GenomeNet

Database: PDB
Entry: 1PMO
LinkDB: 1PMO
Original site: 1PMO 
HEADER    LYASE                                   11-JUN-03   1PMO              
TITLE     CRYSTAL STRUCTURE OF ESCHERICHIA COLI GADB (NEUTRAL PH)               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMATE DECARBOXYLASE BETA;                              
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 FRAGMENT: GADB;                                                      
COMPND   5 SYNONYM: GAD-BETA;                                                   
COMPND   6 EC: 4.1.1.15;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: GADB;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: JM109;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PQE60                                     
KEYWDS    NEUTRAL-PH FORM OF GADB, LYASE                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.CAPITANI,D.DE BIASE,C.AURIZI,H.GUT,F.BOSSA,M.G.GRUTTER              
REVDAT   2   24-FEB-09 1PMO    1       VERSN                                    
REVDAT   1   17-FEB-04 1PMO    0                                                
JRNL        AUTH   G.CAPITANI,D.DE BIASE,C.AURIZI,H.GUT,F.BOSSA,                
JRNL        AUTH 2 M.G.GRUTTER                                                  
JRNL        TITL   CRYSTAL STRUCTURE AND FUNCTIONAL ANALYSIS OF                 
JRNL        TITL 2 ESCHERICHIA COLI GLUTAMATE DECARBOXYLASE                     
JRNL        REF    EMBO J.                       V.  22  4027 2003              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   12912902                                                     
JRNL        DOI    10.1093/EMBOJ/CDG403                                         
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
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)   (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 136306                         
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) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.233                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2749                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.38                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2630                       
REMARK   3   BIN FREE R VALUE                    : 0.3010                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 269                          
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            : 21799                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 234                                     
REMARK   3   SOLVENT ATOMS            : 1169                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.59300                                             
REMARK   3    B22 (A**2) : -0.59300                                             
REMARK   3    B33 (A**2) : 1.18600                                              
REMARK   3    B12 (A**2) : -3.58500                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.27                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.31                            
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) : 0.32                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.34                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.27                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.83                            
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 1PMO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUN-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB019430.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-NOV-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : DIAMOND (111)                      
REMARK 200  OPTICS                         : MULTILAYER                         
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   : 136310                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 2.200                              
REMARK 200  R MERGE                    (I) : 0.09700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.35                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, TRIS, PH 7.6,         
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      138.23333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       69.11667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HEXAMER                         
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 56230 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 84340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -138.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     VAL A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     ARG A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ASP C     2                                                      
REMARK 465     LYS C     3                                                      
REMARK 465     LYS C     4                                                      
REMARK 465     GLN C     5                                                      
REMARK 465     VAL C     6                                                      
REMARK 465     THR C     7                                                      
REMARK 465     ASP C     8                                                      
REMARK 465     LEU C     9                                                      
REMARK 465     ARG C    10                                                      
REMARK 465     SER C    11                                                      
REMARK 465     GLU C    12                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ASP D     2                                                      
REMARK 465     LYS D     3                                                      
REMARK 465     LYS D     4                                                      
