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Entry: 3VPB
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HEADER    LIGASE                                  29-FEB-12   3VPB              
TITLE     ARGX FROM SULFOLOBUS TOKODAII COMPLEXED WITH                          
TITLE    2 LYSW/GLU/ADP/MG/ZN/SULFATE                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE ACETYLORNITHINE DEACETYLASE;                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 3.5.1.16;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: ALPHA-AMINOADIPATE CARRIER PROTEIN LYSW;                   
COMPND   8 CHAIN: E, F;                                                         
COMPND   9 SYNONYM: AAA CARRIER PROTEIN LYSW;                                   
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SULFOLOBUS TOKODAII;                            
SOURCE   3 ORGANISM_TAXID: 273063;                                              
SOURCE   4 STRAIN: DSM 16993, JCM 10545, NBRC 100140, 7;                        
SOURCE   5 GENE: ARGE, STK_15050;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21CODONPLUS(DE3);                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-26B(+), PET-STARGX;                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: SULFOLOBUS TOKODAII;                            
SOURCE  13 ORGANISM_TAXID: 273063;                                              
SOURCE  14 STRAIN: DSM 16993, JCM 10545, NBRC 100140, 7;                        
SOURCE  15 GENE: LYSW, STK_01925, STS023;                                       
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21CODONPLUS(DE3);                        
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET-26B(+), PET-STLYSW                    
KEYWDS    ATP-DEPENDENT AMINE/THIOL LIGASE FAMILY, ATP-DEPENDENT AMINE/THIOL    
KEYWDS   2 LIGASE, LYSW, ENZYME-CARRIER PROTEIN COMPLEX, LIGASE                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.TOMITA,T.OUCHI,T.KUZUYAMA,M.NISHIYAMA                               
REVDAT   2   31-JUL-13 3VPB    1       JRNL                                     
REVDAT   1   27-FEB-13 3VPB    0                                                
JRNL        AUTH   T.OUCHI,T.TOMITA,A.HORIE,A.YOSHIDA,K.TAKAHASHI,H.NISHIDA,    
JRNL        AUTH 2 K.LASSAK,H.TAKA,R.MINEKI,T.FUJIMURA,S.KOSONO,C.NISHIYAMA,    
JRNL        AUTH 3 R.MASUI,S.KURAMITSU,S.V.ALBERS,T.KUZUYAMA,M.NISHIYAMA        
JRNL        TITL   LYSINE AND ARGININE BIOSYNTHESES MEDIATED BY A COMMON        
JRNL        TITL 2 CARRIER PROTEIN IN SULFOLOBUS                                
JRNL        REF    NAT.CHEM.BIOL.                V.   9   277 2013              
JRNL        REFN                   ISSN 1552-4450                               
JRNL        PMID   23434852                                                     
JRNL        DOI    10.1038/NCHEMBIO.1200                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0088                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.91                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 106366                         
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) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5608                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.84                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7735                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.08                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2750                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 415                          
REMARK   3   BIN FREE R VALUE                    : 0.3060                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9709                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 186                                     
REMARK   3   SOLVENT ATOMS            : 1040                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.17                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : 0.03000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
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): 0.144         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.139         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.094         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.958         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.933                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10158 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13830 ; 1.454 ; 1.992       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1260 ; 5.675 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   454 ;38.641 ;24.758       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1787 ;15.665 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    62 ;17.695 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1581 ; 0.100 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7566 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  6224 ; 0.792 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10116 ; 1.499 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3934 ; 2.433 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3699 ; 4.059 ; 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 : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3VPB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-MAR-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB095331.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-OCT-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NW12A                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : MIRROR                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 106366                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: PHASER                                                
