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Database: PDB
Entry: 4V33
LinkDB: 4V33
Original site: 4V33 
HEADER    HYDROLASE                               16-OCT-14   4V33              
TITLE     CRYSTAL STRUCTURE OF THE PUTATIVE POLYSACCHARIDE DEACETYLASE BA0330   
TITLE    2 FROM BACILLUS ANTHRACIS                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POLYSACCHARIDE DEACETYLASE-LIKE PROTEIN;                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: POLYSACCHARIDE DEACETYLASE BA0330;                          
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: HYDROXY PROLINE IN POSITION 302                       
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;                             
SOURCE   3 ORGANISM_TAXID: 1392;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21                                       
KEYWDS    HYDROLASE, FIBRONECTIN TYPE III DOMAIN                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.GIASTAS,A.ANDREOU,V.BOURIOTIS,E.ELIOPOULOS                          
REVDAT   4   10-JAN-24 4V33    1       REMARK SHEET  LINK                       
REVDAT   3   10-JUN-15 4V33    1       JRNL                                     
REVDAT   2   15-APR-15 4V33    1       JRNL                                     
REVDAT   1   08-APR-15 4V33    0                                                
JRNL        AUTH   S.ARNAOUTELI,P.GIASTAS,A.ANDREOU,M.TZANODASKALAKI,           
JRNL        AUTH 2 C.ALDRIDGE,S.J.TZARTOS,W.VOLLMER,E.ELIOPOULOS,V.BOURIOTIS    
JRNL        TITL   TWO PUTATIVE POLYSACCHARIDE DEACETYLASES ARE REQUIRED FOR    
JRNL        TITL 2 OSMOTIC STABILITY AND CELL SHAPE MAINTENANCE IN BACILLUS     
JRNL        TITL 3 ANTHRACIS.                                                   
JRNL        REF    J.BIOL.CHEM.                  V. 290 13465 2015              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   25825488                                                     
JRNL        DOI    10.1074/JBC.M115.640029                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.48 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.48                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.02                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 155203                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.157                           
REMARK   3   R VALUE            (WORKING SET) : 0.157                           
REMARK   3   FREE R VALUE                     : 0.175                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 14922                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 48.0468 -  4.5966    0.96     9612   500  0.1409 0.1516        
REMARK   3     2  4.5966 -  3.6489    0.95     9577   498  0.1278 0.1471        
REMARK   3     3  3.6489 -  3.1878    0.95     9570   497  0.1468 0.1671        
REMARK   3     4  3.1878 -  2.8963    0.95     9612   512  0.1532 0.1735        
REMARK   3     5  2.8963 -  2.6888    0.95     9500   491  0.1522 0.1601        
REMARK   3     6  2.6888 -  2.5302    0.96     9685   518  0.1517 0.1615        
REMARK   3     7  2.5302 -  2.4035    0.95     9580   502  0.1499 0.1768        
REMARK   3     8  2.4035 -  2.2989    0.96     9545   503  0.1380 0.1664        
REMARK   3     9  2.2989 -  2.2104    0.96     9667   507  0.1474 0.1713        
REMARK   3    10  2.2104 -  2.1341    0.96     9637   508  0.1484 0.1647        
REMARK   3    11  2.1341 -  2.0674    0.96     9622   509  0.1580 0.1783        
REMARK   3    12  2.0674 -  2.0083    0.96     9516   495  0.1523 0.1772        
REMARK   3    13  2.0083 -  1.9554    0.95     9633   503  0.1485 0.1689        
REMARK   3    14  1.9554 -  1.9077    0.95     9530   503  0.1475 0.1702        
REMARK   3    15  1.9077 -  1.8644    0.95     9604   509  0.1512 0.1800        
REMARK   3    16  1.8644 -  1.8247    0.95     9505   499  0.1550 0.1627        
REMARK   3    17  1.8247 -  1.7882    0.95     9429   493  0.1655 0.1899        
REMARK   3    18  1.7882 -  1.7544    0.94     9553   499  0.1721 0.1807        
REMARK   3    19  1.7544 -  1.7231    0.95     9534   494  0.1756 0.2069        
REMARK   3    20  1.7231 -  1.6939    0.94     9400   495  0.1896 0.2171        
REMARK   3    21  1.6939 -  1.6666    0.94     9562   494  0.1868 0.1982        
REMARK   3    22  1.6666 -  1.6409    0.94     9387   484  0.1843 0.1905        
REMARK   3    23  1.6409 -  1.6168    0.94     9452   497  0.1855 0.1967        
REMARK   3    24  1.6168 -  1.5940    0.94     9467   503  0.1961 0.2222        
REMARK   3    25  1.5940 -  1.5725    0.93     9320   484  0.2096 0.2335        
REMARK   3    26  1.5725 -  1.5520    0.93     9477   500  0.2258 0.2289        
REMARK   3    27  1.5520 -  1.5326    0.93     9154   482  0.2333 0.2532        
REMARK   3    28  1.5326 -  1.5142    0.93     9465   503  0.2522 0.2693        
REMARK   3    29  1.5142 -  1.4966    0.92     9159   481  0.2619 0.2860        
REMARK   3    30  1.4966 -  1.4798    0.86     8819   459  0.2799 0.2921        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.140            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.110           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.19                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.010           5279                                  
