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Database: PDB
Entry: 1XQL
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HEADER    ISOMERASE                               12-OCT-04   1XQL              
TITLE     EFFECT OF A Y265F MUTANT ON THE TRANSAMINATION BASED CYCLOSERINE      
TITLE    2 INACTIVATION OF ALANINE RACEMASE                                     
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;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GEOBACILLUS STEAROTHERMOPHILUS;                 
SOURCE   3 ORGANISM_TAXID: 1422;                                                
SOURCE   4 GENE: ALR, DAL;                                                      
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: DE3                                        
KEYWDS    ALANINE RACEMASE, CYCLOSERINE, TIM BARREL, ISOMERASE                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.D.FENN,T.HOLYOAK,G.F.STAMPER,D.RINGE                                
REVDAT   6   02-MAY-18 1XQL    1       REMARK                                   
REVDAT   5   31-JAN-18 1XQL    1       REMARK                                   
REVDAT   4   13-JUL-11 1XQL    1       VERSN                                    
REVDAT   3   24-FEB-09 1XQL    1       VERSN                                    
REVDAT   2   26-APR-05 1XQL    1       JRNL                                     
REVDAT   1   18-JAN-05 1XQL    0                                                
JRNL        AUTH   T.D.FENN,T.HOLYOAK,G.F.STAMPER,D.RINGE                       
JRNL        TITL   EFFECT OF A Y265F MUTANT ON THE TRANSAMINATION-BASED         
JRNL        TITL 2 CYCLOSERINE INACTIVATION OF ALANINE RACEMASE                 
JRNL        REF    BIOCHEMISTRY                  V.  44  5317 2005              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   15807525                                                     
JRNL        DOI    10.1021/BI047842L                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.20                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 481235.530                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 51218                          
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 SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.214                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2591                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.91                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 9623                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2790                       
REMARK   3   BIN FREE R VALUE                    : 0.3000                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 520                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.013                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6055                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 128                                     
REMARK   3   SOLVENT ATOMS            : 331                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.83000                                              
REMARK   3    B22 (A**2) : 3.83000                                              
REMARK   3    B33 (A**2) : -4.65000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.20                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.22                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.24                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.24                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.860                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.270 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.990 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.030 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.030 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.33                                                 