REMARK 200 STARTING MODEL: 1UC8                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 13% PEG-MME 5000, 0.1M AMMONIUM          
REMARK 280  SULFATE, 0.1M MES-NAOH (PH6.0), VAPOR DIFFUSION, HANGING DROP,      
REMARK 280  TEMPERATURE 293K                                                    
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       56.99400            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 22440 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -332.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, F, E                      
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 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     LYS A   282                                                      
REMARK 465     LYS C   282                                                      
REMARK 465     LYS D   282                                                      
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   OE1  GLU D   220     O    HOH D   740              2.13            
REMARK 500   OH   TYR C    58     O    HOH C   746              2.14            
REMARK 500   OE1  GLN B    12     NZ   LYS B    15              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 251   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A   8      -59.23   -125.30                                   
REMARK 500    GLN A 171      118.47   -166.76                                   
REMARK 500    PHE A 257       19.05   -152.13                                   
REMARK 500    ASP B   8      -56.52   -124.47                                   
REMARK 500    GLN B 171      118.77   -168.74                                   
REMARK 500    PHE B 257       17.71   -150.97                                   
REMARK 500    ASP C   8      -60.10   -124.38                                   
REMARK 500    TYR C 172      -60.31   -145.23                                   
REMARK 500    PHE C 257       15.14   -150.07                                   
REMARK 500    ASP D   8      -58.50   -124.71                                   
REMARK 500    TYR D 172      -57.32   -143.36                                   
REMARK 500    PHE D 257       18.67   -143.91                                   
REMARK 500    HIS E  39     -113.28     64.68                                   
REMARK 500    HIS F  39     -104.73     56.30                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 820        DISTANCE =  5.71 ANGSTROMS                       
REMARK 525    HOH A 823        DISTANCE =  6.77 ANGSTROMS                       
REMARK 525    HOH A 828        DISTANCE =  5.44 ANGSTROMS                       
REMARK 525    HOH A 829        DISTANCE =  6.32 ANGSTROMS                       
REMARK 525    HOH B 818        DISTANCE =  7.48 ANGSTROMS                       
REMARK 525    HOH B 824        DISTANCE =  7.70 ANGSTROMS                       
REMARK 525    HOH C 801        DISTANCE =  7.14 ANGSTROMS                       
REMARK 525    HOH C 806        DISTANCE =  6.94 ANGSTROMS                       
REMARK 525    HOH C 812        DISTANCE =  7.06 ANGSTROMS                       
REMARK 525    HOH C 822        DISTANCE =  6.71 ANGSTROMS                       
REMARK 525    HOH C 828        DISTANCE =  7.49 ANGSTROMS                       
REMARK 525    HOH C 829        DISTANCE =  5.24 ANGSTROMS                       
REMARK 525    HOH C 830        DISTANCE =  5.68 ANGSTROMS                       
REMARK 525    HOH C 831        DISTANCE =  7.23 ANGSTROMS                       
REMARK 525    HOH C 832        DISTANCE =  5.51 ANGSTROMS                       
REMARK 525    HOH D 693        DISTANCE =  6.47 ANGSTROMS                       
REMARK 525    HOH D 802        DISTANCE =  6.92 ANGSTROMS                       
REMARK 525    HOH D 816        DISTANCE =  6.18 ANGSTROMS                       
REMARK 525    HOH D 824        DISTANCE =  6.87 ANGSTROMS                       
REMARK 525    HOH D 826        DISTANCE =  5.16 ANGSTROMS                       
REMARK 525    HOH D 833        DISTANCE =  7.99 ANGSTROMS                       
REMARK 525    HOH D 834        DISTANCE =  5.62 ANGSTROMS                       
REMARK 525    HOH E 235        DISTANCE =  6.63 ANGSTROMS                       
REMARK 525    HOH E 238        DISTANCE =  6.08 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 502  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A 500   O2A                                                    
REMARK 620 2 GLU A 250   OE2  96.0                                              
REMARK 620 3 ASP A 237   OD1  97.4  90.3                                        
REMARK 620 4 SO4 A 504   O4  166.1  88.0  95.8                                  
REMARK 620 5 ADP A 500   O2B  84.5  95.7 173.4  81.8                            
REMARK 620 6 HOH A 642   O    94.3 168.4  83.0  83.2  90.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A 500   O1B                                                    
REMARK 620 2 SO4 A 504   O2  102.2                                              
REMARK 620 3 GLU A 250   OE2  88.4  98.4                                        
REMARK 620 4 GLU A 250   OE1  90.4 154.5  59.5                                  
REMARK 620 5 ASN A 252   OD1 168.8  87.7  95.4  82.5                            
REMARK 620 6 HOH A 696   O    93.9 105.9 154.5  95.1  78.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP B 500   O1B                                                    
REMARK 620 2 SO4 B 504   O1   98.4                                              