REMARK   3   ANGLE     :  1.024           7132                                  
REMARK   3   CHIRALITY :  0.070            791                                  
REMARK   3   PLANARITY :  0.005            905                                  
REMARK   3   DIHEDRAL  : 12.650           2009                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 45 THROUGH 149 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):   3.6759  33.3366  62.2485              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1976 T22:   0.3013                                     
REMARK   3      T33:   0.1511 T12:   0.0275                                     
REMARK   3      T13:   0.0214 T23:   0.0373                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9154 L22:   0.6418                                     
REMARK   3      L33:   3.0383 L12:   0.3458                                     
REMARK   3      L13:  -1.4735 L23:  -1.1285                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1935 S12:  -0.3016 S13:  -0.1718                       
REMARK   3      S21:   0.0191 S22:  -0.0267 S23:  -0.0951                       
REMARK   3      S31:   0.2688 S32:   0.3665 S33:   0.2004                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 150 THROUGH 198 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   7.1429  50.7550  32.2788              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1055 T22:   0.1233                                     
REMARK   3      T33:   0.1166 T12:  -0.0476                                     
REMARK   3      T13:   0.0148 T23:  -0.0022                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7910 L22:   1.2988                                     
REMARK   3      L33:   2.0483 L12:   0.0471                                     
REMARK   3      L13:   0.5965 L23:   0.2835                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0178 S12:   0.0421 S13:   0.0989                       
REMARK   3      S21:  -0.1199 S22:   0.0595 S23:   0.0638                       
REMARK   3      S31:  -0.1575 S32:   0.0136 S33:  -0.0361                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 199 THROUGH 360 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.1072  54.9730  36.1181              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1202 T22:   0.1617                                     
REMARK   3      T33:   0.0841 T12:  -0.0316                                     
REMARK   3      T13:   0.0211 T23:  -0.0199                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5114 L22:   0.9631                                     
REMARK   3      L33:   1.1946 L12:   0.5234                                     
REMARK   3      L13:   0.0044 L23:  -0.3373                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0593 S12:  -0.1976 S13:   0.0705                       
REMARK   3      S21:   0.0872 S22:  -0.0701 S23:   0.0239                       
REMARK   3      S31:  -0.0903 S32:   0.0958 S33:   0.0127                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 45 THROUGH 179 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -29.9260  31.5403  -5.0991              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2781 T22:   0.1211                                     
REMARK   3      T33:   0.2723 T12:  -0.0283                                     
REMARK   3      T13:  -0.1219 T23:  -0.0373                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2018 L22:   1.6896                                     
REMARK   3      L33:   0.4750 L12:  -0.4052                                     
REMARK   3      L13:  -0.3242 L23:  -0.3885                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2525 S12:   0.2834 S13:  -0.2473                       
REMARK   3      S21:  -0.5463 S22:  -0.0293 S23:   0.4380                       
REMARK   3      S31:   0.2648 S32:  -0.1484 S33:  -0.0749                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 180 THROUGH 360 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.7821  36.2525  11.6091              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1136 T22:   0.0674                                     
REMARK   3      T33:   0.1070 T12:  -0.0038                                     
REMARK   3      T13:   0.0001 T23:  -0.0043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0830 L22:   0.5817                                     
REMARK   3      L33:   0.5533 L12:   0.4502                                     
REMARK   3      L13:   0.0898 L23:  -0.0818                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0069 S12:  -0.0364 S13:   0.0217                       
REMARK   3      S21:  -0.0004 S22:  -0.0158 S23:   0.0346                       
REMARK   3      S31:  -0.0046 S32:   0.0119 S33:   0.0085                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: RESIDUES 1-44 WERE NOT LOCATED IN THE     
REMARK   3  EXPERIMENT                                                          
REMARK   4                                                                      
REMARK   4 4V33 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-OCT-14.                  
