HOH B 796   O    92.2 167.2  90.8 108.5  67.7                      
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 NA A 600                  
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 NA B 600                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMZ A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP B 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMZ B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2R85   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN WITH COMPLEXED WITH AMP                                 
REMARK 900 RELATED ID: 2R86   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN WITH COMPLEXED WITH ATP                                 
REMARK 900 RELATED ID: 2R87   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN WITH COMPLEXED WITH ADP                                 
DBREF  2R84 A    1   334  UNP    Q8U0R7   Q8U0R7_PYRFU     1    334             
DBREF  2R84 B    1   334  UNP    Q8U0R7   Q8U0R7_PYRFU     1    334             
SEQRES   1 A  334  MET LYS VAL ARG ILE ALA THR TYR ALA SER HIS SER ALA          
SEQRES   2 A  334  LEU GLN ILE LEU LYS GLY ALA LYS ASP GLU GLY PHE GLU          
SEQRES   3 A  334  THR ILE ALA PHE GLY SER SER LYS VAL LYS PRO LEU TYR          
SEQRES   4 A  334  THR LYS TYR PHE PRO VAL ALA ASP TYR PHE ILE GLU GLU          
SEQRES   5 A  334  LYS TYR PRO GLU GLU GLU LEU LEU ASN LEU ASN ALA VAL          
SEQRES   6 A  334  VAL VAL PRO THR GLY SER PHE VAL ALA HIS LEU GLY ILE          
SEQRES   7 A  334  GLU LEU VAL GLU ASN MET LYS VAL PRO TYR PHE GLY ASN          
SEQRES   8 A  334  LYS ARG VAL LEU ARG TRP GLU SER ASP ARG ASN LEU GLU          
SEQRES   9 A  334  ARG LYS TRP LEU LYS LYS ALA GLY ILE ARG VAL PRO GLU          
SEQRES  10 A  334  VAL TYR GLU ASP PRO ASP ASP ILE GLU LYS PRO VAL ILE          
SEQRES  11 A  334  VAL LYS PRO HIS GLY ALA LYS GLY GLY LYS GLY TYR PHE          
SEQRES  12 A  334  LEU ALA LYS ASP PRO GLU ASP PHE TRP ARG LYS ALA GLU          
SEQRES  13 A  334  LYS PHE LEU GLY ILE LYS ARG LYS GLU ASP LEU LYS ASN          
SEQRES  14 A  334  ILE GLN ILE GLN GLU TYR VAL LEU GLY VAL PRO VAL TYR          
SEQRES  15 A  334  PRO HIS TYR PHE TYR SER LYS VAL ARG GLU GLU LEU GLU          
SEQRES  16 A  334  LEU MET SER ILE ASP ARG ARG TYR GLU SER ASN VAL ASP          
SEQRES  17 A  334  ALA ILE GLY ARG ILE PRO ALA LYS ASP GLN LEU GLU PHE          
SEQRES  18 A  334  ASP MET ASP ILE THR TYR THR VAL ILE GLY ASN ILE PRO          
SEQRES  19 A  334  ILE VAL LEU ARG GLU SER LEU LEU MET ASP VAL ILE GLU          
SEQRES  20 A  334  ALA GLY GLU ARG VAL VAL LYS ALA ALA GLU GLU LEU MET          
SEQRES  21 A  334  GLY GLY LEU TRP GLY PRO PHE CYS LEU GLU GLY VAL PHE          
SEQRES  22 A  334  THR PRO ASP LEU GLU PHE VAL VAL PHE GLU ILE SER ALA          
SEQRES  23 A  334  ARG ILE VAL ALA GLY THR ASN ILE PHE VAL ASN GLY SER          
SEQRES  24 A  334  PRO TYR THR TRP LEU ARG TYR ASP ARG PRO VAL SER THR          
SEQRES  25 A  334  GLY ARG ARG ILE ALA MET GLU ILE ARG GLU ALA ILE GLU          
SEQRES  26 A  334  ASN ASP MET LEU GLU LYS VAL LEU THR                          
SEQRES   1 B  334  MET LYS VAL ARG ILE ALA THR TYR ALA SER HIS SER ALA          
SEQRES   2 B  334  LEU GLN ILE LEU LYS GLY ALA LYS ASP GLU GLY PHE GLU          
SEQRES   3 B  334  THR ILE ALA PHE GLY SER SER LYS VAL LYS PRO LEU TYR          
SEQRES   4 B  334  THR LYS TYR PHE PRO VAL ALA ASP TYR PHE ILE GLU GLU          
SEQRES   5 B  334  LYS TYR PRO GLU GLU GLU LEU LEU ASN LEU ASN ALA VAL          
SEQRES   6 B  334  VAL VAL PRO THR GLY SER PHE VAL ALA HIS LEU GLY ILE          
SEQRES   7 B  334  GLU LEU VAL GLU ASN MET LYS VAL PRO TYR PHE GLY ASN          
SEQRES   8 B  334  LYS ARG VAL LEU ARG TRP GLU SER ASP ARG ASN LEU GLU          
SEQRES   9 B  334  ARG LYS TRP LEU LYS LYS ALA GLY ILE ARG VAL PRO GLU          
SEQRES  10 B  334  VAL TYR GLU ASP PRO ASP ASP ILE GLU LYS PRO VAL ILE          