REMARK 620 3 GLU B 250   OE1  88.1 100.4                                        
REMARK 620 4 ASN B 252   OD1 168.3  93.3  91.0                                  
REMARK 620 5 GLU B 250   OE2  90.8 156.9  58.6  78.8                            
REMARK 620 6 HOH B 651   O    95.1 102.9 155.8  81.0  97.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 502  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP B 500   O2A                                                    
REMARK 620 2 ASP B 237   OD2  92.3                                              
REMARK 620 3 GLU B 250   OE1  96.3  92.5                                        
REMARK 620 4 SO4 B 504   O3  166.8  98.1  91.4                                  
REMARK 620 5 ADP B 500   O2B  84.6 169.2  98.1  83.7                            
REMARK 620 6 HOH B 650   O    91.3  80.5 169.9  82.4  89.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 100  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  27   ND1                                                    
REMARK 620 2 CYS E   6   SG  109.3                                              
REMARK 620 3 CYS E   9   SG   98.1 109.2                                        
REMARK 620 4 CYS E  29   SG  111.4 114.5 113.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 502  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 250   OE1                                                    
REMARK 620 2 SO4 C 503   O1   93.5                                              
REMARK 620 3 ASP C 237   OD2  86.0  94.1                                        
REMARK 620 4 ADP C 500   O2A  94.6 167.5  96.0                                  
REMARK 620 5 ADP C 500   O2B 100.7  87.7 172.9  81.5                            
REMARK 620 6 HOH C 709   O   167.0  81.1  82.7  92.9  90.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 100  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  27   ND1                                                    
REMARK 620 2 CYS F   9   SG   97.9                                              
REMARK 620 3 CYS F   6   SG  110.0 110.8                                        
REMARK 620 4 CYS F  29   SG  113.2 111.2 112.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 502  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SO4 D 503   O2                                                     
REMARK 620 2 ADP D 500   O2A 167.9                                              
REMARK 620 3 ADP D 500   O2B  87.1  81.9                                        
REMARK 620 4 GLU D 250   OE2  91.6  95.1 100.2                                  
REMARK 620 5 ASP D 237   OD1  95.6  95.5 177.3  80.3                            
REMARK 620 6 HOH D 690   O    84.7  91.9  97.4 161.9  82.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLU A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLU B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLU C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP D 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLU D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 100                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 100                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3VPC   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3VPD   RELATED DB: PDB                                   
DBREF  3VPB A    1   282  UNP    Q970U6   Q970U6_SULTO     1    282             
DBREF  3VPB B    1   282  UNP    Q970U6   Q970U6_SULTO     1    282             
DBREF  3VPB C    1   282  UNP    Q970U6   Q970U6_SULTO     1    282             
DBREF  3VPB D    1   282  UNP    Q970U6   Q970U6_SULTO     1    282             
DBREF  3VPB E    1    56  UNP    Q976J8   LYSW_SULTO       1     56             
DBREF  3VPB F    1    56  UNP    Q976J8   LYSW_SULTO       1     56             
SEQRES   1 A  282  MET ARG VAL VAL LEU ILE VAL ASP ILE VAL ARG GLN GLU          
SEQRES   2 A  282  GLU LYS LEU ILE ALA LYS ALA LEU GLU GLU ASN LYS VAL          
SEQRES   3 A  282  GLN TYR ASP ILE ILE ASN VAL ALA GLN GLU PRO LEU PRO          
SEQRES   4 A  282  PHE ASN LYS ALA LEU GLY ARG TYR ASP VAL ALA ILE ILE          
SEQRES   5 A  282  ARG PRO VAL SER MET TYR ARG ALA LEU TYR SER SER ALA          
SEQRES   6 A  282  VAL LEU GLU ALA ALA GLY VAL HIS THR ILE ASN SER SER          
SEQRES   7 A  282  ASP VAL ILE ASN VAL CYS GLY ASP LYS ILE LEU THR TYR          
SEQRES   8 A  282  SER LYS LEU TYR ARG GLU GLY ILE PRO ILE PRO ASP SER          
SEQRES   9 A  282  ILE ILE ALA LEU SER ALA GLU ALA ALA LEU LYS ALA TYR          
SEQRES  10 A  282  GLU GLN ARG GLY PHE PRO LEU ILE ASP LYS PRO PRO ILE          
SEQRES  11 A  282  GLY SER TRP GLY ARG LEU VAL SER LEU ILE ARG ASP VAL          
SEQRES  12 A  282  PHE GLU GLY LYS THR ILE ILE GLU HIS ARG GLU LEU MET          
SEQRES  13 A  282  GLY ASN SER ALA LEU LYS ALA HIS ILE VAL GLN GLU TYR          
SEQRES  14 A  282  ILE GLN TYR LYS GLY ARG ASP ILE ARG CYS ILE ALA ILE          
SEQRES  15 A  282  GLY GLU GLU LEU LEU GLY CYS TYR ALA ARG ASN ILE PRO          
SEQRES  16 A  282  PRO ASN GLU TRP ARG ALA ASN VAL ALA LEU GLY GLY THR          
SEQRES  17 A  282  PRO SER ASN ILE GLU VAL ASP GLU LYS LEU LYS GLU THR          
SEQRES  18 A  282  VAL VAL LYS ALA VAL SER ILE VAL HIS GLY GLU PHE VAL          
SEQRES  19 A  282  SER ILE ASP ILE LEU GLU HIS PRO ASN LYS GLY TYR VAL          
SEQRES  20 A  282  VAL ASN GLU LEU ASN ASP VAL PRO GLU PHE LYS GLY PHE          
SEQRES  21 A  282  MET VAL ALA THR ASN ILE ASN VAL ALA GLN LYS LEU VAL          
SEQRES  22 A  282  GLU TYR ILE LYS GLU ASN TYR SER LYS                          
SEQRES   1 B  282  MET ARG VAL VAL LEU ILE VAL ASP ILE VAL ARG GLN GLU          
