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Database: PDB
Entry: 3OAJ
LinkDB: 3OAJ
Original site: 3OAJ 
HEADER    STRUCTURAL GENOMICS, UNKNOWN FUNCTION   05-AUG-10   3OAJ              
TITLE     CRYSTAL STRUCTURE OF PUTATIVE DIOXYGENASE FROM BACILLUS SUBTILIS      
TITLE    2 SUBSP. SUBTILIS STR. 168                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE RING-CLEAVING DIOXYGENASE MHQO;                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.13.11.-;                                                       
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS;              
SOURCE   3 ORGANISM_TAXID: 224308;                                              
SOURCE   4 STRAIN: 168;                                                         
SOURCE   5 GENE: BSU05490, CAB12356.1, MHQO, YDFO;                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)CODON+RIL;                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: BC-PSGX3(BC)                              
KEYWDS    STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, PSI-BIOLOGY,       
KEYWDS   2 UNKNOWN FUNCTION, NEW YORK STRUCTURAL GENOMICS RESEARCH CONSORTIUM,  
KEYWDS   3 NYSGRC                                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.N.MALASHKEVICH,R.TORO,R.SEIDEL,S.GARRETT,R.FOTI,S.C.ALMO,NEW YORK   
AUTHOR   2 STRUCTURAL GENOMICS RESEARCH CONSORTIUM (NYSGRC)                     
REVDAT   3   16-MAR-11 3OAJ    1       REMARK                                   
REVDAT   2   12-JAN-11 3OAJ    1       KEYWDS REMARK                            
REVDAT   1   18-AUG-10 3OAJ    0                                                
JRNL        AUTH   V.N.MALASHKEVICH,R.TORO,R.SEIDEL,S.GARRETT,R.FOTI,S.C.ALMO   
JRNL        TITL   CRYSTAL STRUCTURE OF PUTATIVE DIOXYGENASE FROM BACILLUS      
JRNL        TITL 2 SUBTILIS SUBSP. SUBTILIS STR. 168                            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 111391                         
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) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5602                            
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) : 1.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.44                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6758                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.82                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3360                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 345                          
REMARK   3   BIN FREE R VALUE                    : 0.4170                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4926                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 12                                      
REMARK   3   SOLVENT ATOMS            : 695                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.43                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.03000                                             
REMARK   3    B22 (A**2) : -0.06000                                             
REMARK   3    B33 (A**2) : 0.10000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.076         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.050         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.829         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.953                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5136 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6982 ; 1.263 ; 1.942       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   638 ; 6.422 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   272 ;32.220 ;24.228       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   823 ;13.059 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    32 ;17.666 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   722 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4070 ; 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):  3086 ; 1.253 ; 3.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4974 ; 2.617 ;50.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2050 ; 3.817 ;50.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1998 ; 1.634 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  5136 ; 0.815 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A  -99999       A   99999      1                     
REMARK   3           1     B  -99999       B   99999      1                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   2443 ; 0.330 ; 5.000           
