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Database: PDB
Entry: 2DGM
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Original site: 2DGM 
HEADER    LYASE                                   14-MAR-06   2DGM              
TITLE     CRYSTAL STRUCTURE OF ESCHERICHIA COLI GADB IN COMPLEX WITH IODIDE     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMATE DECARBOXYLASE BETA;                              
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 SYNONYM: GAD-BETA, GADB;                                             
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 STRAIN: JM109;                                                       
SOURCE   5 GENE: GADB;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: JM109;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PQE60                                     
KEYWDS    GADB COMPLEXED WITH IODIDE, LYASE                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.G.GRUETTER,G.CAPITANI,H.GUT                                         
REVDAT   3   13-JUL-11 2DGM    1       VERSN                                    
REVDAT   2   24-FEB-09 2DGM    1       VERSN                                    
REVDAT   1   20-JUN-06 2DGM    0                                                
JRNL        AUTH   H.GUT,E.PENNACCHIETTI,R.A.JOHN,F.BOSSA,G.CAPITANI,           
JRNL        AUTH 2 D.DE BIASE,M.G.GRUETTER                                      
JRNL        TITL   ESCHERICHIA COLI ACID RESISTANCE: PH-SENSING, ACTIVATION BY  
JRNL        TITL 2 CHLORIDE AND AUTOINHIBITION IN GADB                          
JRNL        REF    EMBO J.                       V.  25  2643 2006              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   16675957                                                     
JRNL        DOI    10.1038/SJ.EMBOJ.7601107                                     
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   G.CAPITANI,D.DE BIASE,C.AURIZI,H.GUT,F.BOSSA,M.G.GRUETTER    
REMARK   1  TITL   CRYSTAL STRUCTURE AND FUNCTIONAL ANALYSIS OF ESCHERICHIA     
REMARK   1  TITL 2 COLI GLUTAMATE DECARBOXYLASE                                 
REMARK   1  REF    EMBO J.                       V.  22  4027 2003              
REMARK   1  REFN                   ISSN 0261-4189                               
REMARK   1  PMID   12912902                                                     
REMARK   1  DOI    10.1093/EMBOJ/CDG403                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
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)   (%) : 92.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 191251                         
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) : 0.227                           
REMARK   3   FREE R VALUE                     : 0.267                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 5338                            
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) : 1.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.02                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 77.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2500                       
REMARK   3   BIN FREE R VALUE                    : 0.2960                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 296                          
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            : 21578                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 172                                     
REMARK   3   SOLVENT ATOMS            : 1923                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.16                            
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) : 0.30                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.21                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.26                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
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 2DGM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-MAR-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB025394.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-MAY-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 90.0                               
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) : 1.300                              
REMARK 200  MONOCHROMATOR                  : LN2 COOLED FIXED-EXIT SI(111)      
REMARK 200                                   MONOCHROMATOR                      
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   : 191280                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.7                               
REMARK 200  DATA REDUNDANCY                : 1.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.12000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.26000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1PMM                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.135M SODIUM ACETATE, 0.7M SODIUM       
REMARK 280  FORMATE, 13% PEG 4000, PH 4.6, VAPOR DIFFUSION, SITTING DROP,       
REMARK 280  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 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: 57140 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 86370 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     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     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     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     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   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     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    LEU A 187       48.43    -90.87                                   