SEQRES   2 B  282  GLU LYS LEU ILE ALA LYS ALA LEU GLU GLU ASN LYS VAL          
SEQRES   3 B  282  GLN TYR ASP ILE ILE ASN VAL ALA GLN GLU PRO LEU PRO          
SEQRES   4 B  282  PHE ASN LYS ALA LEU GLY ARG TYR ASP VAL ALA ILE ILE          
SEQRES   5 B  282  ARG PRO VAL SER MET TYR ARG ALA LEU TYR SER SER ALA          
SEQRES   6 B  282  VAL LEU GLU ALA ALA GLY VAL HIS THR ILE ASN SER SER          
SEQRES   7 B  282  ASP VAL ILE ASN VAL CYS GLY ASP LYS ILE LEU THR TYR          
SEQRES   8 B  282  SER LYS LEU TYR ARG GLU GLY ILE PRO ILE PRO ASP SER          
SEQRES   9 B  282  ILE ILE ALA LEU SER ALA GLU ALA ALA LEU LYS ALA TYR          
SEQRES  10 B  282  GLU GLN ARG GLY PHE PRO LEU ILE ASP LYS PRO PRO ILE          
SEQRES  11 B  282  GLY SER TRP GLY ARG LEU VAL SER LEU ILE ARG ASP VAL          
SEQRES  12 B  282  PHE GLU GLY LYS THR ILE ILE GLU HIS ARG GLU LEU MET          
SEQRES  13 B  282  GLY ASN SER ALA LEU LYS ALA HIS ILE VAL GLN GLU TYR          
SEQRES  14 B  282  ILE GLN TYR LYS GLY ARG ASP ILE ARG CYS ILE ALA ILE          
SEQRES  15 B  282  GLY GLU GLU LEU LEU GLY CYS TYR ALA ARG ASN ILE PRO          
SEQRES  16 B  282  PRO ASN GLU TRP ARG ALA ASN VAL ALA LEU GLY GLY THR          
SEQRES  17 B  282  PRO SER ASN ILE GLU VAL ASP GLU LYS LEU LYS GLU THR          
SEQRES  18 B  282  VAL VAL LYS ALA VAL SER ILE VAL HIS GLY GLU PHE VAL          
SEQRES  19 B  282  SER ILE ASP ILE LEU GLU HIS PRO ASN LYS GLY TYR VAL          
SEQRES  20 B  282  VAL ASN GLU LEU ASN ASP VAL PRO GLU PHE LYS GLY PHE          
SEQRES  21 B  282  MET VAL ALA THR ASN ILE ASN VAL ALA GLN LYS LEU VAL          
SEQRES  22 B  282  GLU TYR ILE LYS GLU ASN TYR SER LYS                          
SEQRES   1 C  282  MET ARG VAL VAL LEU ILE VAL ASP ILE VAL ARG GLN GLU          
SEQRES   2 C  282  GLU LYS LEU ILE ALA LYS ALA LEU GLU GLU ASN LYS VAL          
SEQRES   3 C  282  GLN TYR ASP ILE ILE ASN VAL ALA GLN GLU PRO LEU PRO          
SEQRES   4 C  282  PHE ASN LYS ALA LEU GLY ARG TYR ASP VAL ALA ILE ILE          
SEQRES   5 C  282  ARG PRO VAL SER MET TYR ARG ALA LEU TYR SER SER ALA          
SEQRES   6 C  282  VAL LEU GLU ALA ALA GLY VAL HIS THR ILE ASN SER SER          
SEQRES   7 C  282  ASP VAL ILE ASN VAL CYS GLY ASP LYS ILE LEU THR TYR          
SEQRES   8 C  282  SER LYS LEU TYR ARG GLU GLY ILE PRO ILE PRO ASP SER          
SEQRES   9 C  282  ILE ILE ALA LEU SER ALA GLU ALA ALA LEU LYS ALA TYR          
SEQRES  10 C  282  GLU GLN ARG GLY PHE PRO LEU ILE ASP LYS PRO PRO ILE          
SEQRES  11 C  282  GLY SER TRP GLY ARG LEU VAL SER LEU ILE ARG ASP VAL          
SEQRES  12 C  282  PHE GLU GLY LYS THR ILE ILE GLU HIS ARG GLU LEU MET          
SEQRES  13 C  282  GLY ASN SER ALA LEU LYS ALA HIS ILE VAL GLN GLU TYR          
SEQRES  14 C  282  ILE GLN TYR LYS GLY ARG ASP ILE ARG CYS ILE ALA ILE          
SEQRES  15 C  282  GLY GLU GLU LEU LEU GLY CYS TYR ALA ARG ASN ILE PRO          
SEQRES  16 C  282  PRO ASN GLU TRP ARG ALA ASN VAL ALA LEU GLY GLY THR          
SEQRES  17 C  282  PRO SER ASN ILE GLU VAL ASP GLU LYS LEU LYS GLU THR          
SEQRES  18 C  282  VAL VAL LYS ALA VAL SER ILE VAL HIS GLY GLU PHE VAL          
SEQRES  19 C  282  SER ILE ASP ILE LEU GLU HIS PRO ASN LYS GLY TYR VAL          
SEQRES  20 C  282  VAL ASN GLU LEU ASN ASP VAL PRO GLU PHE LYS GLY PHE          
SEQRES  21 C  282  MET VAL ALA THR ASN ILE ASN VAL ALA GLN LYS LEU VAL          
SEQRES  22 C  282  GLU TYR ILE LYS GLU ASN TYR SER LYS                          
SEQRES   1 D  282  MET ARG VAL VAL LEU ILE VAL ASP ILE VAL ARG GLN GLU          
SEQRES   2 D  282  GLU LYS LEU ILE ALA LYS ALA LEU GLU GLU ASN LYS VAL          
SEQRES   3 D  282  GLN TYR ASP ILE ILE ASN VAL ALA GLN GLU PRO LEU PRO          
SEQRES   4 D  282  PHE ASN LYS ALA LEU GLY ARG TYR ASP VAL ALA ILE ILE          
SEQRES   5 D  282  ARG PRO VAL SER MET TYR ARG ALA LEU TYR SER SER ALA          
SEQRES   6 D  282  VAL LEU GLU ALA ALA GLY VAL HIS THR ILE ASN SER SER          
SEQRES   7 D  282  ASP VAL ILE ASN VAL CYS GLY ASP LYS ILE LEU THR TYR          
SEQRES   8 D  282  SER LYS LEU TYR ARG GLU GLY ILE PRO ILE PRO ASP SER          
SEQRES   9 D  282  ILE ILE ALA LEU SER ALA GLU ALA ALA LEU LYS ALA TYR          
SEQRES  10 D  282  GLU GLN ARG GLY PHE PRO LEU ILE ASP LYS PRO PRO ILE          
SEQRES  11 D  282  GLY SER TRP GLY ARG LEU VAL SER LEU ILE ARG ASP VAL          
SEQRES  12 D  282  PHE GLU GLY LYS THR ILE ILE GLU HIS ARG GLU LEU MET          
SEQRES  13 D  282  GLY ASN SER ALA LEU LYS ALA HIS ILE VAL GLN GLU TYR          
SEQRES  14 D  282  ILE GLN TYR LYS GLY ARG ASP ILE ARG CYS ILE ALA ILE          
SEQRES  15 D  282  GLY GLU GLU LEU LEU GLY CYS TYR ALA ARG ASN ILE PRO          
SEQRES  16 D  282  PRO ASN GLU TRP ARG ALA ASN VAL ALA LEU GLY GLY THR          
SEQRES  17 D  282  PRO SER ASN ILE GLU VAL ASP GLU LYS LEU LYS GLU THR          
SEQRES  18 D  282  VAL VAL LYS ALA VAL SER ILE VAL HIS GLY GLU PHE VAL          
SEQRES  19 D  282  SER ILE ASP ILE LEU GLU HIS PRO ASN LYS GLY TYR VAL          
SEQRES  20 D  282  VAL ASN GLU LEU ASN ASP VAL PRO GLU PHE LYS GLY PHE          
SEQRES  21 D  282  MET VAL ALA THR ASN ILE ASN VAL ALA GLN LYS LEU VAL          
SEQRES  22 D  282  GLU TYR ILE LYS GLU ASN TYR SER LYS                          
SEQRES   1 E   56  MET VAL VAL LEU LYS CYS PRO VAL CYS ASN GLY ASP VAL          
SEQRES   2 E   56  ASN VAL PRO ASP ASP ALA LEU PRO GLY GLU ILE VAL GLU          
SEQRES   3 E   56  HIS GLU CYS GLY ALA GLN LEU GLU VAL TYR ASN ASP HIS          
SEQRES   4 E   56  GLY ARG LEU ALA LEU ARG LEU ALA GLU GLN VAL GLY GLU          
SEQRES   5 E   56  ASP TRP GLY GLU                                              
SEQRES   1 F   56  MET VAL VAL LEU LYS CYS PRO VAL CYS ASN GLY ASP VAL          