REMARK 100 THE DEPOSITION ID IS D_1290062009.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-AUG-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06DA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 155207                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.480                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.020                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.48                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.59000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
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: PDB ENTRY 4HD5                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CACODYLATE PH 6.5, 20%     
REMARK 280  PEG 3350                                                            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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       54.48200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.38150            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       54.48200            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.38150            
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      HOH A2035  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A2076  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     TYR A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     ILE A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     CYS A    10                                                      
REMARK 465     THR A    11                                                      
REMARK 465     SER A    12                                                      
REMARK 465     ALA A    13                                                      
REMARK 465     ILE A    14                                                      
REMARK 465     LEU A    15                                                      
REMARK 465     ALA A    16                                                      
REMARK 465     GLY A    17                                                      
REMARK 465     CYS A    18                                                      
REMARK 465     ASN A    19                                                      
REMARK 465     THR A    20                                                      
REMARK 465     SER A    21                                                      
REMARK 465     ASN A    22                                                      
REMARK 465     VAL A    23                                                      
REMARK 465     SER A    24                                                      
REMARK 465     GLN A    25                                                      
REMARK 465     GLU A    26                                                      
REMARK 465     PRO A    27                                                      
REMARK 465     ASN A    28                                                      
REMARK 465     LYS A    29                                                      
REMARK 465     GLU A    30                                                      
REMARK 465     ARG A    31                                                      
REMARK 465     LYS A    32                                                      
REMARK 465     VAL A    33                                                      
REMARK 465     GLN A    34                                                      
REMARK 465     GLU A    35                                                      
REMARK 465     THR A    36                                                      
REMARK 465     LYS A    37                                                      
REMARK 465     LYS A    38                                                      
REMARK 465     GLN A    39                                                      
REMARK 465     ALA A    40                                                      
REMARK 465     GLU A    41                                                      
REMARK 465     THR A    42                                                      
REMARK 465     VAL A    43                                                      
REMARK 465     GLN A    44                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ARG B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     TYR B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     ALA B     6                                                      
