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Database: PDB
Entry: 1L6F
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HEADER    ISOMERASE                               09-MAR-02   1L6F              
TITLE     ALANINE RACEMASE BOUND WITH N-(5'-PHOSPHOPYRIDOXYL)-L-                
TITLE    2 ALANINE                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALANINE RACEMASE;                                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 5.1.1.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GEOBACILLUS STEAROTHERMOPHILUS;                 
SOURCE   3 ORGANISM_TAXID: 1422;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PAR310                                    
KEYWDS    ALANINE RACEMASE, REACTION MECHANISM, N-(5'-                          
KEYWDS   2 PHOSPHOPYRIDOXYL)-ALANINE, ISOMERASE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.WATANABE,T.YOSHIMURA,B.MIKAMI,H.HAYASHI,H.KAGAMIYAMA,               
AUTHOR   2 N.ESAKI                                                              
REVDAT   4   24-FEB-09 1L6F    1       VERSN                                    
REVDAT   3   01-APR-03 1L6F    1       JRNL                                     
REVDAT   2   20-NOV-02 1L6F    1       REMARK                                   
REVDAT   1   05-JUN-02 1L6F    0                                                
JRNL        AUTH   A.WATANABE,T.YOSHIMURA,B.MIKAMI,H.HAYASHI,                   
JRNL        AUTH 2 H.KAGAMIYAMA,N.ESAKI                                         
JRNL        TITL   REACTION MECHANISM OF ALANINE RACEMASE FROM                  
JRNL        TITL 2 BACILLUS STEAROTHERMOPHILUS: X-RAY                           
JRNL        TITL 3 CRYSTALLOGRAPHIC STUDIES OF THE ENZYME BOUND WITH            
JRNL        TITL 4 N-(5'-PHOSPHOPYRIDOXYL)ALANINE.                              
JRNL        REF    J.BIOL.CHEM.                  V. 277 19166 2002              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   11886871                                                     
JRNL        DOI    10.1074/JBC.M201615200                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.P.SHAW,G.A.PETSKO,D.RINGE                                  
REMARK   1  TITL   DETERMINATION OF THE STRUCTURE OF ALANINE RACEMASE           
REMARK   1  TITL 2 FROM BACILLUS STEAROTHERMOPHILUS AT 1.9-A                    
REMARK   1  TITL 3 RESOLUTION                                                   
REMARK   1  REF    BIOCHEMISTRY                  V.  36  1329 1997              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  DOI    10.1021/BI961856C                                            
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   G.F.STAMPER,A.A.MOROLLO,D.RINGE                              
REMARK   1  TITL   REACTION OF ALANINE RACEMASE WITH                            
REMARK   1  TITL 2 1-AMINOETHYLPHOSPHONIC ACID FORMS A STABLE                   
REMARK   1  TITL 3 EXTERNAL ALDIMINE                                            
REMARK   1  REF    BIOCHEMISTRY                  V.  37 10438 1998              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  DOI    10.1021/BI980692S                                            
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   A.A.MOROLLO,G.A.PETSKO,D.RINGE                               
REMARK   1  TITL   STRUCTURE OF A MICHAELIS COMPLEX ANALOGUE:                   
REMARK   1  TITL 2 PROPIONATE BINDS IN THE SUBSTRATE CARBOXYLATE SITE           
REMARK   1  TITL 3 OF ALANINE RACEMASE                                          
REMARK   1  REF    BIOCHEMISTRY                  V.  38  3293 1999              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  DOI    10.1021/BI9822729                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 7.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 493425.010                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 79.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 41051                          
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) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 4165                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.12                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 52.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4048                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2600                       
REMARK   3   BIN FREE R VALUE                    : 0.3100                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 433                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.015                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6066                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 42                                      
REMARK   3   SOLVENT ATOMS            : 292                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 6.10                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.75000                                              
REMARK   3    B22 (A**2) : -0.15000                                             
REMARK   3    B33 (A**2) : -2.60000                                             
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) : 0.21                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.25                            
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) : 0.27                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.30                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.67                            
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) : 2.100 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.980 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.350 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.630 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.49                                                 