SEQRES   2 F   56  ASN VAL PRO ASP ASP ALA LEU PRO GLY GLU ILE VAL GLU          
SEQRES   3 F   56  HIS GLU CYS GLY ALA GLN LEU GLU VAL TYR ASN ASP HIS          
SEQRES   4 F   56  GLY ARG LEU ALA LEU ARG LEU ALA GLU GLN VAL GLY GLU          
SEQRES   5 F   56  ASP TRP GLY GLU                                              
HET    ADP  A 500      27                                                       
HET    GLU  A 501      10                                                       
HET     MG  A 502       1                                                       
HET     ZN  A 503       1                                                       
HET    SO4  A 504       5                                                       
HET    ADP  B 500      27                                                       
HET    GLU  B 501      10                                                       
HET     MG  B 502       1                                                       
HET     ZN  B 503       1                                                       
HET    SO4  B 504       5                                                       
HET    ADP  C 500      27                                                       
HET    GLU  C 501      10                                                       
HET     MG  C 502       1                                                       
HET    SO4  C 503       5                                                       
HET    SO4  C 504       5                                                       
HET    ADP  D 500      27                                                       
HET    GLU  D 501      10                                                       
HET     MG  D 502       1                                                       
HET    SO4  D 503       5                                                       
HET    SO4  D 504       5                                                       
HET     ZN  E 100       1                                                       
HET     ZN  F 100       1                                                       
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     GLU GLUTAMIC ACID                                                    
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
FORMUL   7  ADP    4(C10 H15 N5 O10 P2)                                         
FORMUL   8  GLU    4(C5 H9 N O4)                                                
FORMUL   9   MG    4(MG 2+)                                                     
FORMUL  10   ZN    4(ZN 2+)                                                     
FORMUL  11  SO4    6(O4 S 2-)                                                   
FORMUL  29  HOH   *1040(H2 O)                                                   
HELIX    1   1 ARG A   11  ASN A   24  1                                  14    
HELIX    2   2 ASN A   41  TYR A   47  5                                   7    
HELIX    3   3 SER A   56  ALA A   70  1                                  15    
HELIX    4   4 SER A   77  GLY A   85  1                                   9    
HELIX    5   5 ASP A   86  GLU A   97  1                                  12    
HELIX    6   6 SER A  109  GLY A  121  1                                  13    
HELIX    7   7 ASP A  142  GLU A  154  1                                  13    
HELIX    8   8 ASN A  158  ALA A  163  5                                   6    
HELIX    9   9 ASN A  202  GLY A  206  5                                   5    
HELIX   10  10 ASP A  215  HIS A  230  1                                  16    
HELIX   11  11 PHE A  257  ASN A  265  1                                   9    
HELIX   12  12 ASN A  267  SER A  281  1                                  15    
HELIX   13  13 ARG B   11  ASN B   24  1                                  14    
HELIX   14  14 ASN B   41  TYR B   47  5                                   7    
HELIX   15  15 SER B   56  ALA B   70  1                                  15    
HELIX   16  16 SER B   77  GLY B   85  1                                   9    
HELIX   17  17 ASP B   86  GLU B   97  1                                  12    
HELIX   18  18 SER B  109  GLY B  121  1                                  13    
HELIX   19  19 ASP B  142  GLU B  154  1                                  13    
HELIX   20  20 ASN B  158  ALA B  163  5                                   6    
HELIX   21  21 ASN B  202  GLY B  206  5                                   5    
HELIX   22  22 ASP B  215  HIS B  230  1                                  16    
HELIX   23  23 PHE B  257  ASN B  265  1                                   9    
HELIX   24  24 ASN B  267  SER B  281  1                                  15    
HELIX   25  25 ARG C   11  ASN C   24  1                                  14    
HELIX   26  26 LYS C   42  TYR C   47  5                                   6    
HELIX   27  27 SER C   56  ALA C   70  1                                  15    
HELIX   28  28 SER C   77  GLY C   85  1                                   9    
HELIX   29  29 ASP C   86  GLY C   98  1                                  13    
HELIX   30  30 SER C  109  GLY C  121  1                                  13    
HELIX   31  31 ASP C  142  LEU C  155  1                                  14    
HELIX   32  32 ASN C  158  ALA C  163  5                                   6    
HELIX   33  33 ASN C  202  GLY C  206  5                                   5    
HELIX   34  34 ASP C  215  HIS C  230  1                                  16    
HELIX   35  35 PHE C  257  ASN C  265  1                                   9    
HELIX   36  36 ASN C  267  SER C  281  1                                  15    
HELIX   37  37 ARG D   11  ASN D   24  1                                  14    