REMARK   3   TIGHT THERMAL      1    A (A**2):   2443 ; 1.250 ;10.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   -10        A  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.4045  10.5262  39.2518              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0175 T22:   0.0224                                     
REMARK   3      T33:   0.0082 T12:   0.0016                                     
REMARK   3      T13:  -0.0090 T23:   0.0004                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3559 L22:   0.6074                                     
REMARK   3      L33:   0.1827 L12:   0.1207                                     
REMARK   3      L13:  -0.0981 L23:  -0.1154                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0046 S12:   0.0100 S13:   0.0043                       
REMARK   3      S21:   0.0124 S22:   0.0010 S23:   0.0383                       
REMARK   3      S31:  -0.0146 S32:  -0.0062 S33:  -0.0057                       
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   -10        B  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A):  55.8137  16.3867   3.0479              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0294 T22:   0.0381                                     
REMARK   3      T33:   0.0055 T12:   0.0015                                     
REMARK   3      T13:   0.0101 T23:   0.0018                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3938 L22:   0.7010                                     
REMARK   3      L33:   0.3046 L12:   0.1047                                     
REMARK   3      L13:   0.1038 L23:   0.1349                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0062 S12:   0.0371 S13:  -0.0064                       
REMARK   3      S21:  -0.0406 S22:   0.0208 S23:  -0.0469                       
REMARK   3      S31:  -0.0051 S32:   0.0139 S33:  -0.0147                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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 U VALUES : RESIDUAL ONLY                                  
REMARK   4                                                                      
REMARK   4 3OAJ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-AUG-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB060871.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-MAY-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 112088                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.9                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 71.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.69700                            
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: 1ZSW                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG4000, 0.2 M AMMONIUM SULFATE,     
REMARK 280  PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K             
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       43.09050            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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     VAL A     1                                                      
REMARK 465     MET A     2                                                      
REMARK 465     ASP A   313                                                      
REMARK 465     ALA A   314                                                      
REMARK 465     GLU A   315                                                      
REMARK 465     ASN A   316                                                      
REMARK 465     LEU A   317                                                      
REMARK 465     TYR A   318                                                      
REMARK 465     PHE A   319                                                      
REMARK 465     GLN A   320                                                      
REMARK 465     SER A   321                                                      
REMARK 465     HIS A   322                                                      
REMARK 465     HIS A   323                                                      
REMARK 465     HIS A   324                                                      
REMARK 465     HIS A   325                                                      
REMARK 465     HIS A   326                                                      
REMARK 465     HIS A   327                                                      
REMARK 465     TRP A   328                                                      
REMARK 465     SER A   329                                                      
