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Database: PDB
Entry: 1PMM
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Original site: 1PMM 
HEADER    LYASE                                   11-JUN-03   1PMM              
TITLE     CRYSTAL STRUCTURE OF ESCHERICHIA COLI GADB (LOW PH)                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMATE DECARBOXYLASE BETA;                              
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 SYNONYM: GAD-BETA;                                                   
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: GADB;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: JM109;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PQE60                                     
KEYWDS    LOW-PH FORM OF GADB, LYASE                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.CAPITANI,D.DE BIASE,C.AURIZI,H.GUT,F.BOSSA,M.G.GRUTTER              
REVDAT   3   13-JUL-11 1PMM    1       VERSN                                    
REVDAT   2   24-FEB-09 1PMM    1       VERSN                                    
REVDAT   1   17-FEB-04 1PMM    0                                                
JRNL        AUTH   G.CAPITANI,D.DE BIASE,C.AURIZI,H.GUT,F.BOSSA,M.G.GRUTTER     
JRNL        TITL   CRYSTAL STRUCTURE AND FUNCTIONAL ANALYSIS OF ESCHERICHIA     
JRNL        TITL 2 COLI GLUTAMATE DECARBOXYLASE                                 
JRNL        REF    EMBO J.                       V.  22  4027 2003              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   12912902                                                     
JRNL        DOI    10.1093/EMBOJ/CDG403                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.62                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 178480                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.213                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 5238                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.03                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2250                       
REMARK   3   BIN FREE R VALUE                    : 0.1870                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 148                          
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            : 21444                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 114                                     
REMARK   3   SOLVENT ATOMS            : 1842                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.37700                                              
REMARK   3    B22 (A**2) : -0.37600                                             
REMARK   3    B33 (A**2) : -0.12400                                             
REMARK   3    B12 (A**2) : 0.50600                                              
REMARK   3    B13 (A**2) : -0.25300                                             
REMARK   3    B23 (A**2) : -0.34900                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.20                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.08                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.24                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.14                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.23                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.75                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
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 1PMM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUN-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB019428.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-MAR-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 90                                 
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9184                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : DYNAMICALLY BENDABLE MIRROR        
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
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   : 178481                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.620                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY                : 2.600                              
REMARK 200  R MERGE                    (I) : 0.08700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.16200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM FORMATE, SODIUM ACETATE, PEG      
REMARK 280  4000, PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HEXAMER                         
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                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 48750 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 86180 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -209.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ASP A     2                                                      
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     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 465     MET C     1                                                      
REMARK 465     ASP C     2                                                      
REMARK 465     LYS C     3                                                      
REMARK 465     LYS C   453                                                      
REMARK 465     LEU C   454                                                      
REMARK 465     GLN C   455                                                      
REMARK 465     GLY C   456                                                      
REMARK 465     ILE C   457                                                      
REMARK 465     ALA C   458                                                      
REMARK 465     GLN C   459                                                      
