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Database: PDB
Entry: 2R87
LinkDB: 2R87
Original site: 2R87 
HEADER    UNKNOWN FUNCTION                        10-SEP-07   2R87              
TITLE     CRYSTAL STRUCTURE OF PURP FROM PYROCOCCUS FURIOSUS COMPLEXED WITH ADP 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PURP PROTEIN PF1517;                                       
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
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 2R87    1       REMARK                                   
REVDAT   3   24-FEB-09 2R87    1       VERSN                                    
REVDAT   2   22-JUL-08 2R87    1       JRNL                                     
REVDAT   1   04-DEC-07 2R87    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.    2.30 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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.64                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 98928                          
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) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4941                            
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6810                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.73                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2380                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 329                          
REMARK   3   BIN FREE R VALUE                    : 0.3190                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 16230                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 257                                     
REMARK   3   SOLVENT ATOMS            : 541                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.25                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.37000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : -1.11000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.66000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.382         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.244         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.168         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.766         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.929                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.897                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 16858 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 22848 ; 1.067 ; 1.994       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1998 ; 5.711 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   774 ;32.627 ;23.721       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2988 ;14.870 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   120 ; 9.230 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2460 ; 0.074 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12630 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  7872 ; 0.175 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 11525 ; 0.302 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   918 ; 0.117 ; 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):    74 ; 0.153 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    19 ; 0.098 ; 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): 10376 ; 0.419 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 16212 ; 0.735 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7541 ; 0.827 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  6636 ; 1.414 ; 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 : 3                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D E F                     
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     160      5                      
REMARK   3           1     B      1       B     160      5                      
REMARK   3           1     C      1       C     160      5                      
REMARK   3           1     D      1       D     160      5                      
REMARK   3           1     E      1       E     160      5                      
REMARK   3           1     F      1       F     160      5                      
REMARK   3           2     A    170       A     334      5                      
REMARK   3           2     B    170       B     334      5                      
REMARK   3           2     C    170       C     334      5                      
REMARK   3           2     D    170       D     334      5                      
REMARK   3           2     E    170       E     334      5                      
REMARK   3           2     F    170       F     334      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1300 ; 0.210 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1300 ; 0.190 ; 0.000           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   1300 ; 0.180 ; 0.000           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   1300 ; 0.150 ; 0.000           
REMARK   3   MEDIUM POSITIONAL  1    E    (A):   1300 ; 0.250 ; 0.000           
REMARK   3   MEDIUM POSITIONAL  1    F    (A):   1300 ; 0.180 ; 0.000           
REMARK   3   LOOSE POSITIONAL   1    A    (A):   1326 ; 0.580 ; 5.000           
REMARK   3   LOOSE POSITIONAL   1    B    (A):   1326 ; 0.480 ; 0.000           
REMARK   3   LOOSE POSITIONAL   1    C    (A):   1326 ; 0.580 ; 0.000           
REMARK   3   LOOSE POSITIONAL   1    D    (A):   1326 ; 0.440 ; 0.000           
REMARK   3   LOOSE POSITIONAL   1    E    (A):   1326 ; 0.580 ; 0.000           
REMARK   3   LOOSE POSITIONAL   1    F    (A):   1326 ; 0.480 ; 0.000           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1300 ; 1.300 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1300 ; 0.850 ; 0.000           
REMARK   3   MEDIUM THERMAL     1    C (A**2):   1300 ; 1.940 ; 0.000           
REMARK   3   MEDIUM THERMAL     1    D (A**2):   1300 ; 1.480 ; 0.000           
REMARK   3   MEDIUM THERMAL     1    E (A**2):   1300 ; 1.760 ; 0.000           
REMARK   3   MEDIUM THERMAL     1    F (A**2):   1300 ; 1.390 ; 0.000           
REMARK   3   LOOSE THERMAL      1    A (A**2):   1326 ; 1.500 ;10.000           
