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Database: PDB
Entry: 1XEY
LinkDB: 1XEY
Original site: 1XEY 
HEADER    LYASE                                   13-SEP-04   1XEY              
TITLE     CRYSTAL STRUCTURE OF THE COMPLEX OF ESCHERICHIA COLI GADA WITH        
TITLE    2 GLUTARATE AT 2.05 A RESOLUTION                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMATE DECARBOXYLASE ALPHA;                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: GAD-ALPHA;                                                  
COMPND   5 EC: 4.1.1.15;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: GADA;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGAD1                                     
KEYWDS    LYASE, GLUTAMATE DECARBOXYLASE, COMPLEX WITH GLUTARATE                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.I.DUTYSHEV,E.L.DARII,N.P.FOMENKOVA,I.V.PECHIK,K.M.POLYAKOV,         
AUTHOR   2 S.V.NIKONOV,N.S.ANDREEVA,B.S.SUKHAREVA                               
REVDAT   4   13-JUL-11 1XEY    1       VERSN                                    
REVDAT   3   24-FEB-09 1XEY    1       VERSN                                    
REVDAT   2   12-APR-05 1XEY    1       JRNL                                     
REVDAT   1   05-OCT-04 1XEY    0                                                
JRNL        AUTH   D.I.DUTYSHEV,E.L.DARII,N.P.FOMENKOVA,I.V.PECHIK,             
JRNL        AUTH 2 K.M.POLYAKOV,S.V.NIKONOV,N.S.ANDREEVA,B.S.SUKHAREVA          
JRNL        TITL   STRUCTURE OF ESCHERICHIA COLI GLUTAMATE DECARBOXYLASE        
JRNL        TITL 2 (GADALPHA) IN COMPLEX WITH GLUTARATE AT 2.05 ANGSTROMS       
JRNL        TITL 3 RESOLUTION.                                                  
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  61   230 2005              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   15735332                                                     
JRNL        DOI    10.1107/S0907444904032147                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 53367                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.151                           
REMARK   3   R VALUE            (WORKING SET) : 0.148                           
REMARK   3   FREE R VALUE                     : 0.199                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2857                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.05                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.10                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3738                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2660                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 225                          
REMARK   3   BIN FREE R VALUE                    : 0.3180                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7107                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 390                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.89000                                             
REMARK   3    B22 (A**2) : -0.89000                                             
REMARK   3    B33 (A**2) : 1.33000                                              
REMARK   3    B12 (A**2) : -0.44000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.183         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.162         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.108         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.085         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.967                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.944                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7357 ; 0.018 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9973 ; 1.446 ; 1.951       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   895 ; 5.940 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1039 ; 0.100 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5735 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2697 ; 0.202 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   301 ; 0.124 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    74 ; 0.228 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    19 ; 0.157 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4484 ; 0.862 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7176 ; 1.588 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2873 ; 2.640 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2797 ; 4.330 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1XEY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-SEP-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB030283.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-APR-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 4.60                               
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          : ELLIOTT GX-6                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 60197                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.270                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.9700                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.26000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.460                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1PMM                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PYRIDINE CHLORIDE, GLYCEROL,SODIUM       
REMARK 280  CHLORIDE, SODIUM ACETATE, PEG 3000, PH 4.60, VAPOR DIFFUSION,       
REMARK 280  HANGING DROP, TEMPERATURE 290K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       58.55000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       33.80386            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       65.46667            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       58.55000            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       33.80386            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       65.46667            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       58.55000            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       33.80386            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       65.46667            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       67.60772            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000      130.93333            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       67.60772            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000      130.93333            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       67.60772            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      130.93333            