REMARK   3   BSOL        : 47.38                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1XQL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-OCT-04.                  
REMARK 100 THE DEPOSITION ID IS D_1000030651.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-NOV-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
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 RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : SUPPER MIRRORS                     
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51218                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
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     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1SFT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4K, NAAC, PH 8.5, VAPOR DIFFUSION,   
REMARK 280  HANGING DROP, TEMPERATURE 398K, TEMPERATURE 298.0K                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       49.38800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.58850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.89750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       42.58850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       49.38800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.89750            
REMARK 290   SMTRY3   4  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: 9910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 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     GLY A   384                                                      
REMARK 465     GLU A   385                                                      
REMARK 465     SER A   386                                                      
REMARK 465     SER A   387                                                      
REMARK 465     ALA A   388                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B   382                                                      
REMARK 465     ARG B   383                                                      
REMARK 465     GLY B   384                                                      
REMARK 465     GLU B   385                                                      
REMARK 465     SER B   386                                                      
REMARK 465     SER B   387                                                      
REMARK 465     ALA B   388                                                      
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 383    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 136      -81.78    -94.33                                   
REMARK 500    CYS A 201      -24.33   -152.42                                   
REMARK 500    ASN A 203     -159.77   -101.37                                   
REMARK 500    PHE A 215     -134.18     59.09                                   
REMARK 500    SER A 230      142.37   -172.30                                   
REMARK 500    SER A 264     -176.94     63.06                                   
REMARK 500    PHE B 106       10.51   -157.78                                   
REMARK 500    ARG B 136      -81.68    -91.87                                   
REMARK 500    CYS B 201      -22.30   -155.48                                   
REMARK 500    ASN B 203     -166.75   -107.52                                   
REMARK 500    PHE B 215     -133.79     68.35                                   
REMARK 500    SER B 264     -177.82     67.09                                   
REMARK 500    HIS B 294       -8.55     80.01                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 PMP = PYRIDOXAMINE MONOPHOSPHATE                                     
REMARK 600 ACY = ACETATE                                                        
REMARK 600 PMH = PMP-HYDROXYISOXAZOLE                                           
REMARK 600 PLP = PYRIDOXAL 5'-PHOSPHATE                                         
REMARK 600 4AX = L-CYCLOSERINE (4-AMINO 3-ISOXAZOLIDINONE)                      
REMARK 600 PMP AND ACY FORM ONE CONFORMATION, PMH FORMS                         