REMARK 465     HIS A   330                                                      
REMARK 465     PRO A   331                                                      
REMARK 465     GLN A   332                                                      
REMARK 465     PHE A   333                                                      
REMARK 465     GLU A   334                                                      
REMARK 465     LYS A   335                                                      
REMARK 465     VAL B     1                                                      
REMARK 465     MET B     2                                                      
REMARK 465     ASP B   313                                                      
REMARK 465     ALA B   314                                                      
REMARK 465     GLU B   315                                                      
REMARK 465     ASN B   316                                                      
REMARK 465     LEU B   317                                                      
REMARK 465     TYR B   318                                                      
REMARK 465     PHE B   319                                                      
REMARK 465     GLN B   320                                                      
REMARK 465     SER B   321                                                      
REMARK 465     HIS B   322                                                      
REMARK 465     HIS B   323                                                      
REMARK 465     HIS B   324                                                      
REMARK 465     HIS B   325                                                      
REMARK 465     HIS B   326                                                      
REMARK 465     HIS B   327                                                      
REMARK 465     TRP B   328                                                      
REMARK 465     SER B   329                                                      
REMARK 465     HIS B   330                                                      
REMARK 465     PRO B   331                                                      
REMARK 465     GLN B   332                                                      
REMARK 465     PHE B   333                                                      
REMARK 465     GLU B   334                                                      
REMARK 465     LYS B   335                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TYR A 189   CD1   TYR A 189   CE1    -0.093                       
REMARK 500    TYR A 189   CE1   TYR A 189   CZ     -0.080                       
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    ALA A  70       77.47     45.15                                   
REMARK 500    ASN A 250      -52.29     77.71                                   
REMARK 500    ASN B 250      -49.34     75.79                                   
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 398        DISTANCE =  5.67 ANGSTROMS                       
REMARK 525    HOH B 480        DISTANCE =  6.19 ANGSTROMS                       
REMARK 525    HOH B 493        DISTANCE =  5.22 ANGSTROMS                       
REMARK 525    HOH B 636        DISTANCE =  5.77 ANGSTROMS                       
REMARK 525    HOH A 663        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH B 688        DISTANCE =  5.03 ANGSTROMS                       
REMARK 525    HOH B 721        DISTANCE =  6.05 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                              ZN A 500  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 266   OE1                                                    
REMARK 620 2 HIS A  11   NE2 106.1                                              
REMARK 620 3 SO4 A 501   O3  163.2  90.6                                        
REMARK 620 4 SO4 A 501   O4  108.6  96.2  67.0                                  
REMARK 620 5 HIS A 218   NE2  88.7 130.4  81.4 124.0                            
REMARK 620 6 SO4 A 501   S   132.6 107.6  35.9  35.8  93.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 500  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 266   OE1                                                    
REMARK 620 2 HIS B  11   NE2 104.9                                              
REMARK 620 3 SO4 B 501   O4  162.1  92.4                                        
REMARK 620 4 SO4 B 501   O3  104.1  98.6  68.0                                  
REMARK 620 5 HIS B 218   NE2  87.4 131.7  84.5 123.9                            
REMARK 620 6 SO4 B 501   S   129.1 110.4  36.4  36.3  95.0                      