REMARK 465     GLN C   460                                                      
REMARK 465     ASN C   461                                                      
REMARK 465     SER C   462                                                      
REMARK 465     PHE C   463                                                      
REMARK 465     LYS C   464                                                      
REMARK 465     HIS C   465                                                      
REMARK 465     THR C   466                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ASP D     2                                                      
REMARK 465     LYS D   453                                                      
REMARK 465     LEU D   454                                                      
REMARK 465     GLN D   455                                                      
REMARK 465     GLY D   456                                                      
REMARK 465     ILE D   457                                                      
REMARK 465     ALA D   458                                                      
REMARK 465     GLN D   459                                                      
REMARK 465     GLN D   460                                                      
REMARK 465     ASN D   461                                                      
REMARK 465     SER D   462                                                      
REMARK 465     PHE D   463                                                      
REMARK 465     LYS D   464                                                      
REMARK 465     HIS D   465                                                      
REMARK 465     THR D   466                                                      
REMARK 465     MET E     1                                                      
REMARK 465     ASP E     2                                                      
REMARK 465     LYS E     3                                                      
REMARK 465     LYS E   453                                                      
REMARK 465     LEU E   454                                                      
REMARK 465     GLN E   455                                                      
REMARK 465     GLY E   456                                                      
REMARK 465     ILE E   457                                                      
REMARK 465     ALA E   458                                                      
REMARK 465     GLN E   459                                                      
REMARK 465     GLN E   460                                                      
REMARK 465     ASN E   461                                                      
REMARK 465     SER E   462                                                      
REMARK 465     PHE E   463                                                      
REMARK 465     LYS E   464                                                      
REMARK 465     HIS E   465                                                      
REMARK 465     THR E   466                                                      
REMARK 465     MET F     1                                                      
REMARK 465     ASP F     2                                                      
REMARK 465     LYS F   453                                                      
REMARK 465     LEU F   454                                                      
REMARK 465     GLN F   455                                                      
REMARK 465     GLY F   456                                                      
REMARK 465     ILE F   457                                                      
REMARK 465     ALA F   458                                                      
REMARK 465     GLN F   459                                                      
REMARK 465     GLN F   460                                                      
REMARK 465     ASN F   461                                                      
REMARK 465     SER F   462                                                      
REMARK 465     PHE F   463                                                      
REMARK 465     LYS F   464                                                      
REMARK 465     HIS F   465                                                      
REMARK 465     THR F   466                                                      
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    ALA A 244       42.50   -107.37                                   
REMARK 500    LEU A 250      -62.56   -121.84                                   
REMARK 500    ALA A 255       58.03   -150.71                                   
REMARK 500    ASP A 261     -147.02    -98.39                                   
REMARK 500    LYS A 276     -114.14   -102.21                                   
REMARK 500    TYR A 305      111.06   -160.41                                   
REMARK 500    PHE A 317      -99.20   -116.47                                   
REMARK 500    SER B  29       -0.94   -141.88                                   
REMARK 500    GLN B 186       77.30   -154.32                                   
REMARK 500    LEU B 187       41.68    -88.93                                   
REMARK 500    ALA B 244       40.78   -106.56                                   
REMARK 500    LEU B 250      -66.50   -124.07                                   
REMARK 500    ALA B 255       60.07   -151.03                                   
REMARK 500    ASP B 261     -144.23   -102.36                                   
REMARK 500    LYS B 276     -115.18   -101.68                                   
REMARK 500    PHE B 317      -99.30   -119.20                                   
REMARK 500    PHE B 429       64.39   -119.11                                   
REMARK 500    SER C  29       -1.92   -142.62                                   