REMARK 500    ALA A 244       42.47   -104.29                                   
REMARK 500    LEU A 250      -63.35   -123.65                                   
REMARK 500    ASP A 261     -144.69    -99.52                                   
REMARK 500    LYS A 276     -114.67   -105.50                                   
REMARK 500    PHE A 317     -100.31   -112.61                                   
REMARK 500    PHE A 429       71.84   -115.61                                   
REMARK 500    PRO B 184      119.94    -37.93                                   
REMARK 500    GLN B 186       68.71   -154.14                                   
REMARK 500    LEU B 187       38.28    -83.88                                   
REMARK 500    ALA B 244       41.12   -103.51                                   
REMARK 500    LEU B 250      -67.87   -125.75                                   
REMARK 500    ASP B 261     -143.63    -95.59                                   
REMARK 500    LYS B 276     -117.38   -102.69                                   
REMARK 500    ASP B 291     -177.23   -170.55                                   
REMARK 500    TYR B 305      105.08   -162.17                                   
REMARK 500    PHE B 317      -94.62   -111.62                                   
REMARK 500    PHE B 429       69.00   -111.54                                   
REMARK 500    SER C  29       -3.95   -143.76                                   
REMARK 500    LEU C 187       49.15    -89.96                                   
REMARK 500    LEU C 250      -68.82   -124.52                                   
REMARK 500    ASP C 261     -144.55    -96.41                                   
REMARK 500    LYS C 276     -120.22   -102.24                                   
REMARK 500    LEU C 306       70.73     37.84                                   
REMARK 500    PHE C 317     -103.38   -115.40                                   
REMARK 500    PHE C 429       71.96   -111.25                                   
REMARK 500    PRO D 161       71.67    -68.28                                   
REMARK 500    GLN D 186       71.93   -153.82                                   
REMARK 500    LEU D 187       44.10    -86.39                                   
REMARK 500    ALA D 244       40.35   -103.68                                   
REMARK 500    LEU D 250      -68.25   -122.27                                   
REMARK 500    ALA D 255       61.47   -151.09                                   
REMARK 500    ASP D 261     -146.92    -97.89                                   
REMARK 500    LYS D 276     -112.74   -100.49                                   
REMARK 500    PHE D 317     -100.41   -116.67                                   
REMARK 500    PHE D 429       66.61   -115.02                                   
REMARK 500    PRO E 184      125.21    -37.21                                   
REMARK 500    GLN E 186       74.42   -150.31                                   
REMARK 500    LEU E 187       46.23    -86.54                                   
REMARK 500    ALA E 244       41.93   -105.37                                   
REMARK 500    ASP E 261     -147.15    -94.65                                   
REMARK 500    LYS E 276     -116.75   -102.94                                   
REMARK 500    PHE E 317     -103.79   -116.61                                   
REMARK 500    PHE E 429       67.55   -117.95                                   
REMARK 500    SER F  29       -7.08   -140.92                                   
REMARK 500    GLN F 186       76.58   -150.38                                   
REMARK 500    LEU F 187       42.15    -88.33                                   
REMARK 500    ALA F 244       40.59   -106.70                                   
REMARK 500    LEU F 250      -65.25   -123.06                                   
REMARK 500    ALA F 255       60.58   -152.06                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      55 RAMACHANDRAN OUTLIERS.                        
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 A2800        DISTANCE =  5.18 ANGSTROMS                       
REMARK 525    HOH A2865        DISTANCE =  5.34 ANGSTROMS                       
REMARK 525    HOH A2894        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH B2986        DISTANCE =  5.21 ANGSTROMS                       
REMARK 525    HOH C2845        DISTANCE =  5.26 ANGSTROMS                       
REMARK 525    HOH D2932        DISTANCE =  5.16 ANGSTROMS                       
REMARK 525    HOH D2962        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH E2968        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH F2856        DISTANCE =  5.13 ANGSTROMS                       
REMARK 525    HOH F2929        DISTANCE =  5.13 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 2331                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 2332                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 2333                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D 2334                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD E 2335                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD F 2336                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 2337                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 2338                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD C 2339                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD F 2342                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 2343                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D 2346                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD E 2347                