REMARK 600 A SECOND CONFORMATION, AND PLP TOGETHER WITH 4AX                     
REMARK 600 FORM THE THIRD ALTERNATE CONFORMATION.                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMH A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4AX B 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMH B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4AX A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 602                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1SFT   RELATED DB: PDB                                   
REMARK 900 DETERMINATION OF THE STRUCTURE OF ALANINE RACEMASE FROM BACILLUS     
REMARK 900 STEAROTHERMOPHILUS AT 1.9-A RESOLUTION                               
REMARK 900 RELATED ID: 1XQK   RELATED DB: PDB                                   
REMARK 900 EFFECT OF A Y265F MUTANT ON THE TRANSAMINATION BASED CYCLOSERINE     
REMARK 900 INACTIVATION OF ALANINE RACEMASE                                     
DBREF  1XQL A    1   382  UNP    P10724   ALR_BACST        1    382             
DBREF  1XQL B    1   382  UNP    P10724   ALR_BACST        1    382             
SEQADV 1XQL KCX A  129  UNP  P10724    LYS   129 MODIFIED RESIDUE               
SEQADV 1XQL PHE A  265  UNP  P10724    TYR   265 ENGINEERED                     
SEQADV 1XQL KCX B  129  UNP  P10724    LYS   129 MODIFIED RESIDUE               
SEQADV 1XQL PHE B  265  UNP  P10724    TYR   265 ENGINEERED                     
SEQRES   1 A  388  MET ASN ASP PHE HIS ARG ASP THR TRP ALA GLU VAL ASP          
SEQRES   2 A  388  LEU ASP ALA ILE TYR ASP ASN VAL GLU ASN LEU ARG ARG          
SEQRES   3 A  388  LEU LEU PRO ASP ASP THR HIS ILE MET ALA VAL VAL LYS          
SEQRES   4 A  388  ALA ASN ALA TYR GLY HIS GLY ASP VAL GLN VAL ALA ARG          
SEQRES   5 A  388  THR ALA LEU GLU ALA GLY ALA SER ARG LEU ALA VAL ALA          
SEQRES   6 A  388  PHE LEU ASP GLU ALA LEU ALA LEU ARG GLU LYS GLY ILE          
SEQRES   7 A  388  GLU ALA PRO ILE LEU VAL LEU GLY ALA SER ARG PRO ALA          
SEQRES   8 A  388  ASP ALA ALA LEU ALA ALA GLN GLN ARG ILE ALA LEU THR          
SEQRES   9 A  388  VAL PHE ARG SER ASP TRP LEU GLU GLU ALA SER ALA LEU          
SEQRES  10 A  388  TYR SER GLY PRO PHE PRO ILE HIS PHE HIS LEU KCX MET          
SEQRES  11 A  388  ASP THR GLY MET GLY ARG LEU GLY VAL LYS ASP GLU GLU          
SEQRES  12 A  388  GLU THR LYS ARG ILE VAL ALA LEU ILE GLU ARG HIS PRO          
SEQRES  13 A  388  HIS PHE VAL LEU GLU GLY LEU TYR THR HIS PHE ALA THR          
SEQRES  14 A  388  ALA ASP GLU VAL ASN THR ASP TYR PHE SER TYR GLN TYR          
SEQRES  15 A  388  THR ARG PHE LEU HIS MET LEU GLU TRP LEU PRO SER ARG          
SEQRES  16 A  388  PRO PRO LEU VAL HIS CYS ALA ASN SER ALA ALA SER LEU          
SEQRES  17 A  388  ARG PHE PRO ASP ARG THR PHE ASN MET VAL ARG PHE GLY          
SEQRES  18 A  388  ILE ALA MET TYR GLY LEU ALA PRO SER PRO GLY ILE LYS          
SEQRES  19 A  388  PRO LEU LEU PRO TYR PRO LEU LYS GLU ALA PHE SER LEU          
SEQRES  20 A  388  HIS SER ARG LEU VAL HIS VAL LYS LYS LEU GLN PRO GLY          
SEQRES  21 A  388  GLU LYS VAL SER PHE GLY ALA THR TYR THR ALA GLN THR          
SEQRES  22 A  388  GLU GLU TRP ILE GLY THR ILE PRO ILE GLY TYR ALA ASP          
SEQRES  23 A  388  GLY TRP LEU ARG ARG LEU GLN HIS PHE HIS VAL LEU VAL          
SEQRES  24 A  388  ASP GLY GLN LYS ALA PRO ILE VAL GLY ARG ILE CYS MET          
SEQRES  25 A  388  ASP GLN CYS MET ILE ARG LEU PRO GLY PRO LEU PRO VAL          
SEQRES  26 A  388  GLY THR LYS VAL THR LEU ILE GLY ARG GLN GLY ASP GLU          
SEQRES  27 A  388  VAL ILE SER ILE ASP ASP VAL ALA ARG HIS LEU GLU THR          
SEQRES  28 A  388  ILE ASN TYR GLU VAL PRO CYS THR ILE SER TYR ARG VAL          
SEQRES  29 A  388  PRO ARG ILE PHE PHE ARG HIS LYS ARG ILE MET GLU VAL          
SEQRES  30 A  388  ARG ASN ALA ILE GLY ARG GLY GLU SER SER ALA                  
SEQRES   1 B  388  MET ASN ASP PHE HIS ARG ASP THR TRP ALA GLU VAL ASP          
SEQRES   2 B  388  LEU ASP ALA ILE TYR ASP ASN VAL GLU ASN LEU ARG ARG          