REMARK 500    LEU C 187       48.83    -89.00                                   
REMARK 500    LEU C 250      -64.96   -120.94                                   
REMARK 500    ASP C 261     -144.96    -97.50                                   
REMARK 500    LYS C 276     -111.94   -100.03                                   
REMARK 500    PHE C 317     -101.23   -116.01                                   
REMARK 500    PHE C 429       69.26   -111.45                                   
REMARK 500    LEU D 187       42.12    -87.60                                   
REMARK 500    ALA D 244       40.69   -104.75                                   
REMARK 500    LEU D 250      -66.27   -125.76                                   
REMARK 500    ALA D 255       59.13   -148.90                                   
REMARK 500    ASP D 261     -143.17   -100.56                                   
REMARK 500    LYS D 276     -113.52    -98.84                                   
REMARK 500    TYR D 305      107.51   -163.86                                   
REMARK 500    PHE D 317      -97.68   -117.63                                   
REMARK 500    HIS D 451       63.97   -151.12                                   
REMARK 500    SER E  29       -4.43   -142.40                                   
REMARK 500    LEU E 187       44.61    -84.49                                   
REMARK 500    ALA E 255       60.42   -154.38                                   
REMARK 500    ASP E 261     -145.45    -95.82                                   
REMARK 500    LYS E 276     -111.33   -100.67                                   
REMARK 500    PHE E 317      -98.79   -117.25                                   
REMARK 500    PHE E 429       66.77   -118.17                                   
REMARK 500    LEU F 187       46.57    -86.56                                   
REMARK 500    LEU F 250      -65.02   -123.07                                   
REMARK 500    ASP F 261     -147.06   -101.59                                   
REMARK 500    LYS F 276     -115.51    -99.69                                   
REMARK 500    PHE F 317      -99.84   -119.70                                   
REMARK 500    PHE F 429       68.68   -117.07                                   
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 A5675        DISTANCE =  5.77 ANGSTROMS                       
REMARK 525    HOH A5730        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH B6817        DISTANCE =  5.09 ANGSTROMS                       
REMARK 525    HOH C8766        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH D7759        DISTANCE =  5.67 ANGSTROMS                       
REMARK 525    HOH D7811        DISTANCE =  5.16 ANGSTROMS                       
REMARK 525    HOH D7837        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH D7848        DISTANCE =  5.32 ANGSTROMS                       
REMARK 525    HOH E9716        DISTANCE =  5.61 ANGSTROMS                       
REMARK 525    HOH F 699        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH F 775        DISTANCE =  5.09 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 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP E 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP F 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 5518                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY B 6518                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY D 7518                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY C 8518                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY E 9518                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY E 9519                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1PMO   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN AT NEUTRAL PH                                       
DBREF  1PMM A    1   466  UNP    P69910   DCEB_ECOLI       1    466             
DBREF  1PMM B    1   466  UNP    P69910   DCEB_ECOLI       1    466             
DBREF  1PMM C    1   466  UNP    P69910   DCEB_ECOLI       1    466             
DBREF  1PMM D    1   466  UNP    P69910   DCEB_ECOLI       1    466             
DBREF  1PMM E    1   466  UNP    P69910   DCEB_ECOLI       1    466             
DBREF  1PMM F    1   466  UNP    P69910   DCEB_ECOLI       1    466             
SEQRES   1 A  466  MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU          
SEQRES   2 A  466  LEU ASP SER ARG PHE GLY ALA LYS SER 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 LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU          
SEQRES   2 B  466  LEU ASP SER ARG PHE GLY ALA LYS SER 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                  
SEQRES   1 C  466  MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU          
SEQRES   2 C  466  LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE          
SEQRES   3 C  466  ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP          
SEQRES   4 C  466  ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU          
SEQRES   5 C  466  ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN          
SEQRES   6 C  466  THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU          
SEQRES   7 C  466  SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO          
SEQRES   8 C  466  GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL          
SEQRES   9 C  466  ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN          
SEQRES  10 C  466  ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS          
SEQRES  11 C  466  MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS          
SEQRES  12 C  466  ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN          
SEQRES  13 C  466  LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE          