REMARK   3   BSOL        : 116.24                                               
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : PLP.PARAM                                      
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : PLP.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1L6F COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-MAR-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB015683.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-SEP-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
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          : MACSCIENCE                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : CARBON MONOCHROMETER               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS HI-STAR                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SAINT                              
REMARK 200  DATA SCALING SOFTWARE          : SAINT                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52427                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.930                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.4                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 1.4800                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 73.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.82                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.47600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.480                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1SFT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, SODIUM ACETATE, TRIS-          
REMARK 280  BUFFER, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K     
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       49.98000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.70850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.43300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       42.70850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       49.98000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.43300            
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: 6280 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   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 470     ARG B 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    PHE A 106        7.81   -153.02                                   
REMARK 500    SER A 119       46.02   -150.88                                   
REMARK 500    ARG A 136      -84.43    -88.93                                   
REMARK 500    CYS A 201      -24.53   -156.24                                   
REMARK 500    ASN A 203     -163.79   -105.65                                   
REMARK 500    PHE A 215     -136.92     69.09                                   
REMARK 500    SER A 264     -178.53     64.92                                   
REMARK 500    MET A 375      -61.74    -93.65                                   
REMARK 500    PHE B 106       10.75   -155.55                                   
REMARK 500    SER B 119       42.24   -149.35                                   
REMARK 500    ARG B 136      -79.78    -89.52                                   
REMARK 500    CYS B 201      -23.94   -153.84                                   
REMARK 500    ASN B 203     -164.90   -104.38                                   
REMARK 500    PHE B 215     -139.14     66.94                                   
REMARK 500    SER B 264     -179.05     65.78                                   
REMARK 500    HIS B 371       32.63     70.03                                   
REMARK 500    MET B 375      -63.45    -91.56                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 583        DISTANCE =  5.11 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PP3 A 390                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PP3 B 1390                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1L6G   RELATED DB: PDB                                   
REMARK 900 1L6G CONTAINS THE SAME PROTEIN BOUND WITH N-(5'-                     
REMARK 900 PHOSPHOPYRIDOXYL)-D-ALANINE                                          
DBREF  1L6F A    1   388  UNP    P10724   ALR_BACST        1    388             
DBREF  1L6F B    1   388  UNP    P10724   ALR_BACST        1    388             
SEQADV 1L6F KCX A  129  UNP  P10724    LYS   129 MODIFIED RESIDUE               
SEQADV 1L6F KCX B  129  UNP  P10724    LYS   129 MODIFIED RESIDUE               
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 1L6F KCX A  129  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 1L6F KCX B  129  LYS  LYSINE NZ-CARBOXYLIC ACID                          
HET    KCX  A 129      12                                                       
HET    KCX  B 129      12                                                       
HET    PP3  A 390      21                                                       
HET    PP3  B1390      21                                                       
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID                                        
HETNAM     PP3 ALANYL-PYRIDOXAL-5'-PHOSPHATE                                    
HETSYN     PP3 PYRIDOXYL-ALANINE-5-PHOSPHATE; VITAMIN B6 COMPLEXED              
HETSYN   2 PP3  WITH ALANINE                                                    
FORMUL   1  KCX    2(C7 H14 N2 O4)                                              
FORMUL   3  PP3    2(C11 H17 N2 O7 P)                                           
FORMUL   5  HOH   *292(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  ARG A  100  1                                   9    
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 ILE A  233  LEU A  237  5                                   5    