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 52070 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 86240 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -178.0 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   BIOMT1   2 -0.500000 -0.866025  0.000000       58.55000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000      101.41157            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000      -58.55000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      101.41157            
REMARK 350   BIOMT3   3  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     ASP A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     PRO A   452                                                      
REMARK 465     LYS A   453                                                      
REMARK 465     LEU A   454                                                      
REMARK 465     GLN A   455                                                      
REMARK 465     GLY A   456                                                      
REMARK 465     ILE A   457                                                      
REMARK 465     ALA A   458                                                      
REMARK 465     GLN A   459                                                      
REMARK 465     GLN A   460                                                      
REMARK 465     ASN A   461                                                      
REMARK 465     SER A   462                                                      
REMARK 465     PHE A   463                                                      
REMARK 465     LYS A   464                                                      
REMARK 465     HIS A   465                                                      
REMARK 465     THR A   466                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     GLN B     3                                                      
REMARK 465     LYS B   453                                                      
REMARK 465     LEU B   454                                                      
REMARK 465     GLN B   455                                                      
REMARK 465     GLY B   456                                                      
REMARK 465     ILE B   457                                                      
REMARK 465     ALA B   458                                                      
REMARK 465     GLN B   459                                                      
REMARK 465     GLN B   460                                                      
REMARK 465     ASN B   461                                                      
REMARK 465     SER B   462                                                      
REMARK 465     PHE B   463                                                      
REMARK 465     LYS B   464                                                      
REMARK 465     HIS B   465                                                      
REMARK 465     THR B   466                                                      
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     LYS A   4    CG   CD   CE   NZ                                   
REMARK 470     LEU A   5    CG   CD1  CD2                                       
REMARK 470     LEU A   6    CG   CD1  CD2                                       
REMARK 470     PHE A   9    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B   4    CG   CD   CE   NZ                                   
REMARK 470     LEU B   5    CG   CD1  CD2                                       
REMARK 470     LEU B   6    CG   CD1  CD2                                       
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    ASP A 440   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP B  39   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP B 106   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 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    LEU A 187       38.90    -96.28                                   
REMARK 500    ALA A 244       40.59   -109.09                                   
REMARK 500    LEU A 250      -66.89   -120.34                                   
REMARK 500    ASP A 261     -144.48   -112.25                                   
REMARK 500    LYS A 276     -112.31    -90.95                                   
REMARK 500    LEU A 282      123.64    -35.91                                   
REMARK 500    PHE A 317     -104.39   -115.85                                   
REMARK 500    LEU B 187       36.41    -88.70                                   
REMARK 500    LEU B 250      -66.55   -120.37                                   
REMARK 500    ALA B 255       61.12   -153.79                                   
REMARK 500    ASP B 261     -145.76   -111.66                                   
REMARK 500    LYS B 276     -110.81    -93.41                                   
REMARK 500    PHE B 317     -103.17   -113.54                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ARG A 290        24.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GUA B 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GUA A 506                 
DBREF  1XEY A    1   466  UNP    P69908   DCEA_ECOLI       1    466             
DBREF  1XEY B    1   466  UNP    P69908   DCEA_ECOLI       1    466             
SEQRES   1 A  466  MET ASP GLN LYS LEU LEU THR ASP PHE ARG SER GLU LEU          
SEQRES   2 A  466  LEU ASP SER ARG PHE GLY ALA LYS ALA ILE SER THR ILE          
SEQRES   3 A  466  ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP          
SEQRES   4 A  466  ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU          
SEQRES   5 A  466  ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN          
SEQRES   6 A  466  THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU          
SEQRES   7 A  466  SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO          
SEQRES   8 A  466  GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL          
SEQRES   9 A  466  ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN          
SEQRES  10 A  466  ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS          
SEQRES  11 A  466  MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS          
SEQRES  12 A  466  ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN          
SEQRES  13 A  466  LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE          