SEQRES   3 B  388  LEU LEU PRO ASP ASP THR HIS ILE MET ALA VAL VAL LYS          
SEQRES   4 B  388  ALA ASN ALA TYR GLY HIS GLY ASP VAL GLN VAL ALA ARG          
SEQRES   5 B  388  THR ALA LEU GLU ALA GLY ALA SER ARG LEU ALA VAL ALA          
SEQRES   6 B  388  PHE LEU ASP GLU ALA LEU ALA LEU ARG GLU LYS GLY ILE          
SEQRES   7 B  388  GLU ALA PRO ILE LEU VAL LEU GLY ALA SER ARG PRO ALA          
SEQRES   8 B  388  ASP ALA ALA LEU ALA ALA GLN GLN ARG ILE ALA LEU THR          
SEQRES   9 B  388  VAL PHE ARG SER ASP TRP LEU GLU GLU ALA SER ALA LEU          
SEQRES  10 B  388  TYR SER GLY PRO PHE PRO ILE HIS PHE HIS LEU KCX MET          
SEQRES  11 B  388  ASP THR GLY MET GLY ARG LEU GLY VAL LYS ASP GLU GLU          
SEQRES  12 B  388  GLU THR LYS ARG ILE VAL ALA LEU ILE GLU ARG HIS PRO          
SEQRES  13 B  388  HIS PHE VAL LEU GLU GLY LEU TYR THR HIS PHE ALA THR          
SEQRES  14 B  388  ALA ASP GLU VAL ASN THR ASP TYR PHE SER TYR GLN TYR          
SEQRES  15 B  388  THR ARG PHE LEU HIS MET LEU GLU TRP LEU PRO SER ARG          
SEQRES  16 B  388  PRO PRO LEU VAL HIS CYS ALA ASN SER ALA ALA SER LEU          
SEQRES  17 B  388  ARG PHE PRO ASP ARG THR PHE ASN MET VAL ARG PHE GLY          
SEQRES  18 B  388  ILE ALA MET TYR GLY LEU ALA PRO SER PRO GLY ILE LYS          
SEQRES  19 B  388  PRO LEU LEU PRO TYR PRO LEU LYS GLU ALA PHE SER LEU          
SEQRES  20 B  388  HIS SER ARG LEU VAL HIS VAL LYS LYS LEU GLN PRO GLY          
SEQRES  21 B  388  GLU LYS VAL SER PHE GLY ALA THR TYR THR ALA GLN THR          
SEQRES  22 B  388  GLU GLU TRP ILE GLY THR ILE PRO ILE GLY TYR ALA ASP          
SEQRES  23 B  388  GLY TRP LEU ARG ARG LEU GLN HIS PHE HIS VAL LEU VAL          
SEQRES  24 B  388  ASP GLY GLN LYS ALA PRO ILE VAL GLY ARG ILE CYS MET          
SEQRES  25 B  388  ASP GLN CYS MET ILE ARG LEU PRO GLY PRO LEU PRO VAL          
SEQRES  26 B  388  GLY THR LYS VAL THR LEU ILE GLY ARG GLN GLY ASP GLU          
SEQRES  27 B  388  VAL ILE SER ILE ASP ASP VAL ALA ARG HIS LEU GLU THR          
SEQRES  28 B  388  ILE ASN TYR GLU VAL PRO CYS THR ILE SER TYR ARG VAL          
SEQRES  29 B  388  PRO ARG ILE PHE PHE ARG HIS LYS ARG ILE MET GLU VAL          
SEQRES  30 B  388  ARG ASN ALA ILE GLY ARG GLY GLU SER SER ALA                  
MODRES 1XQL KCX A  129  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 1XQL KCX B  129  LYS  LYSINE NZ-CARBOXYLIC ACID                          
HET    KCX  A 129      12                                                       
HET    KCX  B 129      12                                                       
HET    PMP  A 501      16                                                       
HET    PMH  A 503      22                                                       
HET    PLP  A 504      15                                                       
HET    4AX  A 605       7                                                       
HET    ACY  A 602       4                                                       
HET    4AX  B 505       7                                                       
HET    PMP  B 601      16                                                       
HET    PMH  B 603      22                                                       
HET    PLP  B 604      15                                                       
HET    ACY  B 502       4                                                       
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID                                        
HETNAM     PMP 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE                          
HETNAM     PMH (5-HYDROXY-4-{[(3-HYDROXYISOXAZOL-4-YL)AMINO]METHYL}-6-          
HETNAM   2 PMH  METHYLPYRIDIN-3-YL)METHYL DIHYDROGEN PHOSPHATE                  
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETNAM     4AX (R)-4-AMINO-ISOXAZOLIDIN-3-ONE                                   
HETNAM     ACY ACETIC ACID                                                      
HETSYN     PMP PYRIDOXAMINE-5'-PHOSPHATE                                        
