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Database: PDB
Entry: 2DY3
LinkDB: 2DY3
Original site: 2DY3 
HEADER    ISOMERASE                               05-SEP-06   2DY3              
TITLE     CRYSTAL STRUCTURE OF ALANINE RACEMASE FROM CORYNEBACTERIUM GLUTAMICUM 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALANINE RACEMASE;                                          
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 5.1.1.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CORYNEBACTERIUM GLUTAMICUM;                     
SOURCE   3 ORGANISM_TAXID: 1718;                                                
SOURCE   4 GENE: ALR;                                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET3B, ALARCCGL                           
KEYWDS    ALPHA/BETA BARREL, ISOMERASE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.MIYAGUCHI,C.SASAKI,R.KATO,T.OIKAWA,S.SUGIO                          
REVDAT   3   13-JUL-11 2DY3    1       VERSN                                    
REVDAT   2   24-FEB-09 2DY3    1       VERSN                                    
REVDAT   1   11-SEP-07 2DY3    0                                                
JRNL        AUTH   I.MIYAGUCHI,C.SASAKI,R.KATO,T.OIKAWA,S.SUGIO                 
JRNL        TITL   CRYSTAL STRUCTURE OF ALANINE RACEMASE FROM CORYNEBACTERIUM   
JRNL        TITL 2 GLUTAMICUM AT 2.1 A RESOLUTION                               
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 79577                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.227                           
REMARK   3   FREE R VALUE                     : 0.269                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 4012                            
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           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
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            : 10399                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 60                                      
REMARK   3   SOLVENT ATOMS            : 761                                     
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) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.27                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.82                            
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 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 2DY3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-SEP-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB025986.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-FEB-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL24XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.836                              
REMARK 200  MONOCHROMATOR                  : DIAMOND                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 79817                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.2                               
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) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.6                               
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: 1BD0                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.62                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG8000, 200MM AMMONIUM SULFATE,     
REMARK 280  100MM MES, PH 6.0, VAPOR DIFFUSION, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       56.80600            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 5650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25430 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 5860 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     CYS A   161                                                      
REMARK 465     ALA A   162                                                      
REMARK 465     ASP A   163                                                      
REMARK 465     GLU A   164                                                      
REMARK 465     PRO A   165                                                      
REMARK 465     GLU A   166                                                      
REMARK 465     ASN A   167                                                      
REMARK 465     PRO A   168                                                      
