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Database: PDB
Entry: 4EGQ
LinkDB: 4EGQ
Original site: 4EGQ 
HEADER    LIGASE                                  31-MAR-12   4EGQ              
TITLE     CRYSTAL STRUCTURE OF D-ALANINE-D-ALANINE LIGASE B FROM BURKHOLDERIA   
TITLE    2 PSEUDOMALLEI                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-ALANINE--D-ALANINE LIGASE;                               
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: D-ALA-D-ALA LIGASE, D-ALANYLALANINE SYNTHETASE;             
COMPND   5 EC: 6.3.2.4;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BURKHOLDERIA PSEUDOMALLEI;                      
SOURCE   3 ORGANISM_TAXID: 320372;                                              
SOURCE   4 STRAIN: 1710B;                                                       
SOURCE   5 GENE: BURPS1710B_3542, DDL;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PAVA0421                              
KEYWDS    STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR           
KEYWDS   2 INFECTIOUS DISEASE, SSGCID, FLEXIBLE PROTEIN, ATP-DEPENDENT,         
KEYWDS   3 MAGNESIUM DEPENDENT, CELL WALL BIOGENESIS, LIGASE                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)    
REVDAT   1   11-APR-12 4EGQ    0                                                
JRNL        AUTH   T.E.EDWARDS,J.W.FAIRMAN,J.ABENDROTH,                         
JRNL        AUTH 2 SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE    
JRNL        AUTH 3 (SSGCID)                                                     
JRNL        TITL   CRYSTAL STRUCTURE OF D-ALANINE-D-ALANINE LIGASE B FROM       
JRNL        TITL 2 BURKHOLDERIA PSEUDOMALLEI                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.27                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 54818                          
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) : 0.212                           
REMARK   3   R VALUE            (WORKING SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2772                            
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3520                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.73                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2460                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 171                          
REMARK   3   BIN FREE R VALUE                    : 0.2860                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8399                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 193                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.91                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.37000                                             
REMARK   3    B22 (A**2) : -0.69000                                             
REMARK   3    B33 (A**2) : 0.46000                                              
REMARK   3    B12 (A**2) : -0.04000                                             
REMARK   3    B13 (A**2) : 1.48000                                              
REMARK   3    B23 (A**2) : 0.59000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.331         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.230         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.157         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.690        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.909                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8574 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5518 ; 0.007 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11706 ; 1.472 ; 1.976       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 13436 ; 1.411 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1169 ; 5.395 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   304 ;28.622 ;22.895       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1141 ;13.126 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    53 ;18.491 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1360 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9901 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1792 ; 0.006 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     4        A   311                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.7179   5.7003  75.2454              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0903 T22:   0.1335                                     
REMARK   3      T33:   0.0234 T12:  -0.0430                                     
REMARK   3      T13:   0.0154 T23:   0.0180                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6652 L22:   1.3006                                     
REMARK   3      L33:   1.1073 L12:   0.1367                                     
REMARK   3      L13:  -0.0221 L23:  -0.0526                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0508 S12:   0.1642 S13:   0.0980                       
REMARK   3      S21:  -0.2609 S22:   0.0551 S23:  -0.0830                       
REMARK   3      S31:   0.1249 S32:   0.1394 S33:  -0.0043                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     5        B   312                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.8287 -27.6314  28.2687              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0568 T22:   0.0282                                     
REMARK   3      T33:   0.0487 T12:   0.0060                                     
REMARK   3      T13:  -0.0091 T23:   0.0142                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3763 L22:   1.2497                                     
REMARK   3      L33:   0.4139 L12:  -0.0330                                     