HETSYN     PMH PMP-HYDROXYISOXAZOLE, PYRIDOXAMINE-5-PHOSPHATE-                  
HETSYN   2 PMH  HYDROXYISOXAZOLE                                                
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
FORMUL   1  KCX    2(C7 H14 N2 O4)                                              
FORMUL   3  PMP    2(C8 H13 N2 O5 P)                                            
FORMUL   4  PMH    2(C11 H14 N3 O7 P)                                           
FORMUL   5  PLP    2(C8 H10 N O6 P)                                             
FORMUL   6  4AX    2(C3 H6 N2 O2)                                               
FORMUL   7  ACY    2(C2 H4 O2)                                                  
FORMUL  13  HOH   *331(H2 O)                                                    
HELIX    1   1 LEU A   14  LEU A   28  1                                  15    
HELIX    2   2 VAL A   38  GLY A   44  1                                   7    
HELIX    3   3 GLY A   46  GLY A   58  1                                  13    
HELIX    4   4 PHE A   66  LYS A   76  1                                  11    
HELIX    5   5 ARG A   89  ALA A   91  5                                   3    
HELIX    6   6 ASP A   92  GLN A   99  1                                   8    
HELIX    7   7 ARG A  107  TYR A  118  1                                  12    
HELIX    8   8 ASP A  141  HIS A  155  1                                  15    
HELIX    9   9 THR A  175  GLU A  190  1                                  16    
HELIX   10  10 ASN A  203  PHE A  210  1                                   8    
HELIX   11  11 PRO A  211  THR A  214  5                                   4    
HELIX   12  12 GLY A  221  GLY A  226  5                                   6    
HELIX   13  13 SER A  230  LEU A  237  5                                   8    
HELIX   14  14 SER A  264  THR A  268  5                                   5    
HELIX   15  15 GLY A  283  GLY A  287  5                                   5    
HELIX   16  16 LEU A  289  HIS A  294  5                                   6    
HELIX   17  17 SER A  341  GLU A  350  1                                  10    
HELIX   18  18 TYR A  354  ILE A  360  1                                   7    
HELIX   19  19 LEU B   14  ARG B   26  1                                  13    
HELIX   20  20 VAL B   38  GLY B   44  1                                   7    
HELIX   21  21 GLY B   46  GLY B   58  1                                  13    
HELIX   22  22 PHE B   66  LYS B   76  1                                  11    
HELIX   23  23 ARG B   89  ALA B   91  5                                   3    
HELIX   24  24 ASP B   92  GLN B   99  1                                   8    
HELIX   25  25 ARG B  107  TYR B  118  1                                  12    
HELIX   26  26 ASP B  141  HIS B  155  1                                  15    
HELIX   27  27 THR B  175  GLU B  190  1                                  16    
HELIX   28  28 ASN B  203  PHE B  210  1                                   8    
HELIX   29  29 PRO B  211  THR B  214  5                                   4    
HELIX   30  30 GLY B  221  GLY B  226  5                                   6    
HELIX   31  31 SER B  230  LEU B  237  5                                   8    
HELIX   32  32 SER B  264  THR B  268  5                                   5    
HELIX   33  33 GLY B  283  GLY B  287  5                                   5    
HELIX   34  34 LEU B  289  GLN B  293  5                                   5    
HELIX   35  35 SER B  341  GLU B  350  1                                  10    
HELIX   36  36 TYR B  354  ILE B  360  1                                   7    
SHEET    1   A 7 HIS A 253  LEU A 257  0                                        
SHEET    2   A 7 GLU A 275  ILE A 280 -1  O  GLU A 275   N  LEU A 257           
SHEET    3   A 7 CYS A 315  LEU A 319 -1  O  LEU A 319   N  TRP A 276           
SHEET    4   A 7 GLN A 302  VAL A 307 -1  N  VAL A 307   O  MET A 316           
