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Database: PDB
Entry: 3F7J
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Original site: 3F7J 
HEADER    OXIDOREDUCTASE                          09-NOV-08   3F7J              
TITLE     B.SUBTILIS YVGN                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: YVGN PROTEIN;                                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PUTATIVE REDUCTASE PROTEIN, YVGN;                           
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 GENE: YVGN;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    ALDO-KETO REDUCTASE, OXIDOREDUCTASE                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.F.ZHOU,J.LEI,Y.H.LIANG,X.-D.SU                                      
REVDAT   4   29-JAN-14 3F7J    1       JRNL                                     
REVDAT   3   13-JUL-11 3F7J    1       VERSN                                    
REVDAT   2   24-FEB-09 3F7J    1       VERSN                                    
REVDAT   1   25-NOV-08 3F7J    0                                                
SPRSDE     25-NOV-08 3F7J      3B3E                                             
JRNL        AUTH   J.LEI,Y.F.ZHOU,L.F.LI,X.-D.SU                                
JRNL        TITL   STRUCTURAL AND BIOCHEMICAL ANALYSES OF YVGN AND YTBE FROM    
JRNL        TITL 2 BACILLUS SUBTILIS                                            
JRNL        REF    PROTEIN SCI.                  V.  18  1792 2009              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   19585557                                                     
JRNL        DOI    10.1002/PRO.178                                              
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 59998                          
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) : 0.214                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1813                            
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) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4191                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.15                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3100                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 103                          
REMARK   3   BIN FREE R VALUE                    : 0.4240                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4468                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 38                                      
REMARK   3   SOLVENT ATOMS            : 528                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 4.55                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.10000                                              
REMARK   3    B22 (A**2) : -0.58000                                             
REMARK   3    B33 (A**2) : -0.52000                                             
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): 0.135         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.131         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.105         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.252         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4600 ; 0.019 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6208 ; 1.745 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   556 ; 6.257 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   228 ;38.091 ;25.526       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   857 ;16.934 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;24.367 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   673 ; 0.197 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3486 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2756 ; 0.280 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3153 ; 0.308 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   512 ; 0.251 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     2 ; 0.329 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    39 ; 0.316 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    24 ; 0.352 ; 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):  2781 ; 0.596 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4447 ; 1.037 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1835 ; 1.986 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1759 ; 3.094 ; 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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   276                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.6483  10.2456 -22.1653              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1951 T22:  -0.1463                                     
REMARK   3      T33:  -0.1248 T12:   0.0146                                     
REMARK   3      T13:  -0.0060 T23:   0.0053                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6201 L22:   2.4586                                     
REMARK   3      L33:   2.8088 L12:   0.2249                                     
REMARK   3      L13:  -0.1640 L23:   0.8706                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0337 S12:  -0.0099 S13:   0.0245                       
REMARK   3      S21:  -0.2088 S22:  -0.0226 S23:   0.0713                       
REMARK   3      S31:   0.1550 S32:  -0.0793 S33:   0.0563                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   276                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.4220  41.2470  -6.4538              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1700 T22:  -0.1499                                     
REMARK   3      T33:  -0.1154 T12:  -0.0022                                     
REMARK   3      T13:   0.0032 T23:   0.0050                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5748 L22:   2.2499                                     
REMARK   3      L33:   2.9142 L12:  -0.3153                                     
REMARK   3      L13:   0.1236 L23:   1.0960                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0214 S12:  -0.0057 S13:   0.0082                       
REMARK   3      S21:  -0.1480 S22:  -0.0446 S23:   0.0456                       
REMARK   3      S31:  -0.1837 S32:  -0.0503 S33:   0.0232                       
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 3F7J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-NOV-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB050244.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : BW7A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.96                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR                                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 60078                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 66.872                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : 0.06400                            
REMARK 200  R SYM                      (I) : 0.06400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.3080                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.79                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49300                            
REMARK 200  R SYM FOR SHELL            (I) : 0.49300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS, 0.4M SODIUM NITRATE, 40%      
REMARK 280  PEG3350, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       39.82800            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.53750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.82800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       61.53750            
REMARK 290   SMTRY3   4  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 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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 O2   NO3 A 281  LIES ON A SPECIAL POSITION.                          
REMARK 375 N    NO3 A 281  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 661  LIES ON A SPECIAL POSITION.                          