REMARK   3      L13:  -0.0408 L23:   0.2046                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0320 S12:   0.0534 S13:   0.0315                       
REMARK   3      S21:  -0.2223 S22:  -0.0615 S23:  -0.0510                       
REMARK   3      S31:  -0.0114 S32:  -0.0482 S33:   0.0296                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     4        C   311                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.9188  -9.2114   3.0765              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0844 T22:   0.0811                                     
REMARK   3      T33:   0.0629 T12:  -0.0156                                     
REMARK   3      T13:  -0.0024 T23:  -0.0181                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6549 L22:   0.6348                                     
REMARK   3      L33:   0.5921 L12:   0.0812                                     
REMARK   3      L13:   0.3566 L23:   0.0901                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0386 S12:   0.0113 S13:  -0.0433                       
REMARK   3      S21:   0.0092 S22:   0.0320 S23:   0.0066                       
REMARK   3      S31:   0.1348 S32:   0.0393 S33:   0.0066                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     4        D   311                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.4922 -47.7892  47.5769              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0497 T22:   0.0621                                     
REMARK   3      T33:   0.0278 T12:  -0.0296                                     
REMARK   3      T13:   0.0003 T23:  -0.0032                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4959 L22:   0.7595                                     
REMARK   3      L33:   0.8841 L12:   0.2078                                     
REMARK   3      L13:  -0.0080 L23:  -0.0744                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0313 S12:  -0.0767 S13:  -0.0118                       
REMARK   3      S21:   0.0448 S22:  -0.0196 S23:   0.1016                       
REMARK   3      S31:   0.1041 S32:   0.0648 S33:  -0.0117                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  U VALUES: WITH TLS ADDED HYDROGENS HAVE BEEN ADDED IN THE RIDING    
REMARK   3  POSITIONS                                                           
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3  NCS TYPE: LOCAL                                                     
REMARK   3  NUMBER OF DIFFERENT NCS PAIRS:   6                                  
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     5    311       B     5    311    8225  0.09  0.05     
REMARK   3    2     A     4    311       C     4    311    7892  0.13  0.05     
REMARK   3    3     A     4    311       D     4    311    7741  0.11  0.05     
REMARK   3    4     B     5    310       C     5    310    8154  0.13  0.05     
REMARK   3    5     B     5    311       D     5    311    8071  0.12  0.05     
REMARK   3    6     C     4    311       D     4    311    7824  0.12  0.05     
REMARK   4                                                                      
REMARK   4 4EGQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-APR-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB071596.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-AUG-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97946                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54908                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.12400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.4370                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.24                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4EG0                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: BUPSA.00119.A.A1 PW25270 AT 30.8 MG/ML   
REMARK 280  AGAINST WIZARD FULL SCREEN CONDITION D2, 1 M NAK TARTRATE, 0.1 M    
REMARK 280  CHES PH 9.5, 0.2 M LI2SO4, CRYSTAL TRACKING ID 203378D2, VAPOR      
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 289K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5                                           
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 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 46920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000       29.12224            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000       -7.73000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000      -96.89850            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000       45.38900            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  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     GLY A    -3                                                      
REMARK 465     PRO A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     GLU A   152                                                      
REMARK 465     GLY A   153                                                      
REMARK 465     SER A   154                                                      
REMARK 465     ALA A   211                                                      
REMARK 465     GLY A   212                                                      
REMARK 465     GLU A   213                                                      
REMARK 465     PHE A   214                                                      
REMARK 465     TYR A   215                                                      
REMARK 465     ASP A   216                                                      
REMARK 465     TYR A   217                                                      
REMARK 465     HIS A   218                                                      
REMARK 465     ALA A   219                                                      
REMARK 465     LYS A   220                                                      
