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Database: PDB
Entry: 1XFC
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HEADER    ISOMERASE                               14-SEP-04   1XFC              
TITLE     THE 1.9 A CRYSTAL STRUCTURE OF ALANINE RACEMASE FROM MYCOBACTERIUM    
TITLE    2 TUBERCULOSIS CONTAINS A CONSERVED ENTRYWAY INTO THE ACTIVE SITE      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALANINE RACEMASE;                                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 5.1.1.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 1773;                                                
SOURCE   4 GENE: ALR;                                                           
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: PMB1909                                   
KEYWDS    ALPHA-BETA BARREL, BETA-STRUCTURE FOR C-TERMINAL DOMAIN, INTERNAL     
KEYWDS   2 ALDIMINE FORM, ISOMERASE                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.LEMAGUERES,H.IM,J.EBALUNODE,U.STRYCH,M.J.BENEDIK,J.M.BRIGGS,H.KOHN, 
AUTHOR   2 K.L.KRAUSE                                                           
REVDAT   3   13-JUL-11 1XFC    1       VERSN                                    
REVDAT   2   24-FEB-09 1XFC    1       VERSN                                    
REVDAT   1   16-AUG-05 1XFC    0                                                
JRNL        AUTH   P.LEMAGUERES,H.IM,J.EBALUNODE,U.STRYCH,M.J.BENEDIK,          
JRNL        AUTH 2 J.M.BRIGGS,H.KOHN,K.L.KRAUSE                                 
JRNL        TITL   THE 1.9 A CRYSTAL STRUCTURE OF ALANINE RACEMASE FROM         
JRNL        TITL 2 MYCOBACTERIUM TUBERCULOSIS CONTAINS A CONSERVED ENTRYWAY     
JRNL        TITL 3 INTO THE ACTIVE SITE.                                        
JRNL        REF    BIOCHEMISTRY                  V.  44  1471 2005              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   15683232                                                     
JRNL        DOI    10.1021/BI0486583                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   P.LE MAGUERES,H.IM,A.DVORAK,U.STRYCH,M.BENEDIK,K.L.KRAUSE    
REMARK   1  TITL   CRYSTAL STRUCTURE AT 1.45 A RESOLUTION OF ALANINE RACEMASE   
REMARK   1  TITL 2 FROM A PATHOGENIC BACTERIUM, PSEUDOMONAS AERUGINOSA,         
REMARK   1  TITL 3 CONTAINS BOTH INTERNAL AND EXTERNAL ALDIMINE FORMS           
REMARK   1  REF    BIOCHEMISTRY                  V.  42 14752 2003              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  PMID   14674749                                                     
REMARK   1  DOI    10.1021/BI030165V                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
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) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.214                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.254                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 1747                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 63019                  
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      : 5360                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 30                                            
REMARK   3   SOLVENT ATOMS      : 350                                           
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) : 0.006                   
REMARK   3   ANGLE DISTANCES                      (A) : 1.900                   
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 1XFC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-SEP-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB030297.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUN-02; 30-JUN-02               
REMARK 200  TEMPERATURE           (KELVIN) : 93; 93                             
REMARK 200  PH                             : 9.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : CHESS; CHESS                       
REMARK 200  BEAMLINE                       : F1; F1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.916; 0.9788, 0.9790, 0.9562,     