REMARK 465     ALA A   250                                                      
REMARK 465     GLY A   251                                                      
REMARK 465     GLN A   252                                                      
REMARK 465     GLY A   253                                                      
REMARK 465     THR A   254                                                      
REMARK 465     SER A   255                                                      
REMARK 465     TYR A   256                                                      
REMARK 465     GLY A   257                                                      
REMARK 465     LEU A   258                                                      
REMARK 465     THR A   259                                                      
REMARK 465     TRP A   260                                                      
REMARK 465     ARG A   261                                                      
REMARK 465     ALA A   262                                                      
REMARK 465     GLU A   263                                                      
REMARK 465     ASP A   264                                                      
REMARK 465     ASP B   163                                                      
REMARK 465     GLU B   164                                                      
REMARK 465     PRO B   165                                                      
REMARK 465     GLU B   166                                                      
REMARK 465     ASN B   167                                                      
REMARK 465     GLU B   249                                                      
REMARK 465     ALA B   250                                                      
REMARK 465     GLY B   251                                                      
REMARK 465     GLN B   252                                                      
REMARK 465     GLY B   253                                                      
REMARK 465     THR B   254                                                      
REMARK 465     SER B   255                                                      
REMARK 465     TYR B   256                                                      
REMARK 465     GLY B   257                                                      
REMARK 465     LEU B   258                                                      
REMARK 465     THR B   259                                                      
REMARK 465     TRP B   260                                                      
REMARK 465     ARG B   261                                                      
REMARK 465     ALA B   262                                                      
REMARK 465     GLU B   263                                                      
REMARK 465     ASP B   264                                                      
REMARK 465     GLU C   166                                                      
REMARK 465     ASN C   167                                                      
REMARK 465     GLU C   249                                                      
REMARK 465     ALA C   250                                                      
REMARK 465     GLY C   251                                                      
REMARK 465     GLN C   252                                                      
REMARK 465     GLY C   253                                                      
REMARK 465     THR C   254                                                      
REMARK 465     SER C   255                                                      
REMARK 465     TYR C   256                                                      
REMARK 465     GLY C   257                                                      
REMARK 465     LEU C   258                                                      
REMARK 465     THR C   259                                                      
REMARK 465     TRP C   260                                                      
REMARK 465     ARG C   261                                                      
REMARK 465     ALA C   262                                                      
REMARK 465     GLU C   263                                                      
REMARK 465     ASP C   264                                                      