SEQRES  11 B  334  VAL LYS PRO HIS GLY ALA LYS GLY GLY LYS GLY TYR PHE          
SEQRES  12 B  334  LEU ALA LYS ASP PRO GLU ASP PHE TRP ARG LYS ALA GLU          
SEQRES  13 B  334  LYS PHE LEU GLY ILE LYS ARG LYS GLU ASP LEU LYS ASN          
SEQRES  14 B  334  ILE GLN ILE GLN GLU TYR VAL LEU GLY VAL PRO VAL TYR          
SEQRES  15 B  334  PRO HIS TYR PHE TYR SER LYS VAL ARG GLU GLU LEU GLU          
SEQRES  16 B  334  LEU MET SER ILE ASP ARG ARG TYR GLU SER ASN VAL ASP          
SEQRES  17 B  334  ALA ILE GLY ARG ILE PRO ALA LYS ASP GLN LEU GLU PHE          
SEQRES  18 B  334  ASP MET ASP ILE THR TYR THR VAL ILE GLY ASN ILE PRO          
SEQRES  19 B  334  ILE VAL LEU ARG GLU SER LEU LEU MET ASP VAL ILE GLU          
SEQRES  20 B  334  ALA GLY GLU ARG VAL VAL LYS ALA ALA GLU GLU LEU MET          
SEQRES  21 B  334  GLY GLY LEU TRP GLY PRO PHE CYS LEU GLU GLY VAL PHE          
SEQRES  22 B  334  THR PRO ASP LEU GLU PHE VAL VAL PHE GLU ILE SER ALA          
SEQRES  23 B  334  ARG ILE VAL ALA GLY THR ASN ILE PHE VAL ASN GLY SER          
SEQRES  24 B  334  PRO TYR THR TRP LEU ARG TYR ASP ARG PRO VAL SER THR          
SEQRES  25 B  334  GLY ARG ARG ILE ALA MET GLU ILE ARG GLU ALA ILE GLU          
SEQRES  26 B  334  ASN ASP MET LEU GLU LYS VAL LEU THR                          
HET     NA  A 600       1                                                       
HET     CL  A 601       1                                                       
HET    AMP  A 400      23                                                       
HET    AMZ  A 401      44                                                       
HET    MPD  A 500       8                                                       
HET    MPD  A 501       8                                                       
HET     NA  B 600       1                                                       
HET     CL  B 601       1                                                       
HET    AMP  B 400      23                                                       
HET    AMZ  B 401      44                                                       
HET    MPD  B 501       8                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
HETNAM     AMZ AMINOIMIDAZOLE 4-CARBOXAMIDE RIBONUCLEOTIDE                      
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
HETSYN     AMZ AICAR                                                            
FORMUL   3   NA    2(NA 1+)                                                     
FORMUL   4   CL    2(CL 1-)                                                     
FORMUL   5  AMP    2(C10 H14 N5 O7 P)                                           
FORMUL   6  AMZ    2(C9 H15 N4 O8 P)                                            
FORMUL   7  MPD    3(C6 H14 O2)                                                 
FORMUL  14  HOH   *624(H2 O)                                                    
HELIX    1   1 SER A   12  GLU A   23  1                                  12    
HELIX    2   2 SER A   32  LYS A   34  5                                   3    
HELIX    3   3 VAL A   35  LYS A   41  1                                   7    
HELIX    4   4 PRO A   55  LEU A   62  1                                   8    
HELIX    5   5 GLY A   70  LEU A   76  1                                   7    
HELIX    6   6 GLY A   77  MET A   84  1                                   8    
HELIX    7   7 ARG A   93  ASP A  100  1                                   8    
HELIX    8   8 ASP A  100  ALA A  111  1                                  12    
HELIX    9   9 ASP A  121  ILE A  125  5                                   5    
HELIX   10  10 ASP A  147  GLY A  160  1                                  14    
HELIX   11  11 ARG A  163  LEU A  167  5                                   5    
HELIX   12  12 ALA A  209  ILE A  213  5                                   5    
HELIX   13  13 PRO A  214  LEU A  219  1                                   6    
