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Database: PDB
Entry: 3HA1
LinkDB: 3HA1
Original site: 3HA1 
HEADER    ISOMERASE                               30-APR-09   3HA1              
TITLE     ALANINE RACEMASE FROM BACILLUS ANTHRACIS (AMES)                       
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: BACILLUS ANTHRACIS;                             
SOURCE   3 ORGANISM_COMMON: ANTHRAX,ANTHRAX BACTERIUM;                          
SOURCE   4 ORGANISM_TAXID: 1392;                                                
SOURCE   5 STRAIN: AMES;                                                        
SOURCE   6 GENE: DAL-1, DAL1;                                                   
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET28-TEV-DAL                             
KEYWDS    ALANINE RACEMASE, ISOMERASE, PLP, PYRIDOXAL PHOSPHATE                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.M.COUNAGO,M.DAVLIEVA,U.STRYCH,R.E.HILL,K.L.KRAUSE                   
REVDAT   1   15-SEP-09 3HA1    0                                                
JRNL        AUTH   R.M.COUNAGO,M.DAVLIEVA,U.STRYCH,R.E.HILL,K.L.KRAUSE          
JRNL        TITL   BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF               
JRNL        TITL 2 ALANINE RACEMASE FROM BACILLUS ANTHRACIS (AMES).             
JRNL        REF    BMC STRUCT.BIOL.              V.   9    53 2009              
JRNL        REFN                   ESSN 1472-6807                               
JRNL        PMID   19695097                                                     
JRNL        DOI    10.1186/1472-6807-9-53                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.79                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 53387                          
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) : 0.161                           
REMARK   3   R VALUE            (WORKING SET) : 0.160                           
REMARK   3   FREE R VALUE                     : 0.201                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1627                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.00                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2518                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 59.80                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1940                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 72                           
REMARK   3   BIN FREE R VALUE                    : 0.2340                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6068                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 358                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 29.12                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.69                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.56000                                              
REMARK   3    B22 (A**2) : -1.51000                                             
REMARK   3    B33 (A**2) : 0.20000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.55000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.161         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.144         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.096         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.304         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6222 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8487 ; 1.459 ; 1.956       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   770 ; 7.467 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   275 ;33.734 ;23.382       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   966 ;13.200 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    40 ;14.626 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   966 ; 0.120 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4750 ; 0.014 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  3844 ; 1.273 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6211 ; 1.912 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2378 ; 3.226 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2276 ; 4.742 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     4        A   389                          
REMARK   3    RESIDUE RANGE :   B     4        B   389                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.9820  -0.9620  12.3810              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1105 T22:   0.1302                                     
REMARK   3      T33:   0.0834 T12:  -0.0019                                     
REMARK   3      T13:   0.0307 T23:   0.0293                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5425 L22:   2.9722                                     
REMARK   3      L33:   0.8029 L12:   0.4525                                     
REMARK   3      L13:  -0.2239 L23:  -0.9074                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0366 S12:   0.0698 S13:   0.0878                       
REMARK   3      S21:  -0.1212 S22:   0.2327 S23:   0.4015                       
REMARK   3      S31:  -0.0113 S32:  -0.1290 S33:  -0.1961                       
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: ATOM RECORD SHOWS TOTAL B FACTORS.        