REMARK   3   LOOSE THERMAL      1    B (A**2):   1326 ; 1.040 ; 0.010           
REMARK   3   LOOSE THERMAL      1    C (A**2):   1326 ; 2.110 ; 0.000           
REMARK   3   LOOSE THERMAL      1    D (A**2):   1326 ; 1.600 ; 0.000           
REMARK   3   LOOSE THERMAL      1    E (A**2):   1326 ; 1.810 ; 0.000           
REMARK   3   LOOSE THERMAL      1    F (A**2):   1326 ; 1.460 ; 0.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A D F                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    161       A     169      5                      
REMARK   3           1     D    161       D     169      5                      
REMARK   3           1     F    161       F     169      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    A    (A):     36 ; 0.130 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  2    B    (A):     36 ; 0.150 ; 0.010           
REMARK   3   MEDIUM POSITIONAL  2    C    (A):     36 ; 0.140 ; 0.000           
REMARK   3   LOOSE POSITIONAL   2    D    (A):     43 ; 0.580 ; 5.000           
REMARK   3   LOOSE POSITIONAL   2    E    (A):     43 ; 0.760 ; 0.120           
REMARK   3   LOOSE POSITIONAL   2    F    (A):     43 ; 0.600 ; 0.000           
REMARK   3   MEDIUM THERMAL     2    A (A**2):     36 ; 0.110 ; 2.000           
REMARK   3   MEDIUM THERMAL     2    B (A**2):     36 ; 0.170 ; 0.060           
REMARK   3   MEDIUM THERMAL     2    C (A**2):     36 ; 0.080 ; 0.000           
REMARK   3   LOOSE THERMAL      2    D (A**2):     43 ; 0.120 ;10.000           
REMARK   3   LOOSE THERMAL      2    E (A**2):     43 ; 0.140 ; 0.230           
REMARK   3   LOOSE THERMAL      2    F (A**2):     43 ; 0.120 ; 0.010           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : C B E                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C    161       C     169      5                      
REMARK   3           1     B    161       B     169      5                      
REMARK   3           1     E    161       E     169      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  3    A    (A):     36 ; 0.150 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  3    B    (A):     36 ; 0.150 ; 0.010           
REMARK   3   MEDIUM POSITIONAL  3    C    (A):     36 ; 0.150 ; 0.000           
REMARK   3   LOOSE POSITIONAL   3    D    (A):     43 ; 0.390 ; 5.000           
REMARK   3   LOOSE POSITIONAL   3    E    (A):     43 ; 0.380 ; 0.120           
REMARK   3   LOOSE POSITIONAL   3    F    (A):     43 ; 0.350 ; 0.000           
REMARK   3   MEDIUM THERMAL     3    A (A**2):     36 ; 0.310 ; 2.000           
REMARK   3   MEDIUM THERMAL     3    B (A**2):     36 ; 0.230 ; 0.060           
REMARK   3   MEDIUM THERMAL     3    C (A**2):     36 ; 0.120 ; 0.000           
REMARK   3   LOOSE THERMAL      3    D (A**2):     43 ; 0.230 ;10.000           
REMARK   3   LOOSE THERMAL      3    E (A**2):     43 ; 0.210 ; 0.230           
REMARK   3   LOOSE THERMAL      3    F (A**2):     43 ; 0.140 ; 0.010           
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   : 1.20                                          
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 2R87 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_1000044546.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-07; 05-MAY-07               
REMARK 200  TEMPERATURE           (KELVIN) : 100; NULL                          
REMARK 200  PH                             : 4.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; N                               
REMARK 200  RADIATION SOURCE               : CHESS; ROTATING ANODE              
REMARK 200  BEAMLINE                       : F1; NULL                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL; RIGAKU                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; NULL                            
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91770; 1.54178                   
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; IMAGE PLATE                   
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270; RIGAKU RAXIS     
REMARK 200                                   IV                                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 98928                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
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     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : 0.13800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL                        
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   (%): 50.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% 2-PROPANOL, 200 MM LI2SO4, 100 MM    
REMARK 280  NA PHOSPHATE-CITRATE, PH 4.2, VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       63.61100            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
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                                                      
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: 16940 ANGSTROM**2                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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                                                                      
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: 16720 ANGSTROM**2                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG1  THR F   274     OD2  ASP F   276              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A  11      -59.66     67.68                                   
REMARK 500    SER A  12       25.95   -153.75                                   
REMARK 500    ASP A 166       65.41   -116.97                                   
REMARK 500    LYS A 168       57.31     39.97                                   
REMARK 500    MET A 260       16.08   -142.53                                   
REMARK 500    ASN A 297       37.09    -95.15                                   
REMARK 500    MET A 328       28.37   -144.01                                   
REMARK 500    HIS B  11      -59.10     67.67                                   
REMARK 500    SER B  12       23.41   -155.91                                   
REMARK 500    LYS B 164       68.13     66.53                                   
