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Database: PDB
Entry: 1RCQ
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Original site: 1RCQ 
HEADER    ISOMERASE                               04-NOV-03   1RCQ              
TITLE     THE 1.45 A CRYSTAL STRUCTURE OF ALANINE RACEMASE FROM A PATHOGENIC    
TITLE    2 BACTERIUM, PSEUDOMONAS AERUGINOSA, CONTAINS BOTH INTERNAL AND        
TITLE    3 EXTERNAL ALDIMINE FORMS                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CATABOLIC ALANINE RACEMASE DADX;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 5.1.1.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 287;                                                 
SOURCE   4 GENE: DADX;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET26                                     
KEYWDS    ALPHA-BETA BARREL, BETA-STRUCTURE FOR C-TERMINAL DOMAIN,              
KEYWDS   2 INTERNAL/EXTERNAL ALDIMINE FORMS, ISOMERASE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.LE MAGUERES,H.IM,A.DVORAK,U.STRYCH,M.BENEDIK,K.L.KRAUSE             
REVDAT   3   13-JUL-11 1RCQ    1       VERSN                                    
REVDAT   2   24-FEB-09 1RCQ    1       VERSN                                    
REVDAT   1   01-JUN-04 1RCQ    0                                                
JRNL        AUTH   P.LEMAGUERES,H.IM,A.DVORAK,U.STRYCH,M.BENEDIK,K.L.KRAUSE     
JRNL        TITL   CRYSTAL STRUCTURE AT 1.45 A RESOLUTION OF ALANINE RACEMASE   
JRNL        TITL 2 FROM A PATHOGENIC BACTERIUM, PSEUDOMONAS AERUGINOSA,         
JRNL        TITL 3 CONTAINS BOTH INTERNAL AND EXTERNAL ALDIMINE FORMS.          
JRNL        REF    BIOCHEMISTRY                  V.  42 14752 2003              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   14674749                                                     
JRNL        DOI    10.1021/BI030165V                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   U.STRYCH,H.C.HUANG,K.L.KRAUSE,M.J.BENEDIK                    
REMARK   1  TITL   CHARACTERIZATION OF THE ALANINE RACEMASES FROM PSEUDOMONAS   
REMARK   1  TITL 2 AERUGINOSA PAO1                                              
REMARK   1  REF    CURR.MICROBIOL.               V.  41   290 2000              
REMARK   1  REFN                   ISSN 0343-8651                               
REMARK   1  DOI    10.1007/S002840010136                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.153                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.206                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 2559                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 54137                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL                   
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 2753                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 25                                            
REMARK   3   SOLVENT ATOMS      : 306                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : NULL                    
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : NULL                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL                    
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : NULL                    
REMARK   3   NUMBER OF RESTRAINTS                     : NULL                    
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.010                   
REMARK   3   ANGLE DISTANCES                      (A) : 2.180                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL                    
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : NULL                    
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : NULL                    
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : NULL                    
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : NULL                    
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : NULL                    
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : NULL                    
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : NULL                    
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER                        
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1RCQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB020651.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-SEP-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 14-BM-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9840, 0.9795, 0.9791, 0.9611     
REMARK 200  MONOCHROMATOR                  : 0.95 POLARIZATION                  
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56981                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 84.7                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : 0.03000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 51.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 36.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.15000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, AMMONIUM SULFATE, HEPES, PH     
REMARK 280  7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.13300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       68.13300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  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       36.33950            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       38.06450            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       36.33950            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       38.06450            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       68.13300            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       36.33950            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       38.06450            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       68.13300            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       36.33950            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       38.06450            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
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 300 REMARK: THE SECOND MONOMER OF THE BIOLOGICAL ASSEMBLY IS GENERATED   
REMARK 300 BY A TWO-FOLD AXIS: X, -Y+1, -Z                                      
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 6950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       76.12900            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 507  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 511  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 706  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 728  LIES ON A SPECIAL POSITION.                          