REMARK 465     TYR A   221                                                      
REMARK 465     ILE A   222                                                      
REMARK 465     ALA A   223                                                      
REMARK 465     ASN A   224                                                      
REMARK 465     ASP A   225                                                      
REMARK 465     THR A   226                                                      
REMARK 465     GLN A   227                                                      
REMARK 465     ASP A   312                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     PRO B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     ILE B     4                                                      
REMARK 465     GLU B   152                                                      
REMARK 465     GLY B   153                                                      
REMARK 465     SER B   154                                                      
REMARK 465     SER B   155                                                      
REMARK 465     VAL B   156                                                      
REMARK 465     ALA B   157                                                      
REMARK 465     GLY C    -3                                                      
REMARK 465     PRO C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     SER C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     GLY C     3                                                      
REMARK 465     SER C   151                                                      
REMARK 465     GLU C   152                                                      
REMARK 465     GLY C   153                                                      
REMARK 465     SER C   154                                                      
REMARK 465     SER C   155                                                      
REMARK 465     VAL C   156                                                      
REMARK 465     ASP C   312                                                      
REMARK 465     GLY D    -3                                                      
REMARK 465     PRO D    -2                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     SER D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     GLY D     3                                                      
REMARK 465     GLY D   127                                                      
REMARK 465     ASP D   128                                                      
REMARK 465     ALA D   150                                                      
REMARK 465     SER D   151                                                      
REMARK 465     GLU D   152                                                      
REMARK 465     GLY D   153                                                      
REMARK 465     SER D   154                                                      
REMARK 465     SER D   155                                                      
REMARK 465     VAL D   156                                                      
REMARK 465     ALA D   157                                                      
REMARK 465     VAL D   158                                                      
REMARK 465     GLU D   159                                                      
REMARK 465     LYS D   160                                                      
REMARK 465     VAL D   161                                                      
REMARK 465     LYS D   162                                                      
REMARK 465     SER D   163                                                      
REMARK 465     ALA D   164                                                      
REMARK 465     ASP D   165                                                      
REMARK 465     ASP D   225                                                      
REMARK 465     THR D   226                                                      
REMARK 465     ASP D   312                                                      
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     ILE A   4    CG1  CG2  CD1                                       
REMARK 470     ASP A   5    CG   OD1  OD2                                       
REMARK 470     LYS A   7    CG   CD   CE   NZ                                   
REMARK 470     ARG A   8    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  24    CG   CD   OE1  OE2                                  
REMARK 470     LEU A  27    CG   CD1  CD2                                       
REMARK 470     ASN A  28    CG   OD1  ND2                                       
REMARK 470     ARG A  31    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  58    CG   CD   CE   NZ                                   
REMARK 470     GLU A  60    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  75    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 104    CG   CD   CE   NZ                                   
REMARK 470     ASP A 136    CG   OD1  OD2                                       
REMARK 470     LYS A 140    CG   CD   CE   NZ                                   
REMARK 470     LYS A 148    CG   CD   CE   NZ                                   
REMARK 470     SER A 151    OG                                                  
REMARK 470     SER A 155    OG                                                  
REMARK 470     LYS A 160    CG   CD   CE   NZ                                   
REMARK 470     LYS A 162    CG   CD   CE   NZ                                   
REMARK 470     ASP A 165    CG   OD1  OD2                                       
REMARK 470     GLU A 172    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 176    CG   CD   CE   NZ                                   