SHEET    5   A 7 HIS A 296  VAL A 299 -1  N  VAL A 297   O  ALA A 304           
SHEET    6   A 7 LYS A 328  GLN A 335 -1  O  THR A 330   N  LEU A 298           
SHEET    7   A 7 GLU A 338  ILE A 340 -1  O  ILE A 340   N  GLY A 333           
SHEET    1   B10 HIS A 253  LEU A 257  0                                        
SHEET    2   B10 GLU A 275  ILE A 280 -1  O  GLU A 275   N  LEU A 257           
SHEET    3   B10 CYS A 315  LEU A 319 -1  O  LEU A 319   N  TRP A 276           
SHEET    4   B10 GLN A 302  VAL A 307 -1  N  VAL A 307   O  MET A 316           
SHEET    5   B10 HIS A 296  VAL A 299 -1  N  VAL A 297   O  ALA A 304           
SHEET    6   B10 LYS A 328  GLN A 335 -1  O  THR A 330   N  LEU A 298           
SHEET    7   B10 PHE A 245  ARG A 250 -1  N  SER A 249   O  VAL A 329           
SHEET    8   B10 THR A   8  ASP A  13 -1  N  TRP A   9   O  HIS A 248           
SHEET    9   B10 ARG A 366  ARG A 370  1  O  ILE A 367   N  VAL A  12           
SHEET   10   B10 ARG A 373  ARG A 378 -1  O  MET A 375   N  PHE A 368           
SHEET    1   C 9 HIS A  33  VAL A  37  0                                        
SHEET    2   C 9 ARG A  61  VAL A  64  1  O  ARG A  61   N  ALA A  36           
SHEET    3   C 9 ILE A  82  VAL A  84  1  O  LEU A  83   N  LEU A  62           
SHEET    4   C 9 ILE A 101  VAL A 105  1  O  ALA A 102   N  ILE A  82           
SHEET    5   C 9 ILE A 124  KCX A 129  1  O  HIS A 127   N  LEU A 103           
SHEET    6   C 9 PHE A 158  TYR A 164  1  O  VAL A 159   N  PHE A 126           
SHEET    7   C 9 LEU A 198  HIS A 200  1  O  HIS A 200   N  LEU A 163           
SHEET    8   C 9 MET A 217  PHE A 220  1  N  MET A 217   O  VAL A 199           
SHEET    9   C 9 HIS A  33  VAL A  37  1  N  MET A  35   O  VAL A 218           
SHEET    1   D 2 LYS A 262  VAL A 263  0                                        
SHEET    2   D 2 TYR A 269  THR A 270 -1  O  TYR A 269   N  VAL A 263           
SHEET    1   E 7 HIS B 253  LEU B 257  0                                        
SHEET    2   E 7 GLU B 275  ILE B 280 -1  O  ILE B 277   N  LYS B 255           
SHEET    3   E 7 CYS B 315  LEU B 319 -1  O  ILE B 317   N  GLY B 278           
SHEET    4   E 7 GLN B 302  VAL B 307 -1  N  VAL B 307   O  MET B 316           
SHEET    5   E 7 HIS B 296  VAL B 299 -1  N  VAL B 297   O  ALA B 304           
SHEET    6   E 7 LYS B 328  GLN B 335 -1  O  THR B 330   N  LEU B 298           
SHEET    7   E 7 GLU B 338  ILE B 340 -1  O  GLU B 338   N  GLN B 335           
SHEET    1   F10 HIS B 253  LEU B 257  0                                        
SHEET    2   F10 GLU B 275  ILE B 280 -1  O  ILE B 277   N  LYS B 255           
SHEET    3   F10 CYS B 315  LEU B 319 -1  O  ILE B 317   N  GLY B 278           
SHEET    4   F10 GLN B 302  VAL B 307 -1  N  VAL B 307   O  MET B 316           
SHEET    5   F10 HIS B 296  VAL B 299 -1  N  VAL B 297   O  ALA B 304           
SHEET    6   F10 LYS B 328  GLN B 335 -1  O  THR B 330   N  LEU B 298           
SHEET    7   F10 PHE B 245  ARG B 250 -1  N  SER B 249   O  VAL B 329           
SHEET    8   F10 THR B   8  ASP B  13 -1  N  TRP B   9   O  HIS B 248           
SHEET    9   F10 ARG B 366  ARG B 370  1  O  ILE B 367   N  VAL B  12           
SHEET   10   F10 ARG B 373  ARG B 378 -1  O  MET B 375   N  PHE B 368           
SHEET    1   G 9 HIS B  33  VAL B  37  0                                        
SHEET    2   G 9 ARG B  61  VAL B  64  1  O  ARG B  61   N  ALA B  36           
SHEET    3   G 9 ILE B  82  VAL B  84  1  O  LEU B  83   N  LEU B  62           
SHEET    4   G 9 ILE B 101  VAL B 105  1  O  ALA B 102   N  ILE B  82           
SHEET    5   G 9 ILE B 124  KCX B 129  1  O  KCX B 129   N  VAL B 105           
SHEET    6   G 9 PHE B 158  TYR B 164  1  O  VAL B 159   N  PHE B 126           
SHEET    7   G 9 LEU B 198  HIS B 200  1  O  LEU B 198   N  GLU B 161           
SHEET    8   G 9 MET B 217  PHE B 220  1  N  MET B 217   O  VAL B 199           
SHEET    9   G 9 HIS B  33  VAL B  37  1  N  MET B  35   O  VAL B 218           