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 A   2   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A   5   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG A  21   CD  -  NE  -  CZ  ANGL. DEV. =  -9.9 DEGREES          
REMARK 500    ARG A  21   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ARG A  21   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A  67   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG A 115   CD  -  NE  -  CZ  ANGL. DEV. =  12.0 DEGREES          
REMARK 500    ARG A 115   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A 143   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A 169   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG A 208   NE  -  CZ  -  NH1 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    ARG A 208   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG A 243   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    ARG A 261   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG A 264   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A 294   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG A 319   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    TYR A 341   CB  -  CG  -  CD1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ARG A 352   NE  -  CZ  -  NH2 ANGL. DEV. =   4.1 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    ARG A 129     -101.91   -102.12                                   
REMARK 500    ALA A 151     -104.16    -92.35                                   
REMARK 500    SER A 204      128.57   -176.74                                   
REMARK 500    ARG A 349      -47.45     69.42                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 728        DISTANCE =  5.37 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 358                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DLY A 359                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1SFT   RELATED DB: PDB                                   
REMARK 900 ALANINE RACEMASE FROM BACILLUS STEAROTHERMOPHILUS COMPLEXED          
REMARK 900 WITH ACETATE                                                         
REMARK 900 RELATED ID: 1BDO   RELATED DB: PDB                                   
REMARK 900 ALANINE RACEMASE COMPLEXED WITH ALANINE PHOSPHONATE                  
REMARK 900 RELATED ID: 1EPV   RELATED DB: PDB                                   
REMARK 900 ALANINE RACEMASE WITH BOUND INHIBITOR DERIVED FROM D-                
REMARK 900 CYCLOSERINE                                                          
REMARK 900 RELATED ID: 1L6F   RELATED DB: PDB                                   
REMARK 900 ALANINE RACEMASE BOUND WITH N-(5'-PHOSPHOPYRIDOXYL)-L-               
REMARK 900 ALANINE                                                              
REMARK 900 RELATED ID: 2SFP   RELATED DB: PDB                                   
REMARK 900 ALANINE RACEMASE WITH BOUND PROPIONATE INHIBITOR                     
DBREF  1RCQ A    1   357  UNP    Q9HTQ2   ALR2_PSEAE       1    357             
SEQADV 1RCQ KCX A  122  UNP  Q9HTQ2    LYS   122 MODIFIED RESIDUE               
SEQRES   1 A  357  MET ARG PRO ALA ARG ALA LEU ILE ASP LEU GLN ALA LEU          
SEQRES   2 A  357  ARG HIS ASN TYR ARG LEU ALA ARG GLU ALA THR GLY ALA          
SEQRES   3 A  357  ARG ALA LEU ALA VAL ILE LYS ALA ASP ALA TYR GLY HIS          
SEQRES   4 A  357  GLY ALA VAL ARG CYS ALA GLU ALA LEU ALA ALA GLU ALA          
SEQRES   5 A  357  ASP GLY PHE ALA VAL ALA CYS ILE GLU GLU GLY LEU GLU          
SEQRES   6 A  357  LEU ARG GLU ALA GLY ILE ARG GLN PRO ILE LEU LEU LEU          
SEQRES   7 A  357  GLU GLY PHE PHE GLU ALA SER GLU LEU GLU LEU ILE VAL          
SEQRES   8 A  357  ALA HIS ASP PHE TRP CYS VAL VAL HIS CYS ALA TRP GLN          
SEQRES   9 A  357  LEU GLU ALA ILE GLU ARG ALA SER LEU ALA ARG PRO LEU          
SEQRES  10 A  357  ASN VAL TRP LEU KCX MET ASP SER GLY MET HIS ARG VAL          
SEQRES  11 A  357  GLY PHE PHE PRO GLU ASP PHE ARG ALA ALA HIS GLU ARG          
SEQRES  12 A  357  LEU ARG ALA SER GLY LYS VAL ALA LYS ILE VAL MET MET          
SEQRES  13 A  357  SER HIS PHE SER ARG ALA ASP GLU LEU ASP CYS PRO ARG          
SEQRES  14 A  357  THR GLU GLU GLN LEU ALA ALA PHE SER ALA ALA SER GLN          
SEQRES  15 A  357  GLY LEU GLU GLY GLU ILE SER LEU ARG ASN SER PRO ALA          
SEQRES  16 A  357  VAL LEU GLY TRP PRO LYS VAL PRO SER ASP TRP VAL ARG          
SEQRES  17 A  357  PRO GLY ILE LEU LEU TYR GLY ALA THR PRO PHE GLU ARG          
SEQRES  18 A  357  ALA HIS PRO LEU ALA ASP ARG LEU ARG PRO VAL MET THR          
SEQRES  19 A  357  LEU GLU SER LYS VAL ILE SER VAL ARG ASP LEU PRO ALA          
SEQRES  20 A  357  GLY GLU PRO VAL GLY TYR GLY ALA ARG TYR SER THR GLU          
SEQRES  21 A  357  ARG ARG GLN ARG ILE GLY VAL VAL ALA MET GLY TYR ALA          
SEQRES  22 A  357  ASP GLY TYR PRO ARG HIS ALA ALA ASP GLY THR LEU VAL          
SEQRES  23 A  357  PHE ILE ASP GLY LYS PRO GLY ARG LEU VAL GLY ARG VAL          
SEQRES  24 A  357  SER MET ASP MET LEU THR VAL ASP LEU THR ASP HIS PRO          
SEQRES  25 A  357  GLN ALA GLY LEU GLY SER ARG VAL GLU LEU TRP GLY PRO          
SEQRES  26 A  357  ASN VAL PRO VAL GLY ALA LEU ALA ALA GLN PHE GLY SER          
SEQRES  27 A  357  ILE PRO TYR GLN LEU LEU CYS ASN LEU LYS ARG VAL PRO          
SEQRES  28 A  357  ARG VAL TYR SER GLY ALA                                      