REMARK 470     LYS A 179    CG   CD   CE   NZ                                   
REMARK 470     GLU A 184    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 188    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 192    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 200    CG   OD1  OD2                                       
REMARK 470     VAL A 209    CG1  CG2                                            
REMARK 470     TYR A 228    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE A 230    CG1  CG2  CD1                                       
REMARK 470     ASP A 235    CG   OD1  OD2                                       
REMARK 470     LYS A 238    CG   CD   CE   NZ                                   
REMARK 470     ASP A 284    CG   OD1  OD2                                       
REMARK 470     HIS A 285    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 290    CG   CD   CE   NZ                                   
REMARK 470     LYS A 305    CG   CD   CE   NZ                                   
REMARK 470     LYS B   7    CG   CD   CE   NZ                                   
REMARK 470     GLU B  22    CG   CD   OE1  OE2                                  
REMARK 470     VAL B  25    CG1  CG2                                            
REMARK 470     ASN B  28    CG   OD1  ND2                                       
REMARK 470     ASP B  59    CG   OD1  OD2                                       
REMARK 470     GLU B  75    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 135    CG   CD   OE1  NE2                                  
REMARK 470     ASP B 136    CG   OD1  OD2                                       
REMARK 470     LYS B 140    CG   CD   CE   NZ                                   
REMARK 470     LYS B 148    CG   CD   CE   NZ                                   
REMARK 470     SER B 151    OG                                                  
REMARK 470     VAL B 158    CG1  CG2                                            
REMARK 470     GLU B 159    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 160    CG   CD   CE   NZ                                   
REMARK 470     LYS B 162    CG   CD   CE   NZ                                   
REMARK 470     ASP B 165    CG   OD1  OD2                                       
REMARK 470     GLU B 172    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 173    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 176    CG   CD   CE   NZ                                   
REMARK 470     HIS B 177    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B 179    CG   CD   CE   NZ                                   
REMARK 470     PHE B 214    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B 220    CG   CD   CE   NZ                                   
REMARK 470     ILE B 222    CG1  CG2  CD1                                       
REMARK 470     ASN B 224    CG   OD1  ND2                                       
REMARK 470     ASP B 235    CG   OD1  OD2                                       
REMARK 470     LYS B 238    CG   CD   CE   NZ                                   
REMARK 470     ARG B 244    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 247    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 248    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 284    CG   OD1  OD2                                       
REMARK 470     HIS B 285    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B 290    CG   CD   CE   NZ                                   
REMARK 470     ASP B 312    CG   OD1  OD2                                       
REMARK 470     ASP C   5    CG   OD1  OD2                                       
REMARK 470     LYS C   7    CG   CD   CE   NZ                                   
REMARK 470     ARG C   8    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C  19    CG   OD1  OD2                                       
REMARK 470     GLU C  22    CG   CD   OE1  OE2                                  
REMARK 470     ARG C  31    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU C  32    CG   CD1  CD2                                       
REMARK 470     GLN C  35    CG   CD   OE1  NE2                                  
REMARK 470     ARG C  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C  51    CG   CD   OE1  NE2                                  
REMARK 470     LYS C  58    CG   CD   CE   NZ                                   
REMARK 470     ASP C  59    CG   OD1  OD2                                       
REMARK 470     GLU C  75    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 126    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C 135    CG   CD   OE1  NE2                                  
REMARK 470     ASP C 136    CG   OD1  OD2                                       
REMARK 470     LYS C 140    CG   CD   CE   NZ                                   
REMARK 470     LYS C 148    CG   CD   CE   NZ                                   
REMARK 470     LYS C 160    CG   CD   CE   NZ                                   
REMARK 470     LYS C 162    CG   CD   CE   NZ                                   
REMARK 470     LYS C 179    CG   CD   CE   NZ                                   
REMARK 470     LYS C 185    CG   CD   CE   NZ                                   
REMARK 470     GLU C 188    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 192    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 213    CG   CD   OE1  OE2                                  
REMARK 470     ASN C 224    CG   OD1  ND2                                       
REMARK 470     ASP C 225    CG   OD1  OD2                                       
REMARK 470     GLU C 239    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 301    CG   CD   OE1  OE2                                  
REMARK 470     VAL C 303    CG1  CG2                                            