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   O    HOH A   569     O    HOH B   371              1.45            
REMARK 500   O    HOH B   301     O    HOH B   467              1.58            
REMARK 500   CD1  ILE B   245     O    HOH B   523              1.63            
REMARK 500   CG   GLN B   194     O    HOH B   463              1.85            
REMARK 500   N    ASN B   142     O    HOH B   521              1.90            
REMARK 500   O    HOH A   302     O    HOH A   641              1.90            
REMARK 500   O    ASP A   244     O    HOH A   643              1.91            
REMARK 500   CG   GLU B   165     O    HOH B   645              1.93            
REMARK 500   CD   GLU B   165     O    HOH B   552              1.94            
REMARK 500   O    HOH A   329     O    HOH A   544              1.96            
REMARK 500   O    HOH A   516     O    HOH A   530              1.98            
REMARK 500   O    HOH B   446     O    HOH B   637              2.02            
REMARK 500   O    HOH A   373     O    HOH A   480              2.06            
REMARK 500   CD2  LEU B   274     O    HOH A   660              2.08            
REMARK 500   O    TYR B   105     O    HOH B   469              2.09            
REMARK 500   OE1  GLU B   165     O    HOH B   552              2.10            
REMARK 500   O    HOH B   358     O    HOH B   656              2.11            
REMARK 500   O    HOH B   301     O    HOH B   379              2.11            
REMARK 500   CB   THR A   204     O    HOH A   482              2.11            
REMARK 500   O    PRO B   191     O    HOH B   524              2.12            
REMARK 500   O    HOH B   365     O    HOH B   623              2.12            
REMARK 500   O    HOH A   377     O    HOH A   570              2.12            
REMARK 500   OH   TYR A    54     O    HOH A   431              2.13            
REMARK 500   NH2  ARG B   100     O    HOH B   353              2.13            
REMARK 500   OE1  GLU B    83     O    HOH B   593              2.15            
REMARK 500   O    GLN B   163     O    HOH B   521              2.16            
REMARK 500   CG1  VAL B   164     O    HOH B   521              2.16            
REMARK 500   O    MET B   160     O    HOH B   457              2.16            
REMARK 500   CG   GLU B   249     O    HOH B   670              2.17            
REMARK 500   CB   LEU B   103     O    HOH B   535              2.18            
REMARK 500   O    HOH A   350     O    HOH A   563              2.18            
REMARK 500   CD   GLU B    58     O    HOH B   607              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   618     O    HOH A   618     2455     1.25            
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    VAL A 140   CG1 -  CB  -  CG2 ANGL. DEV. =  10.9 DEGREES          
REMARK 500    VAL A 140   CA  -  CB  -  CG1 ANGL. DEV. =  12.4 DEGREES          
REMARK 500    ARG B 176   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG B 176   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 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 117       24.99   -158.71                                   
REMARK 500    LYS B  26       27.61     47.80                                   
REMARK 500    LYS B 116      -63.76    -94.17                                   
REMARK 500    ASP B 117       28.21   -151.30                                   
REMARK 500    ASP B 264       55.51     35.06                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B 281   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 NO3 A 280   O3                                                     
REMARK 620 2 ASN B  82   OD1 124.8                                              
REMARK 620 3 NO3 A 280   O2   44.8  80.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B 282   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 486   O                                                      