HELIX   14  14 ARG A  238  SER A  240  5                                   3    
HELIX   15  15 LEU A  241  MET A  260  1                                  20    
HELIX   16  16 VAL A  289  VAL A  296  5                                   8    
HELIX   17  17 TYR A  301  ARG A  305  5                                   5    
HELIX   18  18 SER A  311  ASN A  326  1                                  16    
HELIX   19  19 MET A  328  LYS A  331  5                                   4    
HELIX   20  20 SER B   12  GLU B   23  1                                  12    
HELIX   21  21 SER B   32  LYS B   34  5                                   3    
HELIX   22  22 VAL B   35  LYS B   41  1                                   7    
HELIX   23  23 PRO B   55  LEU B   62  1                                   8    
HELIX   24  24 GLY B   70  LEU B   76  1                                   7    
HELIX   25  25 GLY B   77  MET B   84  1                                   8    
HELIX   26  26 ARG B   93  ASP B  100  1                                   8    
HELIX   27  27 ASP B  100  ALA B  111  1                                  12    
HELIX   28  28 ASP B  121  ILE B  125  5                                   5    
HELIX   29  29 ASP B  147  GLU B  156  1                                  10    
HELIX   30  30 ALA B  209  ILE B  213  5                                   5    
HELIX   31  31 PRO B  214  GLU B  220  1                                   7    
HELIX   32  32 ARG B  238  SER B  240  5                                   3    
HELIX   33  33 LEU B  241  MET B  260  1                                  20    
HELIX   34  34 VAL B  289  VAL B  296  5                                   8    
HELIX   35  35 TYR B  301  ARG B  305  5                                   5    
HELIX   36  36 SER B  311  ASN B  326  1                                  16    
HELIX   37  37 MET B  328  LYS B  331  5                                   4    
SHEET    1   A 4 TYR A  48  ILE A  50  0                                        
SHEET    2   A 4 THR A  27  PHE A  30  1  N  ALA A  29   O  TYR A  48           
SHEET    3   A 4 ARG A   4  TYR A   8  1  N  ILE A   5   O  ILE A  28           
SHEET    4   A 4 ALA A  64  VAL A  66  1  O  VAL A  65   N  ALA A   6           
SHEET    1   B 2 TYR A  88  PHE A  89  0                                        
SHEET    2   B 2 LEU A 333  THR A 334 -1  O  THR A 334   N  TYR A  88           
SHEET    1   C 3 PHE A 143  ALA A 145  0                                        
SHEET    2   C 3 VAL A 129  LYS A 132 -1  N  VAL A 131   O  PHE A 143           
SHEET    3   C 3 GLN A 171  GLU A 174 -1  O  GLN A 173   N  ILE A 130           
SHEET    1   D 5 TYR A 227  PRO A 234  0                                        
SHEET    2   D 5 GLU A 193  ASN A 206 -1  N  TYR A 203   O  GLY A 231           
SHEET    3   D 5 VAL A 179  SER A 188 -1  N  HIS A 184   O  SER A 198           
SHEET    4   D 5 GLY A 265  PHE A 273 -1  O  GLY A 265   N  TYR A 187           
SHEET    5   D 5 PHE A 279  SER A 285 -1  O  GLU A 283   N  GLU A 270           
SHEET    1   E 4 TYR B  48  ILE B  50  0                                        
SHEET    2   E 4 THR B  27  PHE B  30  1  N  ALA B  29   O  TYR B  48           
SHEET    3   E 4 ARG B   4  TYR B   8  1  N  ILE B   5   O  ILE B  28           
SHEET    4   E 4 ALA B  64  VAL B  66  1  O  VAL B  65   N  ALA B   6           
SHEET    1   F 2 TYR B  88  PHE B  89  0                                        
SHEET    2   F 2 LEU B 333  THR B 334 -1  O  THR B 334   N  TYR B  88           
SHEET    1   G 3 PHE B 143  ALA B 145  0                                        
SHEET    2   G 3 VAL B 129  LYS B 132 -1  N  VAL B 129   O  ALA B 145           
SHEET    3   G 3 GLN B 171  GLU B 174 -1  O  GLN B 173   N  ILE B 130           
SHEET    1   H 5 TYR B 227  PRO B 234  0                                        
SHEET    2   H 5 GLU B 193  ASN B 206 -1  N  TYR B 203   O  GLY B 231           