REMARK 500    GLU B 165     -152.96     65.31                                   
REMARK 500    LYS B 168       75.92    -69.75                                   
REMARK 500    SER B 198      172.58    178.89                                   
REMARK 500    MET B 260       17.83   -144.13                                   
REMARK 500    ASN B 297       35.64    -95.48                                   
REMARK 500    MET B 328       29.62   -143.11                                   
REMARK 500    HIS C  11      -63.01     71.03                                   
REMARK 500    SER C  12       18.13   -151.66                                   
REMARK 500    LYS C 164       92.72     70.83                                   
REMARK 500    GLU C 165     -155.78     47.60                                   
REMARK 500    LYS C 168       85.42    -64.15                                   
REMARK 500    ASN C 169       47.58     27.44                                   
REMARK 500    MET C 260       23.39   -141.89                                   
REMARK 500    ALA C 286       57.10    -90.49                                   
REMARK 500    ASN C 297       41.30    -93.66                                   
REMARK 500    MET C 328       25.46   -147.66                                   
REMARK 500    HIS D  11      -57.00     69.71                                   
REMARK 500    SER D  12       17.25   -158.34                                   
REMARK 500    LYS D  41      -62.86   -105.90                                   
REMARK 500    ILE D 125      105.77    -59.54                                   
REMARK 500    ASN D 169       53.25     29.08                                   
REMARK 500    PHE D 295       40.60   -105.45                                   
REMARK 500    ASN D 297       37.57    -94.55                                   
REMARK 500    MET D 328       23.44   -146.02                                   
REMARK 500    HIS E  11      -55.38     72.30                                   
REMARK 500    SER E  12       17.83   -156.78                                   
REMARK 500    HIS E 134      113.74    -27.01                                   
REMARK 500    LYS E 164       74.06     64.83                                   
REMARK 500    GLU E 165     -154.18     60.08                                   
REMARK 500    LYS E 168       90.13    -63.76                                   
REMARK 500    ASN E 169       57.58     34.10                                   
REMARK 500    SER E 198      167.42    176.19                                   
REMARK 500    MET E 260       14.77   -140.36                                   
REMARK 500    ASN E 297       37.53    -96.37                                   
REMARK 500    HIS F  11      -60.65     71.44                                   
REMARK 500    SER F  12       23.15   -154.94                                   
REMARK 500    GLU F  51       59.37    -92.86                                   
REMARK 500    TYR F  54       89.38   -152.57                                   
REMARK 500    ASP F 166       53.32   -103.96                                   
REMARK 500    LYS F 168       56.98     31.69                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      54 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 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 PO4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 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 PO4 B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 F 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 F 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 F 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP D 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP F 400                 
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: 2R86   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN WITH COMPLEXED WITH ATP                                 
DBREF  2R87 A    1   334  UNP    Q8U0R7   Q8U0R7_PYRFU     1    334             
DBREF  2R87 B    1   334  UNP    Q8U0R7   Q8U0R7_PYRFU     1    334             
DBREF  2R87 C    1   334  UNP    Q8U0R7   Q8U0R7_PYRFU     1    334             
DBREF  2R87 D    1   334  UNP    Q8U0R7   Q8U0R7_PYRFU     1    334             
DBREF  2R87 E    1   334  UNP    Q8U0R7   Q8U0R7_PYRFU     1    334             
DBREF  2R87 F    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                          
SEQRES   1 C  334  MET LYS VAL ARG ILE ALA THR TYR ALA SER HIS SER ALA          
SEQRES   2 C  334  LEU GLN ILE LEU LYS GLY ALA LYS ASP GLU GLY PHE GLU          
SEQRES   3 C  334  THR ILE ALA PHE GLY SER SER LYS VAL LYS PRO LEU TYR          
SEQRES   4 C  334  THR LYS TYR PHE PRO VAL ALA ASP TYR PHE ILE GLU GLU          
SEQRES   5 C  334  LYS TYR PRO GLU GLU GLU LEU LEU ASN LEU ASN ALA VAL          
SEQRES   6 C  334  VAL VAL PRO THR GLY SER PHE VAL ALA HIS LEU GLY ILE          
SEQRES   7 C  334  GLU LEU VAL GLU ASN MET LYS VAL PRO TYR PHE GLY ASN          
SEQRES   8 C  334  LYS ARG VAL LEU ARG TRP GLU SER ASP ARG ASN LEU GLU          
SEQRES   9 C  334  ARG LYS TRP LEU LYS LYS ALA GLY ILE ARG VAL PRO GLU          
SEQRES  10 C  334  VAL TYR GLU ASP PRO ASP ASP ILE GLU LYS PRO VAL ILE          
SEQRES  11 C  334  VAL LYS PRO HIS GLY ALA LYS GLY GLY LYS GLY TYR PHE          
SEQRES  12 C  334  LEU ALA LYS ASP PRO GLU ASP PHE TRP ARG LYS ALA GLU          
SEQRES  13 C  334  LYS PHE LEU GLY ILE LYS ARG LYS GLU ASP LEU LYS ASN          
SEQRES  14 C  334  ILE GLN ILE GLN GLU TYR VAL LEU GLY VAL PRO VAL TYR          
SEQRES  15 C  334  PRO HIS TYR PHE TYR SER LYS VAL ARG GLU GLU LEU GLU          
SEQRES  16 C  334  LEU MET SER ILE ASP ARG ARG TYR GLU SER ASN VAL ASP          
SEQRES  17 C  334  ALA ILE GLY ARG ILE PRO ALA LYS ASP GLN LEU GLU PHE          
SEQRES  18 C  334  ASP MET ASP ILE THR TYR THR VAL ILE GLY ASN ILE PRO          
SEQRES  19 C  334  ILE VAL LEU ARG GLU SER LEU LEU MET ASP VAL ILE GLU          
SEQRES  20 C  334  ALA GLY GLU ARG VAL VAL LYS ALA ALA GLU GLU LEU MET          
SEQRES  21 C  334  GLY GLY LEU TRP GLY PRO PHE CYS LEU GLU GLY VAL PHE          
SEQRES  22 C  334  THR PRO ASP LEU GLU PHE VAL VAL PHE GLU ILE SER ALA          