REMARK 465     GLU D   166                                                      
REMARK 465     ASN D   167                                                      
REMARK 465     PRO D   168                                                      
REMARK 465     GLU D   169                                                      
REMARK 465     GLY D   253                                                      
REMARK 465     THR D   254                                                      
REMARK 465     SER D   255                                                      
REMARK 465     TYR D   256                                                      
REMARK 465     GLY D   257                                                      
REMARK 465     LEU D   258                                                      
REMARK 465     THR D   259                                                      
REMARK 465     TRP D   260                                                      
REMARK 465     ARG D   261                                                      
REMARK 465     ALA D   262                                                      
REMARK 465     GLU D   263                                                      
REMARK 465     ASP D   264                                                      
REMARK 465     ARG D   265                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 272   C   -  N   -  CA  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    PRO C 192   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    PRO D 272   C   -  N   -  CA  ANGL. DEV. =   9.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 129     -114.40    -99.87                                   
REMARK 500    TRP A 137      -71.35    -36.48                                   
REMARK 500    VAL A 196      -14.01   -143.72                                   
REMARK 500    ARG A 205       75.06   -118.43                                   
REMARK 500    MET A 210     -146.52     52.22                                   
REMARK 500    ALA A 226       89.91    -62.65                                   
REMARK 500    PRO A 272       57.84    -59.16                                   
REMARK 500    THR A 353     -158.13   -154.38                                   
REMARK 500    ARG B 129     -111.93    -96.03                                   
REMARK 500    LEU B 159       99.05    -57.83                                   
REMARK 500    ALA B 160      154.19    -47.13                                   
REMARK 500    VAL B 196      -22.29   -142.69                                   
REMARK 500    THR B 204      -10.01   -150.80                                   
REMARK 500    MET B 210     -142.80     52.84                                   
REMARK 500    PRO B 272       61.46    -62.97                                   
REMARK 500    THR B 353     -159.54   -150.20                                   
REMARK 500    SER C 125       35.75    -99.57                                   
REMARK 500    ARG C 129      -92.53   -112.45                                   
REMARK 500    GLU C 169      -57.49    -21.93                                   
REMARK 500    VAL C 196      -14.29   -145.57                                   
REMARK 500    MET C 210     -153.47     56.14                                   
REMARK 500    PRO C 272       66.70    -69.71                                   
REMARK 500    THR C 343     -157.43   -142.75                                   
REMARK 500    THR C 353     -159.39   -156.88                                   
REMARK 500    ARG D 129     -108.23   -102.89                                   
REMARK 500    MET D 210     -148.54     51.85                                   
REMARK 500    GLU D 249     -154.65    -77.43                                   
REMARK 500    ALA D 250       -5.91    -51.78                                   
REMARK 500    PRO D 272       53.39    -63.76                                   
REMARK 500    THR D 353     -156.47   -154.64                                   
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 A 512        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH D 588        DISTANCE =  5.10 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP D 401                 
DBREF  2DY3 A    1   361  UNP    Q8RSU9   ALR_CORGL        1    361             