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD F 2348                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 2349                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 2350                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD C 2351                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D 2352                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD E 2353                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD F 2354                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 2355                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 2356                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD C 2357                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D 2358                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD E 2359                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD F 2360                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP E 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP F 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 2550                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 2560                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 2570                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 2580                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT F 2590                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 2600                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 2610                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT E 2620                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 2630                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT F 2640                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 2650                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT F 2660                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT F 2670                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY E 2519                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG E 2833                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1PMM   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ESCHERICHIA COLI GADB (LOW PH)                  
REMARK 900 RELATED ID: 1PMO   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ESCHERICHIA COLI GADB (NEUTRAL PH)              
REMARK 900 RELATED ID: 2DGK   RELATED DB: PDB                                   
REMARK 900 N-TERMINAL DELETION MUTANT OF THE SAME PROTEIN IN AN                 
REMARK 900 AUTOINHIBITED STATE (ALDAMINE)                                       
REMARK 900 RELATED ID: 2DGL   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH BROMIDE                             
DBREF  2DGM A    1   466  UNP    P69910   DCEB_ECOLI       1    466             
DBREF  2DGM B    1   466  UNP    P69910   DCEB_ECOLI       1    466             
DBREF  2DGM C    1   466  UNP    P69910   DCEB_ECOLI       1    466             
DBREF  2DGM D    1   466  UNP    P69910   DCEB_ECOLI       1    466             
DBREF  2DGM E    1   466  UNP    P69910   DCEB_ECOLI       1    466             
DBREF  2DGM 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    IOD  A2331       1                                                       
HET    IOD  B2332       1                                                       
HET    IOD  B2333       1                                                       
HET    IOD  D2334       1                                                       
HET    IOD  E2335       1                                                       
HET    IOD  F2336       1                                                       
HET    IOD  A2337       1                                                       
HET    IOD  B2338       1                                                       
HET    IOD  C2339       1                                                       
HET    IOD  D2340       1                                                       
HET    IOD  E2341       1                                                       
HET    IOD  F2342       1                                                       
HET    IOD  A2343       1                                                       
HET    IOD  B2344       1                                                       
HET    IOD  C2345       1                                                       
HET    IOD  D2346       1                                                       
HET    IOD  E2347       1                                                       
HET    IOD  F2348       1                                                       
HET    IOD  A2349       1                                                       
HET    IOD  B2350       1                                                       
HET    IOD  C2351       1                                                       
HET    IOD  D2352       1                                                       
HET    IOD  E2353       1                                                       
HET    IOD  F2354       1                                                       
HET    IOD  A2355       1                                                       
HET    IOD  B2356       1                                                       
HET    IOD  C2357       1                                                       
HET    IOD  D2358       1                                                       
HET    IOD  E2359       1                                                       
HET    IOD  F2360       1                                                       