SEQRES  14 C  466  ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET          
SEQRES  15 C  466  ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE          
SEQRES  16 C  466  GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR          
SEQRES  17 C  466  PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN          
SEQRES  18 C  466  PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR          
SEQRES  19 C  466  GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY          
SEQRES  20 C  466  GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP          
SEQRES  21 C  466  ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER          
SEQRES  22 C  466  GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP          
SEQRES  23 C  466  VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU          
SEQRES  24 C  466  VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR          
SEQRES  25 C  466  PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE          
SEQRES  26 C  466  ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY          
SEQRES  27 C  466  TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA          
SEQRES  28 C  466  TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU          
SEQRES  29 C  466  PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA          
SEQRES  30 C  466  VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR          
SEQRES  31 C  466  THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY          
SEQRES  32 C  466  TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR          
SEQRES  33 C  466  ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE          
SEQRES  34 C  466  GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS          
SEQRES  35 C  466  ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN          
SEQRES  36 C  466  GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR                  
SEQRES   1 D  466  MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU          
SEQRES   2 D  466  LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE          
SEQRES   3 D  466  ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP          
SEQRES   4 D  466  ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU          
SEQRES   5 D  466  ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN          
SEQRES   6 D  466  THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU          
SEQRES   7 D  466  SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO          
SEQRES   8 D  466  GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL          
SEQRES   9 D  466  ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN          
SEQRES  10 D  466  ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS          
SEQRES  11 D  466  MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS          
SEQRES  12 D  466  ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN          
SEQRES  13 D  466  LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE          
SEQRES  14 D  466  ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET          
SEQRES  15 D  466  ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE          
SEQRES  16 D  466  GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR          
SEQRES  17 D  466  PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN          
SEQRES  18 D  466  PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR          
SEQRES  19 D  466  GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY          
SEQRES  20 D  466  GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP          
SEQRES  21 D  466  ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER          
SEQRES  22 D  466  GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP          
SEQRES  23 D  466  VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU          
SEQRES  24 D  466  VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR          
SEQRES  25 D  466  PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE          
SEQRES  26 D  466  ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY          
SEQRES  27 D  466  TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA          
SEQRES  28 D  466  TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU          
SEQRES  29 D  466  PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA          
SEQRES  30 D  466  VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR          
SEQRES  31 D  466  THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY          
SEQRES  32 D  466  TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR          
SEQRES  33 D  466  ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE          
SEQRES  34 D  466  GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS          
SEQRES  35 D  466  ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN          
SEQRES  36 D  466  GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR                  
SEQRES   1 E  466  MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU          
SEQRES   2 E  466  LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE          
SEQRES   3 E  466  ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP          
SEQRES   4 E  466  ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU          
SEQRES   5 E  466  ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN          
SEQRES   6 E  466  THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU          
SEQRES   7 E  466  SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO          
SEQRES   8 E  466  GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL          
SEQRES   9 E  466  ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN          
SEQRES  10 E  466  ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS          
SEQRES  11 E  466  MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS          