DBREF  2DY3 B    1   361  UNP    Q8RSU9   ALR_CORGL        1    361             
DBREF  2DY3 C    1   361  UNP    Q8RSU9   ALR_CORGL        1    361             
DBREF  2DY3 D    1   361  UNP    Q8RSU9   ALR_CORGL        1    361             
SEQRES   1 A  361  MET ASN LEU LEU THR THR LYS ILE ASP LEU ASP ALA ILE          
SEQRES   2 A  361  ALA HIS ASN THR ARG VAL LEU LYS GLN MET ALA GLY PRO          
SEQRES   3 A  361  ALA LYS LEU MET ALA VAL VAL LYS ALA ASN ALA TYR ASN          
SEQRES   4 A  361  HIS GLY VAL GLU LYS VAL ALA PRO VAL ILE ALA ALA HIS          
SEQRES   5 A  361  GLY ALA ASP ALA PHE GLY VAL ALA THR LEU ALA GLU ALA          
SEQRES   6 A  361  MET GLN LEU ARG ASP ILE GLY ILE SER GLN GLU VAL LEU          
SEQRES   7 A  361  CYS TRP ILE TRP THR PRO GLU GLN ASP PHE ARG ALA ALA          
SEQRES   8 A  361  ILE ASP ARG ASN ILE ASP LEU ALA VAL ILE SER PRO ALA          
SEQRES   9 A  361  HIS ALA LYS ALA LEU ILE GLU THR ASP ALA GLU HIS ILE          
SEQRES  10 A  361  ARG VAL SER ILE LYS ILE ASP SER GLY LEU HIS ARG SER          
SEQRES  11 A  361  GLY VAL ASP GLU GLN GLU TRP GLU GLY VAL PHE SER ALA          
SEQRES  12 A  361  LEU ALA ALA ALA PRO HIS ILE GLU VAL THR GLY MET PHE          
SEQRES  13 A  361  THR HIS LEU ALA CYS ALA ASP GLU PRO GLU ASN PRO GLU          
SEQRES  14 A  361  THR ASP ARG GLN ILE ILE ALA PHE ARG ARG ALA LEU ALA          
SEQRES  15 A  361  LEU ALA ARG LYS HIS GLY LEU GLU CYS PRO VAL ASN HIS          
SEQRES  16 A  361  VAL CYS ASN SER PRO ALA PHE LEU THR ARG SER ASP LEU          
SEQRES  17 A  361  HIS MET GLU MET VAL ARG PRO GLY LEU ALA PHE TYR GLY          
SEQRES  18 A  361  LEU GLU PRO VAL ALA GLY LEU GLU HIS GLY LEU LYS PRO          
SEQRES  19 A  361  ALA MET THR TRP GLU ALA LYS VAL SER VAL VAL LYS GLN          
SEQRES  20 A  361  ILE GLU ALA GLY GLN GLY THR SER TYR GLY LEU THR TRP          
SEQRES  21 A  361  ARG ALA GLU ASP ARG GLY PHE VAL ALA VAL VAL PRO ALA          
SEQRES  22 A  361  GLY TYR ALA ASP GLY MET PRO ARG HIS ALA GLN GLY LYS          
SEQRES  23 A  361  PHE SER VAL THR ILE ASP GLY LEU ASP TYR PRO GLN VAL          
SEQRES  24 A  361  GLY ARG VAL CYS MET ASP GLN PHE VAL ILE SER LEU GLY          
SEQRES  25 A  361  ASP ASN PRO HIS GLY VAL GLU ALA GLY ALA LYS ALA VAL          
SEQRES  26 A  361  ILE PHE GLY GLU ASN GLY HIS ASP ALA THR ASP PHE ALA          
SEQRES  27 A  361  GLU ARG LEU ASP THR ILE ASN TYR GLU VAL VAL CYS ARG          
SEQRES  28 A  361  PRO THR GLY ARG THR VAL ARG ALA TYR VAL                      
SEQRES   1 B  361  MET ASN LEU LEU THR THR LYS ILE ASP LEU ASP ALA ILE          
SEQRES   2 B  361  ALA HIS ASN THR ARG VAL LEU LYS GLN MET ALA GLY PRO          
SEQRES   3 B  361  ALA LYS LEU MET ALA VAL VAL LYS ALA ASN ALA TYR ASN          
SEQRES   4 B  361  HIS GLY VAL GLU LYS VAL ALA PRO VAL ILE ALA ALA HIS          
SEQRES   5 B  361  GLY ALA ASP ALA PHE GLY VAL ALA THR LEU ALA GLU ALA          
SEQRES   6 B  361  MET GLN LEU ARG ASP ILE GLY ILE SER GLN GLU VAL LEU          
SEQRES   7 B  361  CYS TRP ILE TRP THR PRO GLU GLN ASP PHE ARG ALA ALA          
SEQRES   8 B  361  ILE ASP ARG ASN ILE ASP LEU ALA VAL ILE SER PRO ALA          
SEQRES   9 B  361  HIS ALA LYS ALA LEU ILE GLU THR ASP ALA GLU HIS ILE          
SEQRES  10 B  361  ARG VAL SER ILE LYS ILE ASP SER GLY LEU HIS ARG SER          
SEQRES  11 B  361  GLY VAL ASP GLU GLN GLU TRP GLU GLY VAL PHE SER ALA          
SEQRES  12 B  361  LEU ALA ALA ALA PRO HIS ILE GLU VAL THR GLY MET PHE          
SEQRES  13 B  361  THR HIS LEU ALA CYS ALA ASP GLU PRO GLU ASN PRO GLU          
SEQRES  14 B  361  THR ASP ARG GLN ILE ILE ALA PHE ARG ARG ALA LEU ALA          
SEQRES  15 B  361  LEU ALA ARG LYS HIS GLY LEU GLU CYS PRO VAL ASN HIS          
SEQRES  16 B  361  VAL CYS ASN SER PRO ALA PHE LEU THR ARG SER ASP LEU          
SEQRES  17 B  361  HIS MET GLU MET VAL ARG PRO GLY LEU ALA PHE TYR GLY          
SEQRES  18 B  361  LEU GLU PRO VAL ALA GLY LEU GLU HIS GLY LEU LYS PRO          
SEQRES  19 B  361  ALA MET THR TRP GLU ALA LYS VAL SER VAL VAL LYS GLN          
SEQRES  20 B  361  ILE GLU ALA GLY GLN GLY THR SER TYR GLY LEU THR TRP          
SEQRES  21 B  361  ARG ALA GLU ASP ARG GLY PHE VAL ALA VAL VAL PRO ALA          
SEQRES  22 B  361  GLY TYR ALA ASP GLY MET PRO ARG HIS ALA GLN GLY LYS          
