GenomeNet

Database: PDB
Entry: 2UYA
LinkDB: 2UYA
Original site: 2UYA 
HEADER    LYASE                                   03-APR-07   2UYA              
TITLE     DEL162-163 MUTANT OF BACILLUS SUBTILIS OXALATE                        
TITLE    2 DECARBOXYLASE OXDC                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: OXALATE DECARBOXYLASE OXDC;                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 1-161,164-385;                                    
COMPND   5 EC: 4.1.1.2;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 STRAIN: 168;                                                         
SOURCE   5 ATCC: 23857;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET32A;                                    
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PLB36                                     
KEYWDS    LYASE, CUPIN, FORMATE, OXALATE, MANGANESE, METAL BINDING              
KEYWDS   2 PROTEIN, METAL-BINDING, DECARBOXYLASE, DEL162-163 MUTANT             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.J.JUST,M.R.BURRELL,L.BOWATER,I.MCROBBIE,C.E.M.STEVENSON,            
AUTHOR   2 D.M.LAWSON,S.BORNEMANN                                               
REVDAT   2   24-FEB-09 2UYA    1       VERSN                                    
REVDAT   1   21-AUG-07 2UYA    0                                                
JRNL        AUTH   V.J.JUST,M.R.BURRELL,L.BOWATER,I.MCROBBIE,                   
JRNL        AUTH 2 C.E.M.STEVENSON,D.M.LAWSON,S.BORNEMANN                       
JRNL        TITL   THE IDENTITY OF THE ACTIVE SITE OF OXALATE                   
JRNL        TITL 2 DECARBOXYLASE AND THE IMPORTANCE OF THE STABILITY            
JRNL        TITL 3 OF ACTIVE-SITE LID CONFORMATIONS.                            
JRNL        REF    BIOCHEM.J.                    V. 407   397 2007              
JRNL        REFN                   ISSN 0264-6021                               
JRNL        PMID   17680775                                                     
JRNL        DOI    10.1042/BJ20070708                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 58.93                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 38269                          
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) : 0.130                           
REMARK   3   R VALUE            (WORKING SET) : 0.129                           
REMARK   3   FREE R VALUE                     : 0.166                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1908                            
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) : 8.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 58.93                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 460                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2080                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 27                           
REMARK   3   BIN FREE R VALUE                    : 0.2600                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2983                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 17                                      
REMARK   3   SOLVENT ATOMS            : 411                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.51                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.78                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.34900                                             
REMARK   3    B22 (A**2) : -0.34900                                             
REMARK   3    B33 (A**2) : 0.52300                                              
REMARK   3    B12 (A**2) : -0.17400                                             
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): 0.101         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.104         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.060         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.054         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3077 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4177 ; 1.499 ; 1.950       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   373 ; 6.408 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   150 ;30.037 ;24.400       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   497 ;11.601 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;20.167 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   442 ; 0.099 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3432 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   493 ; 0.210 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1440 ; 0.175 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   308 ; 0.179 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    45 ; 0.194 ; 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):  2042 ; 1.160 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3026 ; 1.576 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1342 ; 2.614 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1151 ; 3.869 ; 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 : MASK BULK SOLVENT                                    
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2UYA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  03-APR-07.                 