SHEET    1   H 2 LYS B 262  VAL B 263  0                                        
SHEET    2   H 2 TYR B 269  THR B 270 -1  O  TYR B 269   N  VAL B 263           
LINK         NZ BLYS B  39                 C4ADPLP B 604     1555   1555  1.70  
LINK         NZ BLYS A  39                 C4ADPLP A 504     1555   1555  2.00  
LINK         C   LEU A 128                 N   KCX A 129     1555   1555  1.33  
LINK         C   KCX A 129                 N   MET A 130     1555   1555  1.33  
LINK         C   LEU B 128                 N   KCX B 129     1555   1555  1.33  
LINK         C   KCX B 129                 N   MET B 130     1555   1555  1.33  
CISPEP   1 GLY A  120    PRO A  121          0         0.22                     
CISPEP   2 GLY B  120    PRO B  121          0         0.21                     
SITE     1 AC1 14 LYS A  39  TYR A  43  ARG A 136  HIS A 166                    
SITE     2 AC1 14 ASN A 203  SER A 204  ARG A 219  GLY A 221                    
SITE     3 AC1 14 ILE A 222  TYR A 354  HOH A 661  HOH A 670                    
SITE     4 AC1 14 HOH A 695  PHE B 265                                          
SITE     1 AC2 20 LYS A  39  TYR A  43  KCX A 129  ARG A 136                    
SITE     2 AC2 20 HIS A 166  ASN A 203  SER A 204  ARG A 219                    
SITE     3 AC2 20 GLY A 221  ILE A 222  TYR A 354  HOH A 661                    
SITE     4 AC2 20 HOH A 670  HOH A 695  HOH A 697  PHE B 265                    
SITE     5 AC2 20 TYR B 284  CYS B 311  MET B 312  HOH B 672                    
SITE     1 AC3 13 LYS A  39  TYR A  43  LEU A  85  HIS A 166                    
SITE     2 AC3 13 ASN A 203  SER A 204  ARG A 219  GLY A 221                    
SITE     3 AC3 13 ILE A 222  TYR A 354  HOH A 661  HOH A 670                    
SITE     4 AC3 13 HOH A 695                                                     
SITE     1 AC4  9 LYS A  39  ARG A 136  PLP A 504  HOH A 697                    
SITE     2 AC4  9 PHE B 265  TYR B 284  CYS B 311  MET B 312                    
SITE     3 AC4  9 HOH B 672                                                     
SITE     1 AC5 14 VAL B  37  LYS B  39  TYR B  43  ARG B 136                    
SITE     2 AC5 14 HIS B 166  ASN B 203  SER B 204  ARG B 219                    
SITE     3 AC5 14 GLY B 221  ILE B 222  TYR B 354  HOH B 605                    
SITE     4 AC5 14 HOH B 643  HOH B 678                                          
SITE     1 AC6 19 PHE A 265  TYR A 284  CYS A 311  MET A 312                    
SITE     2 AC6 19 HOH A 678  LYS B  39  TYR B  43  ARG B 136                    
SITE     3 AC6 19 HIS B 166  ASN B 203  SER B 204  ARG B 219                    
SITE     4 AC6 19 GLY B 221  ILE B 222  TYR B 354  HOH B 605                    
SITE     5 AC6 19 HOH B 628  HOH B 643  HOH B 678                               
SITE     1 AC7 13 LYS B  39  TYR B  43  LEU B  85  ARG B 136                    
SITE     2 AC7 13 HIS B 166  ASN B 203  SER B 204  ARG B 219                    
SITE     3 AC7 13 GLY B 221  ILE B 222  TYR B 354  HOH B 605                    
SITE     4 AC7 13 HOH B 678                                                     
SITE     1 AC8  9 PHE A 265  TYR A 284  MET A 312  HOH A 678                    
SITE     2 AC8  9 HOH A 746  LYS B  39  ARG B 136  TYR B 354                    
SITE     3 AC8  9 HOH B 628                                                     
SITE     1 AC9  5 LYS A  39  ARG A 136  PHE B 265  CYS B 311                    
SITE     2 AC9  5 MET B 312                                                     
SITE     1 BC1  5 PHE A 265  CYS A 311  MET A 312  LYS B  39                    
SITE     2 BC1  5 ARG B 136                                                     
CRYST1   98.776   89.795   85.177  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010124  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011136  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011740        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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