HELIX   38  38 LYS D   42  TYR D   47  5                                   6    
HELIX   39  39 SER D   56  ALA D   70  1                                  15    
HELIX   40  40 SER D   77  GLY D   85  1                                   9    
HELIX   41  41 ASP D   86  GLY D   98  1                                  13    
HELIX   42  42 SER D  109  GLY D  121  1                                  13    
HELIX   43  43 ASP D  142  LEU D  155  1                                  14    
HELIX   44  44 ASN D  158  ALA D  163  5                                   6    
HELIX   45  45 ASN D  202  GLY D  206  5                                   5    
HELIX   46  46 ASP D  215  HIS D  230  1                                  16    
HELIX   47  47 PHE D  257  ASN D  265  1                                   9    
HELIX   48  48 ASN D  267  SER D  281  1                                  15    
SHEET    1   A 4 GLN A  27  ASN A  32  0                                        
SHEET    2   A 4 ARG A   2  VAL A   7  1  N  LEU A   5   O  ASP A  29           
SHEET    3   A 4 VAL A  49  ILE A  52  1  O  ILE A  51   N  ILE A   6           
SHEET    4   A 4 HIS A  73  ILE A  75  1  O  ILE A  75   N  ILE A  52           
SHEET    1   B 5 LEU A  38  PRO A  39  0                                        
SHEET    2   B 5 SER B 104  ALA B 107 -1  O  ILE B 106   N  LEU A  38           
SHEET    3   B 5 HIS B 164  GLU B 168 -1  O  HIS B 164   N  ALA B 107           
SHEET    4   B 5 LEU B 124  LYS B 127 -1  N  ILE B 125   O  GLN B 167           
SHEET    5   B 5 SER B 138  ILE B 140 -1  O  ILE B 140   N  LEU B 124           
SHEET    1   C 5 SER A 138  ILE A 140  0                                        
SHEET    2   C 5 LEU A 124  LYS A 127 -1  N  LEU A 124   O  ILE A 140           
SHEET    3   C 5 HIS A 164  GLU A 168 -1  O  GLN A 167   N  ILE A 125           
SHEET    4   C 5 SER A 104  ALA A 107 -1  N  ALA A 107   O  HIS A 164           
SHEET    5   C 5 LEU B  38  PRO B  39 -1  O  LEU B  38   N  ILE A 106           
SHEET    1   D 5 THR A 208  SER A 210  0                                        
SHEET    2   D 5 GLU A 185  ASN A 193 -1  N  ALA A 191   O  SER A 210           
SHEET    3   D 5 ARG A 175  ILE A 182 -1  N  ARG A 178   O  TYR A 190           
SHEET    4   D 5 PHE A 233  HIS A 241 -1  O  ILE A 238   N  ILE A 177           
SHEET    5   D 5 GLY A 245  ASN A 252 -1  O  GLY A 245   N  HIS A 241           
SHEET    1   E 4 GLN B  27  ASN B  32  0                                        
SHEET    2   E 4 ARG B   2  VAL B   7  1  N  LEU B   5   O  ASP B  29           
SHEET    3   E 4 VAL B  49  ILE B  52  1  O  ILE B  51   N  VAL B   4           
SHEET    4   E 4 HIS B  73  ILE B  75  1  O  ILE B  75   N  ILE B  52           
SHEET    1   F 5 THR B 208  ASN B 211  0                                        
SHEET    2   F 5 GLU B 185  ASN B 193 -1  N  ALA B 191   O  SER B 210           
SHEET    3   F 5 ARG B 175  ILE B 182 -1  N  ILE B 180   O  LEU B 187           
SHEET    4   F 5 PHE B 233  HIS B 241 -1  O  ILE B 238   N  ILE B 177           
SHEET    5   F 5 GLY B 245  ASN B 252 -1  O  GLY B 245   N  HIS B 241           
SHEET    1   G 4 GLN C  27  ASN C  32  0                                        
SHEET    2   G 4 ARG C   2  VAL C   7  1  N  LEU C   5   O  ASP C  29           
SHEET    3   G 4 VAL C  49  ILE C  52  1  O  ILE C  51   N  ILE C   6           
SHEET    4   G 4 HIS C  73  ILE C  75  1  O  ILE C  75   N  ALA C  50           
SHEET    1   H 5 LEU C  38  PRO C  39  0                                        
SHEET    2   H 5 SER D 104  ALA D 107 -1  O  ILE D 106   N  LEU C  38           
SHEET    3   H 5 HIS D 164  GLU D 168 -1  O  HIS D 164   N  ALA D 107           
SHEET    4   H 5 LEU D 124  LYS D 127 -1  N  ILE D 125   O  GLN D 167           
SHEET    5   H 5 SER D 138  ILE D 140 -1  O  SER D 138   N  ASP D 126           
SHEET    1   I 5 SER C 138  ILE C 140  0                                        
SHEET    2   I 5 LEU C 124  LYS C 127 -1  N  LEU C 124   O  ILE C 140           
SHEET    3   I 5 HIS C 164  GLN C 167 -1  O  GLN C 167   N  ILE C 125           
SHEET    4   I 5 SER C 104  ALA C 107 -1  N  ALA C 107   O  HIS C 164           
SHEET    5   I 5 LEU D  38  PRO D  39 -1  O  LEU D  38   N  ILE C 106           
SHEET    1   J 5 THR C 208  SER C 210  0                                        
SHEET    2   J 5 GLU C 185  ASN C 193 -1  N  ALA C 191   O  SER C 210           
SHEET    3   J 5 ARG C 175  ILE C 182 -1  N  ILE C 180   O  LEU C 187           
SHEET    4   J 5 PHE C 233  HIS C 241 -1  O  ILE C 238   N  ILE C 177           
SHEET    5   J 5 GLY C 245  ASN C 252 -1  O  GLU C 250   N  ASP C 237           
SHEET    1   K 4 GLN D  27  ASN D  32  0                                        
SHEET    2   K 4 ARG D   2  VAL D   7  1  N  LEU D   5   O  ASP D  29           
SHEET    3   K 4 VAL D  49  ILE D  52  1  O  ILE D  51   N  ILE D   6           
SHEET    4   K 4 HIS D  73  ILE D  75  1  O  ILE D  75   N  ALA D  50           
SHEET    1   L 5 THR D 208  SER D 210  0                                        
SHEET    2   L 5 GLU D 185  ASN D 193 -1  N  ASN D 193   O  THR D 208           
SHEET    3   L 5 ARG D 175  ILE D 182 -1  N  ILE D 180   O  LEU D 187           
SHEET    4   L 5 PHE D 233  HIS D 241 -1  O  ILE D 238   N  ILE D 177           
SHEET    5   L 5 GLY D 245  ASN D 252 -1  O  VAL D 247   N  LEU D 239           
SHEET    1   M 2 VAL E   2  LYS E   5  0                                        
SHEET    2   M 2 ASP E  12  VAL E  15 -1  O  VAL E  13   N  LEU E   4           
SHEET    1   N 3 ILE E  24  GLU E  26  0                                        
SHEET    2   N 3 GLN E  32  ASP E  38 -1  O  LEU E  33   N  VAL E  25           