REMARK 470     ILE D   4    CG1  CG2  CD1                                       
REMARK 470     ARG D   8    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D  22    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  24    CG   CD   OE1  OE2                                  
REMARK 470     ASN D  28    CG   OD1  ND2                                       
REMARK 470     GLN D  51    CG   CD   OE1  NE2                                  
REMARK 470     GLU D  60    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  75    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 104    CG   CD   CE   NZ                                   
REMARK 470     ASP D 129    CG   OD1  OD2                                       
REMARK 470     GLN D 135    CG   CD   OE1  NE2                                  
REMARK 470     ASP D 136    CG   OD1  OD2                                       
REMARK 470     LYS D 140    CG   CD   CE   NZ                                   
REMARK 470     LEU D 141    CG   CD1  CD2                                       
REMARK 470     VAL D 143    CG1  CG2                                            
REMARK 470     LEU D 145    CG   CD1  CD2                                       
REMARK 470     PHE D 146    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS D 148    CG   CD   CE   NZ                                   
REMARK 470     GLU D 172    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 173    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 176    CG   CD   CE   NZ                                   
REMARK 470     HIS D 177    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP D 178    CG   OD1  OD2                                       
REMARK 470     LYS D 179    CG   CD   CE   NZ                                   
REMARK 470     LYS D 185    CG   CD   CE   NZ                                   
REMARK 470     GLU D 188    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 192    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 213    CG   CD   OE1  OE2                                  
REMARK 470     HIS D 218    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS D 220    CG   CD   CE   NZ                                   
REMARK 470     GLN D 227    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 238    CG   CD   CE   NZ                                   
REMARK 470     GLU D 241    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 244    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP D 284    CG   OD1  OD2                                       
REMARK 470     HIS D 285    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU D 301    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE2  GLU B    60     OD1  ASP C   165     1445     2.09            
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    ARG B  52   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    LEU D  34   CB  -  CG  -  CD2 ANGL. DEV. = -10.8 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    LYS A   7      -16.16    106.51                                   
REMARK 500    ALA A 199     -133.97     53.51                                   
REMARK 500    ALA B 199     -132.22     52.53                                   
REMARK 500    ASP B 225     -118.78     65.63                                   
REMARK 500    LYS C 179      -45.37     84.47                                   
REMARK 500    ALA C 199     -129.76     50.18                                   
REMARK 500    ALA D 199     -133.92     52.88                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS A    7     ARG A    8                  148.13                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4EG0   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN BURKHOLDERIA AMBIFARIA, BUAMA.00119.A                   
REMARK 900 RELATED ID: BUPSA.00119.A   RELATED DB: TARGETTRACK                  
REMARK 900 RELATED ID: 4EGJ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF D-ALANINE-D-ALANINE LIGASE FROM                 
REMARK 900 BURKHOLDERIA XENOVORANS                                              
DBREF  4EGQ A    1   312  UNP    Q3JNE1   DDL_BURP1        1    312             
DBREF  4EGQ B    1   312  UNP    Q3JNE1   DDL_BURP1        1    312             
DBREF  4EGQ C    1   312  UNP    Q3JNE1   DDL_BURP1        1    312             
DBREF  4EGQ D    1   312  UNP    Q3JNE1   DDL_BURP1        1    312             
SEQADV 4EGQ GLY A   -3  UNP  Q3JNE1              EXPRESSION TAG                 
SEQADV 4EGQ PRO A   -2  UNP  Q3JNE1              EXPRESSION TAG                 
SEQADV 4EGQ GLY A   -1  UNP  Q3JNE1              EXPRESSION TAG                 
SEQADV 4EGQ SER A    0  UNP  Q3JNE1              EXPRESSION TAG                 
SEQADV 4EGQ GLY B   -3  UNP  Q3JNE1              EXPRESSION TAG                 
SEQADV 4EGQ PRO B   -2  UNP  Q3JNE1              EXPRESSION TAG                 
SEQADV 4EGQ GLY B   -1  UNP  Q3JNE1              EXPRESSION TAG                 
SEQADV 4EGQ SER B    0  UNP  Q3JNE1              EXPRESSION TAG                 
SEQADV 4EGQ GLY C   -3  UNP  Q3JNE1              EXPRESSION TAG                 
SEQADV 4EGQ PRO C   -2  UNP  Q3JNE1              EXPRESSION TAG                 
SEQADV 4EGQ GLY C   -1  UNP  Q3JNE1              EXPRESSION TAG                 
SEQADV 4EGQ SER C    0  UNP  Q3JNE1              EXPRESSION TAG                 
SEQADV 4EGQ GLY D   -3  UNP  Q3JNE1              EXPRESSION TAG                 
SEQADV 4EGQ PRO D   -2  UNP  Q3JNE1              EXPRESSION TAG                 
SEQADV 4EGQ GLY D   -1  UNP  Q3JNE1              EXPRESSION TAG                 
SEQADV 4EGQ SER D    0  UNP  Q3JNE1              EXPRESSION TAG                 
SEQRES   1 A  316  GLY PRO GLY SER MET SER GLY ILE ASP PRO LYS ARG PHE          