SEQRES  23 C  334  ARG ILE VAL ALA GLY THR ASN ILE PHE VAL ASN GLY SER          
SEQRES  24 C  334  PRO TYR THR TRP LEU ARG TYR ASP ARG PRO VAL SER THR          
SEQRES  25 C  334  GLY ARG ARG ILE ALA MET GLU ILE ARG GLU ALA ILE GLU          
SEQRES  26 C  334  ASN ASP MET LEU GLU LYS VAL LEU THR                          
SEQRES   1 D  334  MET LYS VAL ARG ILE ALA THR TYR ALA SER HIS SER ALA          
SEQRES   2 D  334  LEU GLN ILE LEU LYS GLY ALA LYS ASP GLU GLY PHE GLU          
SEQRES   3 D  334  THR ILE ALA PHE GLY SER SER LYS VAL LYS PRO LEU TYR          
SEQRES   4 D  334  THR LYS TYR PHE PRO VAL ALA ASP TYR PHE ILE GLU GLU          
SEQRES   5 D  334  LYS TYR PRO GLU GLU GLU LEU LEU ASN LEU ASN ALA VAL          
SEQRES   6 D  334  VAL VAL PRO THR GLY SER PHE VAL ALA HIS LEU GLY ILE          
SEQRES   7 D  334  GLU LEU VAL GLU ASN MET LYS VAL PRO TYR PHE GLY ASN          
SEQRES   8 D  334  LYS ARG VAL LEU ARG TRP GLU SER ASP ARG ASN LEU GLU          
SEQRES   9 D  334  ARG LYS TRP LEU LYS LYS ALA GLY ILE ARG VAL PRO GLU          
SEQRES  10 D  334  VAL TYR GLU ASP PRO ASP ASP ILE GLU LYS PRO VAL ILE          
SEQRES  11 D  334  VAL LYS PRO HIS GLY ALA LYS GLY GLY LYS GLY TYR PHE          
SEQRES  12 D  334  LEU ALA LYS ASP PRO GLU ASP PHE TRP ARG LYS ALA GLU          
SEQRES  13 D  334  LYS PHE LEU GLY ILE LYS ARG LYS GLU ASP LEU LYS ASN          
SEQRES  14 D  334  ILE GLN ILE GLN GLU TYR VAL LEU GLY VAL PRO VAL TYR          
SEQRES  15 D  334  PRO HIS TYR PHE TYR SER LYS VAL ARG GLU GLU LEU GLU          
SEQRES  16 D  334  LEU MET SER ILE ASP ARG ARG TYR GLU SER ASN VAL ASP          
SEQRES  17 D  334  ALA ILE GLY ARG ILE PRO ALA LYS ASP GLN LEU GLU PHE          
SEQRES  18 D  334  ASP MET ASP ILE THR TYR THR VAL ILE GLY ASN ILE PRO          
SEQRES  19 D  334  ILE VAL LEU ARG GLU SER LEU LEU MET ASP VAL ILE GLU          
SEQRES  20 D  334  ALA GLY GLU ARG VAL VAL LYS ALA ALA GLU GLU LEU MET          
SEQRES  21 D  334  GLY GLY LEU TRP GLY PRO PHE CYS LEU GLU GLY VAL PHE          
SEQRES  22 D  334  THR PRO ASP LEU GLU PHE VAL VAL PHE GLU ILE SER ALA          
SEQRES  23 D  334  ARG ILE VAL ALA GLY THR ASN ILE PHE VAL ASN GLY SER          
SEQRES  24 D  334  PRO TYR THR TRP LEU ARG TYR ASP ARG PRO VAL SER THR          
SEQRES  25 D  334  GLY ARG ARG ILE ALA MET GLU ILE ARG GLU ALA ILE GLU          
SEQRES  26 D  334  ASN ASP MET LEU GLU LYS VAL LEU THR                          
SEQRES   1 E  334  MET LYS VAL ARG ILE ALA THR TYR ALA SER HIS SER ALA          
SEQRES   2 E  334  LEU GLN ILE LEU LYS GLY ALA LYS ASP GLU GLY PHE GLU          
SEQRES   3 E  334  THR ILE ALA PHE GLY SER SER LYS VAL LYS PRO LEU TYR          
SEQRES   4 E  334  THR LYS TYR PHE PRO VAL ALA ASP TYR PHE ILE GLU GLU          
SEQRES   5 E  334  LYS TYR PRO GLU GLU GLU LEU LEU ASN LEU ASN ALA VAL          
SEQRES   6 E  334  VAL VAL PRO THR GLY SER PHE VAL ALA HIS LEU GLY ILE          
SEQRES   7 E  334  GLU LEU VAL GLU ASN MET LYS VAL PRO TYR PHE GLY ASN          
SEQRES   8 E  334  LYS ARG VAL LEU ARG TRP GLU SER ASP ARG ASN LEU GLU          
SEQRES   9 E  334  ARG LYS TRP LEU LYS LYS ALA GLY ILE ARG VAL PRO GLU          
SEQRES  10 E  334  VAL TYR GLU ASP PRO ASP ASP ILE GLU LYS PRO VAL ILE          
SEQRES  11 E  334  VAL LYS PRO HIS GLY ALA LYS GLY GLY LYS GLY TYR PHE          
SEQRES  12 E  334  LEU ALA LYS ASP PRO GLU ASP PHE TRP ARG LYS ALA GLU          
SEQRES  13 E  334  LYS PHE LEU GLY ILE LYS ARG LYS GLU ASP LEU LYS ASN          
SEQRES  14 E  334  ILE GLN ILE GLN GLU TYR VAL LEU GLY VAL PRO VAL TYR          
SEQRES  15 E  334  PRO HIS TYR PHE TYR SER LYS VAL ARG GLU GLU LEU GLU          
SEQRES  16 E  334  LEU MET SER ILE ASP ARG ARG TYR GLU SER ASN VAL ASP          
SEQRES  17 E  334  ALA ILE GLY ARG ILE PRO ALA LYS ASP GLN LEU GLU PHE          
SEQRES  18 E  334  ASP MET ASP ILE THR TYR THR VAL ILE GLY ASN ILE PRO          
SEQRES  19 E  334  ILE VAL LEU ARG GLU SER LEU LEU MET ASP VAL ILE GLU          
SEQRES  20 E  334  ALA GLY GLU ARG VAL VAL LYS ALA ALA GLU GLU LEU MET          
SEQRES  21 E  334  GLY GLY LEU TRP GLY PRO PHE CYS LEU GLU GLY VAL PHE          
SEQRES  22 E  334  THR PRO ASP LEU GLU PHE VAL VAL PHE GLU ILE SER ALA          
SEQRES  23 E  334  ARG ILE VAL ALA GLY THR ASN ILE PHE VAL ASN GLY SER          
SEQRES  24 E  334  PRO TYR THR TRP LEU ARG TYR ASP ARG PRO VAL SER THR          
SEQRES  25 E  334  GLY ARG ARG ILE ALA MET GLU ILE ARG GLU ALA ILE GLU          
SEQRES  26 E  334  ASN ASP MET LEU GLU LYS VAL LEU THR                          
SEQRES   1 F  334  MET LYS VAL ARG ILE ALA THR TYR ALA SER HIS SER ALA          
SEQRES   2 F  334  LEU GLN ILE LEU LYS GLY ALA LYS ASP GLU GLY PHE GLU          
SEQRES   3 F  334  THR ILE ALA PHE GLY SER SER LYS VAL LYS PRO LEU TYR          
SEQRES   4 F  334  THR LYS TYR PHE PRO VAL ALA ASP TYR PHE ILE GLU GLU          
SEQRES   5 F  334  LYS TYR PRO GLU GLU GLU LEU LEU ASN LEU ASN ALA VAL          
SEQRES   6 F  334  VAL VAL PRO THR GLY SER PHE VAL ALA HIS LEU GLY ILE          
SEQRES   7 F  334  GLU LEU VAL GLU ASN MET LYS VAL PRO TYR PHE GLY ASN          
SEQRES   8 F  334  LYS ARG VAL LEU ARG TRP GLU SER ASP ARG ASN LEU GLU          
SEQRES   9 F  334  ARG LYS TRP LEU LYS LYS ALA GLY ILE ARG VAL PRO GLU          
SEQRES  10 F  334  VAL TYR GLU ASP PRO ASP ASP ILE GLU LYS PRO VAL ILE          
SEQRES  11 F  334  VAL LYS PRO HIS GLY ALA LYS GLY GLY LYS GLY TYR PHE          
SEQRES  12 F  334  LEU ALA LYS ASP PRO GLU ASP PHE TRP ARG LYS ALA GLU          
SEQRES  13 F  334  LYS PHE LEU GLY ILE LYS ARG LYS GLU ASP LEU LYS ASN          
SEQRES  14 F  334  ILE GLN ILE GLN GLU TYR VAL LEU GLY VAL PRO VAL TYR          
SEQRES  15 F  334  PRO HIS TYR PHE TYR SER LYS VAL ARG GLU GLU LEU GLU          
SEQRES  16 F  334  LEU MET SER ILE ASP ARG ARG TYR GLU SER ASN VAL ASP          
SEQRES  17 F  334  ALA ILE GLY ARG ILE PRO ALA LYS ASP GLN LEU GLU PHE          
SEQRES  18 F  334  ASP MET ASP ILE THR TYR THR VAL ILE GLY ASN ILE PRO          
SEQRES  19 F  334  ILE VAL LEU ARG GLU SER LEU LEU MET ASP VAL ILE GLU          
SEQRES  20 F  334  ALA GLY GLU ARG VAL VAL LYS ALA ALA GLU GLU LEU MET          
SEQRES  21 F  334  GLY GLY LEU TRP GLY PRO PHE CYS LEU GLU GLY VAL PHE          