HET    IOD  A2361       1                                                       
HET    IOD  D2362       1                                                       
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    FMT  A2550       3                                                       
HET    FMT  A2560       3                                                       
HET    FMT  D2570       3                                                       
HET    FMT  D2580       3                                                       
HET    FMT  F2590       3                                                       
HET    FMT  A2600       3                                                       
HET    FMT  C2610       3                                                       
HET    FMT  E2620       3                                                       
HET    FMT  D2630       3                                                       
HET    FMT  F2640       3                                                       
HET    FMT  B2650       3                                                       
HET    FMT  F2660       3                                                       
HET    FMT  F2670       3                                                       
HET    ACY  E2519       4                                                       
HET    PEG  E2833       7                                                       
HETNAM     IOD IODIDE ION                                                       
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETNAM     FMT FORMIC ACID                                                      
HETNAM     ACY ACETIC ACID                                                      
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
FORMUL   7  IOD    32(I 1-)                                                     
FORMUL  39  PLP    6(C8 H10 N O6 P)                                             
FORMUL  45  FMT    13(C H2 O2)                                                  
FORMUL  58  ACY    C2 H4 O2                                                     
FORMUL  59  PEG    C4 H10 O3                                                    
FORMUL  60  HOH   *1923(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  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  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 GLY A  412  THR A  416  5                                   5    
HELIX   19  19 GLU A  430  HIS A  451  1                                  22    
HELIX   20  20 LYS B    3  ASP B   15  1                                  13    
HELIX   21  21 ALA B   20  SER B   24  5                                   5    
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  147  1                                  23    
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    
HELIX   38  38 LYS C    3  ASP C   15  1                                  13    
HELIX   39  39 ALA C   20  SER C   24  5                                   5    
HELIX   40  40 ARG C   38  LEU C   50  1                                  13    
HELIX   41  41 TYR C   51  ASP C   53  5                                   3    
HELIX   42  42 ASN C   55  ASN C   59  5                                   5    
HELIX   43  43 ASP C   69  SER C   79  1                                  11    
HELIX   44  44 TYR C   90  TRP C  108  1                                  19    
HELIX   45  45 GLY C  125  GLY C  149  1                                  25    
HELIX   46  46 ILE C  164  TRP C  173  1                                  10    
HELIX   47  47 ASP C  190  CYS C  198  1                                   9    
HELIX   48  48 PHE C  219  GLY C  235  1                                  17    
HELIX   49  49 SER C  246  PHE C  249  5                                   4    
HELIX   50  50 LEU C  250  ALA C  255  1                                   6    
HELIX   51  51 ASP C  291  LEU C  295  5                                   5    
HELIX   52  52 PRO C  296  VAL C  300  5                                   5    
HELIX   53  53 ALA C  321  LYS C  359  1                                  39    
HELIX   54  54 THR C  391  LEU C  401  1                                  11    
HELIX   55  55 GLY C  412  THR C  416  5                                   5    
HELIX   56  56 GLU C  430  HIS C  451  1                                  22    
HELIX   57  57 PRO C  452  GLN C  455  5                                   4    
HELIX   58  58 LYS D    3  ASP D   15  1                                  13    
HELIX   59  59 ALA D   20  SER D   24  5                                   5    
HELIX   60  60 ARG D   38  LEU D   50  1                                  13    
HELIX   61  61 TYR D   51  GLY D   54  5                                   4    
HELIX   62  62 ASN D   55  ASN D   59  5                                   5    
HELIX   63  63 ASP D   69  ILE D   80  1                                  12    
HELIX   64  64 TYR D   90  TRP D  108  1                                  19    
HELIX   65  65 GLY D  125  ALA D  147  1                                  23    
HELIX   66  66 ILE D  164  TRP D  173  1                                  10    
HELIX   67  67 ASP D  190  CYS D  198  1                                   9    
HELIX   68  68 PHE D  219  GLY D  235  1                                  17    
HELIX   69  69 SER D  246  PHE D  249  5                                   4    
HELIX   70  70 LEU D  250  ALA D  255  1                                   6    
HELIX   71  71 ASP D  291  LEU D  295  5                                   5    
HELIX   72  72 PRO D  296  VAL D  300  5                                   5    
HELIX   73  73 ALA D  321  LYS D  359  1                                  39    