REMARK 620 2 HOH B 668   O   139.9                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 277                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 278                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 279                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 280                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 281                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 277                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 278                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 279                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 280                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 281                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 282                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3B3D   RELATED DB: PDB                                   
REMARK 900 APOYTBE                                                              
REMARK 900 RELATED ID: 3B3F   RELATED DB: PDB                                   
REMARK 900 HOLOYVGN                                                             
DBREF  3F7J A    1   276  UNP    O32210   O32210_BACSU     1    276             
DBREF  3F7J B    1   276  UNP    O32210   O32210_BACSU     1    276             
SEQRES   1 A  276  MET PRO THR SER LEU LYS ASP THR VAL LYS LEU HIS ASN          
SEQRES   2 A  276  GLY VAL GLU MET PRO TRP PHE GLY LEU GLY VAL PHE LYS          
SEQRES   3 A  276  VAL GLU ASN GLY ASN GLU ALA THR GLU SER VAL LYS ALA          
SEQRES   4 A  276  ALA ILE LYS ASN GLY TYR ARG SER ILE ASP THR ALA ALA          
SEQRES   5 A  276  ILE TYR LYS ASN GLU GLU GLY VAL GLY ILE GLY ILE LYS          
SEQRES   6 A  276  GLU SER GLY VAL ALA ARG GLU GLU LEU PHE ILE THR SER          
SEQRES   7 A  276  LYS VAL TRP ASN GLU ASP GLN GLY TYR GLU THR THR LEU          
SEQRES   8 A  276  ALA ALA PHE GLU LYS SER LEU GLU ARG LEU GLN LEU ASP          
SEQRES   9 A  276  TYR LEU ASP LEU TYR LEU ILE HIS TRP PRO GLY LYS ASP          
SEQRES  10 A  276  LYS TYR LYS ASP THR TRP ARG ALA LEU GLU LYS LEU TYR          
SEQRES  11 A  276  LYS ASP GLY LYS ILE ARG ALA ILE GLY VAL SER ASN PHE          
SEQRES  12 A  276  GLN VAL HIS HIS LEU GLU GLU LEU LEU LYS ASP ALA GLU          
SEQRES  13 A  276  ILE LYS PRO MET VAL ASN GLN VAL GLU PHE HIS PRO ARG          
SEQRES  14 A  276  LEU THR GLN LYS GLU LEU ARG ASP TYR CYS LYS GLY GLN          
SEQRES  15 A  276  GLY ILE GLN LEU GLU ALA TRP SER PRO LEU MET GLN GLY          
SEQRES  16 A  276  GLN LEU LEU ASP ASN GLU VAL LEU THR GLN ILE ALA GLU          
SEQRES  17 A  276  LYS HIS ASN LYS SER VAL ALA GLN VAL ILE LEU ARG TRP          
SEQRES  18 A  276  ASP LEU GLN HIS GLY VAL VAL THR ILE PRO LYS SER ILE          
SEQRES  19 A  276  LYS GLU HIS ARG ILE ILE GLU ASN ALA ASP ILE PHE ASP          
SEQRES  20 A  276  PHE GLU LEU SER GLN GLU ASP MET ASP LYS ILE ASP ALA          
SEQRES  21 A  276  LEU ASN LYS ASP GLU ARG VAL GLY PRO ASN PRO ASP GLU          
SEQRES  22 A  276  LEU LEU PHE                                                  
SEQRES   1 B  276  MET PRO THR SER LEU LYS ASP THR VAL LYS LEU HIS ASN          
SEQRES   2 B  276  GLY VAL GLU MET PRO TRP PHE GLY LEU GLY VAL PHE LYS          
SEQRES   3 B  276  VAL GLU ASN GLY ASN GLU ALA THR GLU SER VAL LYS ALA          
SEQRES   4 B  276  ALA ILE LYS ASN GLY TYR ARG SER ILE ASP THR ALA ALA          
SEQRES   5 B  276  ILE TYR LYS ASN GLU GLU GLY VAL GLY ILE GLY ILE LYS          
SEQRES   6 B  276  GLU SER GLY VAL ALA ARG GLU GLU LEU PHE ILE THR SER          
SEQRES   7 B  276  LYS VAL TRP ASN GLU ASP GLN GLY TYR GLU THR THR LEU          
SEQRES   8 B  276  ALA ALA PHE GLU LYS SER LEU GLU ARG LEU GLN LEU ASP          
SEQRES   9 B  276  TYR LEU ASP LEU TYR LEU ILE HIS TRP PRO GLY LYS ASP          
SEQRES  10 B  276  LYS TYR LYS ASP THR TRP ARG ALA LEU GLU LYS LEU TYR          
SEQRES  11 B  276  LYS ASP GLY LYS ILE ARG ALA ILE GLY VAL SER ASN PHE          
SEQRES  12 B  276  GLN VAL HIS HIS LEU GLU GLU LEU LEU LYS ASP ALA GLU          
SEQRES  13 B  276  ILE LYS PRO MET VAL ASN GLN VAL GLU PHE HIS PRO ARG          
SEQRES  14 B  276  LEU THR GLN LYS GLU LEU ARG ASP TYR CYS LYS GLY GLN          
SEQRES  15 B  276  GLY ILE GLN LEU GLU ALA TRP SER PRO LEU MET GLN GLY          