SEQRES  22 F  334  THR PRO ASP LEU GLU PHE VAL VAL PHE GLU ILE SER ALA          
SEQRES  23 F  334  ARG ILE VAL ALA GLY THR ASN ILE PHE VAL ASN GLY SER          
SEQRES  24 F  334  PRO TYR THR TRP LEU ARG TYR ASP ARG PRO VAL SER THR          
SEQRES  25 F  334  GLY ARG ARG ILE ALA MET GLU ILE ARG GLU ALA ILE GLU          
SEQRES  26 F  334  ASN ASP MET LEU GLU LYS VAL LEU THR                          
HET    PO4  A 402       5                                                       
HET    PO4  A 501       5                                                       
HET    PO4  A 401       5                                                       
HET    ADP  A 400      27                                                       
HET    PO4  B 402       5                                                       
HET    PO4  B 501       5                                                       
HET    PO4  B 401       5                                                       
HET    ADP  B 400      27                                                       
HET    PO4  C 401       5                                                       
HET    PO4  C 402       5                                                       
HET    PO4  C 500       5                                                       
HET    PO4  C 501       5                                                       
HET    ADP  C 400      27                                                       
HET    PO4  D 402       5                                                       
HET    PO4  D 501       5                                                       
HET    PO4  D 401       5                                                       
HET    ADP  D 400      27                                                       
HET    PO4  E 402       5                                                       
HET    PO4  E 501       5                                                       
HET    PO4  E 401       5                                                       
HET    ADP  E 400      27                                                       
HET    PO4  F 401       5                                                       
HET    PO4  F 402       5                                                       
HET    PO4  F 501       5                                                       
HET    ADP  F 400      27                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
FORMUL   7  PO4    19(O4 P 3-)                                                  
FORMUL  10  ADP    6(C10 H15 N5 O10 P2)                                         
FORMUL  32  HOH   *541(H2 O)                                                    
HELIX    1   1 SER A   12  GLU A   23  1                                  12    
HELIX    2   2 VAL A   35  LYS A   41  1                                   7    
HELIX    3   3 PRO A   55  LEU A   62  1                                   8    
HELIX    4   4 SER A   71  GLY A   77  1                                   7    
HELIX    5   5 GLY A   77  MET A   84  1                                   8    
HELIX    6   6 ARG A   93  ASP A  100  1                                   8    
HELIX    7   7 ASP A  100  ALA A  111  1                                  12    
HELIX    8   8 ASP A  121  ILE A  125  5                                   5    
HELIX    9   9 ASP A  147  GLY A  160  1                                  14    
HELIX   10  10 ARG A  163  LEU A  167  5                                   5    
HELIX   11  11 ALA A  209  ILE A  213  5                                   5    
HELIX   12  12 PRO A  214  ASP A  222  5                                   9    
HELIX   13  13 LEU A  241  GLY A  261  1                                  21    
HELIX   14  14 VAL A  289  GLY A  298  5                                  10    
HELIX   15  15 TYR A  301  ARG A  305  5                                   5    
HELIX   16  16 SER A  311  ASN A  326  1                                  16    
HELIX   17  17 MET A  328  LYS A  331  5                                   4    
HELIX   18  18 SER B   12  GLU B   23  1                                  12    
HELIX   19  19 SER B   32  LYS B   34  5                                   3    
HELIX   20  20 VAL B   35  LYS B   41  1                                   7    
HELIX   21  21 PRO B   55  LEU B   62  1                                   8    
HELIX   22  22 SER B   71  GLY B   77  1                                   7    
HELIX   23  23 GLY B   77  MET B   84  1                                   8    
HELIX   24  24 ARG B   93  ASP B  100  1                                   8    
HELIX   25  25 ASP B  100  ALA B  111  1                                  12    
HELIX   26  26 ASP B  121  ILE B  125  5                                   5    
HELIX   27  27 ASP B  147  LEU B  159  1                                  13    
HELIX   28  28 ALA B  209  ILE B  213  5                                   5    
HELIX   29  29 PRO B  214  LEU B  219  1                                   6    
HELIX   30  30 GLU B  220  ASP B  222  5                                   3    
HELIX   31  31 LEU B  241  MET B  260  1                                  20    
HELIX   32  32 VAL B  289  VAL B  296  5                                   8    
HELIX   33  33 TYR B  301  ARG B  305  5                                   5    
HELIX   34  34 SER B  311  ASN B  326  1                                  16    
HELIX   35  35 MET B  328  LYS B  331  5                                   4    
HELIX   36  36 SER C   12  GLU C   23  1                                  12    
HELIX   37  37 SER C   32  LYS C   34  5                                   3    
HELIX   38  38 VAL C   35  LYS C   41  1                                   7    
HELIX   39  39 PRO C   55  LEU C   62  1                                   8    
HELIX   40  40 SER C   71  GLY C   77  1                                   7    
HELIX   41  41 GLY C   77  MET C   84  1                                   8    
HELIX   42  42 ASN C   91  ARG C   93  5                                   3    
HELIX   43  43 VAL C   94  SER C   99  1                                   6    
HELIX   44  44 ASP C  100  ALA C  111  1                                  12    