REMARK 200                                   0.9809                             
REMARK 200  MONOCHROMATOR                  : 0.9 POLARIZATION; 0.95             
REMARK 200                                   POLARIZATION                       
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4; ADSC QUANTUM 4     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 67592                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.2                               
REMARK 200  DATA REDUNDANCY                : 11.500                             
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 34.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.67200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD                         
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   (%): 48.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CARBONATE/BICARBONATE, CACL2,     
REMARK 280  PEG400, HEPES, PH 9.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE   
REMARK 280  277K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
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   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       28.94000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       82.39000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       82.39000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       14.47000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       82.39000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       82.39000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       43.41000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       82.39000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       82.39000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       14.47000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       82.39000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       82.39000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       43.41000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       28.94000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 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                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4930 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 482  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 391  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 493  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     ILE A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     LEU A    10                                                      
REMARK 465     VAL A   174                                                      
REMARK 465     TYR A   175                                                      
REMARK 465     ALA A   176                                                      
REMARK 465     ASP A   177                                                      
REMARK 465     LYS A   178                                                      
REMARK 465     GLU A   382                                                      
REMARK 465     ASN A   383                                                      
REMARK 465     ARG A   384                                                      
REMARK 465     MET B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     PRO B     3                                                      
REMARK 465     ILE B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     GLN B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     PRO B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     LEU B    10                                                      
REMARK 465     ARG B   264                                                      
REMARK 465     ALA B   265                                                      
REMARK 465     GLY B   266                                                      
REMARK 465     GLU B   267                                                      
REMARK 465     GLY B   268                                                      
REMARK 465     VAL B   269                                                      