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 ZN A 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: NYSGRC-000379   RELATED DB: TARGETDB                     
DBREF  3OAJ A    2   313  UNP    P96693   MHQO_BACSU       1    312             
DBREF  3OAJ B    2   313  UNP    P96693   MHQO_BACSU       1    312             
SEQADV 3OAJ VAL A    1  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ ALA A  314  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ GLU A  315  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ ASN A  316  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ LEU A  317  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ TYR A  318  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ PHE A  319  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ GLN A  320  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ SER A  321  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ HIS A  322  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ HIS A  323  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ HIS A  324  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ HIS A  325  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ HIS A  326  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ HIS A  327  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ TRP A  328  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ SER A  329  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ HIS A  330  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ PRO A  331  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ GLN A  332  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ PHE A  333  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ GLU A  334  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ LYS A  335  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ VAL B    1  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ ALA B  314  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ GLU B  315  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ ASN B  316  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ LEU B  317  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ TYR B  318  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ PHE B  319  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ GLN B  320  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ SER B  321  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ HIS B  322  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ HIS B  323  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ HIS B  324  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ HIS B  325  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ HIS B  326  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ HIS B  327  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ TRP B  328  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ SER B  329  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ HIS B  330  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ PRO B  331  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ GLN B  332  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ PHE B  333  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ GLU B  334  UNP  P96693              EXPRESSION TAG                 
SEQADV 3OAJ LYS B  335  UNP  P96693              EXPRESSION TAG                 
SEQRES   1 A  335  VAL MET ALA LYS LYS THR MET GLY ILE HIS HIS ILE THR          
SEQRES   2 A  335  ALA ILE VAL GLY HIS PRO GLN GLU ASN THR ASP PHE TYR          
SEQRES   3 A  335  ALA GLY VAL LEU GLY LEU ARG LEU VAL LYS GLN THR VAL          
SEQRES   4 A  335  ASN PHE ASP ASP PRO GLY THR TYR HIS LEU TYR PHE GLY          
SEQRES   5 A  335  ASN GLU GLY GLY LYS PRO GLY THR ILE ILE THR PHE PHE          
SEQRES   6 A  335  PRO TRP ALA GLY ALA ARG GLN GLY VAL ILE GLY ASP GLY          
SEQRES   7 A  335  GLN VAL GLY VAL THR SER TYR VAL VAL PRO LYS GLY ALA          
SEQRES   8 A  335  MET ALA PHE TRP GLU LYS ARG LEU GLU LYS PHE ASN VAL          
SEQRES   9 A  335  PRO TYR THR LYS ILE GLU ARG PHE GLY GLU GLN TYR VAL          
SEQRES  10 A  335  GLU PHE ASP ASP PRO HIS GLY LEU HIS LEU GLU ILE VAL          
SEQRES  11 A  335  GLU ARG GLU GLU GLY GLU ALA ASN THR TRP THR PHE GLY          
SEQRES  12 A  335  GLU VAL THR PRO ASP VAL ALA ILE LYS GLY PHE GLY GLY          
SEQRES  13 A  335  ALA THR LEU LEU SER GLU GLN PRO ASP LYS THR ALA ASP          
SEQRES  14 A  335  LEU LEU GLU ASN ILE MET GLY LEU GLU ARG VAL GLY LYS          
SEQRES  15 A  335  GLU GLY ASP PHE VAL ARG TYR ARG SER ALA GLY ASP ILE          