SEQRES  16 B  276  GLN LEU LEU ASP ASN GLU VAL LEU THR GLN ILE ALA GLU          
SEQRES  17 B  276  LYS HIS ASN LYS SER VAL ALA GLN VAL ILE LEU ARG TRP          
SEQRES  18 B  276  ASP LEU GLN HIS GLY VAL VAL THR ILE PRO LYS SER ILE          
SEQRES  19 B  276  LYS GLU HIS ARG ILE ILE GLU ASN ALA ASP ILE PHE ASP          
SEQRES  20 B  276  PHE GLU LEU SER GLN GLU ASP MET ASP LYS ILE ASP ALA          
SEQRES  21 B  276  LEU ASN LYS ASP GLU ARG VAL GLY PRO ASN PRO ASP GLU          
SEQRES  22 B  276  LEU LEU PHE                                                  
HET    NO3  A 277       4                                                       
HET    NO3  A 278       4                                                       
HET    NO3  A 279       4                                                       
HET    NO3  A 280       4                                                       
HET    NO3  A 281       4                                                       
HET    NO3  B 277       4                                                       
HET    NO3  B 278       4                                                       
HET    NO3  B 279       4                                                       
HET    NO3  B 280       4                                                       
HET      K  B 281       1                                                       
HET      K  B 282       1                                                       
HETNAM     NO3 NITRATE ION                                                      
HETNAM       K POTASSIUM ION                                                    
FORMUL   3  NO3    9(N O3 1-)                                                   
FORMUL  12    K    2(K 1+)                                                      
FORMUL  14  HOH   *528(H2 O)                                                    
HELIX    1   1 GLY A   30  ASN A   43  1                                  14    
HELIX    2   2 ALA A   51  LYS A   55  5                                   5    
HELIX    3   3 ASN A   56  GLY A   68  1                                  13    
HELIX    4   4 ALA A   70  LEU A   74  5                                   5    
HELIX    5   5 TRP A   81  GLN A   85  5                                   5    
HELIX    6   6 GLY A   86  GLN A  102  1                                  17    
HELIX    7   7 LYS A  118  ASP A  132  1                                  15    
HELIX    8   8 GLN A  144  ALA A  155  1                                  12    
HELIX    9   9 GLN A  172  GLY A  183  1                                  12    
HELIX   10  10 LEU A  192  GLN A  196  5                                   5    
HELIX   11  11 ASN A  200  ASN A  211  1                                  12    
HELIX   12  12 SER A  213  HIS A  225  1                                  13    
HELIX   13  13 LYS A  235  ALA A  243  1                                   9    
HELIX   14  14 SER A  251  ALA A  260  1                                  10    
HELIX   15  15 ASN B   29  ASN B   43  1                                  15    
HELIX   16  16 ALA B   51  LYS B   55  5                                   5    
HELIX   17  17 ASN B   56  GLY B   68  1                                  13    
HELIX   18  18 ALA B   70  LEU B   74  5                                   5    
HELIX   19  19 TRP B   81  GLN B   85  5                                   5    
HELIX   20  20 GLY B   86  GLN B  102  1                                  17    
HELIX   21  21 LYS B  118  ASP B  132  1                                  15    
HELIX   22  22 GLN B  144  ALA B  155  1                                  12    
HELIX   23  23 GLN B  172  GLY B  183  1                                  12    
HELIX   24  24 LEU B  192  GLN B  196  5                                   5    
HELIX   25  25 ASN B  200  ASN B  211  1                                  12    
HELIX   26  26 SER B  213  HIS B  225  1                                  13    
HELIX   27  27 LYS B  235  ALA B  243  1                                   9    
HELIX   28  28 SER B  251  ALA B  260  1                                  10    
SHEET    1   A 2 THR A   8  LYS A  10  0                                        