SEQRES  23 B  361  PHE SER VAL THR ILE ASP GLY LEU ASP TYR PRO GLN VAL          
SEQRES  24 B  361  GLY ARG VAL CYS MET ASP GLN PHE VAL ILE SER LEU GLY          
SEQRES  25 B  361  ASP ASN PRO HIS GLY VAL GLU ALA GLY ALA LYS ALA VAL          
SEQRES  26 B  361  ILE PHE GLY GLU ASN GLY HIS ASP ALA THR ASP PHE ALA          
SEQRES  27 B  361  GLU ARG LEU ASP THR ILE ASN TYR GLU VAL VAL CYS ARG          
SEQRES  28 B  361  PRO THR GLY ARG THR VAL ARG ALA TYR VAL                      
SEQRES   1 C  361  MET ASN LEU LEU THR THR LYS ILE ASP LEU ASP ALA ILE          
SEQRES   2 C  361  ALA HIS ASN THR ARG VAL LEU LYS GLN MET ALA GLY PRO          
SEQRES   3 C  361  ALA LYS LEU MET ALA VAL VAL LYS ALA ASN ALA TYR ASN          
SEQRES   4 C  361  HIS GLY VAL GLU LYS VAL ALA PRO VAL ILE ALA ALA HIS          
SEQRES   5 C  361  GLY ALA ASP ALA PHE GLY VAL ALA THR LEU ALA GLU ALA          
SEQRES   6 C  361  MET GLN LEU ARG ASP ILE GLY ILE SER GLN GLU VAL LEU          
SEQRES   7 C  361  CYS TRP ILE TRP THR PRO GLU GLN ASP PHE ARG ALA ALA          
SEQRES   8 C  361  ILE ASP ARG ASN ILE ASP LEU ALA VAL ILE SER PRO ALA          
SEQRES   9 C  361  HIS ALA LYS ALA LEU ILE GLU THR ASP ALA GLU HIS ILE          
SEQRES  10 C  361  ARG VAL SER ILE LYS ILE ASP SER GLY LEU HIS ARG SER          
SEQRES  11 C  361  GLY VAL ASP GLU GLN GLU TRP GLU GLY VAL PHE SER ALA          
SEQRES  12 C  361  LEU ALA ALA ALA PRO HIS ILE GLU VAL THR GLY MET PHE          
SEQRES  13 C  361  THR HIS LEU ALA CYS ALA ASP GLU PRO GLU ASN PRO GLU          
SEQRES  14 C  361  THR ASP ARG GLN ILE ILE ALA PHE ARG ARG ALA LEU ALA          
SEQRES  15 C  361  LEU ALA ARG LYS HIS GLY LEU GLU CYS PRO VAL ASN HIS          
SEQRES  16 C  361  VAL CYS ASN SER PRO ALA PHE LEU THR ARG SER ASP LEU          
SEQRES  17 C  361  HIS MET GLU MET VAL ARG PRO GLY LEU ALA PHE TYR GLY          
SEQRES  18 C  361  LEU GLU PRO VAL ALA GLY LEU GLU HIS GLY LEU LYS PRO          
SEQRES  19 C  361  ALA MET THR TRP GLU ALA LYS VAL SER VAL VAL LYS GLN          
SEQRES  20 C  361  ILE GLU ALA GLY GLN GLY THR SER TYR GLY LEU THR TRP          
SEQRES  21 C  361  ARG ALA GLU ASP ARG GLY PHE VAL ALA VAL VAL PRO ALA          
SEQRES  22 C  361  GLY TYR ALA ASP GLY MET PRO ARG HIS ALA GLN GLY LYS          
SEQRES  23 C  361  PHE SER VAL THR ILE ASP GLY LEU ASP TYR PRO GLN VAL          
SEQRES  24 C  361  GLY ARG VAL CYS MET ASP GLN PHE VAL ILE SER LEU GLY          
SEQRES  25 C  361  ASP ASN PRO HIS GLY VAL GLU ALA GLY ALA LYS ALA VAL          
SEQRES  26 C  361  ILE PHE GLY GLU ASN GLY HIS ASP ALA THR ASP PHE ALA          
SEQRES  27 C  361  GLU ARG LEU ASP THR ILE ASN TYR GLU VAL VAL CYS ARG          
SEQRES  28 C  361  PRO THR GLY ARG THR VAL ARG ALA TYR VAL                      
SEQRES   1 D  361  MET ASN LEU LEU THR THR LYS ILE ASP LEU ASP ALA ILE          
SEQRES   2 D  361  ALA HIS ASN THR ARG VAL LEU LYS GLN MET ALA GLY PRO          
SEQRES   3 D  361  ALA LYS LEU MET ALA VAL VAL LYS ALA ASN ALA TYR ASN          
SEQRES   4 D  361  HIS GLY VAL GLU LYS VAL ALA PRO VAL ILE ALA ALA HIS          
SEQRES   5 D  361  GLY ALA ASP ALA PHE GLY VAL ALA THR LEU ALA GLU ALA          
SEQRES   6 D  361  MET GLN LEU ARG ASP ILE GLY ILE SER GLN GLU VAL LEU          
SEQRES   7 D  361  CYS TRP ILE TRP THR PRO GLU GLN ASP PHE ARG ALA ALA          
SEQRES   8 D  361  ILE ASP ARG ASN ILE ASP LEU ALA VAL ILE SER PRO ALA          
SEQRES   9 D  361  HIS ALA LYS ALA LEU ILE GLU THR ASP ALA GLU HIS ILE          
SEQRES  10 D  361  ARG VAL SER ILE LYS ILE ASP SER GLY LEU HIS ARG SER          
SEQRES  11 D  361  GLY VAL ASP GLU GLN GLU TRP GLU GLY VAL PHE SER ALA          
SEQRES  12 D  361  LEU ALA ALA ALA PRO HIS ILE GLU VAL THR GLY MET PHE          
SEQRES  13 D  361  THR HIS LEU ALA CYS ALA ASP GLU PRO GLU ASN PRO GLU          
SEQRES  14 D  361  THR ASP ARG GLN ILE ILE ALA PHE ARG ARG ALA LEU ALA          
SEQRES  15 D  361  LEU ALA ARG LYS HIS GLY LEU GLU CYS PRO VAL ASN HIS          
SEQRES  16 D  361  VAL CYS ASN SER PRO ALA PHE LEU THR ARG SER ASP LEU          
SEQRES  17 D  361  HIS MET GLU MET VAL ARG PRO GLY LEU ALA PHE TYR GLY          
SEQRES  18 D  361  LEU GLU PRO VAL ALA GLY LEU GLU HIS GLY LEU LYS PRO          
SEQRES  19 D  361  ALA MET THR TRP GLU ALA LYS VAL SER VAL VAL LYS GLN          
SEQRES  20 D  361  ILE GLU ALA GLY GLN GLY THR SER TYR GLY LEU THR TRP          