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  LEU B   28  1                                  15    
HELIX   20  20 VAL B   38  HIS B   45  1                                   8    
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 ILE B  233  LEU B  237  5                                   5    
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  HIS B  294  5                                   6    
HELIX   35  35 SER B  341  LEU B  349  1                                   9    
HELIX   36  36 TYR B  354  ILE B  360  1                                   7    
SHEET    1   A10 ARG A 373  ARG A 378  0                                        
SHEET    2   A10 ARG A 366  ARG A 370 -1  N  PHE A 368   O  MET A 375           
SHEET    3   A10 THR A   8  ASP A  13  1  N  VAL A  12   O  ILE A 367           
SHEET    4   A10 PHE A 245  ARG A 250 -1  O  HIS A 248   N  TRP A   9           
SHEET    5   A10 LYS A 328  GLN A 335 -1  O  VAL A 329   N  SER A 249           
SHEET    6   A10 HIS A 296  VAL A 299 -1  N  LEU A 298   O  THR A 330           
SHEET    7   A10 GLN A 302  VAL A 307 -1  O  ALA A 304   N  VAL A 297           
SHEET    8   A10 CYS A 315  LEU A 319 -1  O  MET A 316   N  VAL A 307           
SHEET    9   A10 GLU A 275  ILE A 280 -1  N  TRP A 276   O  LEU A 319           
SHEET   10   A10 HIS A 253  LEU A 257 -1  N  LYS A 255   O  ILE A 277           
SHEET    1   B 6 ARG A 373  ARG A 378  0                                        
SHEET    2   B 6 ARG A 366  ARG A 370 -1  N  PHE A 368   O  MET A 375           
SHEET    3   B 6 THR A   8  ASP A  13  1  N  VAL A  12   O  ILE A 367           
SHEET    4   B 6 PHE A 245  ARG A 250 -1  O  HIS A 248   N  TRP A   9           
SHEET    5   B 6 LYS A 328  GLN A 335 -1  O  VAL A 329   N  SER A 249           
SHEET    6   B 6 GLU A 338  ILE A 340 -1  O  ILE A 340   N  GLY A 333           
SHEET    1   C 8 LEU A 198  HIS A 200  0                                        
SHEET    2   C 8 PHE A 158  TYR A 164  1  N  LEU A 163   O  LEU A 198           
SHEET    3   C 8 ILE A 124  KCX A 129  1  N  PHE A 126   O  VAL A 159           
SHEET    4   C 8 ILE A 101  VAL A 105  1  N  VAL A 105   O  KCX A 129           
SHEET    5   C 8 ILE A  82  VAL A  84  1  N  ILE A  82   O  ALA A 102           
SHEET    6   C 8 ARG A  61  VAL A  64  1  N  VAL A  64   O  LEU A  83           
SHEET    7   C 8 HIS A  33  VAL A  37  1  N  ALA A  36   O  ARG A  61           
SHEET    8   C 8 MET A 217  PHE A 220  1  O  VAL A 218   N  MET A  35           
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   E10 ARG B 373  ARG B 378  0                                        
SHEET    2   E10 ARG B 366  ARG B 370 -1  N  ARG B 366   O  ARG B 378           
SHEET    3   E10 THR B   8  ASP B  13  1  N  VAL B  12   O  ILE B 367           
SHEET    4   E10 PHE B 245  ARG B 250 -1  O  SER B 246   N  GLU B  11           
SHEET    5   E10 LYS B 328  GLN B 335 -1  O  VAL B 329   N  SER B 249           
SHEET    6   E10 HIS B 296  VAL B 299 -1  N  LEU B 298   O  THR B 330           
SHEET    7   E10 GLN B 302  VAL B 307 -1  O  GLN B 302   N  VAL B 299           
SHEET    8   E10 CYS B 315  ARG B 318 -1  O  MET B 316   N  VAL B 307           
SHEET    9   E10 GLU B 275  ILE B 280 -1  N  GLY B 278   O  ILE B 317           
SHEET   10   E10 HIS B 253  LEU B 257 -1  N  LEU B 257   O  GLU B 275           
SHEET    1   F 6 ARG B 373  ARG B 378  0                                        
SHEET    2   F 6 ARG B 366  ARG B 370 -1  N  ARG B 366   O  ARG B 378           
SHEET    3   F 6 THR B   8  ASP B  13  1  N  VAL B  12   O  ILE B 367           
SHEET    4   F 6 PHE B 245  ARG B 250 -1  O  SER B 246   N  GLU B  11           
SHEET    5   F 6 LYS B 328  GLN B 335 -1  O  VAL B 329   N  SER B 249           
SHEET    6   F 6 GLU B 338  ILE B 340 -1  O  ILE B 340   N  GLY B 333           
SHEET    1   G 8 LEU B 198  HIS B 200  0                                        
SHEET    2   G 8 PHE B 158  TYR B 164  1  N  LEU B 163   O  LEU B 198           
SHEET    3   G 8 ILE B 124  KCX B 129  1  N  PHE B 126   O  VAL B 159           
SHEET    4   G 8 ILE B 101  VAL B 105  1  N  VAL B 105   O  KCX B 129           
SHEET    5   G 8 ILE B  82  VAL B  84  1  N  VAL B  84   O  ALA B 102           
SHEET    6   G 8 ARG B  61  VAL B  64  1  N  LEU B  62   O  LEU B  83           
SHEET    7   G 8 HIS B  33  VAL B  37  1  N  ALA B  36   O  ARG B  61           
SHEET    8   G 8 MET B 217  PHE B 220  1  O  VAL B 218   N  MET B  35           
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         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         0.26                     
CISPEP   2 GLY B  120    PRO B  121          0        -0.02                     
SITE     1 AC1 17 LYS A  39  TYR A  43  ARG A 136  HIS A 166                    
SITE     2 AC1 17 SER A 204  ARG A 219  GLY A 221  ILE A 222                    
SITE     3 AC1 17 TYR A 354  HOH A 409  HOH A 452  HOH A 460                    
SITE     4 AC1 17 HOH A 461  TYR B 265  TYR B 284  CYS B 311                    
SITE     5 AC1 17 MET B 312                                                     
SITE     1 AC2 20 TYR A 265  TYR A 284  CYS A 311  MET A 312                    
SITE     2 AC2 20 LYS B  39  TYR B  43  KCX B 129  ARG B 136                    
SITE     3 AC2 20 HIS B 166  ASN B 203  SER B 204  ARG B 219                    
SITE     4 AC2 20 GLY B 221  ILE B 222  TYR B 354  HOH B 459                    
SITE     5 AC2 20 HOH B 500  HOH B 504  HOH B 556  HOH B 565                    
CRYST1   99.960   90.866   85.417  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      0.010004  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011005  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011707        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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