REMARK 465     ILE B     7                                                      
REMARK 465     ALA B     8                                                      
REMARK 465     LEU B     9                                                      
REMARK 465     CYS B    10                                                      
REMARK 465     THR B    11                                                      
REMARK 465     SER B    12                                                      
REMARK 465     ALA B    13                                                      
REMARK 465     ILE B    14                                                      
REMARK 465     LEU B    15                                                      
REMARK 465     ALA B    16                                                      
REMARK 465     GLY B    17                                                      
REMARK 465     CYS B    18                                                      
REMARK 465     ASN B    19                                                      
REMARK 465     THR B    20                                                      
REMARK 465     SER B    21                                                      
REMARK 465     ASN B    22                                                      
REMARK 465     VAL B    23                                                      
REMARK 465     SER B    24                                                      
REMARK 465     GLN B    25                                                      
REMARK 465     GLU B    26                                                      
REMARK 465     PRO B    27                                                      
REMARK 465     ASN B    28                                                      
REMARK 465     LYS B    29                                                      
REMARK 465     GLU B    30                                                      
REMARK 465     ARG B    31                                                      
REMARK 465     LYS B    32                                                      
REMARK 465     VAL B    33                                                      
REMARK 465     GLN B    34                                                      
REMARK 465     GLU B    35                                                      
REMARK 465     THR B    36                                                      
REMARK 465     LYS B    37                                                      
REMARK 465     LYS B    38                                                      
REMARK 465     GLN B    39                                                      
REMARK 465     ALA B    40                                                      
REMARK 465     GLU B    41                                                      
REMARK 465     THR B    42                                                      
REMARK 465     VAL B    43                                                      
REMARK 465     GLN B    44                                                      
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 B  2223     O    HOH B  2224              2.11            
REMARK 500   O    HOH B  2067     O    HOH B  2160              2.18            
REMARK 500   O    HOH A  2199     O    HOH A  2200              2.19            
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    ARG A 114     -167.07   -122.96                                   
REMARK 500    LEU A 133      -91.37   -110.78                                   
REMARK 500    HIS A 150      -94.97   -121.94                                   
REMARK 500    ASP A 206      -32.10    115.63                                   
REMARK 500    THR A 265      177.30     72.00                                   
REMARK 500    GLN B  46      -85.26   -131.33                                   
REMARK 500    LYS B  99       42.82   -109.49                                   
REMARK 500    ARG B 114     -157.45   -127.27                                   
REMARK 500    LEU B 133      -87.76    -77.21                                   
REMARK 500    HIS B 150      -95.60   -125.34                                   
REMARK 500    ASP B 206      -31.50    117.18                                   