REMARK 465     GLN D     5                                                      
REMARK 465     VAL D     6                                                      
REMARK 465     THR D     7                                                      
REMARK 465     ASP D     8                                                      
REMARK 465     LEU D     9                                                      
REMARK 465     ARG D    10                                                      
REMARK 465     SER D    11                                                      
REMARK 465     GLU D    12                                                      
REMARK 465     MET E     1                                                      
REMARK 465     ASP E     2                                                      
REMARK 465     LYS E     3                                                      
REMARK 465     MET F     1                                                      
REMARK 465     ASP F     2                                                      
REMARK 465     LYS F     3                                                      
REMARK 465     LYS F     4                                                      
REMARK 465     GLN F     5                                                      
REMARK 465     VAL F     6                                                      
REMARK 465     THR F     7                                                      
REMARK 465     ASP F     8                                                      
REMARK 465     LEU F     9                                                      
REMARK 465     ARG F    10                                                      
REMARK 465     SER F    11                                                      
REMARK 465     GLU F    12                                                      
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    PRO A 161       67.61    -69.35                                   
REMARK 500    ALA A 244       42.66   -106.17                                   
REMARK 500    LEU A 250      -66.69   -120.54                                   
REMARK 500    ALA A 255       63.94   -151.86                                   
REMARK 500    ASP A 261     -147.38    -93.69                                   
REMARK 500    LYS A 276     -121.46   -107.47                                   
REMARK 500    PHE A 317      -96.64   -123.97                                   
REMARK 500    GLU A 386       -4.92   -155.70                                   
REMARK 500    ASP A 387       86.08     10.72                                   
REMARK 500    GLN A 459       31.95   -154.25                                   
REMARK 500    SER B  11       57.18    -98.09                                   
REMARK 500    ASN B 115      -67.88   -148.71                                   
REMARK 500    ASP B 261     -145.63    -92.04                                   
REMARK 500    LYS B 276     -118.95   -108.15                                   
REMARK 500    PHE B 317     -102.70   -116.28                                   
REMARK 500    GLN B 459       25.84   -150.80                                   
REMARK 500    ALA C  27      -96.70    -28.26                                   
REMARK 500    GLU C  28       54.99    -96.75                                   
REMARK 500    ASN C 115      -74.36   -124.29                                   
REMARK 500    THR C 152       31.65   -142.05                                   
REMARK 500    GLN C 186       71.59   -163.80                                   
REMARK 500    ALA C 244       40.56   -106.78                                   
REMARK 500    LEU C 250      -66.30   -121.18                                   
REMARK 500    ASP C 261     -147.56    -93.13                                   
REMARK 500    LYS C 276     -119.96   -109.77                                   
REMARK 500    PHE C 317      -95.93   -125.44                                   
REMARK 500    GLN C 459       28.90   -152.80                                   
REMARK 500    ALA D  27      -71.04    -42.07                                   
REMARK 500    GLU D  28       56.55   -101.70                                   
REMARK 500    PRO D 161       67.30    -68.78                                   
REMARK 500    ALA D 244       41.12   -105.34                                   
REMARK 500    ALA D 255       63.03   -150.56                                   
REMARK 500    ASP D 261     -146.45    -95.36                                   
REMARK 500    LYS D 276     -119.04   -106.36                                   
REMARK 500    PHE D 317     -103.86   -125.50                                   
REMARK 500    ALA D 415       32.10    -79.77                                   
REMARK 500    GLN D 459       29.43   -153.35                                   
REMARK 500    LEU E   9       53.82   -109.82                                   
REMARK 500    SER E  11       42.43    -91.85                                   
REMARK 500    GLU E  12     -156.73    -45.91                                   
REMARK 500    LEU E  13      124.54     73.99                                   
REMARK 500    ALA E  20     -156.89   -137.88                                   
REMARK 500    SER E  22     -154.95     45.81                                   
REMARK 500    ILE E  23       81.39     73.47                                   
REMARK 500    GLN E 186       81.78   -161.73                                   
REMARK 500    ALA E 244       40.05   -106.45                                   
REMARK 500    LEU E 250      -64.81   -122.75                                   
REMARK 500    ALA E 255       62.25   -150.39                                   
REMARK 500    ASP E 261     -144.60    -94.69                                   
REMARK 500    LYS E 276     -122.68   -108.51                                   