REMARK 465     SER B   270                                                      
REMARK 465     TYR B   271                                                      
REMARK 465     GLY B   272                                                      
REMARK 465     HIS B   273                                                      
REMARK 465     THR B   274                                                      
REMARK 465     TRP B   275                                                      
REMARK 465     ILE B   276                                                      
REMARK 465     ALA B   277                                                      
REMARK 465     PRO B   278                                                      
REMARK 465     GLU B   382                                                      
REMARK 465     ASN B   383                                                      
REMARK 465     ARG B   384                                                      
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     ARG A 140    CG   CD   NE   CZ   NH1  NH2                        
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 156   CD  -  NE  -  CZ  ANGL. DEV. =  11.7 DEGREES          
REMARK 500    ARG A 156   NE  -  CZ  -  NH1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG A 310   CD  -  NE  -  CZ  ANGL. DEV. =  12.5 DEGREES          
REMARK 500    ARG A 310   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG B 156   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG B 219   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG B 376   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 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  42      170.75    -58.89                                   
REMARK 500    PHE A 224     -123.00   -100.25                                   
REMARK 500    SER A 270      177.22     65.64                                   
REMARK 500    PRO A 287       41.96    -88.90                                   
REMARK 500    THR A 361     -152.60   -137.29                                   
REMARK 500    ARG A 371     -155.91   -167.79                                   
REMARK 500    ARG B 140     -106.49   -103.11                                   
REMARK 500    ASP B 177       21.33   -142.10                                   
REMARK 500    PRO B 179      -17.28    -46.89                                   
REMARK 500    PHE B 224     -124.36    -99.61                                   
REMARK 500    MET B 245       29.46     47.99                                   
REMARK 500    THR B 361     -153.34   -133.58                                   
REMARK 500    ARG B 371     -159.77   -163.22                                   
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 B 568        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH B 575        DISTANCE =  5.03 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 390                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 390                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1RCQ   RELATED DB: PDB                                   
REMARK 900 ALANINE RACEMASE DADX FROM PSEUDOMONAS AERUGINOSA                    
REMARK 900 RELATED ID: 1SFT   RELATED DB: PDB                                   
REMARK 900 ALANINE RACEMASE ALR FROM GEOBACILLUS STEAROTHERMOPHILUS             
REMARK 900 COMPLEXED WITH ACETATE                                               
REMARK 900 RELATED ID: 2SFP   RELATED DB: PDB                                   
REMARK 900 ALANINE RACEMASE ALR FROM GEOBACILLUS STEAROTHERMOPHILUS             
REMARK 900 COMPLEXED WITH PROPIONATE                                            
REMARK 900 RELATED ID: 1BDO   RELATED DB: PDB                                   
REMARK 900 ALANINE RACEMASE ALR FROM GEOBACILLUS STEAROTHERMOPHILUS             
REMARK 900 COMPLEXED WITH ALANINE PHOSPHONATE                                   
REMARK 900 RELATED ID: 1L6F   RELATED DB: PDB                                   
REMARK 900 ALANINE RACEMASE ALR BOUND WITH N-(5'-PHOSPHOPYRIDOXYL)-L-           
REMARK 900 ALANINE                                                              