REMARK 500    ASP B 223     -166.86   -163.99                                   
REMARK 500    THR B 265      175.49     73.49                                   
REMARK 500    THR B 323     -169.27   -105.32                                   
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 A2145        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH A2192        DISTANCE =  5.99 ANGSTROMS                       
REMARK 525    HOH A2205        DISTANCE =  6.69 ANGSTROMS                       
REMARK 525    HOH B2148        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH B2156        DISTANCE =  6.60 ANGSTROMS                       
REMARK 525    HOH B2170        DISTANCE =  6.58 ANGSTROMS                       
REMARK 525    HOH B2181        DISTANCE =  5.86 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 A1362  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 206   OD1                                                    
REMARK 620 2 HIS A 264   NE2  85.6                                              
REMARK 620 3 HIS A 268   NE2 111.2  98.0                                        
REMARK 620 4 ACT A1361   O   115.9  91.2 132.5                                  
REMARK 620 5 HOH A2196   O    89.4 164.8  97.1  78.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1362  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 206   OD1                                                    
REMARK 620 2 HIS B 264   NE2  86.6                                              
REMARK 620 3 HIS B 268   NE2 109.3  96.3                                        
REMARK 620 4 ACT B1361   O   117.6  90.1 133.0                                  
REMARK 620 5 HOH B2152   O    86.2 164.6  98.8  81.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AC" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  7-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  8-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700 THE SHEETS PRESENTED AS "BC" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  7-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  8-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1361                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1362                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 1361                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1362                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1363                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 1363                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1364                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1365                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1364                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1365                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 HYDROXY PROLINE AT POSITION 302                                      
DBREF  4V33 A    1   360  UNP    Q81ZD9   Q81ZD9_BACAN     1    360             
DBREF  4V33 B    1   360  UNP    Q81ZD9   Q81ZD9_BACAN     1    360             
SEQRES   1 A  360  MET ARG LYS TYR ALA ALA ILE ALA LEU CYS THR SER ALA          
SEQRES   2 A  360  ILE LEU ALA GLY CYS ASN THR SER ASN VAL SER GLN GLU          
SEQRES   3 A  360  PRO ASN LYS GLU ARG LYS VAL GLN GLU THR LYS LYS GLN          
SEQRES   4 A  360  ALA GLU THR VAL GLN GLU GLN GLY LYS ILE SER TYR ASN          
SEQRES   5 A  360  PRO ILE THR HIS GLU SER THR ASN THR THR ILE HIS MET          
SEQRES   6 A  360  THR ASP ILE LYS ASP THR LEU THR GLU VAL GLN TYR LYS          
SEQRES   7 A  360  ILE TRP ARG THR ALA ASP GLY LYS GLU THR ALA LYS SER          
SEQRES   8 A  360  LEU SER SER LYS GLU LYS GLU LYS GLN PHE SER LEU PRO          
SEQRES   9 A  360  PHE ASP THR LYS GLU PHE GLU GLY LYS ARG GLY GLU PHE          
SEQRES  10 A  360  GLN ILE GLU ALA ILE GLY ILE LYS GLU ASP GLY LYS THR          
SEQRES  11 A  360  ILE PRO LEU THR LYS SER ALA ILE THR PHE GLU GLN LYS          
SEQRES  12 A  360  VAL PRO VAL LEU MET TYR HIS ALA ILE ASP ASP TYR HIS          
SEQRES  13 A  360  GLY GLN GLY ILE LYS ASP LEU PHE VAL SER PRO ALA ASN          
SEQRES  14 A  360  PHE GLU ALA GLN MET LYS TYR LEU LYS ASP ASN GLY TYR          
SEQRES  15 A  360  THR LEU LEU THR PHE GLU ARG TRP GLY ASP ILE ASN LYS          
SEQRES  16 A  360  VAL ASN LYS PRO ILE PHE VAL THR PHE ASP ASP GLY MET          