SEQRES  12 E  466  ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN          
SEQRES  13 E  466  LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE          
SEQRES  14 E  466  ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET          
SEQRES  15 E  466  ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE          
SEQRES  16 E  466  GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR          
SEQRES  17 E  466  PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN          
SEQRES  18 E  466  PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR          
SEQRES  19 E  466  GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY          
SEQRES  20 E  466  GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP          
SEQRES  21 E  466  ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER          
SEQRES  22 E  466  GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP          
SEQRES  23 E  466  VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU          
SEQRES  24 E  466  VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR          
SEQRES  25 E  466  PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE          
SEQRES  26 E  466  ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY          
SEQRES  27 E  466  TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA          
SEQRES  28 E  466  TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU          
SEQRES  29 E  466  PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA          
SEQRES  30 E  466  VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR          
SEQRES  31 E  466  THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY          
SEQRES  32 E  466  TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR          
SEQRES  33 E  466  ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE          
SEQRES  34 E  466  GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS          
SEQRES  35 E  466  ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN          
SEQRES  36 E  466  GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR                  
SEQRES   1 F  466  MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU          
SEQRES   2 F  466  LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE          
SEQRES   3 F  466  ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP          
SEQRES   4 F  466  ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU          
SEQRES   5 F  466  ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN          
SEQRES   6 F  466  THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU          
SEQRES   7 F  466  SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO          
SEQRES   8 F  466  GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL          
SEQRES   9 F  466  ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN          
SEQRES  10 F  466  ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS          
SEQRES  11 F  466  MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS          
SEQRES  12 F  466  ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN          
SEQRES  13 F  466  LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE          
SEQRES  14 F  466  ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET          
SEQRES  15 F  466  ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE          
SEQRES  16 F  466  GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR          
SEQRES  17 F  466  PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN          
SEQRES  18 F  466  PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR          
SEQRES  19 F  466  GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY          
SEQRES  20 F  466  GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP          
SEQRES  21 F  466  ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER          
SEQRES  22 F  466  GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP          
SEQRES  23 F  466  VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU          
SEQRES  24 F  466  VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR          
SEQRES  25 F  466  PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE          
SEQRES  26 F  466  ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY          
SEQRES  27 F  466  TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA          
SEQRES  28 F  466  TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU          
SEQRES  29 F  466  PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA          
SEQRES  30 F  466  VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR          
SEQRES  31 F  466  THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY          
SEQRES  32 F  466  TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR          
SEQRES  33 F  466  ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE          
SEQRES  34 F  466  GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS          
SEQRES  35 F  466  ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN          
SEQRES  36 F  466  GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR                  
HET    PLP  A 500      15                                                       
HET    PLP  B 500      15                                                       
HET    PLP  C 501      15                                                       
HET    PLP  D 501      15                                                       
HET    PLP  E 502      15                                                       
HET    PLP  F 502      15                                                       
HET    ACY  A5518       4                                                       
HET    ACY  B6518       4                                                       
HET    ACY  D7518       4                                                       