REMARK 500    PHE E 317     -101.31   -120.90                                   
REMARK 500    GLN E 459       30.22   -154.35                                   
REMARK 500    ALA F 244       41.69   -108.59                                   
REMARK 500    LEU F 250      -70.03   -118.62                                   
REMARK 500    ALA F 255       64.83   -150.78                                   
REMARK 500    ASP F 261     -145.16    -96.02                                   
REMARK 500    LYS F 276     -118.05   -108.87                                   
REMARK 500    PHE F 317      -98.27   -123.91                                   
REMARK 500    GLN F 459       27.36   -153.59                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLR A 1500                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLR B 1501                
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLR C 1502                
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLR D 1503                
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLR E 1504                
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLR F 1505                
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 3236                
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS B 3237                
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS D 3238                
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS E 3239                
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS F 3240                
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 3241                
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS B 3242                
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS C 3243                
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS D 3244                
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS D 3245                
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS E 3246                
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS E 3247                
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS F 3248                
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS F 3249                
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS C 3250                
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 3251                
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS C 3252                
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS E 3253                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1PMM   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN AT LOW PH                                           
DBREF  1PMO A    1   466  UNP    P69910   DCEB_ECOLI       1    466             
DBREF  1PMO B    1   466  UNP    P69910   DCEB_ECOLI       1    466             
DBREF  1PMO C    1   466  UNP    P69910   DCEB_ECOLI       1    466             
DBREF  1PMO D    1   466  UNP    P69910   DCEB_ECOLI       1    466             
DBREF  1PMO E    1   466  UNP    P69910   DCEB_ECOLI       1    466             
DBREF  1PMO 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    PLR  A1500      15                                                       
HET    PLR  B1501      15                                                       
HET    PLR  C1502      15                                                       
HET    PLR  D1503      15                                                       
HET    PLR  E1504      15                                                       
HET    PLR  F1505      15                                                       
HET    TRS  A3236       8                                                       
HET    TRS  B3237       8                                                       
HET    TRS  D3238       8                                                       
HET    TRS  E3239       8                                                       
HET    TRS  F3240       8                                                       
HET    TRS  A3241       8                                                       
HET    TRS  B3242       8                                                       
HET    TRS  C3243       8                                                       
HET    TRS  D3244       8                                                       
HET    TRS  D3245       8                                                       
HET    TRS  E3246       8                                                       
HET    TRS  E3247       8                                                       
HET    TRS  F3248       8                                                       
HET    TRS  F3249       8                                                       
HET    TRS  C3250       8                                                       
HET    TRS  A3251       8                                                       
HET    TRS  C3252       8                                                       
HET    TRS  E3253       8                                                       
HETNAM     PLR (5-HYDROXY-4,6-DIMETHYLPYRIDIN-3-YL)METHYL DIHYDROGEN            
HETNAM   2 PLR  PHOSPHATE                                                       
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETSYN     PLR 4'-DEOXYPYRIDOXINE PHOSPHATE                                     
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   7  PLR    6(C8 H12 N O5 P)                                             
FORMUL  13  TRS    18(C4 H12 N O3 1+)                                           
FORMUL  31  HOH   *1169(H2 O)                                                   
HELIX    1   1 ARG A   38  LEU A   50  1                                  13    
HELIX    2   2 TYR A   51  ASP A   53  5                                   3    