SHEET    3   N 3 ARG E  41  LEU E  46 -1  O  ARG E  41   N  ASP E  38           
SHEET    1   O 2 VAL F   2  LYS F   5  0                                        
SHEET    2   O 2 ASP F  12  VAL F  15 -1  O  VAL F  13   N  LEU F   4           
SHEET    1   P 3 ILE F  24  GLU F  26  0                                        
SHEET    2   P 3 GLN F  32  ASP F  38 -1  O  LEU F  33   N  VAL F  25           
SHEET    3   P 3 ARG F  41  LEU F  46 -1  O  ARG F  41   N  ASP F  38           
SSBOND   1 CYS A  179    CYS A  189                          1555   1555  2.10  
SSBOND   2 CYS B  179    CYS B  189                          1555   1555  2.11  
SSBOND   3 CYS C  179    CYS C  189                          1555   1555  2.11  
SSBOND   4 CYS D  179    CYS D  189                          1555   1555  2.10  
LINK         O2A ADP A 500                MG    MG A 502     1555   1555  1.93  
LINK         O1B ADP A 500                ZN    ZN A 503     1555   1555  1.93  
LINK         O1B ADP B 500                ZN    ZN B 503     1555   1555  1.96  
LINK         O2A ADP B 500                MG    MG B 502     1555   1555  1.97  
LINK        ZN    ZN A 503                 O2  SO4 A 504     1555   1555  1.97  
LINK         OE2 GLU A 250                MG    MG A 502     1555   1555  2.06  
LINK         OD1 ASP A 237                MG    MG A 502     1555   1555  2.06  
LINK         OD2 ASP B 237                MG    MG B 502     1555   1555  2.07  
LINK        ZN    ZN B 503                 O1  SO4 B 504     1555   1555  2.08  
LINK         OE1 GLU B 250                MG    MG B 502     1555   1555  2.09  
LINK        MG    MG A 502                 O4  SO4 A 504     1555   1555  2.10  
LINK         O2B ADP A 500                MG    MG A 502     1555   1555  2.11  
LINK        MG    MG B 502                 O3  SO4 B 504     1555   1555  2.12  
LINK         O2B ADP B 500                MG    MG B 502     1555   1555  2.12  
LINK         ND1 HIS E  27                ZN    ZN E 100     1555   1555  2.13  
LINK         OE1 GLU B 250                ZN    ZN B 503     1555   1555  2.13  
LINK         OE1 GLU C 250                MG    MG C 502     1555   1555  2.13  
LINK         ND1 HIS F  27                ZN    ZN F 100     1555   1555  2.14  
LINK        MG    MG D 502                 O2  SO4 D 503     1555   1555  2.15  
LINK        MG    MG C 502                 O1  SO4 C 503     1555   1555  2.15  
LINK         O2A ADP D 500                MG    MG D 502     1555   1555  2.16  
LINK         O2B ADP D 500                MG    MG D 502     1555   1555  2.17  
LINK         OD2 ASP C 237                MG    MG C 502     1555   1555  2.19  
LINK         OE2 GLU A 250                ZN    ZN A 503     1555   1555  2.19  
LINK         O2A ADP C 500                MG    MG C 502     1555   1555  2.20  
LINK         SG  CYS E   6                ZN    ZN E 100     1555   1555  2.23  
LINK         OE2 GLU D 250                MG    MG D 502     1555   1555  2.23  
LINK         O2B ADP C 500                MG    MG C 502     1555   1555  2.24  
LINK         OD1 ASP D 237                MG    MG D 502     1555   1555  2.24  
LINK         OE1 GLU A 250                ZN    ZN A 503     1555   1555  2.28  
LINK         SG  CYS F   9                ZN    ZN F 100     1555   1555  2.32  
LINK         OD1 ASN A 252                ZN    ZN A 503     1555   1555  2.32  
LINK         SG  CYS E   9                ZN    ZN E 100     1555   1555  2.33  
LINK         SG  CYS E  29                ZN    ZN E 100     1555   1555  2.33  
LINK         SG  CYS F   6                ZN    ZN F 100     1555   1555  2.34  
LINK         SG  CYS F  29                ZN    ZN F 100     1555   1555  2.34  
LINK         OD1 ASN B 252                ZN    ZN B 503     1555   1555  2.35  
LINK         OE2 GLU B 250                ZN    ZN B 503     1555   1555  2.40  
LINK        MG    MG C 502                 O   HOH C 709     1555   1555  2.03  
LINK        MG    MG D 502                 O   HOH D 690     1555   1555  2.05  
LINK        ZN    ZN A 503                 O   HOH A 696     1555   1555  2.08  
LINK        ZN    ZN B 503                 O   HOH B 651     1555   1555  2.10  
LINK        MG    MG A 502                 O   HOH A 642     1555   1555  2.11  
LINK        MG    MG B 502                 O   HOH B 650     1555   1555  2.13  
CISPEP   1 ILE A   75    ASN A   76          0        -5.00                     
CISPEP   2 PHE A  122    PRO A  123          0         4.86                     
CISPEP   3 ILE B   75    ASN B   76          0        -6.97                     
CISPEP   4 PHE B  122    PRO B  123          0         0.79                     
CISPEP   5 ILE C   75    ASN C   76          0        -3.42                     
CISPEP   6 PHE C  122    PRO C  123          0        -3.79                     
CISPEP   7 ILE D   75    ASN D   76          0        -6.43                     
CISPEP   8 PHE D  122    PRO D  123          0        -3.75                     
SITE     1 AC1 26 LYS A  87  LYS A 127  GLY A 131  SER A 132                    
SITE     2 AC1 26 TRP A 133  GLY A 134  VAL A 137  GLN A 167                    
SITE     3 AC1 26 GLU A 168  TYR A 169  ILE A 170  ASP A 176                    
SITE     4 AC1 26 ARG A 200  ALA A 201  ASN A 202  ASP A 237                    
SITE     5 AC1 26 LEU A 239  ASN A 249  GLU A 250   MG A 502                    
SITE     6 AC1 26  ZN A 503  SO4 A 504  HOH A 621  HOH A 624                    
SITE     7 AC1 26 HOH A 642  HOH A 696                                          
SITE     1 AC2 13 TYR A 190  ARG A 192  ASN A 202  VAL A 203                    
SITE     2 AC2 13 ALA A 204  GLU A 256  LYS A 258  GLY A 259                    
