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Database: PDB
Entry: 2SFP
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Original site: 2SFP 
HEADER    RACEMASE                                16-FEB-99   2SFP              
TITLE     ALANINE RACEMASE WITH BOUND PROPIONATE INHIBITOR                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (ALANINE RACEMASE);                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 5.1.1.1;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: PYRIDOXAL PHOSPHATE COFACTOR IN ALDIMINE LINKAGE WITH 
COMPND   7 LYS39. CARBOXYLATED LYS129                                           
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GEOBACILLUS STEAROTHERMOPHILUS;                 
SOURCE   3 ORGANISM_TAXID: 1422;                                                
SOURCE   4 STRAIN: IFO 12550;                                                   
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI STR. K12 SUBSTR. W3110;          
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 316407;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: W3110;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PKK223-3;                                  
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMDALR3;                                  
SOURCE  11 EXPRESSION_SYSTEM_GENE: ALR                                          
KEYWDS    RACEMASE, ISOMERASE, ALANINE, PYRIDOXAL PHOSPHATE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.A.MOROLLO,G.A.PETSKO,D.RINGE                                        
REVDAT   4   13-JUL-11 2SFP    1       VERSN                                    
REVDAT   3   24-FEB-09 2SFP    1       VERSN                                    
REVDAT   2   01-APR-03 2SFP    1       JRNL                                     
REVDAT   1   24-FEB-99 2SFP    0                                                
JRNL        AUTH   A.A.MOROLLO,G.A.PETSKO,D.RINGE                               
JRNL        TITL   STRUCTURE OF A MICHAELIS COMPLEX ANALOGUE: PROPIONATE BINDS  
JRNL        TITL 2 IN THE SUBSTRATE CARBOXYLATE SITE OF ALANINE RACEMASE.       
JRNL        REF    BIOCHEMISTRY                  V.  38  3293 1999              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   10079072                                                     
JRNL        DOI    10.1021/BI9822729                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.G.STAMPER,A.A.MOROLLO,D.RINGE                              
REMARK   1  TITL   REACTION OF ALANINE RACEMASE WITH 1-AMINOETHYLPHOSPHONIC     
REMARK   1  TITL 2 ACID FORMS A STABLE EXTERNAL ALDIMINE INTERMEDIATE           
REMARK   1  REF    BIOCHEMISTRY                  V.  37 10438 1998              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  DOI    10.1021/BI980692S                                            
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   J.P.SHAW,G.A.PETSKO,D.RINGE                                  
REMARK   1  TITL   DETERMINATION OF THE STRUCTURE OF ALANINE RACEMASE FROM      
REMARK   1  TITL 2 BACILLUS STEAROTHERMOPHILUS AT 1.9 ANGSTROMS RESOLUTION      
REMARK   1  REF    BIOCHEMISTRY                  V.  36  1329 1997              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  DOI    10.1021/BI961856C                                            
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   D.J.NEIDHART,M.D.DISTEFANO,K.TANIZAWA,K.SOAD,C.T.WALSH,      
REMARK   1  AUTH 2 G.A.PETSKO                                                   
REMARK   1  TITL   X-RAY CRYSTALLOGRAPHIC STUDIES OF THE ALANINE-SPECIFIC       
REMARK   1  TITL 2 RACEMASE FROM BACILLUS STEAROTHERMOPHILUS. OVERPRODUCTION,   
REMARK   1  TITL 3 CRYSTALLIZATION, AND PRELIMINARY CHARACTERIZATION            
REMARK   1  REF    J.BIOL.CHEM.                  V. 262 15323 1987              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000000.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 82.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 49777                          
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) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1889                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.99                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 48.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3465                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3130                       
REMARK   3   BIN FREE R VALUE                    : 0.3490                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 1.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 135                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6032                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 207                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.37                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 27.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.71                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