REMARK 900 RELATED ID: 1EPV   RELATED DB: PDB                                   
REMARK 900 ALANINE RACEMASE ALR WITH BOUND INHIBITOR DERIVED FROM D-            
REMARK 900 CYCLOSERINE                                                          
DBREF  1XFC A    1   384  UNP    P0A4X2   ALR_MYCTU        3    386             
DBREF  1XFC B    1   384  UNP    P0A4X2   ALR_MYCTU        3    386             
SEQRES   1 A  384  MET THR PRO ILE SER GLN THR PRO GLY LEU LEU ALA GLU          
SEQRES   2 A  384  ALA MET VAL ASP LEU GLY ALA ILE GLU HIS ASN VAL ARG          
SEQRES   3 A  384  VAL LEU ARG GLU HIS ALA GLY HIS ALA GLN LEU MET ALA          
SEQRES   4 A  384  VAL VAL LYS ALA ASP GLY TYR GLY HIS GLY ALA THR ARG          
SEQRES   5 A  384  VAL ALA GLN THR ALA LEU GLY ALA GLY ALA ALA GLU LEU          
SEQRES   6 A  384  GLY VAL ALA THR VAL ASP GLU ALA LEU ALA LEU ARG ALA          
SEQRES   7 A  384  ASP GLY ILE THR ALA PRO VAL LEU ALA TRP LEU HIS PRO          
SEQRES   8 A  384  PRO GLY ILE ASP PHE GLY PRO ALA LEU LEU ALA ASP VAL          
SEQRES   9 A  384  GLN VAL ALA VAL SER SER LEU ARG GLN LEU ASP GLU LEU          
SEQRES  10 A  384  LEU HIS ALA VAL ARG ARG THR GLY ARG THR ALA THR VAL          
SEQRES  11 A  384  THR VAL LYS VAL ASP THR GLY LEU ASN ARG ASN GLY VAL          
SEQRES  12 A  384  GLY PRO ALA GLN PHE PRO ALA MET LEU THR ALA LEU ARG          
SEQRES  13 A  384  GLN ALA MET ALA GLU ASP ALA VAL ARG LEU ARG GLY LEU          
SEQRES  14 A  384  MET SER HIS MET VAL TYR ALA ASP LYS PRO ASP ASP SER          
SEQRES  15 A  384  ILE ASN ASP VAL GLN ALA GLN ARG PHE THR ALA PHE LEU          
SEQRES  16 A  384  ALA GLN ALA ARG GLU GLN GLY VAL ARG PHE GLU VAL ALA          
SEQRES  17 A  384  HIS LEU SER ASN SER SER ALA THR MET ALA ARG PRO ASP          
SEQRES  18 A  384  LEU THR PHE ASP LEU VAL ARG PRO GLY ILE ALA VAL TYR          
SEQRES  19 A  384  GLY LEU SER PRO VAL PRO ALA LEU GLY ASP MET GLY LEU          
SEQRES  20 A  384  VAL PRO ALA MET THR VAL LYS CYS ALA VAL ALA LEU VAL          
SEQRES  21 A  384  LYS SER ILE ARG ALA GLY GLU GLY VAL SER TYR GLY HIS          
SEQRES  22 A  384  THR TRP ILE ALA PRO ARG ASP THR ASN LEU ALA LEU LEU          
SEQRES  23 A  384  PRO ILE GLY TYR ALA ASP GLY VAL PHE ARG SER LEU GLY          
SEQRES  24 A  384  GLY ARG LEU GLU VAL LEU ILE ASN GLY ARG ARG CYS PRO          
SEQRES  25 A  384  GLY VAL GLY ARG ILE CYS MET ASP GLN PHE MET VAL ASP          
SEQRES  26 A  384  LEU GLY PRO GLY PRO LEU ASP VAL ALA GLU GLY ASP GLU          
SEQRES  27 A  384  ALA ILE LEU PHE GLY PRO GLY ILE ARG GLY GLU PRO THR          
SEQRES  28 A  384  ALA GLN ASP TRP ALA ASP LEU VAL GLY THR ILE HIS TYR          
SEQRES  29 A  384  GLU VAL VAL THR SER PRO ARG GLY ARG ILE THR ARG THR          
SEQRES  30 A  384  TYR ARG GLU ALA GLU ASN ARG                                  
SEQRES   1 B  384  MET THR PRO ILE SER GLN THR PRO GLY LEU LEU ALA GLU          
SEQRES   2 B  384  ALA MET VAL ASP LEU GLY ALA ILE GLU HIS ASN VAL ARG          
SEQRES   3 B  384  VAL LEU ARG GLU HIS ALA GLY HIS ALA GLN LEU MET ALA          
SEQRES   4 B  384  VAL VAL LYS ALA ASP GLY TYR GLY HIS GLY ALA THR ARG          
SEQRES   5 B  384  VAL ALA GLN THR ALA LEU GLY ALA GLY ALA ALA GLU LEU          
SEQRES   6 B  384  GLY VAL ALA THR VAL ASP GLU ALA LEU ALA LEU ARG ALA          
SEQRES   7 B  384  ASP GLY ILE THR ALA PRO VAL LEU ALA TRP LEU HIS PRO          
SEQRES   8 B  384  PRO GLY ILE ASP PHE GLY PRO ALA LEU LEU ALA ASP VAL          
SEQRES   9 B  384  GLN VAL ALA VAL SER SER LEU ARG GLN LEU ASP GLU LEU          
SEQRES  10 B  384  LEU HIS ALA VAL ARG ARG THR GLY ARG THR ALA THR VAL          
SEQRES  11 B  384  THR VAL LYS VAL ASP THR GLY LEU ASN ARG ASN GLY VAL          
SEQRES  12 B  384  GLY PRO ALA GLN PHE PRO ALA MET LEU THR ALA LEU ARG          
SEQRES  13 B  384  GLN ALA MET ALA GLU ASP ALA VAL ARG LEU ARG GLY LEU          
SEQRES  14 B  384  MET SER HIS MET VAL TYR ALA ASP LYS PRO ASP ASP SER          
SEQRES  15 B  384  ILE ASN ASP VAL GLN ALA GLN ARG PHE THR ALA PHE LEU          
SEQRES  16 B  384  ALA GLN ALA ARG GLU GLN GLY VAL ARG PHE GLU VAL ALA          