MODRES 1RCQ KCX A  122  LYS  LYSINE NZ-CARBOXYLIC ACID                          
HET    KCX  A 122      12                                                       
HET    PLP  A 358      30                                                       
HET    DLY  A 359      10                                                       
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID                                        
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETNAM     DLY D-LYSINE                                                         
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
FORMUL   1  KCX    C7 H14 N2 O4                                                 
FORMUL   2  PLP    C8 H10 N O6 P                                                
FORMUL   3  DLY    C6 H14 N2 O2                                                 
FORMUL   4  HOH   *306(H2 O)                                                    
HELIX    1   1 LEU A   10  GLY A   25  1                                  16    
HELIX    2   2 ILE A   32  GLY A   38  1                                   7    
HELIX    3   3 GLY A   40  ALA A   49  1                                  10    
HELIX    4   4 CYS A   59  ALA A   69  1                                  11    
HELIX    5   5 GLU A   83  SER A   85  5                                   3    
HELIX    6   6 GLU A   86  HIS A   93  1                                   8    
HELIX    7   7 CYS A  101  ALA A  111  1                                  11    
HELIX    8   8 PHE A  133  SER A  147  1                                  15    
HELIX    9   9 PRO A  168  GLN A  182  1                                  15    
HELIX   10  10 ASN A  192  TRP A  199  1                                   8    
HELIX   11  11 GLY A  210  GLY A  215  5                                   6    
HELIX   12  12 LEU A  225  LEU A  229  5                                   5    
HELIX   13  13 GLY A  252  ARG A  256  5                                   5    
HELIX   14  14 GLY A  271  GLY A  275  5                                   5    
HELIX   15  15 PRO A  328  PHE A  336  1                                   9    
HELIX   16  16 ILE A  339  ASN A  346  1                                   8    
SHEET    1   A 6 LYS A 291  ARG A 294  0                                        
SHEET    2   A 6 LEU A 285  ILE A 288 -1  N  ILE A 288   O  LYS A 291           
SHEET    3   A 6 ARG A 319  TRP A 323 -1  O  GLU A 321   N  PHE A 287           
SHEET    4   A 6 MET A 233  LEU A 245 -1  N  LEU A 235   O  LEU A 322           
SHEET    5   A 6 GLN A 263  VAL A 268 -1  O  GLN A 263   N  LEU A 245           
SHEET    6   A 6 LEU A 304  ASP A 307 -1  O  LEU A 304   N  VAL A 268           
SHEET    1   B 6 LYS A 291  ARG A 294  0                                        
SHEET    2   B 6 LEU A 285  ILE A 288 -1  N  ILE A 288   O  LYS A 291           
SHEET    3   B 6 ARG A 319  TRP A 323 -1  O  GLU A 321   N  PHE A 287           
SHEET    4   B 6 MET A 233  LEU A 245 -1  N  LEU A 235   O  LEU A 322           
SHEET    5   B 6 ARG A   5  ASP A   9 -1  N  LEU A   7   O  THR A 234           
SHEET    6   B 6 ARG A 352  SER A 355  1  O  VAL A 353   N  ILE A   8           
SHEET    1   C 8 ILE A 188  SER A 189  0                                        
SHEET    2   C 8 VAL A 150  MET A 156  1  N  MET A 155   O  SER A 189           
SHEET    3   C 8 LEU A 117  KCX A 122  1  N  LEU A 121   O  MET A 156           
SHEET    4   C 8 PHE A  95  VAL A  99  1  N  VAL A  99   O  TRP A 120           
SHEET    5   C 8 ILE A  75  LEU A  77  1  N  ILE A  75   O  TRP A  96           
SHEET    6   C 8 GLY A  54  VAL A  57  1  N  VAL A  57   O  LEU A  76           
SHEET    7   C 8 ARG A  27  VAL A  31  1  N  ALA A  30   O  GLY A  54           
SHEET    8   C 8 TRP A 206  VAL A 207  1  O  VAL A 207   N  ARG A  27           
SHEET    1   D 2 PRO A 250  VAL A 251  0                                        
SHEET    2   D 2 TYR A 257  SER A 258 -1  O  TYR A 257   N  VAL A 251           
LINK         NZ  LYS A  33                 C4AAPLP A 358     1555   1555  1.31  
LINK         NZ  LYS A  33                 C4ABPLP A 358     1555   1555  1.78  
LINK         C   LEU A 121                 N   KCX A 122     1555   1555  1.33  
LINK         C   KCX A 122                 N   MET A 123     1555   1555  1.33  
LINK         C4ABPLP A 358                 NZ  DLY A 359     1555   1555  1.31  
SITE     1 AC1 16 VAL A  31  LYS A  33  TYR A  37  KCX A 122                    
SITE     2 AC1 16 ARG A 129  HIS A 158  ASN A 192  SER A 193                    
SITE     3 AC1 16 PRO A 194  ARG A 208  GLY A 210  ILE A 211                    
SITE     4 AC1 16 TYR A 341  DLY A 359  HOH A 531  HOH A 603                    
SITE     1 AC2 14 LYS A  33  TYR A  37  ARG A 129  TYR A 253                    
SITE     2 AC2 14 TYR A 272  SER A 300  MET A 301  ASP A 302                    
SITE     3 AC2 14 MET A 303  TYR A 341  PLP A 358  HOH A 518                    
SITE     4 AC2 14 HOH A 601  HOH A 603                                          
CRYST1   72.679   76.129  136.266  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013759  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013136  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007339        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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