REMARK   4                                                                      
REMARK   4 3HA1 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAY-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB052880.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-NOV-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : OSMIC MIRRORS                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 53396                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.790                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.3                               
REMARK 200  DATA REDUNDANCY                : 2.800                              
REMARK 200  R MERGE                    (I) : 0.02900                            
REMARK 200  R SYM                      (I) : 0.02900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.5260                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 67.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.15600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.15600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1SFT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18 %PEG 8000, 0.2 M SODIUM ACETATE,      
REMARK 280  0.1 M SODIUM CACODYLATE, 0.01 M GSH (L-GLUTATHIONE REDUCED),        
REMARK 280  0.01 M GSSG (L-GLUTATHIONE OXIDIZED), PH 6.5, VAPOR DIFFUSION,      
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       70.63550            
REMARK 290   SMTRY3   2  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 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: 8020 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 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 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     GLU A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     LEU A   390                                                      
REMARK 465     GLU A   391                                                      
REMARK 465     GLU A   392                                                      
REMARK 465     ASN A   393                                                      
REMARK 465     LEU A   394                                                      
REMARK 465     TYR A   395                                                      
REMARK 465     PHE A   396                                                      
REMARK 465     GLN A   397                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     LEU B   390                                                      
REMARK 465     GLU B   391                                                      
REMARK 465     GLU B   392                                                      
REMARK 465     ASN B   393                                                      
REMARK 465     LEU B   394                                                      
REMARK 465     TYR B   395                                                      
REMARK 465     PHE B   396                                                      
REMARK 465     GLN B   397                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 100    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 145    CG   CD   CE   NZ                                   
REMARK 470     LYS A 152    CG   CD   CE   NZ                                   
REMARK 470     SER A 153    OG                                                  
REMARK 470     LYS A 182    CG   CD   CE   NZ                                   
REMARK 470     LYS A 195    CG   CD   CE   NZ                                   
REMARK 470     GLN A 216    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 245    CG   CD   CE   NZ                                   
REMARK 470     LYS A 378    CG   CD   CE   NZ                                   
REMARK 470     GLU A 381    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  27    CG   CD   CE   NZ                                   
