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Database: PDB
Entry: 2R86
LinkDB: 2R86
Original site: 2R86 
HEADER    UNKNOWN FUNCTION                        10-SEP-07   2R86              
TITLE     CRYSTAL STRUCTURE OF PURP FROM PYROCOCCUS FURIOSUS COMPLEXED WITH ATP 
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   4   25-OCT-17 2R86    1       REMARK                                   
REVDAT   3   24-FEB-09 2R86    1       VERSN                                    
REVDAT   2   22-JUL-08 2R86    1       JRNL                                     
REVDAT   1   04-DEC-07 2R86    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.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.3.0026                                      
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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.97                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 55970                          
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) : 0.219                           
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2874                            
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3032                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 77.26                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3010                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 168                          
REMARK   3   BIN FREE R VALUE                    : 0.3750                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5291                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 100                                     
REMARK   3   SOLVENT ATOMS            : 133                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.86000                                              
REMARK   3    B22 (A**2) : 1.86000                                              
REMARK   3    B33 (A**2) : -2.80000                                             
REMARK   3    B12 (A**2) : 0.93000                                              
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): 0.235         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.197         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.135         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.915         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.936                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.923                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5522 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7491 ; 1.024 ; 1.997       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   650 ; 5.628 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   254 ;35.099 ;23.661       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   971 ;14.795 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    40 ;11.642 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   809 ; 0.070 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4128 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2224 ; 0.180 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3764 ; 0.305 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   237 ; 0.103 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   150 ; 0.152 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    46 ; 0.139 ; 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):  3258 ; 0.463 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5293 ; 0.870 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2354 ; 0.940 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2198 ; 1.676 ; 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      1       A     334      5                      
REMARK   3           1     B      1       B     334      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1268 ; 0.150 ; 0.500           
REMARK   3   LOOSE POSITIONAL   1    B    (A):   1307 ; 0.370 ; 5.000           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1268 ; 7.810 ; 2.000           
REMARK   3   LOOSE THERMAL      1    B (A**2):   1307 ; 7.870 ;20.000           
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 2R86 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_1000044545.                                   
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                             : 6.1                                
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   : 55970                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
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     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.28300                            
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   (%): 76.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% MPD, 100 MM NA/K PHOSPHATE, PH       
REMARK 280  6.1, 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       61.23850            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       35.35606            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000      186.97500            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       61.23850            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       35.35606            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000      186.97500            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       61.23850            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       35.35606            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      186.97500            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       61.23850            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       35.35606            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      186.97500            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       61.23850            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       35.35606            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      186.97500            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       61.23850            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       35.35606            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      186.97500            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       70.71213            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000      373.95000            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       70.71213            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000      373.95000            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       70.71213            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      373.95000            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       70.71213            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      373.95000            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       70.71213            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000      373.95000            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       70.71213            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000      373.95000            
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: 19440 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      122.47700            
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       61.23850            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      106.06819            
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: 16210 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      122.47700            
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       61.23850            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      106.06819            
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 676  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 688  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 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     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      -62.28     77.16                                   