SEQRES  16 A  335  GLY ASN VAL ILE ASP LEU LYS LEU THR PRO ILE GLY ARG          
SEQRES  17 A  335  GLY GLN MET GLY ALA GLY THR VAL HIS HIS ILE ALA TRP          
SEQRES  18 A  335  ARG ALA ASN ASP ASP GLU ASP GLN LEU ASP TRP GLN ARG          
SEQRES  19 A  335  TYR ILE ALA SER HIS GLY TYR GLY VAL THR PRO VAL ARG          
SEQRES  20 A  335  ASP ARG ASN TYR PHE ASN ALA ILE TYR PHE ARG GLU HIS          
SEQRES  21 A  335  GLY GLU ILE LEU PHE GLU ILE ALA THR ASP PRO PRO GLY          
SEQRES  22 A  335  PHE ALA HIS ASP GLU THR GLN GLU THR MET GLY GLU LYS          
SEQRES  23 A  335  LEU MET LEU PRO VAL GLN TYR GLU PRO HIS ARG THR GLN          
SEQRES  24 A  335  ILE GLU GLN GLY LEU LEU PRO PHE GLU VAL ARG GLU LEU          
SEQRES  25 A  335  ASP ALA GLU ASN LEU TYR PHE GLN SER HIS HIS HIS HIS          
SEQRES  26 A  335  HIS HIS TRP SER HIS PRO GLN PHE GLU LYS                      
SEQRES   1 B  335  VAL MET ALA LYS LYS THR MET GLY ILE HIS HIS ILE THR          
SEQRES   2 B  335  ALA ILE VAL GLY HIS PRO GLN GLU ASN THR ASP PHE TYR          
SEQRES   3 B  335  ALA GLY VAL LEU GLY LEU ARG LEU VAL LYS GLN THR VAL          
SEQRES   4 B  335  ASN PHE ASP ASP PRO GLY THR TYR HIS LEU TYR PHE GLY          
SEQRES   5 B  335  ASN GLU GLY GLY LYS PRO GLY THR ILE ILE THR PHE PHE          
SEQRES   6 B  335  PRO TRP ALA GLY ALA ARG GLN GLY VAL ILE GLY ASP GLY          
SEQRES   7 B  335  GLN VAL GLY VAL THR SER TYR VAL VAL PRO LYS GLY ALA          
SEQRES   8 B  335  MET ALA PHE TRP GLU LYS ARG LEU GLU LYS PHE ASN VAL          
SEQRES   9 B  335  PRO TYR THR LYS ILE GLU ARG PHE GLY GLU GLN TYR VAL          
SEQRES  10 B  335  GLU PHE ASP ASP PRO HIS GLY LEU HIS LEU GLU ILE VAL          
SEQRES  11 B  335  GLU ARG GLU GLU GLY GLU ALA ASN THR TRP THR PHE GLY          
SEQRES  12 B  335  GLU VAL THR PRO ASP VAL ALA ILE LYS GLY PHE GLY GLY          
SEQRES  13 B  335  ALA THR LEU LEU SER GLU GLN PRO ASP LYS THR ALA ASP          
SEQRES  14 B  335  LEU LEU GLU ASN ILE MET GLY LEU GLU ARG VAL GLY LYS          
SEQRES  15 B  335  GLU GLY ASP PHE VAL ARG TYR ARG SER ALA GLY ASP ILE          
SEQRES  16 B  335  GLY ASN VAL ILE ASP LEU LYS LEU THR PRO ILE GLY ARG          
SEQRES  17 B  335  GLY GLN MET GLY ALA GLY THR VAL HIS HIS ILE ALA TRP          
SEQRES  18 B  335  ARG ALA ASN ASP ASP GLU ASP GLN LEU ASP TRP GLN ARG          
SEQRES  19 B  335  TYR ILE ALA SER HIS GLY TYR GLY VAL THR PRO VAL ARG          
SEQRES  20 B  335  ASP ARG ASN TYR PHE ASN ALA ILE TYR PHE ARG GLU HIS          
SEQRES  21 B  335  GLY GLU ILE LEU PHE GLU ILE ALA THR ASP PRO PRO GLY          
SEQRES  22 B  335  PHE ALA HIS ASP GLU THR GLN GLU THR MET GLY GLU LYS          
SEQRES  23 B  335  LEU MET LEU PRO VAL GLN TYR GLU PRO HIS ARG THR GLN          
SEQRES  24 B  335  ILE GLU GLN GLY LEU LEU PRO PHE GLU VAL ARG GLU LEU          
SEQRES  25 B  335  ASP ALA GLU ASN LEU TYR PHE GLN SER HIS HIS HIS HIS          
SEQRES  26 B  335  HIS HIS TRP SER HIS PRO GLN PHE GLU LYS                      
HET     ZN  A 500       1                                                       
HET    SO4  A 501       5                                                       
HET     ZN  B 500       1                                                       
HET    SO4  B 501       5                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  SO4    2(O4 S 2-)                                                   
FORMUL   7  HOH   *695(H2 O)                                                    
HELIX    1   1 HIS A   18  ALA A   27  1                                  10    
HELIX    2   2 ALA A   91  PHE A  102  1                                  12    
HELIX    3   3 GLN A  163  ILE A  174  1                                  12    
HELIX    4   4 ASP A  225  HIS A  239  1                                  15    
HELIX    5   5 PRO A  290  PRO A  295  5                                   6    
HELIX    6   6 HIS A  296  LEU A  304  1                                   9    
HELIX    7   7 HIS B   18  ALA B   27  1                                  10    
HELIX    8   8 ALA B   91  PHE B  102  1                                  12    
HELIX    9   9 GLN B  163  ILE B  174  1                                  12    
HELIX   10  10 ASP B  225  HIS B  239  1                                  15    
HELIX   11  11 PRO B  290  PRO B  295  5                                   6    
HELIX   12  12 HIS B  296  GLY B  303  1                                   8    
SHEET    1   A 8 ARG A  33  VAL A  39  0                                        
SHEET    2   A 8 TYR A  47  GLY A  52 -1  O  GLY A  52   N  ARG A  33           