REMARK 470     ILE B  95    CG1  CG2  CD1                                       
REMARK 470     GLU B 100    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 121    CG   OD1  OD2                                       
REMARK 470     SER B 123    OG                                                  
REMARK 470     SER B 124    OG                                                  
REMARK 470     LYS B 127    CG   CD   CE   NZ                                   
REMARK 470     LYS B 145    CG   CD   CE   NZ                                   
REMARK 470     LYS B 152    CG   CD   CE   NZ                                   
REMARK 470     SER B 153    OG                                                  
REMARK 470     LYS B 182    CG   CD   CE   NZ                                   
REMARK 470     LEU B 188    CG   CD1  CD2                                       
REMARK 470     LYS B 195    CG   CD   CE   NZ                                   
REMARK 470     ASP B 200    CG   OD1  OD2                                       
REMARK 470     GLN B 216    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 378    CG   CD   CE   NZ                                   
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    ASP A  48      116.79     98.29                                   
REMARK 500    PHE A 108       11.84   -152.41                                   
REMARK 500    ARG A 138      -82.74   -100.22                                   
REMARK 500    LYS A 202      -55.27     74.28                                   
REMARK 500    PHE A 220     -130.99     53.90                                   
REMARK 500    SER A 269     -174.73     69.94                                   
REMARK 500    THR A 356     -156.21   -140.17                                   
REMARK 500    ASP B  48      123.02     95.29                                   
REMARK 500    PHE B 108       15.19   -150.79                                   
REMARK 500    ARG B 138      -74.75   -104.21                                   
REMARK 500    LYS B 202      -55.83     82.02                                   
REMARK 500    PHE B 220     -132.28     53.54                                   
REMARK 500    SER B 269     -174.32     73.49                                   
REMARK 500    THR B 356     -156.49   -137.56                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 398                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 399                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 398                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 399                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1SFT   RELATED DB: PDB                                   
REMARK 900 ALANINE RACEMASE FROM G.STEAROTHERMOPHILUS                           
REMARK 900 RELATED ID: 2VD8   RELATED DB: PDB                                   
REMARK 900 ALANINE RACEMASE FROM B.ANTHRACIS (BA0252)                           
REMARK 900 RELATED ID: 1RCQ   RELATED DB: PDB                                   
REMARK 900 ALANINE RACEMASE FROM P.AERUGINOSA                                   
REMARK 900 RELATED ID: 1XFC   RELATED DB: PDB                                   
REMARK 900 ALANINE RACEMASE FROM M.TUBERCULOSIS                                 
DBREF  3HA1 A    1   389  UNP    Q81VF6   Q81VF6_BACAN     1    389             
DBREF  3HA1 B    1   389  UNP    Q81VF6   Q81VF6_BACAN     1    389             
SEQADV 3HA1 LEU A  390  UNP  Q81VF6              EXPRESSION TAG                 
SEQADV 3HA1 GLU A  391  UNP  Q81VF6              EXPRESSION TAG                 
SEQADV 3HA1 GLU A  392  UNP  Q81VF6              EXPRESSION TAG                 
SEQADV 3HA1 ASN A  393  UNP  Q81VF6              EXPRESSION TAG                 
SEQADV 3HA1 LEU A  394  UNP  Q81VF6              EXPRESSION TAG                 
SEQADV 3HA1 TYR A  395  UNP  Q81VF6              EXPRESSION TAG                 