HELIX    3   3 ASP A   69  ILE A   80  1                                  12    
HELIX    4   4 TYR A   90  TRP A  108  1                                  19    
HELIX    5   5 GLY A  125  ALA A  148  1                                  24    
HELIX    6   6 GLN A  163  TRP A  173  1                                  11    
HELIX    7   7 ASP A  190  CYS A  198  1                                   9    
HELIX    8   8 PHE A  219  GLY A  235  1                                  17    
HELIX    9   9 SER A  246  PHE A  249  5                                   4    
HELIX   10  10 LEU A  250  ALA A  255  1                                   6    
HELIX   11  11 ASP A  291  LEU A  295  5                                   5    
HELIX   12  12 PRO A  296  VAL A  300  5                                   5    
HELIX   13  13 ALA A  321  ALA A  358  1                                  38    
HELIX   14  14 THR A  391  LEU A  401  1                                  11    
HELIX   15  15 GLU A  430  HIS A  451  1                                  22    
HELIX   16  16 PRO A  452  GLN A  455  5                                   4    
HELIX   17  17 ARG B   38  LEU B   50  1                                  13    
HELIX   18  18 TYR B   51  ASP B   53  5                                   3    
HELIX   19  19 ASP B   69  ILE B   80  1                                  12    
HELIX   20  20 TYR B   90  TRP B  108  1                                  19    
HELIX   21  21 GLY B  125  ALA B  148  1                                  24    
HELIX   22  22 GLN B  163  TRP B  173  1                                  11    
HELIX   23  23 ASP B  190  CYS B  198  1                                   9    
HELIX   24  24 PHE B  219  GLY B  235  1                                  17    
HELIX   25  25 SER B  246  PHE B  249  5                                   4    
HELIX   26  26 LEU B  250  ALA B  255  1                                   6    
HELIX   27  27 ASP B  291  LEU B  295  5                                   5    
HELIX   28  28 PRO B  296  VAL B  300  5                                   5    
HELIX   29  29 ALA B  321  ALA B  358  1                                  38    
HELIX   30  30 THR B  391  LEU B  401  1                                  11    
HELIX   31  31 GLY B  412  THR B  416  5                                   5    
HELIX   32  32 GLU B  430  HIS B  451  1                                  22    
HELIX   33  33 PRO B  452  GLN B  455  5                                   4    
HELIX   34  34 ARG C   38  LEU C   50  1                                  13    
HELIX   35  35 TYR C   51  ASP C   53  5                                   3    
HELIX   36  36 ASP C   69  ILE C   80  1                                  12    
HELIX   37  37 TYR C   90  TRP C  108  1                                  19    
HELIX   38  38 GLY C  125  ALA C  147  1                                  23    
HELIX   39  39 GLN C  163  TRP C  173  1                                  11    
HELIX   40  40 ASP C  190  CYS C  198  1                                   9    
HELIX   41  41 PHE C  219  GLY C  235  1                                  17    
HELIX   42  42 SER C  246  PHE C  249  5                                   4    
HELIX   43  43 LEU C  250  ALA C  255  1                                   6    
HELIX   44  44 ASP C  291  LEU C  295  5                                   5    
HELIX   45  45 PRO C  296  VAL C  300  5                                   5    
HELIX   46  46 ALA C  321  ALA C  358  1                                  38    
HELIX   47  47 THR C  391  LEU C  401  1                                  11    
HELIX   48  48 GLY C  412  ASP C  417  5                                   6    
HELIX   49  49 GLU C  430  HIS C  451  1                                  22    
HELIX   50  50 PRO C  452  GLN C  455  5                                   4    
HELIX   51  51 ARG D   38  LEU D   50  1                                  13    
HELIX   52  52 TYR D   51  ASP D   53  5                                   3    
HELIX   53  53 ASP D   69  ILE D   80  1                                  12    
HELIX   54  54 TYR D   90  TRP D  108  1                                  19    
HELIX   55  55 GLY D  125  ALA D  148  1                                  24    
HELIX   56  56 GLN D  163  TRP D  173  1                                  11    
HELIX   57  57 ASP D  190  CYS D  198  1                                   9    
HELIX   58  58 PHE D  219  GLY D  235  1                                  17    
HELIX   59  59 SER D  246  PHE D  249  5                                   4    
HELIX   60  60 LEU D  250  ALA D  255  1                                   6    
HELIX   61  61 ASP D  291  LEU D  295  5                                   5    
HELIX   62  62 PRO D  296  VAL D  300  5                                   5    
HELIX   63  63 ALA D  321  ALA D  358  1                                  38    
HELIX   64  64 THR D  391  LEU D  401  1                                  11    
HELIX   65  65 GLU D  414  ASP D  417  5                                   4    
HELIX   66  66 GLU D  430  HIS D  451  1                                  22    
HELIX   67  67 PRO D  452  GLN D  455  5                                   4    
HELIX   68  68 ARG E   38  LEU E   50  1                                  13    
HELIX   69  69 TYR E   51  ASP E   53  5                                   3    
HELIX   70  70 ASP E   69  ILE E   80  1                                  12    
HELIX   71  71 TYR E   90  TRP E  108  1                                  19    
HELIX   72  72 GLY E  125  ALA E  148  1                                  24    
HELIX   73  73 GLN E  163  TRP E  173  1                                  11    
HELIX   74  74 ASP E  190  CYS E  198  1                                   9    
HELIX   75  75 PHE E  219  GLY E  235  1                                  17    