SEQRES  21 D  361  ARG ALA GLU ASP ARG GLY PHE VAL ALA VAL VAL PRO ALA          
SEQRES  22 D  361  GLY TYR ALA ASP GLY MET PRO ARG HIS ALA GLN GLY LYS          
SEQRES  23 D  361  PHE SER VAL THR ILE ASP GLY LEU ASP TYR PRO GLN VAL          
SEQRES  24 D  361  GLY ARG VAL CYS MET ASP GLN PHE VAL ILE SER LEU GLY          
SEQRES  25 D  361  ASP ASN PRO HIS GLY VAL GLU ALA GLY ALA LYS ALA VAL          
SEQRES  26 D  361  ILE PHE GLY GLU ASN GLY HIS ASP ALA THR ASP PHE ALA          
SEQRES  27 D  361  GLU ARG LEU ASP THR ILE ASN TYR GLU VAL VAL CYS ARG          
SEQRES  28 D  361  PRO THR GLY ARG THR VAL ARG ALA TYR VAL                      
HET    PLP  A 401      15                                                       
HET    PLP  B 401      15                                                       
HET    PLP  C 401      15                                                       
HET    PLP  D 401      15                                                       
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
FORMUL   5  PLP    4(C8 H10 N O6 P)                                             
FORMUL   9  HOH   *761(H2 O)                                                    
HELIX    1   1 LEU A   10  GLY A   25  1                                  16    
HELIX    2   2 VAL A   33  HIS A   40  1                                   8    
HELIX    3   3 GLY A   41  HIS A   52  1                                  12    
HELIX    4   4 THR A   61  ILE A   71  1                                  11    
HELIX    5   5 ASP A   87  ASP A   93  1                                   7    
HELIX    6   6 SER A  102  GLU A  111  1                                  10    
HELIX    7   7 ASP A  133  ALA A  146  1                                  14    
HELIX    8   8 GLU A  169  HIS A  187  1                                  19    
HELIX    9   9 ASN A  198  ARG A  205  1                                   8    
HELIX   10  10 SER A  206  HIS A  209  5                                   4    
HELIX   11  11 GLY A  216  GLY A  221  5                                   6    
HELIX   12  12 PRO A  280  GLN A  284  5                                   5    
HELIX   13  13 ASP A  333  LEU A  341  1                                   9    
HELIX   14  14 ILE A  344  ARG A  351  1                                   8    
HELIX   15  15 ASP B    9  GLY B   25  1                                  17    
HELIX   16  16 VAL B   33  ASN B   39  1                                   7    
HELIX   17  17 GLY B   41  ALA B   51  1                                  11    
HELIX   18  18 LEU B   62  ILE B   71  1                                  10    
HELIX   19  19 ASP B   87  ASP B   93  1                                   7    
HELIX   20  20 SER B  102  GLU B  111  1                                  10    
HELIX   21  21 ASP B  133  ALA B  147  1                                  15    
HELIX   22  22 PRO B  168  HIS B  187  1                                  20    
HELIX   23  23 ASN B  198  LEU B  203  1                                   6    
HELIX   24  24 ARG B  205  HIS B  209  5                                   5    
HELIX   25  25 GLY B  216  GLY B  221  5                                   6    
HELIX   26  26 GLY B  274  GLY B  278  5                                   5    
HELIX   27  27 PRO B  280  GLN B  284  5                                   5    
HELIX   28  28 ASP B  333  LEU B  341  1                                   9    
HELIX   29  29 ILE B  344  ARG B  351  1                                   8    
HELIX   30  30 LEU C   10  GLY C   25  1                                  16    
HELIX   31  31 VAL C   33  HIS C   40  1                                   8    
HELIX   32  32 GLY C   41  ALA C   51  1                                  11    
HELIX   33  33 THR C   61  ILE C   71  1                                  11    
HELIX   34  34 ASP C   87  ASP C   93  1                                   7    
HELIX   35  35 SER C  102  GLU C  111  1                                  10    
HELIX   36  36 ASP C  133  ALA C  146  1                                  14    
HELIX   37  37 PRO C  168  HIS C  187  1                                  20    
HELIX   38  38 ASN C  198  ARG C  205  1                                   8    
HELIX   39  39 SER C  206  HIS C  209  5                                   4    