HELIX   45  45 ASP C  121  ILE C  125  5                                   5    
HELIX   46  46 ASP C  147  GLY C  160  1                                  14    
HELIX   47  47 ALA C  209  ILE C  213  5                                   5    
HELIX   48  48 PRO C  214  LEU C  219  1                                   6    
HELIX   49  49 GLU C  220  ASP C  222  5                                   3    
HELIX   50  50 LEU C  241  GLY C  261  1                                  21    
HELIX   51  51 VAL C  289  VAL C  296  5                                   8    
HELIX   52  52 TYR C  301  ARG C  305  5                                   5    
HELIX   53  53 SER C  311  ASN C  326  1                                  16    
HELIX   54  54 MET C  328  LYS C  331  5                                   4    
HELIX   55  55 SER D   12  GLU D   23  1                                  12    
HELIX   56  56 SER D   32  LYS D   34  5                                   3    
HELIX   57  57 VAL D   35  LYS D   41  1                                   7    
HELIX   58  58 PRO D   55  LEU D   62  1                                   8    
HELIX   59  59 SER D   71  GLY D   77  1                                   7    
HELIX   60  60 GLY D   77  MET D   84  1                                   8    
HELIX   61  61 ASN D   91  ARG D   93  5                                   3    
HELIX   62  62 VAL D   94  SER D   99  1                                   6    
HELIX   63  63 ASP D  100  ALA D  111  1                                  12    
HELIX   64  64 ASP D  121  ILE D  125  5                                   5    
HELIX   65  65 ASP D  147  LEU D  159  1                                  13    
HELIX   66  66 ARG D  163  LEU D  167  5                                   5    
HELIX   67  67 VAL D  207  GLY D  211  1                                   5    
HELIX   68  68 PRO D  214  LEU D  219  1                                   6    
HELIX   69  69 GLU D  220  ASP D  222  5                                   3    
HELIX   70  70 LEU D  241  MET D  260  1                                  20    
HELIX   71  71 VAL D  289  VAL D  296  5                                   8    
HELIX   72  72 TYR D  301  ARG D  305  5                                   5    
HELIX   73  73 SER D  311  ASN D  326  1                                  16    
HELIX   74  74 MET D  328  LYS D  331  5                                   4    
HELIX   75  75 SER E   12  GLU E   23  1                                  12    
HELIX   76  76 SER E   32  LYS E   34  5                                   3    
HELIX   77  77 VAL E   35  LYS E   41  1                                   7    
HELIX   78  78 PRO E   55  LEU E   62  1                                   8    
HELIX   79  79 SER E   71  GLY E   77  1                                   7    
HELIX   80  80 GLY E   77  MET E   84  1                                   8    
HELIX   81  81 ARG E   93  ASP E  100  1                                   8    
HELIX   82  82 ASP E  100  ALA E  111  1                                  12    
HELIX   83  83 ASP E  121  ILE E  125  5                                   5    
HELIX   84  84 ASP E  147  LEU E  159  1                                  13    
HELIX   85  85 ALA E  209  ILE E  213  5                                   5    
HELIX   86  86 PRO E  214  ASP E  222  5                                   9    
HELIX   87  87 LEU E  241  MET E  260  1                                  20    
HELIX   88  88 VAL E  289  VAL E  296  5                                   8    
HELIX   89  89 TYR E  301  ARG E  305  5                                   5    
HELIX   90  90 SER E  311  ASN E  326  1                                  16    
HELIX   91  91 MET E  328  LYS E  331  5                                   4    
HELIX   92  92 SER F   12  GLU F   23  1                                  12    
HELIX   93  93 SER F   32  LYS F   34  5                                   3    
HELIX   94  94 VAL F   35  LYS F   41  1                                   7    
HELIX   95  95 PRO F   55  LEU F   62  1                                   8    
HELIX   96  96 SER F   71  GLY F   77  1                                   7    
HELIX   97  97 GLY F   77  ASN F   83  1                                   7    
HELIX   98  98 ARG F   93  ASP F  100  1                                   8    
HELIX   99  99 ASP F  100  ALA F  111  1                                  12    
HELIX  100 100 ASP F  121  ILE F  125  5                                   5    
HELIX  101 101 ASP F  147  LEU F  159  1                                  13    
HELIX  102 102 ARG F  163  LEU F  167  5                                   5    
HELIX  103 103 ALA F  209  ILE F  213  5                                   5    
HELIX  104 104 PRO F  214  ASP F  222  5                                   9    
HELIX  105 105 LEU F  241  MET F  260  1                                  20    
HELIX  106 106 VAL F  289  VAL F  296  5                                   8    
HELIX  107 107 TYR F  301  ARG F  305  5                                   5    
HELIX  108 108 SER F  311  ASN F  326  1                                  16    
HELIX  109 109 MET F  328  LYS F  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 GLN A 171  GLU A 174 -1  O  ILE A 172   N  TYR A 119           
SHEET    3   C 4 VAL A 129  LYS A 132 -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 7 PHE A 279  SER A 285  0                                        
SHEET    2   D 7 GLY A 265  PHE A 273 -1  N  CYS A 268   O  SER A 285           
SHEET    3   D 7 VAL A 179  SER A 188 -1  N  TYR A 185   O  PHE A 267           
SHEET    4   D 7 GLU A 193  ASN A 206 -1  O  SER A 198   N  HIS A 184           
SHEET    5   D 7 TYR A 227  PRO A 234 -1  O  GLY A 231   N  TYR A 203           
SHEET    6   D 7 TYR C 227  LEU C 237 -1  O  VAL C 236   N  ASN A 232           
SHEET    7   D 7 VAL B 236  LEU B 237 -1  N  VAL B 236   O  ASN C 232           
SHEET    1   E10 PHE A 279  SER A 285  0                                        
SHEET    2   E10 GLY A 265  PHE A 273 -1  N  CYS A 268   O  SER A 285           
SHEET    3   E10 VAL A 179  SER A 188 -1  N  TYR A 185   O  PHE A 267           
SHEET    4   E10 GLU A 193  ASN A 206 -1  O  SER A 198   N  HIS A 184           