HELIX   74  74 THR D  391  LEU D  401  1                                  11    
HELIX   75  75 GLY D  412  THR D  416  5                                   5    
HELIX   76  76 GLU D  430  HIS D  451  1                                  22    
HELIX   77  77 PRO D  452  GLN D  455  5                                   4    
HELIX   78  78 LYS E    3  ASP E   15  1                                  13    
HELIX   79  79 ALA E   20  SER E   24  5                                   5    
HELIX   80  80 ARG E   38  LEU E   50  1                                  13    
HELIX   81  81 TYR E   51  GLY E   54  5                                   4    
HELIX   82  82 ASN E   55  ASN E   59  5                                   5    
HELIX   83  83 ASP E   69  ILE E   80  1                                  12    
HELIX   84  84 TYR E   90  TRP E  108  1                                  19    
HELIX   85  85 GLY E  125  GLY E  149  1                                  25    
HELIX   86  86 GLN E  163  TRP E  173  1                                  11    
HELIX   87  87 ASP E  190  CYS E  198  1                                   9    
HELIX   88  88 PHE E  219  GLY E  235  1                                  17    
HELIX   89  89 SER E  246  PHE E  249  5                                   4    
HELIX   90  90 LEU E  250  ALA E  255  1                                   6    
HELIX   91  91 ASP E  291  LEU E  295  5                                   5    
HELIX   92  92 PRO E  296  VAL E  300  5                                   5    
HELIX   93  93 ALA E  321  LYS E  359  1                                  39    
HELIX   94  94 THR E  391  LEU E  401  1                                  11    
HELIX   95  95 GLY E  412  THR E  416  5                                   5    
HELIX   96  96 GLU E  430  ASP E  450  1                                  21    
HELIX   97  97 LYS F    3  ASP F   15  1                                  13    
HELIX   98  98 ALA F   20  SER F   24  5                                   5    
HELIX   99  99 ARG F   38  LEU F   50  1                                  13    
HELIX  100 100 TYR F   51  GLY F   54  5                                   4    
HELIX  101 101 ASN F   55  ASN F   59  5                                   5    
HELIX  102 102 ASP F   69  SER F   79  1                                  11    
HELIX  103 103 TYR F   90  TRP F  108  1                                  19    
HELIX  104 104 GLY F  125  ALA F  147  1                                  23    
HELIX  105 105 ILE F  164  TRP F  173  1                                  10    
HELIX  106 106 ASP F  190  CYS F  198  1                                   9    
HELIX  107 107 PHE F  219  GLY F  235  1                                  17    
HELIX  108 108 SER F  246  PHE F  249  5                                   4    
HELIX  109 109 LEU F  250  ALA F  255  1                                   6    
HELIX  110 110 ASP F  291  LEU F  295  5                                   5    
HELIX  111 111 PRO F  296  VAL F  300  5                                   5    
HELIX  112 112 ALA F  321  LYS F  359  1                                  39    
HELIX  113 113 THR F  391  LEU F  401  1                                  11    
HELIX  114 114 GLY F  412  THR F  416  5                                   5    
HELIX  115 115 GLU F  430  HIS F  451  1                                  22    
HELIX  116 116 PRO F  452  GLN F  455  5                                   4    
SHEET    1   A 4 GLY A 120  THR A 123  0                                        
SHEET    2   A 4 GLY A 285  TRP A 289 -1  O  VAL A 287   N  THR A 121           
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  ILE A 310   N  VAL A 303           
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  ILE B 270   O  ILE B 288           
SHEET    4   E 4 MET B 240  ASP B 243  1  N  MET B 240   O  LYS B 268           
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  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           
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  CYS C 379   N  ILE C 366           
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  MET D 240   O  LYS D 268           
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  CYS D 379   N  ILE D 366           
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  MET E 240   O  LYS E 268           
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  CYS E 379   N  ILE E 366           
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  CYS F 379   N  ILE F 366           
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         C4A PLP A 500                 NZ  LYS A 276     1555   1555  1.34  
LINK         C4A PLP B 500                 NZ  LYS B 276     1555   1555  1.32  
LINK         C4A PLP C 501                 NZ  LYS C 276     1555   1555  1.34  
LINK         C4A PLP D 501                 NZ  LYS D 276     1555   1555  1.33  
LINK         C4A PLP E 502                 NZ  LYS E 276     1555   1555  1.33  
LINK         C4A PLP F 502                 NZ  LYS F 276     1555   1555  1.33  
SITE     1 AC1  2 SER A  16  ARG F 427                                          
SITE     1 AC2  2 SER B  16  ARG C 427                                          
SITE     1 AC3  2 ARG B 427  SER C  16                                          
SITE     1 AC4  2 SER D  16  ARG E 427                                          
SITE     1 AC5  2 ARG D 427  SER E  16                                          
SITE     1 AC6  2 ARG A 427  SER F  16                                          
SITE     1 AC7  2 LYS A 381  ILE A 418                                          
SITE     1 AC8  1 ILE B 418                                                     
SITE     1 AC9  2 LYS C 381  ILE C 418                                          