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 2SFP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-FEB-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB000498.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : MAR-96                             
REMARK 200  TEMPERATURE           (KELVIN) : 296.00                             
REMARK 200  PH                             : 8.50                               
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 RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52775                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.0                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.05400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 54.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: X-PLOR 3.851                                          
REMARK 200 STARTING MODEL: 1SFT                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.50                                  
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       49.35000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.60000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       42.60000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       49.35000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.00000            
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,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 7910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 6.0 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     ASN A     2                                                      
REMARK 465     GLY A   382                                                      
REMARK 465     ARG A   383                                                      
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     ASN B     2                                                      
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 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  30        0.45    -66.28                                   
REMARK 500    PHE A 106        5.99   -153.37                                   
REMARK 500    SER A 119       45.75   -140.59                                   
REMARK 500    ARG A 136      -83.27    -94.19                                   
REMARK 500    CYS A 201      -22.75   -152.64                                   
REMARK 500    ASN A 203     -166.46   -103.25                                   
REMARK 500    ARG A 213       50.79   -110.31                                   
REMARK 500    PHE A 215     -136.01     62.28                                   
REMARK 500    SER A 264     -174.66     70.14                                   
REMARK 500    HIS A 294      -22.06     88.84                                   
REMARK 500    ASP B  30       -9.63    -55.33                                   
REMARK 500    PHE B 106        6.98   -152.34                                   
REMARK 500    SER B 119       41.35   -154.43                                   
REMARK 500    ARG B 136      -89.83    -89.89                                   
REMARK 500    CYS B 201      -25.61   -154.43                                   
REMARK 500    ASN B 203     -162.79   -103.53                                   
REMARK 500    PHE B 215     -137.32     61.81                                   
REMARK 500    SER B 264     -178.39     63.61                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 PLP: THE ALDEHYDE FORMED BY O4 AS LISTED IN THE                      
REMARK 600 HET GROUP DICTIONARY IS NOT PRESENT IN THIS                          
REMARK 600 ENTRY DUE TO FORMATION OF THE ALDIMINE WITH                          
REMARK 600 NZ OF LYS 39.                                                        
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: KC1                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: CARBAMYLATED LYSINE                                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC2                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: CARBAMYLATED LYSINE                                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PP1                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: PROPIONATE INHIBITOR                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PP2                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: PROPIONATE INHIBITOR                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PL1                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: PYRIDOXAL-5-PHOSPHATE COFACTOR                     
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PL2                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: PYRIDOXAL-5-PHOSPHATE COFACTOR                     
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PPI B 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PPI A 400                 