HET    ACY  C8518       4                                                       
HET    ACY  E9518       4                                                       
HET    ACY  E9519       4                                                       
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETNAM     ACY ACETIC ACID                                                      
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
FORMUL   7  PLP    6(C8 H10 N O6 P)                                             
FORMUL  13  ACY    6(C2 H4 O2)                                                  
FORMUL  19  HOH   *1842(H2 O)                                                   
HELIX    1   1 LYS A    3  ASP A   15  1                                  13    
HELIX    2   2 ALA A   20  SER A   24  5                                   5    
HELIX    3   3 ARG A   38  LEU A   50  1                                  13    
HELIX    4   4 TYR A   51  ASP A   53  5                                   3    
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  GLY A  149  1                                  25    
HELIX    9   9 GLN A  163  TRP A  173  1                                  11    
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  LYS A  359  1                                  39    
HELIX   17  17 THR A  391  LEU A  401  1                                  11    
HELIX   18  18 GLU A  430  HIS A  451  1                                  22    
HELIX   19  19 LYS B    3  ASP B   15  1                                  13    
HELIX   20  20 ALA B   20  SER B   24  5                                   5    
HELIX   21  21 ARG B   38  LEU B   50  1                                  13    
HELIX   22  22 TYR B   51  ASP B   53  5                                   3    
HELIX   23  23 ASN B   55  ASN B   59  5                                   5    
HELIX   24  24 ASP B   69  SER B   79  1                                  11    
HELIX   25  25 TYR B   90  TRP B  108  1                                  19    
HELIX   26  26 GLY B  125  ALA B  147  1                                  23    
HELIX   27  27 ILE B  164  TRP B  173  1                                  10    
HELIX   28  28 ASP B  190  CYS B  198  1                                   9    
HELIX   29  29 PHE B  219  GLY B  235  1                                  17    
HELIX   30  30 SER B  246  PHE B  249  5                                   4    
HELIX   31  31 LEU B  250  ALA B  255  1                                   6    
HELIX   32  32 ASP B  291  LEU B  295  5                                   5    
HELIX   33  33 PRO B  296  VAL B  300  5                                   5    
HELIX   34  34 ALA B  321  LYS B  359  1                                  39    
HELIX   35  35 THR B  391  LEU B  401  1                                  11    
HELIX   36  36 GLU B  430  HIS B  451  1                                  22    
HELIX   37  37 LYS C    4  ASP C   15  1                                  12    
HELIX   38  38 ALA C   20  SER C   24  5                                   5    
HELIX   39  39 ARG C   38  LEU C   50  1                                  13    
HELIX   40  40 TYR C   51  ASP C   53  5                                   3    
HELIX   41  41 ASN C   55  ASN C   59  5                                   5    
HELIX   42  42 ASP C   69  SER C   79  1                                  11    
HELIX   43  43 TYR C   90  TRP C  108  1                                  19    
HELIX   44  44 GLY C  125  GLY C  149  1                                  25    
HELIX   45  45 ILE C  164  TRP C  173  1                                  10    
HELIX   46  46 ASP C  190  CYS C  198  1                                   9    
HELIX   47  47 PHE C  219  GLY C  235  1                                  17    
HELIX   48  48 SER C  246  PHE C  249  5                                   4    
HELIX   49  49 LEU C  250  ALA C  255  1                                   6    
HELIX   50  50 ASP C  291  LEU C  295  5                                   5    
HELIX   51  51 PRO C  296  VAL C  300  5                                   5    
HELIX   52  52 ALA C  321  LYS C  359  1                                  39    
HELIX   53  53 THR C  391  LEU C  401  1                                  11    
HELIX   54  54 GLY C  412  THR C  416  5                                   5    
HELIX   55  55 GLU C  430  HIS C  451  1                                  22    
HELIX   56  56 LYS D    3  ASP D   15  1                                  13    
HELIX   57  57 ALA D   20  SER D   24  5                                   5    
HELIX   58  58 ARG D   38  LEU D   50  1                                  13    
HELIX   59  59 TYR D   51  ASP D   53  5                                   3    
HELIX   60  60 ASN D   55  ASN D   59  5                                   5    
HELIX   61  61 ASP D   69  SER D   79  1                                  11    
HELIX   62  62 TYR D   90  TRP D  108  1                                  19    
HELIX   63  63 GLY D  125  ALA D  148  1                                  24    
HELIX   64  64 ILE D  164  TRP D  173  1                                  10    
HELIX   65  65 ASP D  190  CYS D  198  1                                   9    
HELIX   66  66 PHE D  219  GLY D  235  1                                  17    
HELIX   67  67 SER D  246  PHE D  249  5                                   4    
HELIX   68  68 LEU D  250  ALA D  255  1                                   6    
HELIX   69  69 ASP D  291  LEU D  295  5                                   5    
HELIX   70  70 PRO D  296  VAL D  300  5                                   5    
HELIX   71  71 ALA D  321  LYS D  359  1                                  39    
HELIX   72  72 THR D  391  LEU D  401  1                                  11    
HELIX   73  73 GLY D  412  THR D  416  5                                   5    