HELIX   40  40 GLY C  216  GLY C  221  5                                   6    
HELIX   41  41 PRO C  280  GLN C  284  5                                   5    
HELIX   42  42 ASP C  333  LEU C  341  1                                   9    
HELIX   43  43 ILE C  344  ARG C  351  1                                   8    
HELIX   44  44 ASP D    9  GLY D   25  1                                  17    
HELIX   45  45 VAL D   33  ASN D   39  1                                   7    
HELIX   46  46 GLY D   41  HIS D   52  1                                  12    
HELIX   47  47 THR D   61  ILE D   71  1                                  11    
HELIX   48  48 ASP D   87  ASP D   93  1                                   7    
HELIX   49  49 SER D  102  GLU D  111  1                                  10    
HELIX   50  50 ASP D  133  ALA D  146  1                                  14    
HELIX   51  51 THR D  170  HIS D  187  1                                  18    
HELIX   52  52 ASN D  198  ARG D  205  1                                   8    
HELIX   53  53 SER D  206  HIS D  209  5                                   4    
HELIX   54  54 GLY D  216  GLY D  221  5                                   6    
HELIX   55  55 GLY D  274  GLY D  278  5                                   5    
HELIX   56  56 PRO D  280  GLN D  284  5                                   5    
HELIX   57  57 ASP D  333  LEU D  341  1                                   9    
HELIX   58  58 ILE D  344  ARG D  351  1                                   8    
SHEET    1   A 9 VAL A 244  GLN A 247  0                                        
SHEET    2   A 9 PHE A 267  VAL A 271 -1  O  VAL A 268   N  LYS A 246           
SHEET    3   A 9 PHE A 307  GLY A 312 -1  O  PHE A 307   N  VAL A 271           
SHEET    4   A 9 LEU A 294  VAL A 299 -1  N  VAL A 299   O  VAL A 308           
SHEET    5   A 9 SER A 288  ILE A 291 -1  N  ILE A 291   O  LEU A 294           
SHEET    6   A 9 LYS A 323  PHE A 327 -1  O  VAL A 325   N  THR A 290           
SHEET    7   A 9 MET A 236  LYS A 241 -1  N  ALA A 240   O  ALA A 324           
SHEET    8   A 9 LEU A   4  ASP A   9 -1  N  LYS A   7   O  THR A 237           
SHEET    9   A 9 VAL A 357  VAL A 361  1  O  ALA A 359   N  ILE A   8           
SHEET    1   B 7 ILE A 150  PHE A 156  0                                        
SHEET    2   B 7 ILE A 117  LYS A 122  1  N  VAL A 119   O  GLU A 151           
SHEET    3   B 7 ASP A  97  VAL A 100  1  N  VAL A 100   O  SER A 120           
SHEET    4   B 7 GLU A  76  CYS A  79  1  N  VAL A  77   O  ASP A  97           
SHEET    5   B 7 ALA A  56  VAL A  59  1  N  PHE A  57   O  LEU A  78           
SHEET    6   B 7 LYS A  28  VAL A  32  1  N  ALA A  31   O  GLY A  58           
SHEET    7   B 7 MET A 212  VAL A 213  1  O  VAL A 213   N  LYS A  28           
SHEET    1   C 9 VAL B 244  GLN B 247  0                                        
SHEET    2   C 9 PHE B 267  VAL B 271 -1  O  VAL B 268   N  LYS B 246           
SHEET    3   C 9 PHE B 307  GLY B 312 -1  O  ILE B 309   N  ALA B 269           
SHEET    4   C 9 LEU B 294  VAL B 299 -1  N  VAL B 299   O  VAL B 308           
SHEET    5   C 9 SER B 288  ILE B 291 -1  N  ILE B 291   O  LEU B 294           
SHEET    6   C 9 LYS B 323  PHE B 327 -1  O  VAL B 325   N  THR B 290           
SHEET    7   C 9 MET B 236  LYS B 241 -1  N  ALA B 240   O  ALA B 324           
SHEET    8   C 9 LEU B   4  ILE B   8 -1  N  LYS B   7   O  THR B 237           
SHEET    9   C 9 VAL B 357  TYR B 360  1  O  ALA B 359   N  ILE B   8           
SHEET    1   D 7 ILE B 150  PHE B 156  0                                        
SHEET    2   D 7 ILE B 117  LYS B 122  1  N  ILE B 117   O  GLU B 151           
SHEET    3   D 7 ASP B  97  VAL B 100  1  N  VAL B 100   O  SER B 120           
SHEET    4   D 7 GLU B  76  ILE B  81  1  N  VAL B  77   O  ASP B  97           
SHEET    5   D 7 ALA B  56  THR B  61  1  N  ALA B  60   O  ILE B  81           
SHEET    6   D 7 LYS B  28  VAL B  32  1  N  ALA B  31   O  ALA B  56           
SHEET    7   D 7 MET B 212  VAL B 213  1  O  VAL B 213   N  MET B  30           
SHEET    1   E 9 VAL C 244  GLN C 247  0                                        
SHEET    2   E 9 PHE C 267  VAL C 271 -1  O  VAL C 268   N  LYS C 246           
SHEET    3   E 9 PHE C 307  GLY C 312 -1  O  PHE C 307   N  VAL C 271           