SHEET    5   E10 TYR A 227  PRO A 234 -1  O  GLY A 231   N  TYR A 203           
SHEET    6   E10 TYR C 227  LEU C 237 -1  O  VAL C 236   N  ASN A 232           
SHEET    7   E10 GLU C 193  ASN C 206 -1  N  TYR C 203   O  ILE C 230           
SHEET    8   E10 VAL C 179  SER C 188 -1  N  HIS C 184   O  SER C 198           
SHEET    9   E10 GLY C 265  PHE C 273 -1  O  PHE C 267   N  TYR C 185           
SHEET   10   E10 PHE C 279  SER C 285 -1  O  SER C 285   N  CYS C 268           
SHEET    1   F 6 VAL A 236  LEU A 237  0                                        
SHEET    2   F 6 TYR B 227  PRO B 234 -1  O  ASN B 232   N  VAL A 236           
SHEET    3   F 6 GLU B 193  ASN B 206 -1  N  TYR B 203   O  ILE B 230           
SHEET    4   F 6 VAL B 179  SER B 188 -1  N  HIS B 184   O  SER B 198           
SHEET    5   F 6 GLY B 265  PHE B 273 -1  O  PHE B 267   N  TYR B 185           
SHEET    6   F 6 PHE B 279  SER B 285 -1  O  SER B 285   N  CYS B 268           
SHEET    1   G 4 TYR B  48  ILE B  50  0                                        
SHEET    2   G 4 THR B  27  PHE B  30  1  N  ALA B  29   O  TYR B  48           
SHEET    3   G 4 ARG B   4  TYR B   8  1  N  ILE B   5   O  ILE B  28           
SHEET    4   G 4 ALA B  64  VAL B  66  1  O  VAL B  65   N  ALA B   6           
SHEET    1   H 2 TYR B  88  PHE B  89  0                                        
SHEET    2   H 2 LEU B 333  THR B 334 -1  O  THR B 334   N  TYR B  88           
SHEET    1   I 4 VAL B 118  TYR B 119  0                                        
SHEET    2   I 4 GLN B 171  GLU B 174 -1  O  ILE B 172   N  TYR B 119           
SHEET    3   I 4 VAL B 129  LYS B 132 -1  N  LYS B 132   O  GLN B 171           
SHEET    4   I 4 PHE B 143  ALA B 145 -1  O  ALA B 145   N  VAL B 129           
SHEET    1   J 4 TYR C  48  ILE C  50  0                                        
SHEET    2   J 4 THR C  27  PHE C  30  1  N  ALA C  29   O  TYR C  48           
SHEET    3   J 4 ARG C   4  TYR C   8  1  N  ILE C   5   O  ILE C  28           
SHEET    4   J 4 ALA C  64  VAL C  66  1  O  VAL C  65   N  ALA C   6           
SHEET    1   K 2 TYR C  88  PHE C  89  0                                        
SHEET    2   K 2 LEU C 333  THR C 334 -1  O  THR C 334   N  TYR C  88           
SHEET    1   L 4 VAL C 118  TYR C 119  0                                        
SHEET    2   L 4 GLN C 171  GLU C 174 -1  O  ILE C 172   N  TYR C 119           
SHEET    3   L 4 VAL C 129  LYS C 132 -1  N  ILE C 130   O  GLN C 173           
SHEET    4   L 4 PHE C 143  ALA C 145 -1  O  ALA C 145   N  VAL C 129           
SHEET    1   M 4 TYR D  48  ILE D  50  0                                        
SHEET    2   M 4 THR D  27  PHE D  30  1  N  ALA D  29   O  TYR D  48           
SHEET    3   M 4 ARG D   4  TYR D   8  1  N  ILE D   5   O  ILE D  28           
SHEET    4   M 4 ALA D  64  VAL D  66  1  O  VAL D  65   N  ALA D   6           
SHEET    1   N 2 TYR D  88  PHE D  89  0                                        
SHEET    2   N 2 LEU D 333  THR D 334 -1  O  THR D 334   N  TYR D  88           
SHEET    1   O 3 PHE D 143  ALA D 145  0                                        
SHEET    2   O 3 VAL D 129  LYS D 132 -1  N  VAL D 129   O  ALA D 145           
SHEET    3   O 3 GLN D 171  GLU D 174 -1  O  GLN D 173   N  ILE D 130           
SHEET    1   P 7 PHE D 279  SER D 285  0                                        
SHEET    2   P 7 GLY D 265  PHE D 273 -1  N  GLU D 270   O  PHE D 282           
SHEET    3   P 7 VAL D 179  SER D 188 -1  N  TYR D 185   O  PHE D 267           
SHEET    4   P 7 GLU D 193  ASN D 206 -1  O  SER D 198   N  HIS D 184           
SHEET    5   P 7 TYR D 227  PRO D 234 -1  O  ILE D 230   N  TYR D 203           
SHEET    6   P 7 TYR F 227  LEU F 237 -1  O  VAL F 236   N  ASN D 232           
SHEET    7   P 7 VAL E 236  LEU E 237 -1  N  VAL E 236   O  ASN F 232           
SHEET    1   Q10 PHE D 279  SER D 285  0                                        
SHEET    2   Q10 GLY D 265  PHE D 273 -1  N  GLU D 270   O  PHE D 282           
SHEET    3   Q10 VAL D 179  SER D 188 -1  N  TYR D 185   O  PHE D 267           
SHEET    4   Q10 GLU D 193  ASN D 206 -1  O  SER D 198   N  HIS D 184           
SHEET    5   Q10 TYR D 227  PRO D 234 -1  O  ILE D 230   N  TYR D 203           
SHEET    6   Q10 TYR F 227  LEU F 237 -1  O  VAL F 236   N  ASN D 232           
SHEET    7   Q10 GLU F 193  ASN F 206 -1  N  TYR F 203   O  GLY F 231           
SHEET    8   Q10 VAL F 179  SER F 188 -1  N  HIS F 184   O  SER F 198           
SHEET    9   Q10 GLY F 265  PHE F 273 -1  O  PHE F 267   N  TYR F 185           
SHEET   10   Q10 PHE F 279  SER F 285 -1  O  PHE F 282   N  GLU F 270           
SHEET    1   R 6 VAL D 236  LEU D 237  0                                        
SHEET    2   R 6 TYR E 227  PRO E 234 -1  O  ASN E 232   N  VAL D 236           
SHEET    3   R 6 GLU E 193  ASN E 206 -1  N  TYR E 203   O  GLY E 231           
SHEET    4   R 6 VAL E 179  SER E 188 -1  N  HIS E 184   O  SER E 198           
SHEET    5   R 6 GLY E 265  PHE E 273 -1  O  PHE E 267   N  TYR E 185           
SHEET    6   R 6 PHE E 279  SER E 285 -1  O  PHE E 282   N  GLU E 270           
SHEET    1   S 4 TYR E  48  ILE E  50  0                                        
SHEET    2   S 4 THR E  27  PHE E  30  1  N  ALA E  29   O  TYR E  48           
SHEET    3   S 4 ARG E   4  TYR E   8  1  N  ILE E   5   O  ILE E  28           
SHEET    4   S 4 ALA E  64  VAL E  66  1  O  VAL E  65   N  ALA E   6           
SHEET    1   T 2 TYR E  88  PHE E  89  0                                        
SHEET    2   T 2 LEU E 333  THR E 334 -1  O  THR E 334   N  TYR E  88           
SHEET    1   U 4 VAL E 118  TYR E 119  0                                        
SHEET    2   U 4 GLN E 171  GLU E 174 -1  O  ILE E 172   N  TYR E 119           
SHEET    3   U 4 VAL E 129  LYS E 132 -1  N  ILE E 130   O  GLN E 173           
SHEET    4   U 4 PHE E 143  ALA E 145 -1  O  ALA E 145   N  VAL E 129           
SHEET    1   V 4 TYR F  48  ILE F  50  0                                        
SHEET    2   V 4 THR F  27  PHE F  30  1  N  ALA F  29   O  TYR F  48           
SHEET    3   V 4 ARG F   4  TYR F   8  1  N  ILE F   5   O  ILE F  28           