HELIX   74  74 GLU D  430  ASP D  450  1                                  21    
HELIX   75  75 LYS E    4  ASP E   15  1                                  12    
HELIX   76  76 ALA E   20  SER E   24  5                                   5    
HELIX   77  77 ARG E   38  LEU E   50  1                                  13    
HELIX   78  78 TYR E   51  ASP E   53  5                                   3    
HELIX   79  79 ASN E   55  ASN E   59  5                                   5    
HELIX   80  80 ASP E   69  SER E   79  1                                  11    
HELIX   81  81 TYR E   90  TRP E  108  1                                  19    
HELIX   82  82 GLY E  125  GLY E  149  1                                  25    
HELIX   83  83 ILE E  164  TRP E  173  1                                  10    
HELIX   84  84 ASP E  190  CYS E  198  1                                   9    
HELIX   85  85 PHE E  219  GLY E  235  1                                  17    
HELIX   86  86 SER E  246  PHE E  249  5                                   4    
HELIX   87  87 LEU E  250  ALA E  255  1                                   6    
HELIX   88  88 ASP E  291  LEU E  295  5                                   5    
HELIX   89  89 PRO E  296  VAL E  300  5                                   5    
HELIX   90  90 ALA E  321  LYS E  359  1                                  39    
HELIX   91  91 THR E  391  LEU E  401  1                                  11    
HELIX   92  92 GLY E  412  THR E  416  5                                   5    
HELIX   93  93 GLU E  430  ASP E  450  1                                  21    
HELIX   94  94 LYS F    3  ASP F   15  1                                  13    
HELIX   95  95 ALA F   20  SER F   24  5                                   5    
HELIX   96  96 ARG F   38  LEU F   50  1                                  13    
HELIX   97  97 TYR F   51  ASP F   53  5                                   3    
HELIX   98  98 ASN F   55  ASN F   59  5                                   5    
HELIX   99  99 ASP F   69  ILE F   80  1                                  12    
HELIX  100 100 TYR F   90  TRP F  108  1                                  19    
HELIX  101 101 GLY F  125  ALA F  148  1                                  24    
HELIX  102 102 ILE F  164  TRP F  173  1                                  10    
HELIX  103 103 ASP F  190  CYS F  198  1                                   9    
HELIX  104 104 PHE F  219  GLY F  235  1                                  17    
HELIX  105 105 SER F  246  PHE F  249  5                                   4    
HELIX  106 106 LEU F  250  ALA F  255  1                                   6    
HELIX  107 107 ASP F  291  LEU F  295  5                                   5    
HELIX  108 108 PRO F  296  VAL F  300  5                                   5    
HELIX  109 109 ALA F  321  LYS F  359  1                                  39    
HELIX  110 110 THR F  391  ARG F  400  1                                  10    
HELIX  111 111 LEU F  401  GLY F  403  5                                   3    
HELIX  112 112 GLY F  412  THR F  416  5                                   5    
HELIX  113 113 GLU F  430  HIS F  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  ALA A 272   O  TRP A 286           
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  LYS A 381   N  GLU A 364           
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 271           
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  THR B 312   N  PHE B 301           
SHEET    1   H 4 TYR B 363  THR B 368  0                                        
SHEET    2   H 4 ALA B 377  LEU B 382 -1  O  LYS B 381   N  GLU B 364           
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           
SHEET    1   I 4 GLY C 120  THR C 123  0                                        
SHEET    2   I 4 GLY C 285  TRP C 289 -1  O  GLY C 285   N  THR C 123           
SHEET    3   I 4 VAL C 267  SER C 273 -1  N  ALA C 272   O  TRP C 286           
SHEET    4   I 4 MET C 240  ASP C 243  1  N  ILE C 242   O  SER C 271           
SHEET    1   J 3 GLU C 176  GLU C 179  0                                        
SHEET    2   J 3 ASN C 156  CYS C 159  1  N  LEU C 157   O  ARG C 178           
SHEET    3   J 3 THR C 202  VAL C 206  1  O  ILE C 203   N  ASN C 156           
SHEET    1   K 2 PHE C 301  TYR C 305  0                                        
SHEET    2   K 2 GLY C 308  THR C 312 -1  O  THR C 312   N  PHE C 301           
SHEET    1   L 4 TYR C 363  THR C 368  0                                        
SHEET    2   L 4 ALA C 377  LEU C 382 -1  O  LYS C 381   N  GLU C 364           
SHEET    3   L 4 VAL C 419  MET C 424 -1  O  ILE C 423   N  VAL C 378           
SHEET    4   L 4 ALA C 408  THR C 410 -1  N  PHE C 409   O  VAL C 420           
SHEET    1   M 4 GLY D 120  THR D 123  0                                        
SHEET    2   M 4 GLY D 285  TRP D 289 -1  O  GLY D 285   N  THR D 123           
SHEET    3   M 4 VAL D 267  SER D 273 -1  N  ALA D 272   O  TRP D 286           
SHEET    4   M 4 MET D 240  ASP D 243  1  N  ILE D 242   O  SER D 271           
SHEET    1   N 3 GLU D 176  GLU D 179  0                                        
SHEET    2   N 3 ASN D 156  CYS D 159  1  N  LEU D 157   O  ARG D 178           
SHEET    3   N 3 THR D 202  VAL D 206  1  O  ILE D 203   N  ASN D 156           
SHEET    1   O 2 PHE D 301  TYR D 305  0                                        
SHEET    2   O 2 GLY D 308  THR D 312 -1  O  THR D 312   N  PHE D 301           
SHEET    1   P 4 TYR D 363  THR D 368  0                                        
SHEET    2   P 4 ALA D 377  LEU D 382 -1  O  LYS D 381   N  GLU D 364           
SHEET    3   P 4 VAL D 419  MET D 424 -1  O  ILE D 423   N  VAL D 378           
SHEET    4   P 4 ALA D 408  THR D 410 -1  N  PHE D 409   O  VAL D 420           