SEQRES  17 A  360  LYS ASN ASN MET ASN ALA PHE HIS VAL LEU GLN LYS LEU          
SEQRES  18 A  360  LYS ASP ASP THR PHE LYS PRO VAL ALA THR GLU TYR MET          
SEQRES  19 A  360  ILE VAL ASN ASN VAL ASP ALA GLU GLY SER LEU SER THR          
SEQRES  20 A  360  SER ASP ILE LYS GLU MET VAL ASP SER GLY ILE PHE SER          
SEQRES  21 A  360  MET GLN SER HIS THR ALA THR HIS ALA ASP LEU PRO LYS          
SEQRES  22 A  360  ILE THR ASN TYR GLU GLU GLU LEU LYS GLU SER LYS GLU          
SEQRES  23 A  360  LYS LEU GLU LYS ILE THR GLY LYS PRO VAL ILE ALA VAL          
SEQRES  24 A  360  ALA TYR PXU PHE GLY HIS VAL ASP ASP LYS VAL VAL ALA          
SEQRES  25 A  360  GLU THR LYS LYS TYR TYR GLN PHE ALA THR THR THR LYS          
SEQRES  26 A  360  PRO GLY LYS PHE ILE THR LYS GLY GLU PRO ASP GLU LEU          
SEQRES  27 A  360  LEU LYS MET LYS ARG VAL ARG ILE HIS HIS THR THR THR          
SEQRES  28 A  360  VAL GLU GLN PHE ALA SER SER ILE LYS                          
SEQRES   1 B  360  MET ARG LYS TYR ALA ALA ILE ALA LEU CYS THR SER ALA          
SEQRES   2 B  360  ILE LEU ALA GLY CYS ASN THR SER ASN VAL SER GLN GLU          
SEQRES   3 B  360  PRO ASN LYS GLU ARG LYS VAL GLN GLU THR LYS LYS GLN          
SEQRES   4 B  360  ALA GLU THR VAL GLN GLU GLN GLY LYS ILE SER TYR ASN          
SEQRES   5 B  360  PRO ILE THR HIS GLU SER THR ASN THR THR ILE HIS MET          
SEQRES   6 B  360  THR ASP ILE LYS ASP THR LEU THR GLU VAL GLN TYR LYS          
SEQRES   7 B  360  ILE TRP ARG THR ALA ASP GLY LYS GLU THR ALA LYS SER          
SEQRES   8 B  360  LEU SER SER LYS GLU LYS GLU LYS GLN PHE SER LEU PRO          
SEQRES   9 B  360  PHE ASP THR LYS GLU PHE GLU GLY LYS ARG GLY GLU PHE          
SEQRES  10 B  360  GLN ILE GLU ALA ILE GLY ILE LYS GLU ASP GLY LYS THR          
SEQRES  11 B  360  ILE PRO LEU THR LYS SER ALA ILE THR PHE GLU GLN LYS          
SEQRES  12 B  360  VAL PRO VAL LEU MET TYR HIS ALA ILE ASP ASP TYR HIS          
SEQRES  13 B  360  GLY GLN GLY ILE LYS ASP LEU PHE VAL SER PRO ALA ASN          
SEQRES  14 B  360  PHE GLU ALA GLN MET LYS TYR LEU LYS ASP ASN GLY TYR          
SEQRES  15 B  360  THR LEU LEU THR PHE GLU ARG TRP GLY ASP ILE ASN LYS          
SEQRES  16 B  360  VAL ASN LYS PRO ILE PHE VAL THR PHE ASP ASP GLY MET          
SEQRES  17 B  360  LYS ASN ASN MET ASN ALA PHE HIS VAL LEU GLN LYS LEU          
SEQRES  18 B  360  LYS ASP ASP THR PHE LYS PRO VAL ALA THR GLU TYR MET          
SEQRES  19 B  360  ILE VAL ASN ASN VAL ASP ALA GLU GLY SER LEU SER THR          
SEQRES  20 B  360  SER ASP ILE LYS GLU MET VAL ASP SER GLY ILE PHE SER          
SEQRES  21 B  360  MET GLN SER HIS THR ALA THR HIS ALA ASP LEU PRO LYS          
SEQRES  22 B  360  ILE THR ASN TYR GLU GLU GLU LEU LYS GLU SER LYS GLU          
SEQRES  23 B  360  LYS LEU GLU LYS ILE THR GLY LYS PRO VAL ILE ALA VAL          
SEQRES  24 B  360  ALA TYR PXU PHE GLY HIS VAL ASP ASP LYS VAL VAL ALA          
SEQRES  25 B  360  GLU THR LYS LYS TYR TYR GLN PHE ALA THR THR THR LYS          
SEQRES  26 B  360  PRO GLY LYS PHE ILE THR LYS GLY GLU PRO ASP GLU LEU          
SEQRES  27 B  360  LEU LYS MET LYS ARG VAL ARG ILE HIS HIS THR THR THR          
SEQRES  28 B  360  VAL GLU GLN PHE ALA SER SER ILE LYS                          
MODRES 4V33 PXU A  302  PRO  2-HYDROXY-L-PROLINE                                
MODRES 4V33 PXU B  302  PRO  2-HYDROXY-L-PROLINE                                
HET    PXU  A 302       8                                                       
HET    PXU  B 302       8                                                       
HET    ACT  A1361       4                                                       
HET     ZN  A1362       1                                                       
HET    ACT  A1363       4                                                       
HET    EDO  A1364       4                                                       
HET    EDO  A1365       4                                                       
HET    ACT  B1361       4                                                       
HET     ZN  B1362       1                                                       
HET    ACT  B1363       4                                                       
HET    EDO  B1364       4                                                       
HET    EDO  B1365       4                                                       