SEQRES  17 B  384  HIS LEU SER ASN SER SER ALA THR MET ALA ARG PRO ASP          
SEQRES  18 B  384  LEU THR PHE ASP LEU VAL ARG PRO GLY ILE ALA VAL TYR          
SEQRES  19 B  384  GLY LEU SER PRO VAL PRO ALA LEU GLY ASP MET GLY LEU          
SEQRES  20 B  384  VAL PRO ALA MET THR VAL LYS CYS ALA VAL ALA LEU VAL          
SEQRES  21 B  384  LYS SER ILE ARG ALA GLY GLU GLY VAL SER TYR GLY HIS          
SEQRES  22 B  384  THR TRP ILE ALA PRO ARG ASP THR ASN LEU ALA LEU LEU          
SEQRES  23 B  384  PRO ILE GLY TYR ALA ASP GLY VAL PHE ARG SER LEU GLY          
SEQRES  24 B  384  GLY ARG LEU GLU VAL LEU ILE ASN GLY ARG ARG CYS PRO          
SEQRES  25 B  384  GLY VAL GLY ARG ILE CYS MET ASP GLN PHE MET VAL ASP          
SEQRES  26 B  384  LEU GLY PRO GLY PRO LEU ASP VAL ALA GLU GLY ASP GLU          
SEQRES  27 B  384  ALA ILE LEU PHE GLY PRO GLY ILE ARG GLY GLU PRO THR          
SEQRES  28 B  384  ALA GLN ASP TRP ALA ASP LEU VAL GLY THR ILE HIS TYR          
SEQRES  29 B  384  GLU VAL VAL THR SER PRO ARG GLY ARG ILE THR ARG THR          
SEQRES  30 B  384  TYR ARG GLU ALA GLU ASN ARG                                  
HET    PLP  A 390      15                                                       
HET    PLP  B 390      15                                                       
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
FORMUL   3  PLP    2(C8 H10 N O6 P)                                             
FORMUL   5  HOH   *350(H2 O)                                                    
HELIX    1   1 LEU A   18  GLY A   33  1                                  16    
HELIX    2   2 VAL A   41  GLY A   47  1                                   7    
HELIX    3   3 GLY A   49  ALA A   60  1                                  12    
HELIX    4   4 THR A   69  ASP A   79  1                                  11    
HELIX    5   5 PHE A   96  ALA A  102  1                                   7    
HELIX    6   6 SER A  110  GLY A  125  1                                  16    
HELIX    7   7 GLN A  147  GLU A  161  1                                  15    
HELIX    8   8 ASP A  181  GLN A  201  1                                  21    
HELIX    9   9 ASN A  212  ARG A  219  1                                   8    
HELIX   10  10 PRO A  220  THR A  223  5                                   4    
HELIX   11  11 GLY A  230  GLY A  235  5                                   6    
HELIX   12  12 VAL A  239  GLY A  243  5                                   5    
HELIX   13  13 SER A  270  THR A  274  5                                   5    
HELIX   14  14 GLY A  289  GLY A  293  5                                   5    
HELIX   15  15 PHE A  295  GLY A  299  5                                   5    
HELIX   16  16 THR A  351  GLY A  360  1                                  10    
HELIX   17  17 ILE A  362  THR A  368  1                                   7    
HELIX   18  18 LEU B   18  GLY B   33  1                                  16    
HELIX   19  19 VAL B   41  GLY B   47  1                                   7    
HELIX   20  20 GLY B   49  ALA B   60  1                                  12    
HELIX   21  21 THR B   69  ASP B   79  1                                  11    
HELIX   22  22 PHE B   96  ALA B  102  1                                   7    
HELIX   23  23 SER B  110  GLY B  125  1                                  16    
HELIX   24  24 GLN B  147  GLU B  161  1                                  15    
HELIX   25  25 ASP B  181  GLN B  201  1                                  21    
HELIX   26  26 ASN B  212  ARG B  219  1                                   8    
HELIX   27  27 PRO B  220  THR B  223  5                                   4    
HELIX   28  28 GLY B  230  GLY B  235  5                                   6    
HELIX   29  29 VAL B  239  GLY B  243  5                                   5    
HELIX   30  30 GLY B  289  GLY B  293  5                                   5    
HELIX   31  31 PHE B  295  GLY B  299  5                                   5    
HELIX   32  32 THR B  351  GLY B  360  1                                  10    