SEQADV 3HA1 PHE A  396  UNP  Q81VF6              EXPRESSION TAG                 
SEQADV 3HA1 GLN A  397  UNP  Q81VF6              EXPRESSION TAG                 
SEQADV 3HA1 LEU B  390  UNP  Q81VF6              EXPRESSION TAG                 
SEQADV 3HA1 GLU B  391  UNP  Q81VF6              EXPRESSION TAG                 
SEQADV 3HA1 GLU B  392  UNP  Q81VF6              EXPRESSION TAG                 
SEQADV 3HA1 ASN B  393  UNP  Q81VF6              EXPRESSION TAG                 
SEQADV 3HA1 LEU B  394  UNP  Q81VF6              EXPRESSION TAG                 
SEQADV 3HA1 TYR B  395  UNP  Q81VF6              EXPRESSION TAG                 
SEQADV 3HA1 PHE B  396  UNP  Q81VF6              EXPRESSION TAG                 
SEQADV 3HA1 GLN B  397  UNP  Q81VF6              EXPRESSION TAG                 
SEQRES   1 A  397  MET GLU GLU ALA PRO PHE TYR ARG ASP THR TRP VAL GLU          
SEQRES   2 A  397  VAL ASP LEU ASP ALA ILE TYR ASN ASN VAL THR HIS ILE          
SEQRES   3 A  397  LYS GLU PHE ILE PRO SER ASP VAL GLU ILE PHE ALA VAL          
SEQRES   4 A  397  VAL LLP GLY ASN ALA TYR GLY HIS ASP TYR VAL PRO VAL          
SEQRES   5 A  397  ALA LYS ILE ALA LEU GLU ALA GLY ALA THR ARG LEU ALA          
SEQRES   6 A  397  VAL ALA PHE LEU ASP GLU ALA LEU VAL LEU ARG ARG ALA          
SEQRES   7 A  397  GLY ILE THR ALA PRO ILE LEU VAL LEU GLY PRO SER PRO          
SEQRES   8 A  397  PRO ARG ASP ILE ASN VAL ALA ALA GLU ASN ASP VAL ALA          
SEQRES   9 A  397  LEU THR VAL PHE GLN LYS GLU TRP VAL ASP GLU ALA ILE          
SEQRES  10 A  397  LYS LEU TRP ASP GLY SER SER THR MET LYS TYR HIS ILE          
SEQRES  11 A  397  ASN PHE ASP SER GLY MET GLY ARG ILE GLY ILE ARG GLU          
SEQRES  12 A  397  ARG LYS GLU LEU LYS GLY PHE LEU LYS SER LEU GLU GLY          
SEQRES  13 A  397  ALA PRO PHE LEU GLU LEU GLU GLY VAL TYR THR HIS PHE          
SEQRES  14 A  397  ALA THR ALA ASP GLU VAL GLU THR SER TYR PHE ASP LYS          
SEQRES  15 A  397  GLN TYR ASN THR PHE LEU GLU GLN LEU SER TRP LEU LYS          
SEQRES  16 A  397  GLU PHE GLY VAL ASP PRO LYS PHE VAL HIS THR ALA ASN          
SEQRES  17 A  397  SER ALA ALA THR LEU ARG PHE GLN GLY ILE THR PHE ASN          
SEQRES  18 A  397  ALA VAL ARG ILE GLY ILE ALA MET TYR GLY LEU SER PRO          
SEQRES  19 A  397  SER VAL GLU ILE ARG PRO PHE LEU PRO PHE LYS LEU GLU          
SEQRES  20 A  397  PRO ALA LEU SER LEU HIS THR LYS VAL ALA HIS ILE LYS          
SEQRES  21 A  397  GLN VAL ILE LYS GLY ASP GLY ILE SER TYR ASN VAL THR          
SEQRES  22 A  397  TYR ARG THR LYS THR GLU GLU TRP ILE ALA THR VAL ALA          
SEQRES  23 A  397  ILE GLY TYR ALA ASP GLY TRP LEU ARG ARG LEU GLN GLY          
SEQRES  24 A  397  PHE GLU VAL LEU VAL ASN GLY LYS ARG VAL PRO ILE VAL          
SEQRES  25 A  397  GLY ARG VAL THR MET ASP GLN PHE MET ILE HIS LEU PRO          
SEQRES  26 A  397  CYS GLU VAL PRO LEU GLY THR LYS VAL THR LEU ILE GLY          
SEQRES  27 A  397  ARG GLN GLY ASP GLU TYR ILE SER ALA THR GLU VAL ALA          
SEQRES  28 A  397  GLU TYR SER GLY THR ILE ASN TYR GLU ILE ILE THR THR          
SEQRES  29 A  397  ILE SER PHE ARG VAL PRO ARG ILE PHE ILE ARG ASN GLY          
SEQRES  30 A  397  LYS VAL VAL GLU VAL ILE ASN TYR LEU ASN ASP ILE LEU          
SEQRES  31 A  397  GLU GLU ASN LEU TYR PHE GLN                                  
SEQRES   1 B  397  MET GLU GLU ALA PRO PHE TYR ARG ASP THR TRP VAL GLU          
SEQRES   2 B  397  VAL ASP LEU ASP ALA ILE TYR ASN ASN VAL THR HIS ILE          
SEQRES   3 B  397  LYS GLU PHE ILE PRO SER ASP VAL GLU ILE PHE ALA VAL          
SEQRES   4 B  397  VAL LLP GLY ASN ALA TYR GLY HIS ASP TYR VAL PRO VAL          
SEQRES   5 B  397  ALA LYS ILE ALA LEU GLU ALA GLY ALA THR ARG LEU ALA          
SEQRES   6 B  397  VAL ALA PHE LEU ASP GLU ALA LEU VAL LEU ARG ARG ALA          
SEQRES   7 B  397  GLY ILE THR ALA PRO ILE LEU VAL LEU GLY PRO SER PRO          
