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Database: PDB
Entry: 2DCZ
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HEADER    HYDROLASE                               18-JAN-06   2DCZ              
TITLE     THERMAL STABILIZATION OF BACILLUS SUBTILIS FAMILY-11                  
TITLE    2 XYLANASE BY DIRECTED EVOLUTION                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDO-1,4-BETA-XYLANASE A;                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: XYLANASE A, 1,4-BETA-D-XYLAN XYLANOHYDROLASE A;             
COMPND   5 EC: 3.2.1.8;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 GENE: XYNA;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: JM109;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PTD-TAC                                   
KEYWDS    ALL BETA, HYDROLASE                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.KONDO,K.MIYAZAKI,M.TAKENOUCHI,N.NORO,M.SUZUKI,S.TSUDA               
REVDAT   3   24-FEB-09 2DCZ    1       VERSN                                    
REVDAT   2   25-APR-06 2DCZ    1       JRNL                                     
REVDAT   1   07-FEB-06 2DCZ    0                                                
JRNL        AUTH   K.MIYAZAKI,M.TAKENOUCHI,H.KONDO,N.NORO,M.SUZUKI,             
JRNL        AUTH 2 S.TSUDA                                                      
JRNL        TITL   THERMAL STABILIZATION OF BACILLUS SUBTILIS                   
JRNL        TITL 2 FAMILY-11 XYLANASE BY DIRECTED EVOLUTION                     
JRNL        REF    J.BIOL.CHEM.                  V. 281 10236 2006              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   16467302                                                     
JRNL        DOI    10.1074/JBC.M511948200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 33471                          
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) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1764                            
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) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2436                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2260                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 122                          
REMARK   3   BIN FREE R VALUE                    : 0.2840                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2902                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 11                                      
REMARK   3   SOLVENT ATOMS            : 154                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.89                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.44000                                              
REMARK   3    B22 (A**2) : 1.44000                                              
REMARK   3    B33 (A**2) : -2.16000                                             
REMARK   3    B12 (A**2) : 0.72000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.146         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.131         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.085         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.826         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.931                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3013 ; 0.009 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4130 ; 1.114 ; 1.878       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   368 ; 6.888 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   142 ;34.306 ;23.239       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   388 ;11.136 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;10.529 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   416 ; 0.067 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2410 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1168 ; 0.176 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1967 ; 0.308 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   191 ; 0.087 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    55 ; 0.142 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    14 ; 0.054 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1843 ; 0.357 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2914 ; 0.658 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1457 ; 0.788 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1216 ; 1.117 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2DCZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-JAN-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB025268.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-DEC-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NW12A                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35270                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 124.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 10.500                             
REMARK 200  R MERGE                    (I) : 0.06200                            
REMARK 200  R SYM                      (I) : 0.06200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.60                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.22100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.22100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1XNB                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, 1.1-1.2M AMMONIUM              
REMARK 280  SULFATE, 10% DEOXANE, 25MM DTT, PH 6.0, VAPOR DIFFUSION,            
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3                                      
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3                                   
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3                                  
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3                                      
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3                                   
REMARK 290      18555   -X+1/3,-X+Y+2/3,-Z+2/3                                  
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000       39.09150            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       22.56949            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000      124.11633            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       39.09150            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       22.56949            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000      124.11633            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       39.09150            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       22.56949            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      124.11633            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       39.09150            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       22.56949            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      124.11633            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       39.09150            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       22.56949            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      124.11633            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       39.09150            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       22.56949            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      124.11633            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       45.13898            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000      248.23267            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       45.13898            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000      248.23267            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       45.13898            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      248.23267            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       45.13898            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      248.23267            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       45.13898            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000      248.23267            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       45.13898            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000      248.23267            
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2710 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.0 KCAL/MOL                        
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   BIOMT1   2 -0.500000 -0.866025  0.000000      117.27450            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000       67.70846            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      135.41693            
REMARK 350   BIOMT3   3  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 A 306  LIES ON A SPECIAL POSITION.                          