REMARK 100 THE PDBE ID CODE IS EBI-32181.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-SEP-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38270                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.00                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 58.93                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 8.87                               
REMARK 200  R MERGE                    (I) : 0.10                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.21                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.99                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.55                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC5                                               
REMARK 200 STARTING MODEL: PDB ENTRY 1UW8                                       
REMARK 200                                                                      
REMARK 200 REMARK: STARTING PHASES WERE OBTAINED BY RIGID BODY                  
REMARK 200  REFINEMENT OF 1UW8                                                  
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.2                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8-15% PEG 8000, 0.1 M TRIS               
REMARK 280  PH8.5, 0-15% XYLITOL                                                
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       77.42850            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       44.70337            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       41.09133            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       77.42850            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       44.70337            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       41.09133            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       77.42850            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       44.70337            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       41.09133            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       77.42850            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       44.70337            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       41.09133            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       77.42850            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       44.70337            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       41.09133            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       77.42850            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       44.70337            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       41.09133            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       89.40673            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       82.18267            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       89.40673            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       82.18267            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       89.40673            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000       82.18267            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       89.40673            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       82.18267            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       89.40673            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000       82.18267            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       89.40673            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000       82.18267            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 51480 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 84080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -355.9 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        0.00000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
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        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   5 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   6 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     ASN A     5                                                      
REMARK 465     CYS A   383                                                      
REMARK 465     SER A   384                                                      
REMARK 465     LYS A   385                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 221    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 234    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 380    CD   CE   NZ                                        
REMARK 470     LYS A 382    CE   NZ                                             
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   OG   SER A   136  -  O    HOH A  2195              2.18            
REMARK 500   O    SER A   161  -  N    SER A   164              2.19            
REMARK 500   O    HOH A  2024  -  O    HOH A  2058              2.13            
REMARK 500   O    HOH A  2194  -  O    HOH A  2208              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    SER A 161   C     SER A 164   N       0.203                       
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    SER A 161   O   -  C   -  N   ANGL. DEV. = -19.4 DEGREES          
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 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  31       56.55   -118.86                                   
REMARK 500    LEU A  94      122.46    -39.10                                   
REMARK 500    LEU A 145     -156.91    -92.36                                   
REMARK 500    ASP A 156       38.75    -86.51                                   