SEQRES   8 B  397  PRO ARG ASP ILE ASN VAL ALA ALA GLU ASN ASP VAL ALA          
SEQRES   9 B  397  LEU THR VAL PHE GLN LYS GLU TRP VAL ASP GLU ALA ILE          
SEQRES  10 B  397  LYS LEU TRP ASP GLY SER SER THR MET LYS TYR HIS ILE          
SEQRES  11 B  397  ASN PHE ASP SER GLY MET GLY ARG ILE GLY ILE ARG GLU          
SEQRES  12 B  397  ARG LYS GLU LEU LYS GLY PHE LEU LYS SER LEU GLU GLY          
SEQRES  13 B  397  ALA PRO PHE LEU GLU LEU GLU GLY VAL TYR THR HIS PHE          
SEQRES  14 B  397  ALA THR ALA ASP GLU VAL GLU THR SER TYR PHE ASP LYS          
SEQRES  15 B  397  GLN TYR ASN THR PHE LEU GLU GLN LEU SER TRP LEU LYS          
SEQRES  16 B  397  GLU PHE GLY VAL ASP PRO LYS PHE VAL HIS THR ALA ASN          
SEQRES  17 B  397  SER ALA ALA THR LEU ARG PHE GLN GLY ILE THR PHE ASN          
SEQRES  18 B  397  ALA VAL ARG ILE GLY ILE ALA MET TYR GLY LEU SER PRO          
SEQRES  19 B  397  SER VAL GLU ILE ARG PRO PHE LEU PRO PHE LYS LEU GLU          
SEQRES  20 B  397  PRO ALA LEU SER LEU HIS THR LYS VAL ALA HIS ILE LYS          
SEQRES  21 B  397  GLN VAL ILE LYS GLY ASP GLY ILE SER TYR ASN VAL THR          
SEQRES  22 B  397  TYR ARG THR LYS THR GLU GLU TRP ILE ALA THR VAL ALA          
SEQRES  23 B  397  ILE GLY TYR ALA ASP GLY TRP LEU ARG ARG LEU GLN GLY          
SEQRES  24 B  397  PHE GLU VAL LEU VAL ASN GLY LYS ARG VAL PRO ILE VAL          
SEQRES  25 B  397  GLY ARG VAL THR MET ASP GLN PHE MET ILE HIS LEU PRO          
SEQRES  26 B  397  CYS GLU VAL PRO LEU GLY THR LYS VAL THR LEU ILE GLY          
SEQRES  27 B  397  ARG GLN GLY ASP GLU TYR ILE SER ALA THR GLU VAL ALA          
SEQRES  28 B  397  GLU TYR SER GLY THR ILE ASN TYR GLU ILE ILE THR THR          
SEQRES  29 B  397  ILE SER PHE ARG VAL PRO ARG ILE PHE ILE ARG ASN GLY          
SEQRES  30 B  397  LYS VAL VAL GLU VAL ILE ASN TYR LEU ASN ASP ILE LEU          
SEQRES  31 B  397  GLU GLU ASN LEU TYR PHE GLN                                  
MODRES 3HA1 LLP A   41  LYS                                                     
MODRES 3HA1 LLP B   41  LYS                                                     
HET    LLP  A  41      24                                                       
HET    LLP  B  41      24                                                       
HET    ACT  A 398       4                                                       
HET     CL  A 399       1                                                       
HET    ACT  B 398       4                                                       
HET     CL  B 399       1                                                       
HETNAM     LLP 2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-                
HETNAM   2 LLP  PYRIDIN-4-YLMETHANE)                                            
HETNAM     ACT ACETATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETSYN     LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE                             
FORMUL   1  LLP    2(C14 H24 N3 O7 P)                                           
FORMUL   3  ACT    2(C2 H3 O2 1-)                                               
FORMUL   4   CL    2(CL 1-)                                                     
FORMUL   7  HOH   *358(H2 O)                                                    
HELIX    1   1 LEU A   16  ILE A   30  1                                  15    
HELIX    2   2 VAL A   40  GLY A   46  1                                   7    
HELIX    3   3 ASP A   48  ALA A   59  1                                  12    
HELIX    4   4 PHE A   68  ALA A   78  1                                  11    
HELIX    5   5 PRO A   91  ARG A   93  5                                   3    
HELIX    6   6 ASP A   94  ASN A  101  1                                   8    
HELIX    7   7 GLN A  109  TRP A  120  1                                  12    
HELIX    8   8 GLU A  143  GLU A  155  1                                  13    