SEQRES  14 A  466  ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET          
SEQRES  15 A  466  ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE          
SEQRES  16 A  466  GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR          
SEQRES  17 A  466  PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN          
SEQRES  18 A  466  PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR          
SEQRES  19 A  466  GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY          
SEQRES  20 A  466  GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP          
SEQRES  21 A  466  ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER          
SEQRES  22 A  466  GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP          
SEQRES  23 A  466  VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU          
SEQRES  24 A  466  VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR          
SEQRES  25 A  466  PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE          
SEQRES  26 A  466  ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY          
SEQRES  27 A  466  TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA          
SEQRES  28 A  466  TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU          
SEQRES  29 A  466  PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA          
SEQRES  30 A  466  VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR          
SEQRES  31 A  466  THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY          
SEQRES  32 A  466  TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR          
SEQRES  33 A  466  ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE          
SEQRES  34 A  466  GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS          
SEQRES  35 A  466  ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN          
SEQRES  36 A  466  GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR                  
SEQRES   1 B  466  MET ASP GLN LYS LEU LEU THR ASP PHE ARG SER GLU LEU          
SEQRES   2 B  466  LEU ASP SER ARG PHE GLY ALA LYS ALA ILE SER THR ILE          
SEQRES   3 B  466  ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP          
SEQRES   4 B  466  ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU          
SEQRES   5 B  466  ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN          
SEQRES   6 B  466  THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU          
SEQRES   7 B  466  SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO          
SEQRES   8 B  466  GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL          
SEQRES   9 B  466  ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN          
SEQRES  10 B  466  ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS          
SEQRES  11 B  466  MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS          
SEQRES  12 B  466  ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN          
SEQRES  13 B  466  LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE          
SEQRES  14 B  466  ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET          
SEQRES  15 B  466  ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE          
SEQRES  16 B  466  GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR          
SEQRES  17 B  466  PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN          
SEQRES  18 B  466  PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR          
SEQRES  19 B  466  GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY          
SEQRES  20 B  466  GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP          
SEQRES  21 B  466  ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER          
SEQRES  22 B  466  GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP          
SEQRES  23 B  466  VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU          
SEQRES  24 B  466  VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR          
SEQRES  25 B  466  PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE          
SEQRES  26 B  466  ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY          
SEQRES  27 B  466  TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA          
SEQRES  28 B  466  TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU          
SEQRES  29 B  466  PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA          
SEQRES  30 B  466  VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR          
SEQRES  31 B  466  THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY          
SEQRES  32 B  466  TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR          
SEQRES  33 B  466  ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE          
SEQRES  34 B  466  GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS          
SEQRES  35 B  466  ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN          
SEQRES  36 B  466  GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR                  
HET    ACT  A 600       4                                                       
HET    ACT  A 700       4                                                       
HET    PLP  A 500      15                                                       
HET    PLP  B 500      15                                                       
HET    GUA  B 505      15                                                       
HET    GUA  A 506      15                                                       
HETNAM     ACT ACETATE ION                                                      
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETNAM     GUA GLUTARIC ACID                                                    
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
FORMUL   3  ACT    2(C2 H3 O2 1-)                                               
FORMUL   5  PLP    2(C8 H10 N O6 P)                                             
FORMUL   7  GUA    2(C5 H8 O4)                                                  
FORMUL   9  HOH   *390(H2 O)                                                    
HELIX    1   1 LEU A    5  ASP A   15  1                                  11    
HELIX    2   2 ALA A   20  THR A   25  5                                   6    
HELIX    3   3 ARG A   38  LEU A   50  1                                  13    
HELIX    4   4 TYR A   51  GLY A   54  5                                   4    
HELIX    5   5 ASN A   55  ASN A   59  5                                   5    
HELIX    6   6 ASP A   69  SER A   79  1                                  11    
HELIX    7   7 TYR A   90  TRP A  108  1                                  19    