SITE     1 BC1  1 ILE F 418                                                     
SITE     1 BC2  1 LYS A 453                                                     
SITE     1 BC3  1 LYS D 453                                                     
SITE     1 BC4  1 HIS E 451                                                     
SITE     1 BC5  1 LYS F 453                                                     
SITE     1 BC6  2 TRP A  67  HIS A  73                                          
SITE     1 BC7  3 ASN A  81  ASP B  68  HIS B  73                               
SITE     1 BC8  4 TRP C  67  ASP C  68  HIS C  73  ASN D  81                    
SITE     1 BC9  3 ASN C  81  ASP D  68  HIS D  73                               
SITE     1 CC1  4 TRP E  67  ASP E  68  HIS E  73  ASN F  81                    
SITE     1 CC2  1 HIS F  73                                                     
SITE     1 CC3  3 LEU A 382  THR A 391  LEU A 392                               
SITE     1 CC4  3 LEU B 382  THR B 391  LEU B 392                               
SITE     1 CC5  3 LEU C 382  THR C 391  LEU C 392                               
SITE     1 CC6  3 LEU D 382  THR D 391  LEU D 392                               
SITE     1 CC7  2 THR E 391  LEU E 392                                          
SITE     1 CC8  2 THR F 391  LEU F 392                                          
SITE     1 CC9 15 GLY A 125  SER A 126  SER A 127  GLN A 163                    
SITE     2 CC9 15 THR A 208  THR A 212  ASP A 243  ALA A 245                    
SITE     3 CC9 15 SER A 273  HIS A 275  LYS A 276  HOH A2651                    
SITE     4 CC9 15 PHE B 317  SER B 318  HOH B2680                               
SITE     1 DC1 15 PHE A 317  SER A 318  HOH A2637  GLY B 125                    
SITE     2 DC1 15 SER B 126  SER B 127  GLN B 163  CYS B 165                    
SITE     3 DC1 15 THR B 212  ASP B 243  ALA B 245  SER B 273                    
SITE     4 DC1 15 HIS B 275  LYS B 276  HOH B2703                               
SITE     1 DC2 15 GLY C 125  SER C 126  SER C 127  GLN C 163                    
SITE     2 DC2 15 THR C 208  THR C 212  ASP C 243  ALA C 245                    
SITE     3 DC2 15 SER C 273  HIS C 275  LYS C 276  HOH C2619                    
SITE     4 DC2 15 PHE D 317  SER D 318  HOH D2673                               
SITE     1 DC3 15 PHE C 317  SER C 318  HOH C2649  GLY D 125                    
SITE     2 DC3 15 SER D 126  SER D 127  GLN D 163  CYS D 165                    
SITE     3 DC3 15 THR D 212  ASP D 243  ALA D 245  SER D 273                    
SITE     4 DC3 15 HIS D 275  LYS D 276  HOH D2649                               
SITE     1 DC4 15 SER E 126  SER E 127  GLN E 163  CYS E 165                    
SITE     2 DC4 15 THR E 208  THR E 212  ASP E 243  ALA E 245                    
SITE     3 DC4 15 SER E 273  HIS E 275  LYS E 276  HOH E2857                    
SITE     4 DC4 15 PHE F 317  SER F 318  HOH F2688                               
SITE     1 DC5 15 PHE E 317  SER E 318  HOH E2869  GLY F 125                    
SITE     2 DC5 15 SER F 126  SER F 127  GLN F 163  CYS F 165                    
SITE     3 DC5 15 THR F 212  ASP F 243  ALA F 245  SER F 273                    
SITE     4 DC5 15 HIS F 275  LYS F 276  HOH F2711                               
SITE     1 DC6  4 ASN A  83  ASP A  86  THR B  62  PHE B  63                    
SITE     1 DC7  4 THR A  62  PHE A  63  ASN B  83  ASP B  86                    
SITE     1 DC8  4 ASN C  83  ASP C  86  THR D  62  PHE D  63                    
SITE     1 DC9  5 THR C  62  PHE C  63  CYS C  64  ASN D  83                    
SITE     2 DC9  5 ASP D  86                                                     
SITE     1 EC1  4 ASN E  83  ASP E  86  THR F  62  PHE F  63                    
SITE     1 EC2  5 TRP A  84  ASP A  97  THR A 121  ASN A 122                    
SITE     2 EC2  5 HOH A2720                                                     
SITE     1 EC3  5 ASP C  97  LEU C  98  THR C 121  ASN C 122                    
SITE     2 EC3  5 HOH C2725                                                     
SITE     1 EC4  5 TRP E  84  ASP E  97  THR E 121  ASN E 122                    
SITE     2 EC4  5 HOH E2973                                                     
SITE     1 EC5  7 TRP D  84  ASP D  97  LEU D  98  GLY D 120                    
SITE     2 EC5  7 THR D 121  ASN D 122  HOH D2778                               
SITE     1 EC6  5 TRP F  84  ASP F  97  THR F 121  ASN F 122                    
SITE     2 EC6  5 HOH F2726                                                     
SITE     1 EC7  6 TRP B  84  ASP B  97  THR B 121  ASN B 122                    
SITE     2 EC7  6 HOH B2707  HOH B2848                                          
SITE     1 EC8  4 LEU F  98  ALA F 118  GLY F 120  GLY F 311                    
SITE     1 EC9  6 PRO F 111  ARG F 290  ASP F 291  HOH F2678                    
SITE     2 EC9  6 HOH F2793  HOH F2810                                          
SITE     1 FC1  6 THR E  62  PHE E  63  ASN F  83  ASP F  86                    
SITE     2 FC1  6 PHE F 317  SER F 318                                          
SITE     1 FC2  8 ASP E 228  ASP E 237  ASP E 239  PRO E 265                    
SITE     2 FC2  8 ARG E 266  LYS E 268  HOH E2933  HOH E3104                    
CRYST1   91.336   91.804   93.914  76.65  76.94  78.04 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      0.010949 -0.002319 -0.002132        0.00000                         
SCALE2      0.000000  0.011134 -0.002192        0.00000                         
SCALE3      0.000000  0.000000  0.011141        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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