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    CYS A 179   CB    CYS A 179   SG      0.286                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A 179   CB  -  CA  -  C   ANGL. DEV. =  10.2 DEGREES          
REMARK 500    CYS A 179   CA  -  CB  -  SG  ANGL. DEV. =  13.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  32       58.66     38.97                                   
REMARK 500    SER A  74       64.80     60.21                                   
REMARK 500    ALA A 165     -157.70    -92.46                                   
REMARK 500    ALA B 165     -156.46    -98.14                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 201                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO A 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2DCY   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN(WILD TYPE)                                          
DBREF  2DCZ A    1   185  UNP    P18429   XYNA_BACSU      29    213             
DBREF  2DCZ B    1   185  UNP    P18429   XYNA_BACSU      29    213             
SEQADV 2DCZ HIS A    7  UNP  P18429    GLN    35 ENGINEERED                     
SEQADV 2DCZ PHE A    8  UNP  P18429    ASN    36 ENGINEERED                     
SEQADV 2DCZ CYS A  179  UNP  P18429    SER   207 ENGINEERED                     
SEQADV 2DCZ HIS B    7  UNP  P18429    GLN    35 ENGINEERED                     
SEQADV 2DCZ PHE B    8  UNP  P18429    ASN    36 ENGINEERED                     
SEQADV 2DCZ CYS B  179  UNP  P18429    SER   207 ENGINEERED                     
SEQRES   1 A  185  ALA SER THR ASP TYR TRP HIS PHE TRP THR ASP GLY GLY          
SEQRES   2 A  185  GLY ILE VAL ASN ALA VAL ASN GLY SER GLY GLY ASN TYR          
SEQRES   3 A  185  SER VAL ASN TRP SER ASN THR GLY ASN PHE VAL VAL GLY          
SEQRES   4 A  185  LYS GLY TRP THR THR GLY SER PRO PHE ARG THR ILE ASN          
SEQRES   5 A  185  TYR ASN ALA GLY VAL TRP ALA PRO ASN GLY ASN GLY TYR          
SEQRES   6 A  185  LEU THR LEU TYR GLY TRP THR ARG SER PRO LEU ILE GLU          
SEQRES   7 A  185  TYR TYR VAL VAL ASP SER TRP GLY THR TYR ARG PRO THR          
SEQRES   8 A  185  GLY THR TYR LYS GLY THR VAL LYS SER ASP GLY GLY THR          
SEQRES   9 A  185  TYR ASP ILE TYR THR THR THR ARG TYR ASN ALA PRO SER          
SEQRES  10 A  185  ILE ASP GLY ASP ARG THR THR PHE THR GLN TYR TRP SER          
SEQRES  11 A  185  VAL ARG GLN SER LYS ARG PRO THR GLY SER ASN ALA THR          
SEQRES  12 A  185  ILE THR PHE SER ASN HIS VAL ASN ALA TRP LYS SER HIS          
SEQRES  13 A  185  GLY MET ASN LEU GLY SER ASN TRP ALA TYR GLN VAL MET          
SEQRES  14 A  185  ALA THR GLU GLY TYR GLN SER SER GLY CYS SER ASN VAL          
SEQRES  15 A  185  THR VAL TRP                                                  
SEQRES   1 B  185  ALA SER THR ASP TYR TRP HIS PHE TRP THR ASP GLY GLY          
SEQRES   2 B  185  GLY ILE VAL ASN ALA VAL ASN GLY SER GLY GLY ASN TYR          
SEQRES   3 B  185  SER VAL ASN TRP SER ASN THR GLY ASN PHE VAL VAL GLY          
SEQRES   4 B  185  LYS GLY TRP THR THR GLY SER PRO PHE ARG THR ILE ASN          
SEQRES   5 B  185  TYR ASN ALA GLY VAL TRP ALA PRO ASN GLY ASN GLY TYR          
SEQRES   6 B  185  LEU THR LEU TYR GLY TRP THR ARG SER PRO LEU ILE GLU          
SEQRES   7 B  185  TYR TYR VAL VAL ASP SER TRP GLY THR TYR ARG PRO THR          
SEQRES   8 B  185  GLY THR TYR LYS GLY THR VAL LYS SER ASP GLY GLY THR          
SEQRES   9 B  185  TYR ASP ILE TYR THR THR THR ARG TYR ASN ALA PRO SER          
SEQRES  10 B  185  ILE ASP GLY ASP ARG THR THR PHE THR GLN TYR TRP SER          
SEQRES  11 B  185  VAL ARG GLN SER LYS ARG PRO THR GLY SER ASN ALA THR          
SEQRES  12 B  185  ILE THR PHE SER ASN HIS VAL ASN ALA TRP LYS SER HIS          
SEQRES  13 B  185  GLY MET ASN LEU GLY SER ASN TRP ALA TYR GLN VAL MET          