HELIX    8   8 GLY A  125  ALA A  148  1                                  24    
HELIX    9   9 ILE A  164  TRP A  173  1                                  10    
HELIX   10  10 ASP A  190  CYS A  198  1                                   9    
HELIX   11  11 PHE A  219  GLY A  235  1                                  17    
HELIX   12  12 SER A  246  PHE A  249  5                                   4    
HELIX   13  13 LEU A  250  ALA A  255  1                                   6    
HELIX   14  14 ASP A  291  LEU A  295  5                                   5    
HELIX   15  15 PRO A  296  VAL A  300  5                                   5    
HELIX   16  16 ALA A  321  ALA A  358  1                                  38    
HELIX   17  17 THR A  391  LEU A  401  1                                  11    
HELIX   18  18 GLY A  412  THR A  416  5                                   5    
HELIX   19  19 GLU A  430  ASP A  450  1                                  21    
HELIX   20  20 LYS B    4  ASP B   15  1                                  12    
HELIX   21  21 ALA B   20  THR B   25  5                                   6    
HELIX   22  22 ARG B   38  LEU B   50  1                                  13    
HELIX   23  23 TYR B   51  GLY B   54  5                                   4    
HELIX   24  24 ASN B   55  ASN B   59  5                                   5    
HELIX   25  25 ASP B   69  SER B   79  1                                  11    
HELIX   26  26 TYR B   90  TRP B  108  1                                  19    
HELIX   27  27 GLY B  125  ALA B  148  1                                  24    
HELIX   28  28 ILE B  164  TRP B  173  1                                  10    
HELIX   29  29 ASP B  190  CYS B  198  1                                   9    
HELIX   30  30 PHE B  219  GLY B  235  1                                  17    
HELIX   31  31 SER B  246  PHE B  249  5                                   4    
HELIX   32  32 LEU B  250  ALA B  255  1                                   6    
HELIX   33  33 ASP B  291  LEU B  295  5                                   5    
HELIX   34  34 PRO B  296  VAL B  300  5                                   5    
HELIX   35  35 ALA B  321  LYS B  359  1                                  39    
HELIX   36  36 THR B  391  LEU B  401  1                                  11    
HELIX   37  37 GLU B  430  HIS B  451  1                                  22    
SHEET    1   A 4 GLY A 120  THR A 123  0                                        
SHEET    2   A 4 GLY A 285  TRP A 289 -1  O  GLY A 285   N  THR A 123           
SHEET    3   A 4 VAL A 267  SER A 273 -1  N  ILE A 270   O  ILE A 288           
SHEET    4   A 4 MET A 240  ASP A 243  1  N  ILE A 242   O  SER A 271           
SHEET    1   B 3 GLU A 176  GLU A 179  0                                        
SHEET    2   B 3 ASN A 156  CYS A 159  1  N  LEU A 157   O  ARG A 178           
SHEET    3   B 3 THR A 202  VAL A 206  1  O  ILE A 203   N  ASN A 156           
SHEET    1   C 2 PHE A 301  TYR A 305  0                                        
SHEET    2   C 2 GLY A 308  THR A 312 -1  O  THR A 312   N  PHE A 301           
SHEET    1   D 4 TYR A 363  THR A 368  0                                        
SHEET    2   D 4 ALA A 377  LEU A 382 -1  O  CYS A 379   N  ILE A 366           
SHEET    3   D 4 VAL A 419  MET A 424 -1  O  ILE A 423   N  VAL A 378           
SHEET    4   D 4 ALA A 408  THR A 410 -1  N  PHE A 409   O  VAL A 420           
SHEET    1   E 4 GLY B 120  THR B 123  0                                        
SHEET    2   E 4 GLY B 285  TRP B 289 -1  O  GLY B 285   N  THR B 123           
SHEET    3   E 4 VAL B 267  SER B 273 -1  N  ALA B 272   O  TRP B 286           
SHEET    4   E 4 MET B 240  ASP B 243  1  N  ILE B 242   O  SER B 269           
SHEET    1   F 3 GLU B 176  GLU B 179  0                                        
SHEET    2   F 3 ASN B 156  CYS B 159  1  N  LEU B 157   O  ARG B 178           
SHEET    3   F 3 THR B 202  VAL B 206  1  O  ILE B 203   N  ASN B 156           
SHEET    1   G 2 PHE B 301  TYR B 305  0                                        
SHEET    2   G 2 GLY B 308  THR B 312 -1  O  GLY B 308   N  TYR B 305           
SHEET    1   H 4 TYR B 363  CYS B 367  0                                        
SHEET    2   H 4 ALA B 377  LEU B 382 -1  O  CYS B 379   N  ILE B 366           
SHEET    3   H 4 VAL B 419  MET B 424 -1  O  ILE B 423   N  VAL B 378           
SHEET    4   H 4 ALA B 408  THR B 410 -1  N  PHE B 409   O  VAL B 420           
LINK         NZ  LYS A 276                 C4A PLP A 500     1555   1555  1.34  
LINK         NZ  LYS B 276                 C4A PLP B 500     1555   1555  1.32  
SITE     1 AC1  7 LEU A 279  LEU A 334  VAL A 342  ARG A 427                    
SITE     2 AC1  7 HOH A 859  SER B  16  HOH B 858                               
SITE     1 AC2  7 SER A  16  ARG A  17  PHE A  18  HOH A 714                    
SITE     2 AC2  7 TRP B  67  VAL B 342  ARG B 427                               
SITE     1 AC3 17 SER A 126  SER A 127  GLN A 163  CYS A 165                    
SITE     2 AC3 17 THR A 208  THR A 212  ASP A 243  ALA A 245                    
SITE     3 AC3 17 SER A 273  HIS A 275  LYS A 276  HOH A 738                    
SITE     4 AC3 17 HOH A 784  PHE B 317  SER B 318  GUA B 505                    
SITE     5 AC3 17 HOH B 959                                                     
SITE     1 AC4 17 PHE A 317  SER A 318  GUA A 506  GLY B 125                    
SITE     2 AC4 17 SER B 126  SER B 127  GLN B 163  CYS B 165                    
SITE     3 AC4 17 THR B 208  THR B 212  ASP B 243  ALA B 245                    
SITE     4 AC4 17 SER B 273  HIS B 275  LYS B 276  HOH B 826                    
SITE     5 AC4 17 HOH B 879                                                     
SITE     1 AC5 11 THR A  62  PHE A  63  GLN A 163  LYS A 276                    
SITE     2 AC5 11 ARG A 422  PLP A 500  ASN B  83  ASP B  86                    
SITE     3 AC5 11 GLU B  89  HOH B 959  HOH B1074                               
SITE     1 AC6  8 ASN A  83  ASP A  86  GLU A  89  THR B  62                    
SITE     2 AC6  8 PHE B  63  GLN B 163  LYS B 276  PLP B 500                    
CRYST1  117.100  117.100  196.400  90.00  90.00 120.00 H 3          18          
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      0.008540  0.004930  0.000000        0.00000                         
SCALE2      0.000000  0.009861  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005092        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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