SEQRES   2 A  316  GLY LYS VAL ALA VAL LEU LEU GLY GLY ASP SER ALA GLU          
SEQRES   3 A  316  ARG GLU VAL SER LEU ASN SER GLY ARG LEU VAL LEU GLN          
SEQRES   4 A  316  GLY LEU ARG ASP ALA GLY ILE ASP ALA HIS PRO PHE ASP          
SEQRES   5 A  316  PRO ALA GLN ARG PRO LEU ALA ALA LEU LYS ASP GLU GLY          
SEQRES   6 A  316  PHE VAL ARG ALA PHE ASN ALA LEU HIS GLY GLY TYR GLY          
SEQRES   7 A  316  GLU ASN GLY GLN ILE GLN GLY ALA LEU ASP PHE TYR GLY          
SEQRES   8 A  316  ILE ARG TYR THR GLY SER GLY VAL LEU GLY SER ALA LEU          
SEQRES   9 A  316  GLY LEU ASP LYS PHE ARG THR LYS LEU VAL TRP GLN GLN          
SEQRES  10 A  316  THR GLY ILE PRO THR PRO PRO PHE GLU THR VAL MET ARG          
SEQRES  11 A  316  GLY ASP ASP TYR ALA ALA ARG ALA GLN ASP ILE VAL ALA          
SEQRES  12 A  316  LYS LEU GLY VAL PRO LEU PHE VAL LYS PRO ALA SER GLU          
SEQRES  13 A  316  GLY SER SER VAL ALA VAL GLU LYS VAL LYS SER ALA ASP          
SEQRES  14 A  316  ALA LEU PRO ALA ALA LEU GLU GLU ALA ALA LYS HIS ASP          
SEQRES  15 A  316  LYS ILE VAL ILE VAL GLU LYS SER ILE GLU GLY GLY GLY          
SEQRES  16 A  316  GLU TYR THR ALA CYS ILE ALA ALA ASP LEU ASP LEU PRO          
SEQRES  17 A  316  LEU ILE ARG ILE VAL PRO ALA GLY GLU PHE TYR ASP TYR          
SEQRES  18 A  316  HIS ALA LYS TYR ILE ALA ASN ASP THR GLN TYR LEU ILE          
SEQRES  19 A  316  PRO CYS GLY LEU ASP ALA ALA LYS GLU ALA GLU PHE LYS          
SEQRES  20 A  316  ARG ILE ALA ARG ARG ALA PHE ASP VAL LEU GLY CYS THR          
SEQRES  21 A  316  ASP TRP GLY ARG ALA ASP PHE MET LEU ASP ALA ALA GLY          
SEQRES  22 A  316  ASN PRO TYR PHE LEU GLU VAL ASN THR ALA PRO GLY MET          
SEQRES  23 A  316  THR ASP HIS SER LEU PRO PRO LYS ALA ALA ARG ALA VAL          
SEQRES  24 A  316  GLY ILE GLY TYR SER GLU LEU VAL VAL LYS VAL LEU SER          
SEQRES  25 A  316  LEU THR LEU ASP                                              
SEQRES   1 B  316  GLY PRO GLY SER MET SER GLY ILE ASP PRO LYS ARG PHE          
SEQRES   2 B  316  GLY LYS VAL ALA VAL LEU LEU GLY GLY ASP SER ALA GLU          
SEQRES   3 B  316  ARG GLU VAL SER LEU ASN SER GLY ARG LEU VAL LEU GLN          
SEQRES   4 B  316  GLY LEU ARG ASP ALA GLY ILE ASP ALA HIS PRO PHE ASP          
SEQRES   5 B  316  PRO ALA GLN ARG PRO LEU ALA ALA LEU LYS ASP GLU GLY          
SEQRES   6 B  316  PHE VAL ARG ALA PHE ASN ALA LEU HIS GLY GLY TYR GLY          
SEQRES   7 B  316  GLU ASN GLY GLN ILE GLN GLY ALA LEU ASP PHE TYR GLY          
SEQRES   8 B  316  ILE ARG TYR THR GLY SER GLY VAL LEU GLY SER ALA LEU          
SEQRES   9 B  316  GLY LEU ASP LYS PHE ARG THR LYS LEU VAL TRP GLN GLN          
SEQRES  10 B  316  THR GLY ILE PRO THR PRO PRO PHE GLU THR VAL MET ARG          
SEQRES  11 B  316  GLY ASP ASP TYR ALA ALA ARG ALA GLN ASP ILE VAL ALA          
SEQRES  12 B  316  LYS LEU GLY VAL PRO LEU PHE VAL LYS PRO ALA SER GLU          
SEQRES  13 B  316  GLY SER SER VAL ALA VAL GLU LYS VAL LYS SER ALA ASP          
SEQRES  14 B  316  ALA LEU PRO ALA ALA LEU GLU GLU ALA ALA LYS HIS ASP          
SEQRES  15 B  316  LYS ILE VAL ILE VAL GLU LYS SER ILE GLU GLY GLY GLY          
SEQRES  16 B  316  GLU TYR THR ALA CYS ILE ALA ALA ASP LEU ASP LEU PRO          
SEQRES  17 B  316  LEU ILE ARG ILE VAL PRO ALA GLY GLU PHE TYR ASP TYR          
SEQRES  18 B  316  HIS ALA LYS TYR ILE ALA ASN ASP THR GLN TYR LEU ILE          
SEQRES  19 B  316  PRO CYS GLY LEU ASP ALA ALA LYS GLU ALA GLU PHE LYS          
SEQRES  20 B  316  ARG ILE ALA ARG ARG ALA PHE ASP VAL LEU GLY CYS THR          
SEQRES  21 B  316  ASP TRP GLY ARG ALA ASP PHE MET LEU ASP ALA ALA GLY          
SEQRES  22 B  316  ASN PRO TYR PHE LEU GLU VAL ASN THR ALA PRO GLY MET          
SEQRES  23 B  316  THR ASP HIS SER LEU PRO PRO LYS ALA ALA ARG ALA VAL          
SEQRES  24 B  316  GLY ILE GLY TYR SER GLU LEU VAL VAL LYS VAL LEU SER          
SEQRES  25 B  316  LEU THR LEU ASP                                              
SEQRES   1 C  316  GLY PRO GLY SER MET SER GLY ILE ASP PRO LYS ARG PHE          
SEQRES   2 C  316  GLY LYS VAL ALA VAL LEU LEU GLY GLY ASP SER ALA GLU          
SEQRES   3 C  316  ARG GLU VAL SER LEU ASN SER GLY ARG LEU VAL LEU GLN          
SEQRES   4 C  316  GLY LEU ARG ASP ALA GLY ILE ASP ALA HIS PRO PHE ASP          
SEQRES   5 C  316  PRO ALA GLN ARG PRO LEU ALA ALA LEU LYS ASP GLU GLY          
SEQRES   6 C  316  PHE VAL ARG ALA PHE ASN ALA LEU HIS GLY GLY TYR GLY          
SEQRES   7 C  316  GLU ASN GLY GLN ILE GLN GLY ALA LEU ASP PHE TYR GLY          
SEQRES   8 C  316  ILE ARG TYR THR GLY SER GLY VAL LEU GLY SER ALA LEU          
SEQRES   9 C  316  GLY LEU ASP LYS PHE ARG THR LYS LEU VAL TRP GLN GLN          
SEQRES  10 C  316  THR GLY ILE PRO THR PRO PRO PHE GLU THR VAL MET ARG          
SEQRES  11 C  316  GLY ASP ASP TYR ALA ALA ARG ALA GLN ASP ILE VAL ALA          
SEQRES  12 C  316  LYS LEU GLY VAL PRO LEU PHE VAL LYS PRO ALA SER GLU          
SEQRES  13 C  316  GLY SER SER VAL ALA VAL GLU LYS VAL LYS SER ALA ASP          
SEQRES  14 C  316  ALA LEU PRO ALA ALA LEU GLU GLU ALA ALA LYS HIS ASP          
SEQRES  15 C  316  LYS ILE VAL ILE VAL GLU LYS SER ILE GLU GLY GLY GLY          
SEQRES  16 C  316  GLU TYR THR ALA CYS ILE ALA ALA ASP LEU ASP LEU PRO          
SEQRES  17 C  316  LEU ILE ARG ILE VAL PRO ALA GLY GLU PHE TYR ASP TYR          
SEQRES  18 C  316  HIS ALA LYS TYR ILE ALA ASN ASP THR GLN TYR LEU ILE          
SEQRES  19 C  316  PRO CYS GLY LEU ASP ALA ALA LYS GLU ALA GLU PHE LYS          
SEQRES  20 C  316  ARG ILE ALA ARG ARG ALA PHE ASP VAL LEU GLY CYS THR          
SEQRES  21 C  316  ASP TRP GLY ARG ALA ASP PHE MET LEU ASP ALA ALA GLY          
SEQRES  22 C  316  ASN PRO TYR PHE LEU GLU VAL ASN THR ALA PRO GLY MET          
SEQRES  23 C  316  THR ASP HIS SER LEU PRO PRO LYS ALA ALA ARG ALA VAL          