HELIX    9   9 THR A  177  PHE A  197  1                                  21    
HELIX   10  10 ASN A  208  PHE A  215  1                                   8    
HELIX   11  11 ILE A  238  LEU A  242  5                                   5    
HELIX   12  12 SER A  269  THR A  273  5                                   5    
HELIX   13  13 GLY A  288  GLY A  292  5                                   5    
HELIX   14  14 LEU A  294  GLN A  298  5                                   5    
HELIX   15  15 SER A  346  SER A  354  1                                   9    
HELIX   16  16 ILE A  357  THR A  364  1                                   8    
HELIX   17  17 ASN A  384  ILE A  389  5                                   6    
HELIX   18  18 LEU B   16  ILE B   30  1                                  15    
HELIX   19  19 VAL B   40  GLY B   46  1                                   7    
HELIX   20  20 ASP B   48  ALA B   59  1                                  12    
HELIX   21  21 PHE B   68  ALA B   78  1                                  11    
HELIX   22  22 PRO B   91  ARG B   93  5                                   3    
HELIX   23  23 ASP B   94  ASN B  101  1                                   8    
HELIX   24  24 GLN B  109  TRP B  120  1                                  12    
HELIX   25  25 GLU B  143  GLU B  155  1                                  13    
HELIX   26  26 THR B  177  PHE B  197  1                                  21    
HELIX   27  27 ASN B  208  PHE B  215  1                                   8    
HELIX   28  28 GLY B  226  GLY B  231  5                                   6    
HELIX   29  29 ILE B  238  LEU B  242  5                                   5    
HELIX   30  30 SER B  269  THR B  273  5                                   5    
HELIX   31  31 GLY B  288  GLY B  292  5                                   5    
HELIX   32  32 LEU B  294  GLN B  298  5                                   5    
HELIX   33  33 SER B  346  GLY B  355  1                                  10    
HELIX   34  34 ILE B  357  THR B  364  1                                   8    
HELIX   35  35 ASN B  384  ILE B  389  5                                   6    
SHEET    1   A 6 GLU A 343  ILE A 345  0                                        
SHEET    2   A 6 LYS A 333  GLN A 340 -1  N  GLY A 338   O  ILE A 345           
SHEET    3   A 6 LEU A 250  VAL A 262 -1  N  THR A 254   O  VAL A 334           
SHEET    4   A 6 THR A  10  ASP A  15 -1  N  GLU A  13   O  SER A 251           
SHEET    5   A 6 ARG A 371  ARG A 375  1  O  ILE A 372   N  VAL A  14           
SHEET    6   A 6 LYS A 378  ILE A 383 -1  O  GLU A 381   N  PHE A 373           
SHEET    1   B10 GLU A 343  ILE A 345  0                                        
SHEET    2   B10 LYS A 333  GLN A 340 -1  N  GLY A 338   O  ILE A 345           
SHEET    3   B10 GLU A 301  VAL A 304 -1  N  LEU A 303   O  THR A 335           
SHEET    4   B10 LYS A 307  VAL A 312 -1  O  VAL A 309   N  VAL A 302           
SHEET    5   B10 PHE A 320  LEU A 324 -1  O  MET A 321   N  VAL A 312           
SHEET    6   B10 GLU A 280  VAL A 285 -1  N  ALA A 283   O  ILE A 322           
SHEET    7   B10 LEU A 250  VAL A 262 -1  N  VAL A 262   O  GLU A 280           
SHEET    8   B10 THR A  10  ASP A  15 -1  N  GLU A  13   O  SER A 251           
SHEET    9   B10 ARG A 371  ARG A 375  1  O  ILE A 372   N  VAL A  14           
SHEET   10   B10 LYS A 378  ILE A 383 -1  O  GLU A 381   N  PHE A 373           
SHEET    1   C 9 GLU A  35  VAL A  39  0                                        
SHEET    2   C 9 ARG A  63  VAL A  66  1  O  ARG A  63   N  ALA A  38           
SHEET    3   C 9 ILE A  84  VAL A  86  1  O  LEU A  85   N  LEU A  64           
SHEET    4   C 9 VAL A 103  THR A 106  1  O  ALA A 104   N  VAL A  86           
SHEET    5   C 9 MET A 126  ASN A 131  1  O  HIS A 129   N  LEU A 105           