DBREF  2SFP A    1   388  UNP    P10724   ALR_BACST        1    388             
DBREF  2SFP B    1   388  UNP    P10724   ALR_BACST        1    388             
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 TYR 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 TYR 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 2SFP KCX A  129  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 2SFP KCX B  129  LYS  LYSINE NZ-CARBOXYLIC ACID                          
HET    KCX  A 129      12                                                       
HET    KCX  B 129      12                                                       
HET    PLP  A 500      15                                                       
HET    PPI  B 400       5                                                       
HET    PLP  B 500      15                                                       
HET    PPI  A 400       5                                                       
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID                                        
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETNAM     PPI PROPANOIC ACID                                                   
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
FORMUL   1  KCX    2(C7 H14 N2 O4)                                              
FORMUL   3  PLP    2(C8 H10 N O6 P)                                             
FORMUL   4  PPI    2(C3 H6 O2)                                                  
FORMUL   7  HOH   *207(H2 O)                                                    
HELIX    1   1 LEU A   14  LEU A   27  1                                  14    
HELIX    2   2 LYS A   39  GLY A   44  1                                   6    
HELIX    3   3 ASP A   47  ALA A   57  1                                  11    
HELIX    4   4 LEU A   67  GLU A   75  1                                   9    
HELIX    5   5 PRO A   90  GLN A   98  5                                   9    
HELIX    6   6 SER A  108  LEU A  117  1                                  10    
HELIX    7   7 GLU A  142  ARG A  154  1                                  13    
HELIX    8   8 ASP A  176  TRP A  191  1                                  16    
HELIX    9   9 SER A  204  ARG A  209  1                                   6    
HELIX   10  10 PRO A  211  ARG A  213  5                                   3    
HELIX   11  11 ILE A  222  TYR A  225  5                                   4    
HELIX   12  12 PRO A  231  LEU A  236  5                                   6    
HELIX   13  13 TYR A  265  ALA A  267  5                                   3    
HELIX   14  14 TYR A  284  ASP A  286  5                                   3    
HELIX   15  15 ARG A  290  LEU A  292  5                                   3    
HELIX   16  16 ILE A  342  HIS A  348  1                                   7    
HELIX   17  17 ASN A  353  THR A  359  1                                   7    
HELIX   18  18 LEU B   14  LEU B   27  1                                  14    
HELIX   19  19 LYS B   39  GLY B   44  1                                   6    
HELIX   20  20 ASP B   47  ALA B   57  1                                  11    
HELIX   21  21 LEU B   67  GLU B   75  1                                   9    
HELIX   22  22 PRO B   90  GLN B   98  5                                   9    
HELIX   23  23 SER B  108  LEU B  117  1                                  10    
HELIX   24  24 GLU B  142  ARG B  154  1                                  13    
HELIX   25  25 ASP B  176  TRP B  191  1                                  16    
HELIX   26  26 SER B  204  ARG B  209  1                                   6    
HELIX   27  27 ILE B  222  TYR B  225  5                                   4    
HELIX   28  28 LYS B  234  LEU B  236  5                                   3    
HELIX   29  29 TYR B  265  ALA B  267  5                                   3    
HELIX   30  30 TYR B  284  ASP B  286  5                                   3    
HELIX   31  31 ARG B  290  LEU B  292  5                                   3    
HELIX   32  32 ILE B  342  LEU B  349  1                                   8    
HELIX   33  33 ASN B  353  THR B  359  1                                   7    
SHEET    1   A 5 ARG A 373  ARG A 378  0                                        
SHEET    2   A 5 PRO A 365  ARG A 370 -1  N  ARG A 370   O  ARG A 373           
SHEET    3   A 5 THR A   8  ASP A  13  1  N  ALA A  10   O  PRO A 365           
SHEET    4   A 5 PHE A 245  ARG A 250 -1  N  HIS A 248   O  TRP A   9           
SHEET    5   A 5 LYS A 328  ILE A 332 -1  N  ILE A 332   O  LEU A 247           
SHEET    1   B 8 MET A 217  PHE A 220  0                                        
SHEET    2   B 8 HIS A  33  VAL A  37  1  N  HIS A  33   O  VAL A 218           
SHEET    3   B 8 ARG A  61  VAL A  64  1  N  ARG A  61   O  ALA A  36           
SHEET    4   B 8 PRO A  81  VAL A  84  1  N  PRO A  81   O  LEU A  62           
SHEET    5   B 8 ILE A 101  VAL A 105  1  N  ALA A 102   O  ILE A  82           