REMARK 500    SER A  12       25.54   -157.41                                   
REMARK 500    LYS A  41      -61.27   -120.36                                   
REMARK 500    LYS A 137       74.69   -118.80                                   
REMARK 500    ASN A 169       90.15     31.98                                   
REMARK 500    SER A 198      167.16    177.54                                   
REMARK 500    MET A 260       13.48   -145.71                                   
REMARK 500    ASN A 297       33.47    -97.95                                   
REMARK 500    MET A 328       31.92   -140.02                                   
REMARK 500    HIS B  11      -63.50     72.93                                   
REMARK 500    SER B  12       22.95   -154.08                                   
REMARK 500    LYS B  41      -55.62   -129.50                                   
REMARK 500    GLU B  51       43.92    -79.67                                   
REMARK 500    SER B 198      172.84    179.52                                   
REMARK 500    PHE B 295       44.64   -107.17                                   
REMARK 500    ASN B 297       36.07    -94.28                                   
REMARK 500    MET B 328       34.67   -147.63                                   
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 ILE A 284   O   102.3                                              
REMARK 620 3 HOH A 673   O    89.6 145.3                                        
REMARK 620 4 HOH A 601   O   149.7  82.1 103.8                                  
REMARK 620 N                    1     2     3                                   
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 ILE B 284   O   112.8                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 600                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 600                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 400                 
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 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2R84   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN WITH COMPLEXED WITH AMP AND AICAR                       
REMARK 900 RELATED ID: 2R85   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN WITH COMPLEXED WITH AMP                                 
REMARK 900 RELATED ID: 2R87   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN WITH COMPLEXED WITH ADP                                 
DBREF  2R86 A    1   334  UNP    Q8U0R7   Q8U0R7_PYRFU     1    334             
DBREF  2R86 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    PO4  A 401       5                                                       
HET    PO4  A 402       5                                                       
HET     NA  A 600       1                                                       
HET    ATP  A 400      31                                                       
HET    MPD  A 500       8                                                       
HET    MPD  A 501       8                                                       
HET    PO4  B 401       5                                                       
HET    PO4  B 402       5                                                       
HET     NA  B 600       1                                                       
HET    ATP  B 400      31                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM      NA SODIUM ION                                                       
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
FORMUL   3  PO4    4(O4 P 3-)                                                   
FORMUL   5   NA    2(NA 1+)                                                     
FORMUL   6  ATP    2(C10 H16 N5 O13 P3)                                         
FORMUL   7  MPD    2(C6 H14 O2)                                                 
FORMUL  13  HOH   *133(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 SER A   71  GLY A   77  1                                   7    
HELIX    6   6 GLY A   77  ASN A   83  1                                   7    
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  GLU A  220  1                                   7    
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 SER B   71  GLY B   77  1                                   7    
HELIX   25  25 GLY B   77  ASN B   83  1                                   7    
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  PHE B  158  1                                  12    
HELIX   30  30 VAL B  207  GLY B  211  1                                   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 4 VAL A 118  TYR A 119  0                                        
SHEET    2   C 4 ILE A 170  GLU A 174 -1  O  ILE A 172   N  TYR A 119           
SHEET    3   C 4 VAL A 129  PRO A 133 -1  N  ILE A 130   O  GLN A 173           
SHEET    4   C 4 PHE A 143  ALA A 145 -1  O  ALA A 145   N  VAL A 129           
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  ILE A 230           
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  ARG B 201   O  ILE B 233           
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  SER B 285   N  CYS B 268           
LINK         O   GLU A  98                NA    NA A 600     1555   1555  2.58  
LINK         O   ILE A 284                NA    NA A 600     1555   1555  2.60  
LINK         O   GLU B  98                NA    NA B 600     1555   1555  2.58  
LINK         O   ILE B 284                NA    NA B 600     1555   1555  2.64  
LINK        NA    NA A 600                 O   HOH A 673     1555   1555  2.55  
LINK        NA    NA A 600                 O   HOH A 601     1555   1555  2.72  
CISPEP   1 HIS A  134    GLY A  135          0        -4.22                     
CISPEP   2 SER A  205    ASN A  206          0         8.36                     
CISPEP   3 SER B  205    ASN B  206          0         7.07                     
SITE     1 AC1  7 SER A  10  SER A  71  HIS A  75  ARG A 238                    
SITE     2 AC1  7 SER A 240  HOH A 642  HOH A 668                               
SITE     1 AC2  9 HIS A  11  ARG A 202  ARG A 287  ALA A 290                    
SITE     2 AC2  9 HOH A 612  HOH A 644  HOH A 664  HOH A 665                    
SITE     3 AC2  9 HOH A 667                                                     
SITE     1 AC3  5 GLU A  98  GLU A 104  ILE A 284  HOH A 601                    
SITE     2 AC3  5 HOH A 673                                                     
SITE     1 AC4  6 SER B  10  SER B  71  HIS B  75  ARG B 238                    
SITE     2 AC4  6 SER B 240  HOH B 603                                          
SITE     1 AC5  6 HIS B  11  ARG B 202  ARG B 287  ALA B 290                    
SITE     2 AC5  6 HOH B 611  HOH B 618                                          
SITE     1 AC6  3 GLU B  98  GLU B 104  ILE B 284                               
SITE     1 AC7 13 PRO A 116  LYS A 132  ALA A 136  GLY A 138                    
SITE     2 AC7 13 TYR A 142  GLN A 173  GLU A 174  TYR A 175                    
SITE     3 AC7 13 PHE A 282  GLU A 283  HOH A 663  HOH A 687                    
SITE     4 AC7 13 HOH A 691                                                     
SITE     1 AC8  9 PRO B 116  LYS B 132  TYR B 142  GLN B 173                    
SITE     2 AC8  9 GLU B 174  ARG B 212  TYR B 227  PHE B 282                    
SITE     3 AC8  9 HOH B 642                                                     
SITE     1 AC9  4 ILE A 130  TYR A 142  ASP A 217  TYR A 227                    
SITE     1 BC1  3 TYR A 175  LEU A 177  PHE A 221                               
CRYST1  122.477  122.477  560.925  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      0.008165  0.004714  0.000000        0.00000                         
SCALE2      0.000000  0.009428  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.001783        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system