SEQRES  24 C  316  GLY ILE GLY TYR SER GLU LEU VAL VAL LYS VAL LEU SER          
SEQRES  25 C  316  LEU THR LEU ASP                                              
SEQRES   1 D  316  GLY PRO GLY SER MET SER GLY ILE ASP PRO LYS ARG PHE          
SEQRES   2 D  316  GLY LYS VAL ALA VAL LEU LEU GLY GLY ASP SER ALA GLU          
SEQRES   3 D  316  ARG GLU VAL SER LEU ASN SER GLY ARG LEU VAL LEU GLN          
SEQRES   4 D  316  GLY LEU ARG ASP ALA GLY ILE ASP ALA HIS PRO PHE ASP          
SEQRES   5 D  316  PRO ALA GLN ARG PRO LEU ALA ALA LEU LYS ASP GLU GLY          
SEQRES   6 D  316  PHE VAL ARG ALA PHE ASN ALA LEU HIS GLY GLY TYR GLY          
SEQRES   7 D  316  GLU ASN GLY GLN ILE GLN GLY ALA LEU ASP PHE TYR GLY          
SEQRES   8 D  316  ILE ARG TYR THR GLY SER GLY VAL LEU GLY SER ALA LEU          
SEQRES   9 D  316  GLY LEU ASP LYS PHE ARG THR LYS LEU VAL TRP GLN GLN          
SEQRES  10 D  316  THR GLY ILE PRO THR PRO PRO PHE GLU THR VAL MET ARG          
SEQRES  11 D  316  GLY ASP ASP TYR ALA ALA ARG ALA GLN ASP ILE VAL ALA          
SEQRES  12 D  316  LYS LEU GLY VAL PRO LEU PHE VAL LYS PRO ALA SER GLU          
SEQRES  13 D  316  GLY SER SER VAL ALA VAL GLU LYS VAL LYS SER ALA ASP          
SEQRES  14 D  316  ALA LEU PRO ALA ALA LEU GLU GLU ALA ALA LYS HIS ASP          
SEQRES  15 D  316  LYS ILE VAL ILE VAL GLU LYS SER ILE GLU GLY GLY GLY          
SEQRES  16 D  316  GLU TYR THR ALA CYS ILE ALA ALA ASP LEU ASP LEU PRO          
SEQRES  17 D  316  LEU ILE ARG ILE VAL PRO ALA GLY GLU PHE TYR ASP TYR          
SEQRES  18 D  316  HIS ALA LYS TYR ILE ALA ASN ASP THR GLN TYR LEU ILE          
SEQRES  19 D  316  PRO CYS GLY LEU ASP ALA ALA LYS GLU ALA GLU PHE LYS          
SEQRES  20 D  316  ARG ILE ALA ARG ARG ALA PHE ASP VAL LEU GLY CYS THR          
SEQRES  21 D  316  ASP TRP GLY ARG ALA ASP PHE MET LEU ASP ALA ALA GLY          
SEQRES  22 D  316  ASN PRO TYR PHE LEU GLU VAL ASN THR ALA PRO GLY MET          
SEQRES  23 D  316  THR ASP HIS SER LEU PRO PRO LYS ALA ALA ARG ALA VAL          
SEQRES  24 D  316  GLY ILE GLY TYR SER GLU LEU VAL VAL LYS VAL LEU SER          
SEQRES  25 D  316  LEU THR LEU ASP                                              
FORMUL   5  HOH   *193(H2 O)                                                    
HELIX    1   1 GLU A   22  ALA A   40  1                                  19    
HELIX    2   2 ALA A   55  GLU A   60  1                                   6    
HELIX    3   3 GLY A   71  GLU A   75  5                                   5    
HELIX    4   4 GLY A   77  TYR A   86  1                                  10    
HELIX    5   5 GLY A   94  ASP A  103  1                                  10    
HELIX    6   6 ASP A  103  GLY A  115  1                                  13    
HELIX    7   7 ASP A  129  GLY A  142  1                                  14    
HELIX    8   8 SER A  163  ASP A  165  5                                   3    
HELIX    9   9 ALA A  166  ASP A  178  1                                  13    
HELIX   10  10 ASP A  235  LEU A  253  1                                  19    
HELIX   11  11 SER A  286  VAL A  295  1                                  10    
HELIX   12  12 GLY A  298  LEU A  309  1                                  12    
HELIX   13  13 THR A  310  LEU A  311  5                                   2    
HELIX   14  14 ASP B    5  PHE B    9  5                                   5    
HELIX   15  15 GLU B   22  ALA B   40  1                                  19    
HELIX   16  16 ALA B   55  GLU B   60  1                                   6    
HELIX   17  17 GLY B   71  GLU B   75  5                                   5    
HELIX   18  18 GLY B   77  TYR B   86  1                                  10    
HELIX   19  19 GLY B   94  ASP B  103  1                                  10    
HELIX   20  20 ASP B  103  GLY B  115  1                                  13    
HELIX   21  21 ASP B  129  GLY B  142  1                                  14    
HELIX   22  22 SER B  163  ASP B  165  5                                   3    
HELIX   23  23 ALA B  166  ASP B  178  1                                  13    
HELIX   24  24 ASP B  235  LEU B  253  1                                  19    
HELIX   25  25 SER B  286  VAL B  295  1                                  10    
HELIX   26  26 GLY B  298  LEU B  309  1                                  12    
HELIX   27  27 ASP C    5  PHE C    9  5                                   5    
HELIX   28  28 GLU C   22  ALA C   40  1                                  19    
HELIX   29  29 ALA C   55  GLU C   60  1                                   6    
HELIX   30  30 GLY C   71  GLU C   75  5                                   5    
HELIX   31  31 GLY C   77  TYR C   86  1                                  10    
HELIX   32  32 GLY C   94  ASP C  103  1                                  10    
HELIX   33  33 ASP C  103  THR C  114  1                                  12    
HELIX   34  34 ASP C  129  GLY C  142  1                                  14    
HELIX   35  35 SER C  163  ASP C  165  5                                   3    
HELIX   36  36 ALA C  166  LYS C  179  1                                  14    
HELIX   37  37 PRO C  210  PHE C  214  5                                   5    
HELIX   38  38 ASP C  216  ILE C  222  1                                   7    
HELIX   39  39 ASP C  235  LEU C  253  1                                  19    
HELIX   40  40 SER C  286  VAL C  295  1                                  10    
HELIX   41  41 GLY C  298  LEU C  309  1                                  12    
HELIX   42  42 ASP D    5  PHE D    9  5                                   5    
HELIX   43  43 GLU D   22  ALA D   40  1                                  19    
HELIX   44  44 ALA D   55  GLU D   60  1                                   6    
HELIX   45  45 GLY D   71  GLU D   75  5                                   5    