SITE     3 AC2 13 PHE A 260  SO4 A 504  HOH A 626  HOH A 635                    
SITE     4 AC2 13 GLU E  56                                                     
SITE     1 AC3  6 ASP A 237  GLU A 250  ADP A 500   ZN A 503                    
SITE     2 AC3  6 SO4 A 504  HOH A 642                                          
SITE     1 AC4  6 GLU A 250  ASN A 252  ADP A 500   MG A 502                    
SITE     2 AC4  6 SO4 A 504  HOH A 696                                          
SITE     1 AC5 14 SER A 132  TRP A 133  ARG A 178  ARG A 192                    
SITE     2 AC5 14 ASN A 202  ASP A 237  GLU A 250  ASN A 252                    
SITE     3 AC5 14 ADP A 500  GLU A 501   MG A 502   ZN A 503                    
SITE     4 AC5 14 HOH A 642  GLU E  56                                          
SITE     1 AC6 24 LYS B  87  LYS B 127  GLY B 131  SER B 132                    
SITE     2 AC6 24 TRP B 133  GLY B 134  GLN B 167  GLU B 168                    
SITE     3 AC6 24 TYR B 169  ILE B 170  ASP B 176  ARG B 200                    
SITE     4 AC6 24 ALA B 201  ASN B 202  ASP B 237  ASN B 249                    
SITE     5 AC6 24 GLU B 250   MG B 502   ZN B 503  SO4 B 504                    
SITE     6 AC6 24 HOH B 617  HOH B 621  HOH B 650  HOH B 651                    
SITE     1 AC7 15 ARG B 178  TYR B 190  ARG B 192  ASN B 202                    
SITE     2 AC7 15 VAL B 203  ALA B 204  GLU B 256  LYS B 258                    
SITE     3 AC7 15 GLY B 259  PHE B 260  SO4 B 504  HOH B 654                    
SITE     4 AC7 15 HOH B 658  HOH B 689  GLU F  56                               
SITE     1 AC8  6 ASP B 237  GLU B 250  ADP B 500   ZN B 503                    
SITE     2 AC8  6 SO4 B 504  HOH B 650                                          
SITE     1 AC9  6 GLU B 250  ASN B 252  ADP B 500   MG B 502                    
SITE     2 AC9  6 SO4 B 504  HOH B 651                                          
SITE     1 BC1 14 SER B 132  TRP B 133  ARG B 178  ARG B 192                    
SITE     2 BC1 14 ASN B 202  ASP B 237  GLU B 250  ASN B 252                    
SITE     3 BC1 14 ADP B 500  GLU B 501   MG B 502   ZN B 503                    
SITE     4 BC1 14 HOH B 650  GLU F  56                                          
SITE     1 BC2 27 LYS C  87  ILE C 125  LYS C 127  GLY C 131                    
SITE     2 BC2 27 SER C 132  TRP C 133  GLY C 134  ARG C 135                    
SITE     3 BC2 27 VAL C 137  GLN C 167  GLU C 168  TYR C 169                    
SITE     4 BC2 27 ILE C 170  ASP C 176  ARG C 200  ALA C 201                    
SITE     5 BC2 27 ASN C 202  ASP C 237  ASN C 249  GLU C 250                    
SITE     6 BC2 27  MG C 502  SO4 C 503  HOH C 633  HOH C 651                    
SITE     7 BC2 27 HOH C 706  HOH C 709  HOH C 731                               
SITE     1 BC3 12 TRP C 133  TYR C 190  ARG C 192  ASN C 202                    
SITE     2 BC3 12 VAL C 203  ALA C 204  GLU C 256  LYS C 258                    
SITE     3 BC3 12 GLY C 259  PHE C 260  SO4 C 503  HOH C 639                    
SITE     1 BC4  5 ASP C 237  GLU C 250  ADP C 500  SO4 C 503                    
SITE     2 BC4  5 HOH C 709                                                     
SITE     1 BC5 14 SER C 132  TRP C 133  ARG C 178  ARG C 192                    
SITE     2 BC5 14 ASN C 202  ASP C 237  GLU C 250  ASN C 252                    
SITE     3 BC5 14 ADP C 500  GLU C 501   MG C 502  HOH C 601                    
SITE     4 BC5 14 HOH C 633  HOH C 709                                          
SITE     1 BC6  4 SER C  56  MET C  57  TYR C  58  SER D 159                    
SITE     1 BC7 25 LYS D  87  ILE D 125  LYS D 127  GLY D 131                    
SITE     2 BC7 25 SER D 132  TRP D 133  GLY D 134  VAL D 137                    
SITE     3 BC7 25 GLN D 167  GLU D 168  TYR D 169  ILE D 170                    
SITE     4 BC7 25 ASP D 176  ARG D 200  ALA D 201  ASN D 202                    
SITE     5 BC7 25 ASP D 237  ASN D 249  GLU D 250   MG D 502                    
SITE     6 BC7 25 SO4 D 503  HOH D 648  HOH D 654  HOH D 690                    
SITE     7 BC7 25 HOH D 699                                                     
SITE     1 BC8 13 TRP D 133  TYR D 190  ARG D 192  ASN D 202                    
SITE     2 BC8 13 VAL D 203  ALA D 204  GLU D 256  LYS D 258                    
SITE     3 BC8 13 GLY D 259  PHE D 260  SO4 D 503  HOH D 627                    
SITE     4 BC8 13 HOH D 680                                                     
SITE     1 BC9  5 ASP D 237  GLU D 250  ADP D 500  SO4 D 503                    
SITE     2 BC9  5 HOH D 690                                                     
SITE     1 CC1 14 SER D 132  TRP D 133  ARG D 178  ARG D 192                    
SITE     2 CC1 14 ASN D 202  ASP D 237  GLU D 250  ASN D 252                    
SITE     3 CC1 14 ADP D 500  GLU D 501   MG D 502  HOH D 608                    
SITE     4 CC1 14 HOH D 654  HOH D 690                                          
SITE     1 CC2  5 SER C 159  SER D  56  MET D  57  TYR D  58                    
SITE     2 CC2  5 HOH D 803                                                     
SITE     1 CC3  4 CYS E   6  CYS E   9  HIS E  27  CYS E  29                    
SITE     1 CC4  4 CYS F   6  CYS F   9  HIS F  27  CYS F  29                    
CRYST1   70.546  113.988   78.582  90.00 102.43  90.00 P 1 21 1      8          
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      0.014175  0.000000  0.003125        0.00000                         
SCALE2      0.000000  0.008773  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013031        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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