REMARK 500    PHE A 160      126.70    -37.36                                   
REMARK 500    SER A 161      -42.37   -142.53                                   
REMARK 500    TYR A 200      -70.44     70.48                                   
REMARK 500    SER A 296      168.59     76.93                                   
REMARK 500    PHE A 315      116.49    -33.48                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    SER A 161        -27.29                                           
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 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                              MN A1383  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  97   NE2                                                    
REMARK 620 2 GLU A 101   OE1  86.0                                              
REMARK 620 3 HOH A2405   O   166.9  82.3                                        
REMARK 620 4 HOH A2406   O    84.4  94.6  90.6                                  
REMARK 620 5 HIS A  95   NE2 104.0 169.8  87.9  88.5                            
REMARK 620 6 HIS A 140   NE2  92.7  91.5  93.5 173.1  86.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A1384  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 275   NE2                                                    
REMARK 620 2 GLU A 280   OE1  80.9                                              
REMARK 620 3 HIS A 319   NE2 107.4  93.1                                        
REMARK 620 4 HOH A2407   O   154.2  93.2  98.0                                  
REMARK 620 5 HIS A 273   NE2  91.5 170.0  82.9  96.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN A1383                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN A1384                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A1385                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1386                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1387                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1J58   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF OXALATE DECARBOXYLASE                          
REMARK 900 RELATED ID: 1L3J   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF OXALATE DECARBOXYLASE                          
REMARK 900  FORMATE COMPLEX                                                     
REMARK 900 RELATED ID: 1UW8   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF OXALATE DECARBOXYLASE                          
REMARK 900 RELATED ID: 2UY9   RELATED DB: PDB                                   
REMARK 900  E162A MUTANT OF BACILLUS SUBTILIS OXALATE                           
REMARK 900  DECARBOXYLASE OXDC                                                  
REMARK 900 RELATED ID: 2UYB   RELATED DB: PDB                                   
REMARK 900  S161A MUTANT OF BACILLUS SUBTILIS OXALATE                           
REMARK 900  DECARBOXYLASE OXDC                                                  
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 DEL162-163 MUTANT                                                    
DBREF  2UYA A    1   161  UNP    O34714   OXDC_BACSU       1    161             
DBREF  2UYA A  164   385  UNP    O34714   OXDC_BACSU     164    385             
SEQRES   1 A  383  MET LYS LYS GLN ASN ASP ILE PRO GLN PRO ILE ARG GLY          
SEQRES   2 A  383  ASP LYS GLY ALA THR VAL LYS ILE PRO ARG ASN ILE GLU          
SEQRES   3 A  383  ARG ASP ARG GLN ASN PRO ASP MET LEU VAL PRO PRO GLU          
SEQRES   4 A  383  THR ASP HIS GLY THR VAL SER ASN MET LYS PHE SER PHE          
SEQRES   5 A  383  SER ASP THR HIS ASN ARG LEU GLU LYS GLY GLY TYR ALA          
SEQRES   6 A  383  ARG GLU VAL THR VAL ARG GLU LEU PRO ILE SER GLU ASN          
SEQRES   7 A  383  LEU ALA SER VAL ASN MET ARG LEU LYS PRO GLY ALA ILE          
SEQRES   8 A  383  ARG GLU LEU HIS TRP HIS LYS GLU ALA GLU TRP ALA TYR          
SEQRES   9 A  383  MET ILE TYR GLY SER ALA ARG VAL THR ILE VAL ASP GLU          
SEQRES  10 A  383  LYS GLY ARG SER PHE ILE ASP ASP VAL GLY GLU GLY ASP          
SEQRES  11 A  383  LEU TRP TYR PHE PRO SER GLY LEU PRO HIS SER ILE GLN          
SEQRES  12 A  383  ALA LEU GLU GLU GLY ALA GLU PHE LEU LEU VAL PHE ASP          
SEQRES  13 A  383  ASP GLY SER PHE SER SER THR PHE GLN LEU THR ASP TRP          
SEQRES  14 A  383  LEU ALA HIS THR PRO LYS GLU VAL ILE ALA ALA ASN PHE          
SEQRES  15 A  383  GLY VAL THR LYS GLU GLU ILE SER ASN LEU PRO GLY LYS          
SEQRES  16 A  383  GLU LYS TYR ILE PHE GLU ASN GLN LEU PRO GLY SER LEU          
SEQRES  17 A  383  LYS ASP ASP ILE VAL GLU GLY PRO ASN GLY GLU VAL PRO          
SEQRES  18 A  383  TYR PRO PHE THR TYR ARG LEU LEU GLU GLN GLU PRO ILE          
SEQRES  19 A  383  GLU SER GLU GLY GLY LYS VAL TYR ILE ALA ASP SER THR          
SEQRES  20 A  383  ASN PHE LYS VAL SER LYS THR ILE ALA SER ALA LEU VAL          
SEQRES  21 A  383  THR VAL GLU PRO GLY ALA MET ARG GLU LEU HIS TRP HIS          
SEQRES  22 A  383  PRO ASN THR HIS GLU TRP GLN TYR TYR ILE SER GLY LYS          
SEQRES  23 A  383  ALA ARG MET THR VAL PHE ALA SER ASP GLY HIS ALA ARG          
SEQRES  24 A  383  THR PHE ASN TYR GLN ALA GLY ASP VAL GLY TYR VAL PRO          
SEQRES  25 A  383  PHE ALA MET GLY HIS TYR VAL GLU ASN ILE GLY ASP GLU          
SEQRES  26 A  383  PRO LEU VAL PHE LEU GLU ILE PHE LYS ASP ASP HIS TYR          
SEQRES  27 A  383  ALA ASP VAL SER LEU ASN GLN TRP LEU ALA MET LEU PRO          
SEQRES  28 A  383  GLU THR PHE VAL GLN ALA HIS LEU ASP LEU GLY LYS ASP          
SEQRES  29 A  383  PHE THR ASP VAL LEU SER LYS GLU LYS HIS PRO VAL VAL          
SEQRES  30 A  383  LYS LYS LYS CYS SER LYS                                      
HET     MN  A1383       1                                                       
HET     MN  A1384       1                                                       