HELIX   46  46 GLY D   77  TYR D   86  1                                  10    
HELIX   47  47 GLY D   94  ASP D  103  1                                  10    
HELIX   48  48 ASP D  103  THR D  114  1                                  12    
HELIX   49  49 TYR D  130  GLY D  142  1                                  13    
HELIX   50  50 LEU D  167  ASP D  178  1                                  12    
HELIX   51  51 ASP D  235  LEU D  253  1                                  19    
HELIX   52  52 SER D  286  VAL D  295  1                                  10    
HELIX   53  53 GLY D  298  LEU D  309  1                                  12    
SHEET    1   A 4 ASP A  43  PHE A  47  0                                        
SHEET    2   A 4 LYS A  11  LEU A  15  1  N  VAL A  14   O  HIS A  45           
SHEET    3   A 4 ARG A  64  ASN A  67  1  O  PHE A  66   N  ALA A  13           
SHEET    4   A 4 ARG A  89  TYR A  90  1  O  ARG A  89   N  ALA A  65           
SHEET    1   B 4 PHE A 121  MET A 125  0                                        
SHEET    2   B 4 ILE A 180  LYS A 185 -1  O  VAL A 181   N  VAL A 124           
SHEET    3   B 4 LEU A 145  PRO A 149 -1  N  PHE A 146   O  GLU A 184           
SHEET    4   B 4 GLU A 159  VAL A 161 -1  O  VAL A 161   N  LEU A 145           
SHEET    1   C 4 ILE A 206  ILE A 208  0                                        
SHEET    2   C 4 GLU A 192  ALA A 198 -1  N  THR A 194   O  ILE A 206           
SHEET    3   C 4 TRP A 258  LEU A 265 -1  O  PHE A 263   N  TYR A 193           
SHEET    4   C 4 PRO A 271  ASN A 277 -1  O  GLU A 275   N  ASP A 262           
SHEET    1   D 4 ASP B  43  PHE B  47  0                                        
SHEET    2   D 4 LYS B  11  LEU B  15  1  N  VAL B  14   O  HIS B  45           
SHEET    3   D 4 ARG B  64  ASN B  67  1  O  PHE B  66   N  ALA B  13           
SHEET    4   D 4 ARG B  89  TYR B  90  1  O  ARG B  89   N  ALA B  65           
SHEET    1   E 4 PHE B 121  MET B 125  0                                        
SHEET    2   E 4 ILE B 180  LYS B 185 -1  O  VAL B 181   N  VAL B 124           
SHEET    3   E 4 LEU B 145  PRO B 149 -1  N  PHE B 146   O  GLU B 184           
SHEET    4   E 4 GLU B 159  VAL B 161 -1  O  VAL B 161   N  LEU B 145           
SHEET    1   F 5 GLN B 227  LEU B 229  0                                        
SHEET    2   F 5 ILE B 206  VAL B 209 -1  N  VAL B 209   O  GLN B 227           
SHEET    3   F 5 GLU B 192  ALA B 198 -1  N  THR B 194   O  ILE B 206           
SHEET    4   F 5 TRP B 258  LEU B 265 -1  O  PHE B 263   N  TYR B 193           
SHEET    5   F 5 PRO B 271  ASN B 277 -1  O  GLU B 275   N  ASP B 262           
SHEET    1   G 4 ASP C  43  PHE C  47  0                                        
SHEET    2   G 4 LYS C  11  LEU C  15  1  N  VAL C  14   O  HIS C  45           
SHEET    3   G 4 ARG C  64  ASN C  67  1  O  PHE C  66   N  ALA C  13           
SHEET    4   G 4 ARG C  89  TYR C  90  1  O  ARG C  89   N  ALA C  65           
SHEET    1   H 4 PHE C 121  MET C 125  0                                        
SHEET    2   H 4 ILE C 180  LYS C 185 -1  O  VAL C 183   N  GLU C 122           
SHEET    3   H 4 LEU C 145  PRO C 149 -1  N  PHE C 146   O  GLU C 184           
SHEET    4   H 4 GLU C 159  VAL C 161 -1  O  VAL C 161   N  LEU C 145           
SHEET    1   I 5 GLN C 227  LEU C 229  0                                        
SHEET    2   I 5 ILE C 206  VAL C 209 -1  N  VAL C 209   O  GLN C 227           
SHEET    3   I 5 GLU C 192  ALA C 198 -1  N  THR C 194   O  ILE C 206           
SHEET    4   I 5 TRP C 258  LEU C 265 -1  O  PHE C 263   N  TYR C 193           
SHEET    5   I 5 PRO C 271  ASN C 277 -1  O  GLU C 275   N  ASP C 262           
SHEET    1   J 4 ASP D  43  PHE D  47  0                                        
SHEET    2   J 4 LYS D  11  LEU D  15  1  N  VAL D  14   O  HIS D  45           
SHEET    3   J 4 ARG D  64  ASN D  67  1  O  PHE D  66   N  ALA D  13           
SHEET    4   J 4 ARG D  89  TYR D  90  1  O  ARG D  89   N  ALA D  65           
SHEET    1   K 3 PHE D 121  MET D 125  0                                        
SHEET    2   K 3 ILE D 180  LYS D 185 -1  O  VAL D 181   N  VAL D 124           
SHEET    3   K 3 LEU D 145  LYS D 148 -1  N  LYS D 148   O  ILE D 182           
SHEET    1   L 5 TYR D 228  LEU D 229  0                                        
SHEET    2   L 5 ILE D 206  ILE D 208 -1  N  ARG D 207   O  LEU D 229           
SHEET    3   L 5 GLU D 192  ALA D 198 -1  N  GLU D 192   O  ILE D 208           
SHEET    4   L 5 TRP D 258  LEU D 265 -1  O  GLY D 259   N  ILE D 197           
SHEET    5   L 5 PRO D 271  ASN D 277 -1  O  GLU D 275   N  ASP D 262           
SHEET    1   M 2 PHE D 214  TYR D 215  0                                        
SHEET    2   M 2 TYR D 221  ILE D 222 -1  O  ILE D 222   N  PHE D 214           
CISPEP   1 VAL A  143    PRO A  144          0        -1.13                     
CISPEP   2 ILE A  230    PRO A  231          0         0.70                     
CISPEP   3 VAL B  143    PRO B  144          0        -3.80                     
CISPEP   4 ILE B  230    PRO B  231          0        -2.06                     
CISPEP   5 VAL C  143    PRO C  144          0        -9.52                     
CISPEP   6 ILE C  230    PRO C  231          0        -4.91                     
CISPEP   7 ILE D  230    PRO D  231          0        -0.72                     
CRYST1   45.389   66.092   98.558  84.47  80.50  83.59 P 1           4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.022032 -0.002476 -0.003503        0.00000                         
SCALE2      0.000000  0.015226 -0.001214        0.00000                         
SCALE3      0.000000  0.000000  0.010320        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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