SHEET    1   Q 4 GLY E 120  THR E 123  0                                        
SHEET    2   Q 4 GLY E 285  TRP E 289 -1  O  GLY E 285   N  THR E 123           
SHEET    3   Q 4 VAL E 267  SER E 273 -1  N  ALA E 272   O  TRP E 286           
SHEET    4   Q 4 MET E 240  ASP E 243  1  N  ILE E 242   O  SER E 271           
SHEET    1   R 3 GLU E 176  GLU E 179  0                                        
SHEET    2   R 3 ASN E 156  CYS E 159  1  N  LEU E 157   O  ARG E 178           
SHEET    3   R 3 THR E 202  VAL E 206  1  O  ILE E 203   N  ASN E 156           
SHEET    1   S 2 PHE E 301  TYR E 305  0                                        
SHEET    2   S 2 GLY E 308  THR E 312 -1  O  GLY E 308   N  TYR E 305           
SHEET    1   T 4 TYR E 363  THR E 368  0                                        
SHEET    2   T 4 ALA E 377  LEU E 382 -1  O  LYS E 381   N  GLU E 364           
SHEET    3   T 4 VAL E 419  MET E 424 -1  O  ILE E 423   N  VAL E 378           
SHEET    4   T 4 ALA E 408  THR E 410 -1  N  PHE E 409   O  VAL E 420           
SHEET    1   U 4 GLY F 120  THR F 123  0                                        
SHEET    2   U 4 GLY F 285  TRP F 289 -1  O  GLY F 285   N  THR F 123           
SHEET    3   U 4 VAL F 267  SER F 273 -1  N  ALA F 272   O  TRP F 286           
SHEET    4   U 4 MET F 240  ASP F 243  1  N  MET F 240   O  LYS F 268           
SHEET    1   V 3 GLU F 176  GLU F 179  0                                        
SHEET    2   V 3 ASN F 156  CYS F 159  1  N  LEU F 157   O  ARG F 178           
SHEET    3   V 3 THR F 202  VAL F 206  1  O  ILE F 203   N  ASN F 156           
SHEET    1   W 2 PHE F 301  TYR F 305  0                                        
SHEET    2   W 2 GLY F 308  THR F 312 -1  O  THR F 312   N  PHE F 301           
SHEET    1   X 4 TYR F 363  THR F 368  0                                        
SHEET    2   X 4 ALA F 377  LEU F 382 -1  O  LYS F 381   N  GLU F 364           
SHEET    3   X 4 VAL F 419  MET F 424 -1  O  ILE F 423   N  VAL F 378           
SHEET    4   X 4 ALA F 408  THR F 410 -1  N  PHE F 409   O  VAL F 420           
LINK         NZ  LYS A 276                 C4A PLP A 500     1555   1555  1.33  
LINK         NZ  LYS B 276                 C4A PLP B 500     1555   1555  1.33  
LINK         NZ  LYS C 276                 C4A PLP C 501     1555   1555  1.33  
LINK         NZ  LYS D 276                 C4A PLP D 501     1555   1555  1.33  
LINK         NZ  LYS E 276                 C4A PLP E 502     1555   1555  1.33  
LINK         NZ  LYS F 276                 C4A PLP F 502     1555   1555  1.33  
SITE     1 AC1 16 GLY A 125  SER A 126  SER A 127  GLN A 163                    
SITE     2 AC1 16 CYS A 165  THR A 208  THR A 212  ASP A 243                    
SITE     3 AC1 16 ALA A 245  SER A 273  HIS A 275  LYS A 276                    
SITE     4 AC1 16 HOH A5552  HOH A5567  PHE B 317  SER B 318                    
SITE     1 AC2 16 PHE A 317  SER A 318  GLY B 125  SER B 126                    
SITE     2 AC2 16 SER B 127  GLN B 163  CYS B 165  THR B 208                    
SITE     3 AC2 16 THR B 212  ASP B 243  ALA B 245  SER B 273                    
SITE     4 AC2 16 HIS B 275  LYS B 276  HOH B6552  HOH B6574                    
SITE     1 AC3 16 GLY C 125  SER C 126  SER C 127  GLN C 163                    
SITE     2 AC3 16 CYS C 165  THR C 208  THR C 212  ASP C 243                    
SITE     3 AC3 16 ALA C 245  SER C 273  HIS C 275  LYS C 276                    
SITE     4 AC3 16 HOH C8528  PHE D 317  SER D 318  HOH D7561                    
SITE     1 AC4 16 PHE C 317  SER C 318  GLY D 125  SER D 126                    
SITE     2 AC4 16 SER D 127  GLN D 163  CYS D 165  THR D 208                    
SITE     3 AC4 16 THR D 212  ASP D 243  ALA D 245  SER D 273                    
SITE     4 AC4 16 HIS D 275  LYS D 276  HOH D7538  HOH D7566                    
SITE     1 AC5 16 GLY E 125  SER E 126  SER E 127  GLN E 163                    
SITE     2 AC5 16 CYS E 165  THR E 208  THR E 212  ASP E 243                    
SITE     3 AC5 16 ALA E 245  SER E 273  HIS E 275  LYS E 276                    
SITE     4 AC5 16 HOH E9548  PHE F 317  SER F 318  HOH F 520                    
SITE     1 AC6 16 PHE E 317  SER E 318  HOH E9562  GLY F 125                    
SITE     2 AC6 16 SER F 126  SER F 127  GLN F 163  CYS F 165                    
SITE     3 AC6 16 THR F 208  THR F 212  ASP F 243  ALA F 245                    
SITE     4 AC6 16 SER F 273  HIS F 275  LYS F 276  HOH F 544                    
SITE     1 AC7  7 ASN A  83  ASP A  86  PHE A 317  SER A 318                    
SITE     2 AC7  7 HOH A5654  THR B  62  PHE B  63                               
SITE     1 AC8  6 THR A  62  PHE A  63  ASN B  83  ASP B  86                    
SITE     2 AC8  6 SER B 318  HOH B6689                                          
SITE     1 AC9  5 ASN C  83  ASP C  86  SER C 318  THR D  62                    
SITE     2 AC9  5 PHE D  63                                                     
SITE     1 BC1  6 THR C  62  PHE C  63  HOH C8740  ASN D  83                    
SITE     2 BC1  6 ASP D  86  SER D 318                                          
SITE     1 BC2  6 ASN E  83  ASP E  86  SER E 318  HOH E9537                    
SITE     2 BC2  6 THR F  62  PHE F  63                                          
SITE     1 BC3  6 THR E  62  PHE E  63  HOH E9678  ASN F  83                    
SITE     2 BC3  6 ASP F  86  SER F 318                                          
CRYST1   90.780   91.406   93.686  76.80  77.10  78.24 P 1           6          
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      0.011016 -0.002293 -0.002123        0.00000                         
SCALE2      0.000000  0.011175 -0.002182        0.00000                         
SCALE3      0.000000  0.000000  0.011157        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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