HET    TRS  A1385       8                                                       
HET    GOL  A1386       6                                                       
HET     CL  A1387       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   2   MN    2(MN 2+)                                                     
FORMUL   3   CL    CL 1-                                                        
FORMUL   4  GOL    C3 H8 O3                                                     
FORMUL   5  TRS    C4 H12 N O3 1+                                               
FORMUL   6  HOH   *411(H2 O1)                                                   
HELIX    1   1 ASN A   24  ASN A   31  1                                   8    
HELIX    2   2 ASN A   31  VAL A   36  1                                   6    
HELIX    3   3 SER A   53  THR A   55  5                                   3    
HELIX    4   4 LEU A  168  HIS A  174  1                                   7    
HELIX    5   5 PRO A  176  GLY A  185  1                                  10    
HELIX    6   6 LYS A  188  SER A  192  5                                   5    
HELIX    7   7 SER A  209  ILE A  214  1                                   6    
HELIX    8   8 LEU A  231  GLN A  233  5                                   3    
HELIX    9   9 LEU A  345  MET A  351  1                                   7    
HELIX   10  10 PRO A  353  ASP A  362  1                                  10    
HELIX   11  11 GLY A  364  ASP A  369  1                                   6    
SHEET    1  AA 2 ILE A  11  ARG A  12  0                                        
SHEET    2  AA 2 LYS A  15  GLY A  16 -1  O  LYS A  15   N  ARG A  12           
SHEET    1  AB 7 LYS A  49  SER A  51  0                                        
SHEET    2  AB 7 ASP A 309  VAL A 313 -1  O  VAL A 310   N  PHE A  50           
SHEET    3  AB 7 GLU A 280  SER A 286 -1  O  GLU A 280   N  VAL A 313           
SHEET    4  AB 7 LEU A 329  PHE A 335 -1  O  VAL A 330   N  SER A 286           
SHEET    5  AB 7 ALA A 258  VAL A 264 -1  O  ALA A 258   N  PHE A 335           
SHEET    6  AB 7 GLY A 241  ALA A 246 -1  O  LYS A 242   N  THR A 263           
SHEET    7  AB 7 ILE A 236  SER A 238 -1  O  ILE A 236   N  VAL A 243           
SHEET    1  AC 5 ARG A  58  GLU A  60  0                                        
SHEET    2  AC 5 GLY A  63  VAL A  68 -1  O  GLY A  63   N  GLU A  60           
SHEET    3  AC 5 ALA A  80  LEU A  86 -1  O  SER A  81   N  VAL A  68           
SHEET    4  AC 5 HIS A 140  PHE A 155 -1  O  ALA A 149   N  LEU A  86           
SHEET    5  AC 5 ILE A  91  TRP A  96 -1  O  ARG A  92   N  ILE A 142           
SHEET    1  AD 5 ARG A  58  GLU A  60  0                                        
SHEET    2  AD 5 GLY A  63  VAL A  68 -1  O  GLY A  63   N  GLU A  60           
SHEET    3  AD 5 ALA A  80  LEU A  86 -1  O  SER A  81   N  VAL A  68           
SHEET    4  AD 5 HIS A 140  PHE A 155 -1  O  ALA A 149   N  LEU A  86           
SHEET    5  AD 5 GLU A 101  VAL A 115 -1  O  TRP A 102   N  VAL A 154           
SHEET    1  AE 5 HIS A 299  GLN A 306  0                                        
SHEET    2  AE 5 LYS A 288  SER A 296 -1  O  ALA A 289   N  TYR A 305           
SHEET    3  AE 5 HIS A 319  ASN A 323 -1  O  GLU A 322   N  ARG A 290           
SHEET    4  AE 5 ALA A 268  TRP A 274 -1  O  ALA A 268   N  ASN A 323           
SHEET    5  AE 5 VAL A 378  LYS A 380 -1  O  VAL A 379   N  MET A 269           
SHEET    1  AF 5 HIS A 299  GLN A 306  0                                        
SHEET    2  AF 5 LYS A 288  SER A 296 -1  O  ALA A 289   N  TYR A 305           
SHEET    3  AF 5 HIS A 319  ASN A 323 -1  O  GLU A 322   N  ARG A 290           
SHEET    4  AF 5 ALA A 268  TRP A 274 -1  O  ALA A 268   N  ASN A 323           
SHEET    5  AF 5 VAL A 343  SER A 344 -1  O  VAL A 343   N  TRP A 274           
LINK        MN    MN A1383                 NE2 HIS A  97     1555   1555  2.34  
LINK        MN    MN A1383                 OE1 GLU A 101     1555   1555  2.09  
LINK        MN    MN A1383                 O   HOH A2405     1555   1555  2.37  
LINK        MN    MN A1383                 O   HOH A2406     1555   1555  2.31  
LINK        MN    MN A1383                 NE2 HIS A  95     1555   1555  2.28  
LINK        MN    MN A1383                 NE2 HIS A 140     1555   1555  2.29  
LINK        MN    MN A1384                 OE1 GLU A 280     1555   1555  2.06  
LINK        MN    MN A1384                 NE2 HIS A 319     1555   1555  2.30  
LINK        MN    MN A1384                 O   HOH A2407     1555   1555  2.19  
LINK        MN    MN A1384                 NE2 HIS A 273     1555   1555  2.33  
LINK        MN    MN A1384                 NE2 HIS A 275     1555   1555  2.20  
SITE     1 AC1  6 HIS A  95  HIS A  97  GLU A 101  HIS A 140                    
SITE     2 AC1  6 HOH A2405  HOH A2406                                          
SITE     1 AC2  6 HIS A 273  HIS A 275  GLU A 280  HIS A 319                    
SITE     2 AC2  6 GLU A 333  HOH A2407                                          
SITE     1 AC3  9 GLU A 117  PRO A 135  SER A 136  ASN A 277                    
SITE     2 AC3  9 HIS A 339  ALA A 341  HOH A2408  HOH A2409                    
SITE     3 AC3  9 HOH A2410                                                     
SITE     1 AC4  4 GLY A  43  HIS A  56  ARG A  58  HOH A2411                    
SITE     1 AC5  4 ARG A  92  HOH A2149  HOH A2255  HOH A2406                    
CRYST1  154.857  154.857  123.274  90.00  90.00 120.00 H 3 2        18          
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      0.006458  0.003728  0.000000        0.00000                         
SCALE2      0.000000  0.007457  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008112        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system