HELIX   33  33 ILE B  362  THR B  368  1                                   7    
SHEET    1   A 9 LEU A 259  ILE A 263  0                                        
SHEET    2   A 9 THR A 281  LEU A 286 -1  O  THR A 281   N  ILE A 263           
SHEET    3   A 9 PHE A 322  GLY A 327 -1  O  PHE A 322   N  LEU A 286           
SHEET    4   A 9 ARG A 309  VAL A 314 -1  N  PRO A 312   O  ASP A 325           
SHEET    5   A 9 GLU A 303  ILE A 306 -1  N  VAL A 304   O  CYS A 311           
SHEET    6   A 9 GLU A 338  PHE A 342 -1  O  ILE A 340   N  LEU A 305           
SHEET    7   A 9 MET A 251  ALA A 256 -1  N  CYS A 255   O  ALA A 339           
SHEET    8   A 9 ALA A  12  ASP A  17 -1  N  GLU A  13   O  LYS A 254           
SHEET    9   A 9 ILE A 374  ARG A 379  1  O  THR A 377   N  VAL A  16           
SHEET    1   B 8 VAL A 207  HIS A 209  0                                        
SHEET    2   B 8 VAL A 164  MET A 170  1  N  ARG A 167   O  VAL A 207           
SHEET    3   B 8 ALA A 128  LYS A 133  1  N  ALA A 128   O  ARG A 165           
SHEET    4   B 8 GLN A 105  VAL A 108  1  N  VAL A 108   O  THR A 131           
SHEET    5   B 8 VAL A  85  ALA A  87  1  N  ALA A  87   O  ALA A 107           
SHEET    6   B 8 GLU A  64  VAL A  67  1  N  VAL A  67   O  LEU A  86           
SHEET    7   B 8 GLN A  36  VAL A  40  1  N  ALA A  39   O  GLY A  66           
SHEET    8   B 8 LEU A 226  VAL A 227  1  O  VAL A 227   N  MET A  38           
SHEET    1   C 2 GLY A 268  VAL A 269  0                                        
SHEET    2   C 2 TRP A 275  ILE A 276 -1  O  TRP A 275   N  VAL A 269           
SHEET    1   D 4 GLU B 338  PHE B 342  0                                        
SHEET    2   D 4 MET B 251  ALA B 256 -1  N  CYS B 255   O  ALA B 339           
SHEET    3   D 4 ALA B  12  ASP B  17 -1  N  MET B  15   O  THR B 252           
SHEET    4   D 4 ILE B 374  ARG B 379  1  O  THR B 377   N  ALA B  14           
SHEET    1   E 9 GLN B  36  VAL B  40  0                                        
SHEET    2   E 9 GLU B  64  VAL B  67  1  O  GLY B  66   N  ALA B  39           
SHEET    3   E 9 VAL B  85  ALA B  87  1  O  LEU B  86   N  VAL B  67           
SHEET    4   E 9 GLN B 105  VAL B 108  1  O  ALA B 107   N  ALA B  87           
SHEET    5   E 9 ALA B 128  LYS B 133  1  O  LYS B 133   N  VAL B 108           
SHEET    6   E 9 VAL B 164  MET B 170  1  O  ARG B 165   N  ALA B 128           
SHEET    7   E 9 VAL B 207  SER B 211  1  O  HIS B 209   N  LEU B 169           
SHEET    8   E 9 LEU B 226  VAL B 227  1  N  LEU B 226   O  ALA B 208           
SHEET    9   E 9 GLN B  36  VAL B  40  1  N  MET B  38   O  VAL B 227           
SHEET    1   F 5 LEU B 259  ILE B 263  0                                        
SHEET    2   F 5 THR B 281  LEU B 286 -1  O  THR B 281   N  ILE B 263           
SHEET    3   F 5 PHE B 322  GLY B 327 -1  O  LEU B 326   N  ASN B 282           
SHEET    4   F 5 ARG B 309  VAL B 314 -1  N  PRO B 312   O  ASP B 325           
SHEET    5   F 5 GLU B 303  ILE B 306 -1  N  ILE B 306   O  ARG B 309           
LINK         NZ  LYS A  42                 C4A PLP A 390     1555   1555  1.31  
LINK         NZ  LYS B  42                 C4A PLP B 390     1555   1555  1.30  
SITE     1 AC1 13 LYS A  42  TYR A  46  TRP A  88  HIS A 172                    
SITE     2 AC1 13 ASN A 212  SER A 213  ARG A 228  GLY A 230                    
SITE     3 AC1 13 ILE A 231  TYR A 364  HOH A 426  HOH A 543                    
SITE     4 AC1 13 HOH A 551                                                     
SITE     1 AC2 11 LYS B  42  TYR B  46  TRP B  88  HIS B 172                    
SITE     2 AC2 11 SER B 213  ARG B 228  GLY B 230  ILE B 231                    
SITE     3 AC2 11 TYR B 364  HOH B 429  HOH B 537                               
CRYST1  164.780  164.780   57.880  90.00  90.00  90.00 P 41 21 2    16          
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      0.006069  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006069  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017277        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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