SHEET    2   A 2 GLU A  16  PRO A  18 -1  O  MET A  17   N  VAL A   9           
SHEET    1   B 8 LEU A  22  GLY A  23  0                                        
SHEET    2   B 8 SER A  47  ASP A  49  1  O  ASP A  49   N  LEU A  22           
SHEET    3   B 8 PHE A  75  VAL A  80  1  O  PHE A  75   N  ILE A  48           
SHEET    4   B 8 LEU A 106  ILE A 111  1  O  LEU A 110   N  VAL A  80           
SHEET    5   B 8 ILE A 135  SER A 141  1  O  ARG A 136   N  LEU A 106           
SHEET    6   B 8 VAL A 161  GLU A 165  1  O  VAL A 161   N  VAL A 140           
SHEET    7   B 8 GLN A 185  TRP A 189  1  O  GLU A 187   N  VAL A 164           
SHEET    8   B 8 VAL A 228  THR A 229  1  O  VAL A 228   N  ALA A 188           
SHEET    1   C 2 THR B   8  LYS B  10  0                                        
SHEET    2   C 2 GLU B  16  PRO B  18 -1  O  MET B  17   N  VAL B   9           
SHEET    1   D 8 LEU B  22  GLY B  23  0                                        
SHEET    2   D 8 SER B  47  ASP B  49  1  O  ASP B  49   N  LEU B  22           
SHEET    3   D 8 PHE B  75  VAL B  80  1  O  PHE B  75   N  ILE B  48           
SHEET    4   D 8 LEU B 106  ILE B 111  1  O  LEU B 110   N  VAL B  80           
SHEET    5   D 8 ILE B 135  SER B 141  1  O  ARG B 136   N  LEU B 106           
SHEET    6   D 8 VAL B 161  GLU B 165  1  O  VAL B 161   N  VAL B 140           
SHEET    7   D 8 GLN B 185  TRP B 189  1  O  GLU B 187   N  VAL B 164           
SHEET    8   D 8 VAL B 228  THR B 229  1  O  VAL B 228   N  ALA B 188           
LINK         K     K B 281                 O3  NO3 A 280     1555   1555  2.69  
LINK         K     K B 282                 O   HOH A 486     1555   1555  2.96  
LINK         K     K B 282                 O   HOH B 668     1555   1555  2.34  
LINK         OD1 ASN B  82                 K     K B 281     1555   1555  3.01  
LINK         O2  NO3 A 280                 K     K B 281     1555   1555  3.33  
SITE     1 AC1  8 PHE A  25  SER A 190  PRO A 191  LEU A 192                    
SITE     2 AC1  8 MET A 193  GLN A 194  PRO A 231  LYS A 232                    
SITE     1 AC2  8 LEU A 192  GLY A 195  LEU A 198  ALA A 215                    
SITE     2 AC2  8 ARG A 238  HOH A 302  HOH A 329  HOH A 454                    
SITE     1 AC3  7 ASP A 117  LYS A 118  TYR A 119  LYS A 120                    
SITE     2 AC3  7 ASP A 121  HOH A 570  HOH A 666                               
SITE     1 AC4 10 TRP A  81  ASN A  82  LEU A 274  PHE A 276                    
SITE     2 AC4 10 HOH A 422  HOH A 599  HOH A 660  TRP B  81                    
SITE     3 AC4 10 LEU B 274    K B 281                                          
SITE     1 AC5  5 ASP A 177  TYR A 178  GLY A 181  GLN A 182                    
SITE     2 AC5  5 HOH A 577                                                     
SITE     1 AC6  9 PHE B  25  SER B 190  PRO B 191  LEU B 192                    
SITE     2 AC6  9 MET B 193  GLN B 194  PRO B 231  LYS B 232                    
SITE     3 AC6  9 HOH B 508                                                     
SITE     1 AC7 10 LEU B 192  GLY B 195  LEU B 198  VAL B 214                    
SITE     2 AC7 10 ALA B 215  ARG B 238  HOH B 295  HOH B 301                    
SITE     3 AC7 10 HOH B 395  HOH B 467                                          
SITE     1 AC8  6 ASP B 117  LYS B 118  TYR B 119  LYS B 120                    
SITE     2 AC8  6 ASP B 121  HOH B 658                                          
SITE     1 AC9  8 LYS A  55  HOH A 356  ALA B  52  LYS B  55                    
SITE     2 AC9  8 ARG B 100  HOH B 307  HOH B 334  HOH B 421                    
SITE     1 BC1  3 NO3 A 280  TRP B  81  ASN B  82                               
SITE     1 BC2  2 HOH A 486  HOH B 668                                          
CRYST1   79.656  123.075   57.239  90.00  90.00  90.00 P 21 21 2     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      0.012554  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008125  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017471        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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