SHEET    6   B 8 ILE A 124  KCX A 129  1  N  HIS A 127   O  LEU A 103           
SHEET    7   B 8 PHE A 158  TYR A 164  1  N  VAL A 159   O  ILE A 124           
SHEET    8   B 8 LEU A 198  HIS A 200  1  N  LEU A 198   O  LEU A 163           
SHEET    1   C 3 CYS A 315  LEU A 319  0                                        
SHEET    2   C 3 GLU A 275  ILE A 280 -1  N  ILE A 280   O  CYS A 315           
SHEET    3   C 3 LEU A 251  LEU A 257 -1  N  LEU A 257   O  GLU A 275           
SHEET    1   D 2 HIS A 296  VAL A 299  0                                        
SHEET    2   D 2 GLN A 302  PRO A 305 -1  N  ALA A 304   O  VAL A 297           
SHEET    1   E 2 GLY A 333  GLN A 335  0                                        
SHEET    2   E 2 GLU A 338  ILE A 340 -1  N  ILE A 340   O  GLY A 333           
SHEET    1   F 5 ARG B 373  ARG B 378  0                                        
SHEET    2   F 5 PRO B 365  ARG B 370 -1  N  ARG B 370   O  ARG B 373           
SHEET    3   F 5 TRP B   9  ASP B  13  1  N  ALA B  10   O  PRO B 365           
SHEET    4   F 5 PHE B 245  ARG B 250 -1  N  HIS B 248   O  TRP B   9           
SHEET    5   F 5 LYS B 328  ILE B 332 -1  N  ILE B 332   O  LEU B 247           
SHEET    1   G 8 MET B 217  PHE B 220  0                                        
SHEET    2   G 8 HIS B  33  VAL B  37  1  N  HIS B  33   O  VAL B 218           
SHEET    3   G 8 ARG B  61  VAL B  64  1  N  ARG B  61   O  ALA B  36           
SHEET    4   G 8 PRO B  81  VAL B  84  1  N  PRO B  81   O  LEU B  62           
SHEET    5   G 8 ILE B 101  VAL B 105  1  N  ALA B 102   O  ILE B  82           
SHEET    6   G 8 PHE B 158  TYR B 164  1  N  VAL B 159   O  ILE B 124           
SHEET    7   G 8 LEU B 198  HIS B 200  1  N  LEU B 198   O  LEU B 163           
SHEET    1   H 3 CYS B 315  LEU B 319  0                                        
SHEET    2   H 3 GLU B 275  ILE B 280 -1  N  ILE B 280   O  CYS B 315           
SHEET    3   H 3 LEU B 251  LEU B 257 -1  N  LEU B 257   O  GLU B 275           
SHEET    1   I 2 HIS B 296  VAL B 299  0                                        
SHEET    2   I 2 GLN B 302  PRO B 305 -1  N  ALA B 304   O  VAL B 297           
SHEET    1   J 2 GLY B 333  GLN B 335  0                                        
SHEET    2   J 2 GLU B 338  ILE B 340 -1  N  ILE B 340   O  GLY B 333           
LINK         NZ  LYS A  39                 C4A PLP A 500     1555   1555  1.30  
LINK         NZ  LYS B  39                 C4A PLP B 500     1555   1555  1.30  
LINK         C   LEU A 128                 N   KCX A 129     1555   1555  1.33  
LINK         C   KCX A 129                 N   MET A 130     1555   1555  1.32  
LINK         C   LEU B 128                 N   KCX B 129     1555   1555  1.34  
LINK         C   KCX B 129                 N   MET B 130     1555   1555  1.33  
CISPEP   1 GLY A  120    PRO A  121          0         1.01                     
CISPEP   2 GLY B  120    PRO B  121          0         0.41                     
SITE     1 PL1  1 PLP A 500                                                     
SITE     1 PL2  1 PLP B 500                                                     
SITE     1 KC1  1 KCX A 129                                                     
SITE     1 KC2  1 KCX B 129                                                     
SITE     1 PP1  1 PPI B 400                                                     
SITE     1 PP2  1 PPI A 400                                                     
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 512  HOH A 543                    
SITE     4 AC1 14 HOH A 557  PPI B 400                                          
SITE     1 AC2  9 LYS A  39  ARG A 136  TYR A 354  PLP A 500                    
SITE     2 AC2  9 TYR B 265  CYS B 311  MET B 312  HOH B 505                    
SITE     3 AC2  9 HOH B 582                                                     
SITE     1 AC3 13 PPI A 400  LYS B  39  TYR B  43  ARG B 136                    
SITE     2 AC3 13 HIS B 166  SER B 204  ARG B 219  GLY B 221                    
SITE     3 AC3 13 ILE B 222  TYR B 354  HOH B 537  HOH B 551                    
SITE     4 AC3 13 HOH B 581                                                     
SITE     1 AC4 10 TYR A 265  TYR A 284  CYS A 311  MET A 312                    
SITE     2 AC4 10 HOH A 569  HOH A 570  LYS B  39  ARG B 136                    
SITE     3 AC4 10 TYR B 354  PLP B 500                                          
CRYST1   98.700   90.000   85.200  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      0.010132  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011111  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011737        0.00000                         
MTRIX1   1 -0.868100  0.152200 -0.472500       75.61700    1                    
MTRIX2   1  0.152800 -0.823700 -0.546100       94.29800    1                    
MTRIX3   1 -0.472300 -0.546300  0.691800       50.26700    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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