SEQRES  14 B  185  ALA THR GLU GLY TYR GLN SER SER GLY CYS SER ASN VAL          
SEQRES  15 B  185  THR VAL TRP                                                  
HET    SO4  A 201       5                                                       
HET    DIO  A 301       6                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     DIO 1,4-DIETHYLENE DIOXIDE                                           
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  DIO    C4 H8 O2                                                     
FORMUL   5  HOH   *154(H2 O)                                                    
HELIX    1   1 PHE A  146  HIS A  156  1                                  11    
HELIX    2   2 PHE B  146  HIS B  156  1                                  11    
SHEET    1   A 8 TYR A   5  THR A  10  0                                        
SHEET    2   A 8 ASN A  35  TRP A  42 -1  O  GLY A  39   N  HIS A   7           
SHEET    3   A 8 ASN A 163  TRP A 185 -1  O  THR A 171   N  VAL A  38           
SHEET    4   A 8 THR A  50  ARG A  73 -1  N  THR A  67   O  ALA A 170           
SHEET    5   A 8 ILE A  77  TRP A  85 -1  O  TYR A  79   N  GLY A  70           
SHEET    6   A 8 GLY A 120  ARG A 132  1  O  SER A 130   N  VAL A  82           
SHEET    7   A 8 GLY A 103  SER A 117 -1  N  ARG A 112   O  PHE A 125           
SHEET    8   A 8 THR A  93  SER A 100 -1  N  GLY A  96   O  ILE A 107           
SHEET    1   B 5 ILE A  15  ASN A  20  0                                        
SHEET    2   B 5 ASN A  25  SER A  31 -1  O  ASN A  29   N  ASN A  17           
SHEET    3   B 5 ASN A 163  TRP A 185 -1  O  SER A 180   N  VAL A  28           
SHEET    4   B 5 THR A  50  ARG A  73 -1  N  THR A  67   O  ALA A 170           
SHEET    5   B 5 ALA A 142  THR A 145 -1  O  ALA A 142   N  TYR A  53           
SHEET    1   C 8 TYR B   5  THR B  10  0                                        
SHEET    2   C 8 ASN B  35  TRP B  42 -1  O  GLY B  39   N  HIS B   7           
SHEET    3   C 8 ASN B 163  TRP B 185 -1  O  THR B 171   N  VAL B  38           
SHEET    4   C 8 THR B  50  ARG B  73 -1  N  ARG B  73   O  ASN B 163           
SHEET    5   C 8 ILE B  77  TRP B  85 -1  O  SER B  84   N  LEU B  66           
SHEET    6   C 8 GLY B 120  ARG B 132  1  O  SER B 130   N  VAL B  82           
SHEET    7   C 8 GLY B 103  SER B 117 -1  N  ARG B 112   O  PHE B 125           
SHEET    8   C 8 THR B  93  SER B 100 -1  N  GLY B  96   O  ILE B 107           
SHEET    1   D 5 ILE B  15  ASN B  20  0                                        
SHEET    2   D 5 ASN B  25  SER B  31 -1  O  ASN B  29   N  ASN B  17           
SHEET    3   D 5 ASN B 163  TRP B 185 -1  O  VAL B 182   N  TYR B  26           
SHEET    4   D 5 THR B  50  ARG B  73 -1  N  ARG B  73   O  ASN B 163           
SHEET    5   D 5 ALA B 142  THR B 145 -1  O  ALA B 142   N  TYR B  53           
SSBOND   1 CYS A  179    CYS B  179                          1555   1555  2.08  
CISPEP   1 SER A   74    PRO A   75          0        -2.64                     
CISPEP   2 SER B   74    PRO B   75          0        -3.04                     
SITE     1 AC1  8 SER A  74  LEU A  76  THR A  93  THR A 109                    
SITE     2 AC1  8 THR A 111  HOH A 316  HOH A 326  HOH A 353                    
SITE     1 AC2  4 VAL A  16  ALA A  18  VAL B  19  GLY B  21                    
CRYST1   78.183   78.183  372.349  90.00  90.00 120.00 H 3 2        36          
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      0.012791  0.007385  0.000000        0.00000                         
SCALE2      0.000000  0.014769  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002686        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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