HETNAM     PXU 2-HYDROXY-L-PROLINE                                              
HETNAM     ACT ACETATE ION                                                      
HETNAM      ZN ZINC ION                                                         
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  PXU    2(C5 H9 N O3)                                                
FORMUL   3  ACT    4(C2 H3 O2 1-)                                               
FORMUL   4   ZN    2(ZN 2+)                                                     
FORMUL   6  EDO    4(C2 H6 O2)                                                  
FORMUL  13  HOH   *942(H2 O)                                                    
HELIX    1   1 GLY A   85  ALA A   89  5                                   5    
HELIX    2   2 GLU A   96  GLN A  100  5                                   5    
HELIX    3   3 LYS A  108  GLU A  111  5                                   4    
HELIX    4   4 ILE A  160  ASP A  162  5                                   3    
HELIX    5   5 SER A  166  ASN A  180  1                                  15    
HELIX    6   6 THR A  186  ILE A  193  5                                   8    
HELIX    7   7 ASN A  210  LYS A  222  1                                  13    
HELIX    8   8 VAL A  236  VAL A  239  5                                   4    
HELIX    9   9 SER A  246  SER A  256  1                                  11    
HELIX   10  10 ASP A  270  ILE A  274  5                                   5    
HELIX   11  11 ASN A  276  GLY A  293  1                                  18    
HELIX   12  12 ASP A  307  LYS A  316  1                                  10    
HELIX   13  13 ASP A  336  LYS A  340  5                                   5    
HELIX   14  14 THR A  351  LYS A  360  1                                  10    
HELIX   15  15 GLY B   85  ALA B   89  5                                   5    
HELIX   16  16 GLU B   96  GLN B  100  5                                   5    
HELIX   17  17 LYS B  108  GLU B  111  5                                   4    
HELIX   18  18 ILE B  160  ASP B  162  5                                   3    
HELIX   19  19 SER B  166  ASN B  180  1                                  15    
HELIX   20  20 THR B  186  ILE B  193  5                                   8    
HELIX   21  21 ASN B  210  LYS B  222  1                                  13    
HELIX   22  22 VAL B  236  VAL B  239  5                                   4    
HELIX   23  23 SER B  246  SER B  256  1                                  11    
HELIX   24  24 ASP B  270  ILE B  274  5                                   5    
HELIX   25  25 ASN B  276  GLY B  293  1                                  18    
HELIX   26  26 ASP B  307  TYR B  318  1                                  12    
HELIX   27  27 ASP B  336  LYS B  340  5                                   5    
HELIX   28  28 THR B  351  LYS B  360  1                                  10    
SHEET    1  AA 3 LYS A  48  TYR A  51  0                                        
SHEET    2  AA 3 ASN A  60  THR A  66 -1  O  HIS A  64   N  SER A  50           
SHEET    3  AA 3 LEU A 103  ASP A 106 -1  O  LEU A 103   N  ILE A  63           
SHEET    1  AB 4 LYS A  90  SER A  94  0                                        
SHEET    2  AB 4 GLU A  74  ARG A  81 -1  O  VAL A  75   N  SER A  94           
SHEET    3  AB 4 GLY A 115  ILE A 124 -1  O  GLN A 118   N  TRP A  80           
SHEET    4  AB 4 THR A 130  PHE A 140 -1  O  ILE A 131   N  GLY A 123           
SHEET    1  AC 8 VAL A 146  TYR A 149  0                                        
SHEET    2  AC 8 PRO A 199  ASP A 206 -1  O  PHE A 201   N  LEU A 147           
SHEET    3  AC 8 ALA A 230  MET A 234  1  O  THR A 231   N  PHE A 204           
SHEET    4  AC 8 PHE A 259  SER A 263  1  O  SER A 260   N  GLU A 232           
SHEET    5  AC 8 ALA A 298  ALA A 300 -1  O  ALA A 298   N  SER A 263           
SHEET    6  AC 8 PHE A 320  PRO A 326  1  O  PHE A 320   N  VAL A 299           
SHEET    7  AC 8 MET A 341  ARG A 345  1  O  MET A 341   N  THR A 323           
SHEET    8  AC 8 VAL A 146  TYR A 149  0                                        
SHEET    1  AD 2 ALA A 151  ILE A 152  0                                        
SHEET    2  AD 2 PHE A 164  VAL A 165  1  N  VAL A 165   O  ALA A 151           