SHEET    6   C 9 LEU A 160  TYR A 166  1  O  TYR A 166   N  ILE A 130           
SHEET    7   C 9 VAL A 204  ALA A 207  1  O  HIS A 205   N  VAL A 165           
SHEET    8   C 9 ALA A 222  ILE A 225  1  O  ARG A 224   N  ALA A 207           
SHEET    9   C 9 GLU A  35  VAL A  39  1  N  VAL A  39   O  ILE A 225           
SHEET    1   D 2 GLY A 267  ILE A 268  0                                        
SHEET    2   D 2 TYR A 274  ARG A 275 -1  O  TYR A 274   N  ILE A 268           
SHEET    1   E 6 GLU B 343  ILE B 345  0                                        
SHEET    2   E 6 LYS B 333  GLN B 340 -1  N  GLN B 340   O  GLU B 343           
SHEET    3   E 6 LEU B 250  VAL B 262 -1  N  LEU B 252   O  LEU B 336           
SHEET    4   E 6 TRP B  11  ASP B  15 -1  N  GLU B  13   O  SER B 251           
SHEET    5   E 6 ARG B 371  ARG B 375  1  O  ILE B 372   N  VAL B  12           
SHEET    6   E 6 LYS B 378  ILE B 383 -1  O  GLU B 381   N  PHE B 373           
SHEET    1   F10 GLU B 343  ILE B 345  0                                        
SHEET    2   F10 LYS B 333  GLN B 340 -1  N  GLN B 340   O  GLU B 343           
SHEET    3   F10 GLU B 301  VAL B 304 -1  N  LEU B 303   O  THR B 335           
SHEET    4   F10 LYS B 307  VAL B 312 -1  O  LYS B 307   N  VAL B 304           
SHEET    5   F10 PHE B 320  LEU B 324 -1  O  MET B 321   N  VAL B 312           
SHEET    6   F10 GLU B 280  VAL B 285 -1  N  TRP B 281   O  LEU B 324           
SHEET    7   F10 LEU B 250  VAL B 262 -1  N  LYS B 260   O  ILE B 282           
SHEET    8   F10 TRP B  11  ASP B  15 -1  N  GLU B  13   O  SER B 251           
SHEET    9   F10 ARG B 371  ARG B 375  1  O  ILE B 372   N  VAL B  12           
SHEET   10   F10 LYS B 378  ILE B 383 -1  O  GLU B 381   N  PHE B 373           
SHEET    1   G 9 GLU B  35  VAL B  39  0                                        
SHEET    2   G 9 ARG B  63  VAL B  66  1  O  ARG B  63   N  ALA B  38           
SHEET    3   G 9 ILE B  84  VAL B  86  1  O  LEU B  85   N  LEU B  64           
SHEET    4   G 9 VAL B 103  THR B 106  1  O  ALA B 104   N  VAL B  86           
SHEET    5   G 9 MET B 126  ASN B 131  1  O  HIS B 129   N  LEU B 105           
SHEET    6   G 9 LEU B 160  TYR B 166  1  O  GLU B 163   N  TYR B 128           
SHEET    7   G 9 VAL B 204  ALA B 207  1  O  HIS B 205   N  VAL B 165           
SHEET    8   G 9 ALA B 222  ILE B 225  1  O  ARG B 224   N  ALA B 207           
SHEET    9   G 9 GLU B  35  VAL B  39  1  N  PHE B  37   O  VAL B 223           
SHEET    1   H 2 GLY B 267  ILE B 268  0                                        
SHEET    2   H 2 TYR B 274  ARG B 275 -1  O  TYR B 274   N  ILE B 268           
LINK         C   VAL A  40                 N   LLP A  41     1555   1555  1.33  
LINK         C   LLP A  41                 N   GLY A  42     1555   1555  1.34  
LINK         C   VAL B  40                 N   LLP B  41     1555   1555  1.33  
LINK         C   LLP B  41                 N   GLY B  42     1555   1555  1.33  
SITE     1 AC1  7 TYR A 270  TYR A 289  THR A 316  MET A 317                    
SITE     2 AC1  7 HOH A 404  HOH A 496  LLP B  41                               
SITE     1 AC2  2 ASN A 131  ARG A 138                                          
SITE     1 AC3  9 LLP A  41  TYR A 359  TYR B 270  TYR B 289                    
SITE     2 AC3  9 THR B 316  MET B 317  HOH B 465  HOH B 535                    
SITE     3 AC3  9 HOH B 570                                                     
SITE     1 AC4  2 ASN B 131  ARG B 138                                          
CRYST1   49.624  141.271   60.124  90.00 103.11  90.00 P 1 21 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      0.020152  0.000000  0.004692        0.00000                         
SCALE2      0.000000  0.007079  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017077        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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