SHEET    4   V 4 ALA F  64  VAL F  66  1  O  VAL F  65   N  ALA F   6           
SHEET    1   W 2 TYR F  88  PHE F  89  0                                        
SHEET    2   W 2 LEU F 333  THR F 334 -1  O  THR F 334   N  TYR F  88           
SHEET    1   X 3 PHE F 143  ALA F 145  0                                        
SHEET    2   X 3 VAL F 129  LYS F 132 -1  N  VAL F 131   O  PHE F 143           
SHEET    3   X 3 GLN F 171  GLU F 174 -1  O  GLN F 171   N  LYS F 132           
CISPEP   1 SER A  205    ASN A  206          0         3.63                     
CISPEP   2 SER B  205    ASN B  206          0         7.71                     
CISPEP   3 SER C  205    ASN C  206          0         3.95                     
CISPEP   4 SER D  205    ASN D  206          0         8.65                     
CISPEP   5 SER E  205    ASN E  206          0         4.05                     
CISPEP   6 SER F  205    ASN F  206          0         3.60                     
SITE     1 AC1  5 SER A  10  SER A  71  ARG C 238  SER C 240                    
SITE     2 AC1  5 HOH C 505                                                     
SITE     1 AC2  7 HIS A  11  ARG A 202  ARG A 287  ALA A 290                    
SITE     2 AC2  7 HOH A 508  HOH A 601  HOH A 602                               
SITE     1 AC3  2 TYR A 306  ARG A 308                                          
SITE     1 AC4  6 ARG A 238  SER A 240  HOH A 510  SER B  10                    
SITE     2 AC4  6 HIS B  11  SER B  71                                          
SITE     1 AC5  6 HIS B  11  ARG B 202  ARG B 287  ALA B 290                    
SITE     2 AC5  6 HOH B 571  HOH B 574                                          
SITE     1 AC6  4 ARG B 191  ARG B 308  MET B 318  HOH B 589                    
SITE     1 AC7  5 ARG B 238  SER B 240  HOH B 540  SER C  10                    
SITE     2 AC7  5 SER C  71                                                     
SITE     1 AC8  5 HIS C  11  ARG C 202  ARG C 287  ALA C 290                    
SITE     2 AC8  5 HOH C 548                                                     
SITE     1 AC9  4 ARG C 105  LYS C 109  HOH C 558  HOH C 569                    
SITE     1 BC1  5 ARG C 191  TYR C 306  ARG C 308  MET C 318                    
SITE     2 BC1  5 HOH C 589                                                     
SITE     1 BC2  6 SER D  10  SER D  71  HIS D  75  ARG F 238                    
SITE     2 BC2  6 SER F 240  HOH F 504                                          
SITE     1 BC3  5 HIS D  11  ARG D 202  ARG D 287  ALA D 290                    
SITE     2 BC3  5 HOH D 546                                                     
SITE     1 BC4  2 TYR D 306  ARG D 308                                          
SITE     1 BC5  5 ARG D 238  SER D 240  HOH D 513  SER E  10                    
SITE     2 BC5  5 SER E  71                                                     
SITE     1 BC6  5 HIS E  11  ARG E 202  ARG E 287  ALA E 290                    
SITE     2 BC6  5 HOH E 536                                                     
SITE     1 BC7  2 ARG E 191  ARG E 308                                          
SITE     1 BC8  6 ARG E 238  SER E 240  HOH E 508  SER F  10                    
SITE     2 BC8  6 SER F  71  HIS F  75                                          
SITE     1 BC9  5 HIS F  11  ARG F 202  ARG F 287  ALA F 290                    
SITE     2 BC9  5 HOH F 502                                                     
SITE     1 CC1  2 ARG F 191  ARG F 308                                          
SITE     1 CC2 17 PRO A 116  ILE A 130  LYS A 132  GLY A 138                    
SITE     2 CC2 17 GLY A 139  TYR A 142  GLN A 173  GLU A 174                    
SITE     3 CC2 17 TYR A 175  ARG A 202  GLU A 204  GLU A 270                    
SITE     4 CC2 17 PHE A 282  GLU A 283  HOH A 514  HOH A 553                    
SITE     5 CC2 17 ARG B 212                                                     
SITE     1 CC3 18 PRO B 116  ILE B 130  LYS B 132  LYS B 137                    
SITE     2 CC3 18 GLY B 138  GLY B 139  TYR B 142  GLN B 173                    
SITE     3 CC3 18 GLU B 174  TYR B 175  GLU B 204  TYR B 227                    
SITE     4 CC3 18 GLU B 270  PHE B 282  GLU B 283  HOH B 564                    
SITE     5 CC3 18 HOH B 568  ARG C 212                                          
SITE     1 CC4 17 ARG A 212  ILE C 130  LYS C 132  LYS C 137                    
SITE     2 CC4 17 GLY C 138  GLY C 139  TYR C 142  GLN C 173                    
SITE     3 CC4 17 GLU C 174  TYR C 175  GLU C 204  GLU C 270                    
SITE     4 CC4 17 PHE C 282  GLU C 283  HOH C 522  HOH C 531                    
SITE     5 CC4 17 HOH C 541                                                     
SITE     1 CC5 15 PRO D 116  ILE D 130  LYS D 132  GLY D 138                    
SITE     2 CC5 15 GLY D 139  TYR D 142  GLN D 173  GLU D 174                    
SITE     3 CC5 15 TYR D 175  ARG D 202  GLU D 204  GLU D 270                    
SITE     4 CC5 15 PHE D 282  GLU D 283  ARG E 212                               
SITE     1 CC6 16 ILE E 130  LYS E 132  ALA E 136  GLY E 138                    
SITE     2 CC6 16 GLY E 139  TYR E 142  GLN E 173  GLU E 174                    
SITE     3 CC6 16 TYR E 175  ARG E 202  GLU E 204  TYR E 227                    
SITE     4 CC6 16 PHE E 282  GLU E 283  HOH E 516  ARG F 212                    
SITE     1 CC7 17 ARG D 212  ARG F 101  ILE F 130  LYS F 132                    
SITE     2 CC7 17 LYS F 137  GLY F 138  GLY F 139  TYR F 142                    
SITE     3 CC7 17 GLN F 173  GLU F 174  TYR F 175  TYR F 182                    
SITE     4 CC7 17 ARG F 202  GLU F 204  GLU F 270  PHE F 282                    
SITE     5 CC7 17 GLU F 283                                                     
CRYST1   76.095  127.222  121.673  90.00 102.85  90.00 P 1 21 1     12          
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      0.013141  0.000000  0.002998        0.00000                         
SCALE2      0.000000  0.007860  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008430        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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