SHEET    1  BA 3 LYS B  48  TYR B  51  0                                        
SHEET    2  BA 3 ASN B  60  THR B  66 -1  O  HIS B  64   N  SER B  50           
SHEET    3  BA 3 LEU B 103  ASP B 106 -1  O  LEU B 103   N  ILE B  63           
SHEET    1  BB 4 LYS B  90  SER B  94  0                                        
SHEET    2  BB 4 GLU B  74  ARG B  81 -1  O  VAL B  75   N  SER B  94           
SHEET    3  BB 4 GLY B 115  ILE B 124 -1  O  GLN B 118   N  TRP B  80           
SHEET    4  BB 4 THR B 130  PHE B 140 -1  O  ILE B 131   N  GLY B 123           
SHEET    1  BC 8 VAL B 146  TYR B 149  0                                        
SHEET    2  BC 8 PRO B 199  ASP B 206 -1  O  PHE B 201   N  LEU B 147           
SHEET    3  BC 8 ALA B 230  MET B 234  1  O  THR B 231   N  PHE B 204           
SHEET    4  BC 8 PHE B 259  SER B 263  1  O  SER B 260   N  GLU B 232           
SHEET    5  BC 8 ALA B 298  ALA B 300 -1  O  ALA B 298   N  SER B 263           
SHEET    6  BC 8 PHE B 320  PRO B 326  1  O  PHE B 320   N  VAL B 299           
SHEET    7  BC 8 MET B 341  ARG B 345  1  O  MET B 341   N  THR B 323           
SHEET    8  BC 8 VAL B 146  TYR B 149  0                                        
SHEET    1  BD 2 ALA B 151  ILE B 152  0                                        
SHEET    2  BD 2 PHE B 164  VAL B 165  1  N  VAL B 165   O  ALA B 151           
LINK         C   TYR A 301                 N   PXU A 302     1555   1555  1.33  
LINK         C   PXU A 302                 N   PHE A 303     1555   1555  1.34  
LINK         C   TYR B 301                 N   PXU B 302     1555   1555  1.33  
LINK         C   PXU B 302                 N   PHE B 303     1555   1555  1.34  
LINK         OD1 ASP A 206                ZN    ZN A1362     1555   1555  2.14  
LINK         NE2 HIS A 264                ZN    ZN A1362     1555   1555  2.16  
LINK         NE2 HIS A 268                ZN    ZN A1362     1555   1555  2.13  
LINK         O   ACT A1361                ZN    ZN A1362     1555   1555  2.35  
LINK        ZN    ZN A1362                 O   HOH A2196     1555   1555  2.04  
LINK         OD1 ASP B 206                ZN    ZN B1362     1555   1555  2.13  
LINK         NE2 HIS B 264                ZN    ZN B1362     1555   1555  2.18  
LINK         NE2 HIS B 268                ZN    ZN B1362     1555   1555  2.10  
LINK         O   ACT B1361                ZN    ZN B1362     1555   1555  2.39  
LINK        ZN    ZN B1362                 O   HOH B2152     1555   1555  2.04  
SITE     1 AC1 10 HIS A 150  ASP A 205  HIS A 264  HIS A 268                    
SITE     2 AC1 10 TYR A 301  PXU A 302  PHE A 303  THR A 324                    
SITE     3 AC1 10  ZN A1362  HOH A2196                                          
SITE     1 AC2  6 ASP A 206  HIS A 264  HIS A 268  PXU A 302                    
SITE     2 AC2  6 ACT A1361  HOH A2196                                          
SITE     1 AC3 10 HIS B 150  ASP B 205  HIS B 264  HIS B 268                    
SITE     2 AC3 10 TYR B 301  PXU B 302  PHE B 303  THR B 324                    
SITE     3 AC3 10  ZN B1362  HOH B2152                                          
SITE     1 AC4  6 ASP B 206  HIS B 264  HIS B 268  PXU B 302                    
SITE     2 AC4  6 ACT B1361  HOH B2152                                          
SITE     1 AC5  4 TYR A 176  TYR A 182  LYS A 198  HOH A2277                    
SITE     1 AC6  4 TYR B 176  TYR B 182  LYS B 198  HOH B2217                    
SITE     1 AC7  4 PRO B  53  ASN B  60  ASP B 223  ASP B 224                    
SITE     1 AC8  6 TYR B 182  THR B 183  LEU B 184  PHE B 226                    
SITE     2 AC8  6 LYS B 227  HOH B2444                                          
SITE     1 AC9  5 THR A 186  GLU A 188  GLY A 257  HOH A2358                    
SITE     2 AC9  5 HOH A2497                                                     
SITE     1 BC1  7 TYR A 182  THR A 183  LEU A 184  THR A 225                    
SITE     2 BC1  7 PHE A 226  LYS A 227  HOH A2498                               
CRYST1  108.964   68.763  132.022  90.00  96.86  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009177  0.000000  0.001104        0.00000                         
SCALE2      0.000000  0.014543  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007629        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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