SHEET    4   E 9 LEU C 294  VAL C 299 -1  N  VAL C 299   O  VAL C 308           
SHEET    5   E 9 SER C 288  ILE C 291 -1  N  ILE C 291   O  LEU C 294           
SHEET    6   E 9 LYS C 323  PHE C 327 -1  O  VAL C 325   N  THR C 290           
SHEET    7   E 9 MET C 236  LYS C 241 -1  N  ALA C 240   O  ALA C 324           
SHEET    8   E 9 LEU C   4  ASP C   9 -1  N  THR C   5   O  GLU C 239           
SHEET    9   E 9 VAL C 357  VAL C 361  1  O  ALA C 359   N  THR C   6           
SHEET    1   F 7 ILE C 150  PHE C 156  0                                        
SHEET    2   F 7 ILE C 117  LYS C 122  1  N  ILE C 117   O  GLU C 151           
SHEET    3   F 7 ASP C  97  VAL C 100  1  N  VAL C 100   O  SER C 120           
SHEET    4   F 7 GLU C  76  CYS C  79  1  N  VAL C  77   O  ASP C  97           
SHEET    5   F 7 ALA C  56  VAL C  59  1  N  VAL C  59   O  LEU C  78           
SHEET    6   F 7 LYS C  28  VAL C  32  1  N  ALA C  31   O  ALA C  56           
SHEET    7   F 7 MET C 212  VAL C 213  1  O  VAL C 213   N  MET C  30           
SHEET    1   G 9 VAL D 244  GLN D 247  0                                        
SHEET    2   G 9 PHE D 267  VAL D 271 -1  O  VAL D 268   N  LYS D 246           
SHEET    3   G 9 PHE D 307  GLY D 312 -1  O  PHE D 307   N  VAL D 271           
SHEET    4   G 9 LEU D 294  VAL D 299 -1  N  PRO D 297   O  SER D 310           
SHEET    5   G 9 SER D 288  ILE D 291 -1  N  ILE D 291   O  LEU D 294           
SHEET    6   G 9 LYS D 323  PHE D 327 -1  O  VAL D 325   N  THR D 290           
SHEET    7   G 9 MET D 236  LYS D 241 -1  N  ALA D 240   O  ALA D 324           
SHEET    8   G 9 LEU D   4  ILE D   8 -1  N  LYS D   7   O  THR D 237           
SHEET    9   G 9 VAL D 357  TYR D 360  1  O  ALA D 359   N  THR D   6           
SHEET    1   H 7 ILE D 150  PHE D 156  0                                        
SHEET    2   H 7 ILE D 117  LYS D 122  1  N  ILE D 117   O  GLU D 151           
SHEET    3   H 7 ASP D  97  VAL D 100  1  N  VAL D 100   O  LYS D 122           
SHEET    4   H 7 GLU D  76  CYS D  79  1  N  VAL D  77   O  ASP D  97           
SHEET    5   H 7 ALA D  56  VAL D  59  1  N  VAL D  59   O  LEU D  78           
SHEET    6   H 7 LYS D  28  VAL D  32  1  N  ALA D  31   O  GLY D  58           
SHEET    7   H 7 MET D 212  VAL D 213  1  O  VAL D 213   N  MET D  30           
LINK         C4A PLP A 401                 NZ  LYS A  34     1555   1555  1.28  
LINK         C4A PLP B 401                 NZ  LYS B  34     1555   1555  1.29  
LINK         C4A PLP C 401                 NZ  LYS C  34     1555   1555  1.28  
LINK         C4A PLP D 401                 NZ  LYS D  34     1555   1555  1.28  
SITE     1 AC1 13 VAL A  32  LYS A  34  TYR A  38  TRP A  80                    
SITE     2 AC1 13 HIS A 158  ASN A 198  SER A 199  ARG A 214                    
SITE     3 AC1 13 GLY A 216  LEU A 217  TYR A 346  ASP B 305                    
SITE     4 AC1 13 HOH B 567                                                     
SITE     1 AC2 13 HOH A 556  VAL B  32  LYS B  34  TYR B  38                    
SITE     2 AC2 13 TRP B  80  HIS B 158  ASN B 198  SER B 199                    
SITE     3 AC2 13 ARG B 214  PRO B 215  GLY B 216  LEU B 217                    
SITE     4 AC2 13 TYR B 346                                                     
SITE     1 AC3 14 VAL C  32  LYS C  34  TYR C  38  TRP C  80                    
SITE     2 AC3 14 HIS C 158  ASN C 198  SER C 199  PRO C 200                    
SITE     3 AC3 14 ARG C 214  PRO C 215  GLY C 216  LEU C 217                    
SITE     4 AC3 14 TYR C 346  HOH C 535                                          
SITE     1 AC4 14 HOH C 536  VAL D  32  LYS D  34  TYR D  38                    
SITE     2 AC4 14 TRP D  80  HIS D 158  ASN D 198  SER D 199                    
SITE     3 AC4 14 ARG D 214  PRO D 215  GLY D 216  LEU D 217                    
SITE     4 AC4 14 TYR D 346  HOH D 463                                          
CRYST1   78.384  113.612   88.096  90.00  94.73  90.00 P 1 21 1      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      0.012758  0.000000  0.001056        0.00000                         
SCALE2      0.000000  0.008802  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011390        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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