SHEET    3   A 8 ILE A  61  PRO A  66 -1  O  ILE A  62   N  PHE A  51           
SHEET    4   A 8 ILE A   9  VAL A  16  1  N  ILE A  12   O  THR A  63           
SHEET    5   A 8 THR A 215  ALA A 223 -1  O  ALA A 220   N  HIS A  10           
SHEET    6   A 8 LEU A 264  THR A 269  1  O  GLU A 266   N  TRP A 221           
SHEET    7   A 8 ASN A 253  ARG A 258 -1  N  PHE A 257   O  PHE A 265           
SHEET    8   A 8 ARG A 247  ASP A 248 -1  N  ARG A 247   O  ALA A 254           
SHEET    1   B 8 THR A 107  ARG A 111  0                                        
SHEET    2   B 8 GLU A 114  ASP A 120 -1  O  TYR A 116   N  ILE A 109           
SHEET    3   B 8 HIS A 126  GLU A 131 -1  O  LEU A 127   N  PHE A 119           
SHEET    4   B 8 GLN A  79  VAL A  87  1  N  TYR A  85   O  GLU A 128           
SHEET    5   B 8 GLY A 153  LEU A 160 -1  O  LEU A 160   N  GLN A  79           
SHEET    6   B 8 VAL A 198  LYS A 202  1  O  ASP A 200   N  LEU A 159           
SHEET    7   B 8 PHE A 186  ARG A 190 -1  N  VAL A 187   O  LEU A 201           
SHEET    8   B 8 GLU A 178  GLU A 183 -1  N  VAL A 180   O  ARG A 188           
SHEET    1   C 8 ARG B  33  VAL B  39  0                                        
SHEET    2   C 8 TYR B  47  GLY B  52 -1  O  GLY B  52   N  ARG B  33           
SHEET    3   C 8 ILE B  61  PRO B  66 -1  O  ILE B  62   N  PHE B  51           
SHEET    4   C 8 ILE B   9  VAL B  16  1  N  ILE B  12   O  THR B  63           
SHEET    5   C 8 THR B 215  ALA B 223 -1  O  ALA B 220   N  HIS B  11           
SHEET    6   C 8 LEU B 264  THR B 269  1  O  GLU B 266   N  TRP B 221           
SHEET    7   C 8 ASN B 253  ARG B 258 -1  N  PHE B 257   O  PHE B 265           
SHEET    8   C 8 ARG B 247  ASP B 248 -1  N  ARG B 247   O  ALA B 254           
SHEET    1   D 8 THR B 107  ARG B 111  0                                        
SHEET    2   D 8 GLU B 114  ASP B 120 -1  O  GLU B 118   N  THR B 107           
SHEET    3   D 8 HIS B 126  GLU B 131 -1  O  LEU B 127   N  PHE B 119           
SHEET    4   D 8 GLN B  79  VAL B  87  1  N  TYR B  85   O  GLU B 128           
SHEET    5   D 8 GLY B 153  LEU B 160 -1  O  THR B 158   N  GLY B  81           
SHEET    6   D 8 VAL B 198  LYS B 202  1  O  ASP B 200   N  LEU B 159           
SHEET    7   D 8 PHE B 186  ARG B 190 -1  N  TYR B 189   O  ILE B 199           
SHEET    8   D 8 GLU B 178  GLU B 183 -1  N  VAL B 180   O  ARG B 188           
LINK         OE1 GLU A 266                ZN    ZN A 500     1555   1555  1.79  
LINK         OE1 GLU B 266                ZN    ZN B 500     1555   1555  1.86  
LINK         NE2 HIS A  11                ZN    ZN A 500     1555   1555  2.10  
LINK         NE2 HIS B  11                ZN    ZN B 500     1555   1555  2.11  
LINK        ZN    ZN A 500                 O3  SO4 A 501     1555   1555  2.16  
LINK        ZN    ZN B 500                 O4  SO4 B 501     1555   1555  2.16  
LINK        ZN    ZN B 500                 O3  SO4 B 501     1555   1555  2.16  
LINK        ZN    ZN A 500                 O4  SO4 A 501     1555   1555  2.19  
LINK         NE2 HIS A 218                ZN    ZN A 500     1555   1555  2.29  
LINK         NE2 HIS B 218                ZN    ZN B 500     1555   1555  2.29  
LINK        ZN    ZN B 500                 S   SO4 B 501     1555   1555  2.46  
LINK        ZN    ZN A 500                 S   SO4 A 501     1555   1555  2.49  
CISPEP   1 PRO A  271    PRO A  272          0         1.35                     
CISPEP   2 PRO B  271    PRO B  272          0         0.88                     
SITE     1 AC1  4 HIS A  11  HIS A 218  GLU A 266  SO4 A 501                    
SITE     1 AC2 11 HIS A  11  THR A  13  HIS A  48  TYR A  50                    
SITE     2 AC2 11 HIS A 218  PHE A 252  TYR A 256  GLU A 266                    
SITE     3 AC2 11  ZN A 500  HOH A 592  HOH A 678                               
SITE     1 AC3  5 HIS B  11  THR B  13  HIS B 218  GLU B 266                    
SITE     2 AC3  5 SO4 B 501                                                     
SITE     1 AC4  8 HIS B  11  THR B  13  HIS B  48  HIS B 218                    
SITE     2 AC4  8 PHE B 252  TYR B 256  GLU B 266   ZN B 500                    
CRYST1   50.215   86.181   72.968  90.00  91.65  90.00 P 1 21 1      4          
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      0.019914  0.000000  0.000573        0.00000                         
SCALE2      0.000000  0.011603  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013710        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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