SHEET    3   H 5 VAL B 179  SER B 188 -1  N  HIS B 184   O  SER B 198           
SHEET    4   H 5 GLY B 265  PHE B 273 -1  O  GLY B 265   N  TYR B 187           
SHEET    5   H 5 PHE B 279  SER B 285 -1  O  GLU B 283   N  GLU B 270           
LINK         O   GLU A  98                NA    NA A 600     1555   1555  2.46  
LINK         OE2 GLU A 104                NA    NA A 600     1555   1555  2.61  
LINK         O   ILE A 284                NA    NA A 600     1555   1555  2.36  
LINK         O   GLU B  98                NA    NA B 600     1555   1555  2.44  
LINK         OE2 GLU B 104                NA    NA B 600     1555   1555  2.58  
LINK         O   ILE B 284                NA    NA B 600     1555   1555  2.47  
LINK        NA    NA A 600                 O   HOH A 602     1555   1555  2.27  
LINK        NA    NA A 600                 O   HOH A 621     1555   1555  2.38  
LINK        NA    NA B 600                 O   HOH B 842     1555   1555  2.37  
LINK        NA    NA B 600                 O   HOH B 795     1555   1555  2.32  
LINK        NA    NA B 600                 O   HOH B 796     1555   1555  2.41  
CISPEP   1 SER A  205    ASN A  206          0         5.28                     
CISPEP   2 SER B  205    ASN B  206          0         5.00                     
SITE     1 AC1  5 GLU A  98  GLU A 104  ILE A 284  HOH A 602                    
SITE     2 AC1  5 HOH A 621                                                     
SITE     1 AC2  5 HIS A  11  ARG A 202  ARG A 287  ALA A 290                    
SITE     2 AC2  5 HOH A 894                                                     
SITE     1 AC3  6 GLU B  98  GLU B 104  ILE B 284  HOH B 795                    
SITE     2 AC3  6 HOH B 796  HOH B 842                                          
SITE     1 AC4  4 HIS B  11  ARG B 287  ALA B 290  HOH B 837                    
SITE     1 AC5 13 ILE A 130  LYS A 132  TYR A 142  GLN A 173                    
SITE     2 AC5 13 GLU A 174  TYR A 175  ARG A 212  HOH A 610                    
SITE     3 AC5 13 HOH A 612  HOH A 615  HOH A 616  HOH A 823                    
SITE     4 AC5 13 HOH A 931                                                     
SITE     1 AC6 16 SER A  10  HIS A  11  GLY A  70  SER A  71                    
SITE     2 AC6 16 HIS A  75  ARG A 202  ASN A 232  ARG A 238                    
SITE     3 AC6 16 SER A 240  ALA A 290  HOH A 603  HOH A 606                    
SITE     4 AC6 16 HOH A 607  HOH A 608  HOH A 609  HOH A 781                    
SITE     1 AC7 13 PRO B 116  ILE B 130  LYS B 132  TYR B 142                    
SITE     2 AC7 13 GLN B 173  GLU B 174  TYR B 175  GLU B 283                    
SITE     3 AC7 13 HOH B 698  HOH B 700  HOH B 701  HOH B 702                    
SITE     4 AC7 13 HOH B 767                                                     
SITE     1 AC8 16 SER B  10  HIS B  11  GLY B  70  SER B  71                    
SITE     2 AC8 16 HIS B  75  ARG B 202  ASN B 232  ARG B 238                    
SITE     3 AC8 16 SER B 240  ALA B 290  HOH B 603  HOH B 606                    
SITE     4 AC8 16 HOH B 607  HOH B 608  HOH B 609  HOH B 829                    
SITE     1 AC9  4 TYR A 142  ASP A 217  TYR A 227  HOH A 779                    
SITE     1 BC1  6 TYR A 175  LEU A 177  ILE A 213  PHE A 221                    
SITE     2 BC1  6 HOH A 834  HOH A 835                                          
SITE     1 BC2  6 TYR B 175  LEU B 177  ILE B 213  PHE B 221                    
SITE     2 BC2  6 MET B 223  HOH B 856                                          
CRYST1  123.671  123.671  375.359  90.00  90.00 120.00 H 3 2        36          
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      0.008086  0.004668  0.000000        0.00000                         
SCALE2      0.000000  0.009337  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002664        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system