HELIX   76  76 SER E  246  PHE E  249  5                                   4    
HELIX   77  77 LEU E  250  ALA E  255  1                                   6    
HELIX   78  78 ASP E  291  LEU E  295  5                                   5    
HELIX   79  79 PRO E  296  VAL E  300  5                                   5    
HELIX   80  80 ALA E  321  ALA E  358  1                                  38    
HELIX   81  81 THR E  391  LEU E  401  1                                  11    
HELIX   82  82 GLY E  412  THR E  416  5                                   5    
HELIX   83  83 GLU E  430  HIS E  451  1                                  22    
HELIX   84  84 PRO E  452  GLN E  455  5                                   4    
HELIX   85  85 ARG F   38  LEU F   50  1                                  13    
HELIX   86  86 TYR F   51  ASP F   53  5                                   3    
HELIX   87  87 ASP F   69  ILE F   80  1                                  12    
HELIX   88  88 TYR F   90  TRP F  108  1                                  19    
HELIX   89  89 GLY F  125  ALA F  148  1                                  24    
HELIX   90  90 GLN F  163  TRP F  173  1                                  11    
HELIX   91  91 ASP F  190  CYS F  198  1                                   9    
HELIX   92  92 PHE F  219  GLY F  235  1                                  17    
HELIX   93  93 SER F  246  PHE F  249  5                                   4    
HELIX   94  94 LEU F  250  ALA F  255  1                                   6    
HELIX   95  95 ASP F  291  LEU F  295  5                                   5    
HELIX   96  96 PRO F  296  VAL F  300  5                                   5    
HELIX   97  97 ALA F  321  ALA F  358  1                                  38    
HELIX   98  98 THR F  391  LEU F  401  1                                  11    
HELIX   99  99 GLY F  412  THR F  416  5                                   5    
HELIX  100 100 GLU F  430  HIS F  451  1                                  22    
HELIX  101 101 PRO F  452  GLN F  455  5                                   4    
SHEET    1   A 2 LEU A  14  ASP A  15  0                                        
SHEET    2   A 2 ALA A  20  LYS A  21 -1  O  ALA A  20   N  ASP A  15           
SHEET    1   B 4 VAL A 119  THR A 123  0                                        
SHEET    2   B 4 GLY A 285  TRP A 289 -1  O  TRP A 289   N  VAL A 119           
SHEET    3   B 4 VAL A 267  SER A 273 -1  N  ILE A 270   O  ILE A 288           
SHEET    4   B 4 MET A 240  ASP A 243  1  N  MET A 240   O  LYS A 268           
SHEET    1   C 3 GLU A 176  GLU A 179  0                                        
SHEET    2   C 3 ASN A 156  CYS A 159  1  N  LEU A 157   O  ARG A 178           
SHEET    3   C 3 THR A 202  VAL A 206  1  O  ILE A 203   N  ASN A 156           
SHEET    1   D 2 PHE A 301  TYR A 305  0                                        
SHEET    2   D 2 GLY A 308  THR A 312 -1  O  THR A 312   N  PHE A 301           
SHEET    1   E 4 TYR A 363  THR A 368  0                                        
SHEET    2   E 4 ALA A 377  LEU A 382 -1  O  LYS A 381   N  GLU A 364           
SHEET    3   E 4 VAL A 419  MET A 424 -1  O  ILE A 423   N  VAL A 378           
SHEET    4   E 4 ALA A 408  THR A 410 -1  N  PHE A 409   O  VAL A 420           
SHEET    1   F 2 LEU B  14  ASP B  15  0                                        
SHEET    2   F 2 ALA B  20  LYS B  21 -1  O  ALA B  20   N  ASP B  15           
SHEET    1   G 4 VAL B 119  THR B 123  0                                        
SHEET    2   G 4 GLY B 285  TRP B 289 -1  O  TRP B 289   N  VAL B 119           
SHEET    3   G 4 VAL B 267  SER B 273 -1  N  ILE B 270   O  ILE B 288           
SHEET    4   G 4 MET B 240  ASP B 243  1  N  ILE B 242   O  SER B 269           
SHEET    1   H 3 GLU B 176  GLU B 179  0                                        
SHEET    2   H 3 ASN B 156  CYS B 159  1  N  LEU B 157   O  ARG B 178           
SHEET    3   H 3 THR B 202  VAL B 206  1  O  ILE B 203   N  ASN B 156           
SHEET    1   I 2 PHE B 301  VAL B 303  0                                        
SHEET    2   I 2 ILE B 310  THR B 312 -1  O  THR B 312   N  PHE B 301           
SHEET    1   J 4 TYR B 363  THR B 368  0                                        
SHEET    2   J 4 ALA B 377  LEU B 382 -1  O  LYS B 381   N  GLU B 364           
SHEET    3   J 4 VAL B 419  MET B 424 -1  O  ILE B 423   N  VAL B 378           
SHEET    4   J 4 ALA B 408  THR B 410 -1  N  PHE B 409   O  VAL B 420           
SHEET    1   K 2 LEU C  14  ASP C  15  0                                        
SHEET    2   K 2 ALA C  20  LYS C  21 -1  O  ALA C  20   N  ASP C  15           
SHEET    1   L 4 VAL C 119  THR C 123  0                                        
SHEET    2   L 4 GLY C 285  TRP C 289 -1  O  TRP C 289   N  VAL C 119           
SHEET    3   L 4 VAL C 267  SER C 273 -1  N  ILE C 270   O  ILE C 288           
SHEET    4   L 4 MET C 240  ASP C 243  1  N  MET C 240   O  LYS C 268           
SHEET    1   M 3 GLU C 176  GLU C 179  0                                        
SHEET    2   M 3 ASN C 156  CYS C 159  1  N  LEU C 157   O  ARG C 178           
SHEET    3   M 3 THR C 202  VAL C 206  1  O  ILE C 203   N  ASN C 156           
SHEET    1   N 2 PHE C 301  TYR C 305  0                                        
SHEET    2   N 2 GLY C 308  THR C 312 -1  O  GLY C 308   N  TYR C 305           
SHEET    1   O 4 TYR C 363  THR C 368  0                                        
SHEET    2   O 4 ALA C 377  LEU C 382 -1  O  LYS C 381   N  GLU C 364           
SHEET    3   O 4 VAL C 419  MET C 424 -1  O  ILE C 423   N  VAL C 378           
SHEET    4   O 4 ALA C 408  THR C 410 -1  N  PHE C 409   O  VAL C 420           
SHEET    1   P 2 LEU D  14  ASP D  15  0                                        
SHEET    2   P 2 ALA D  20  LYS D  21 -1  O  ALA D  20   N  ASP D  15           
SHEET    1   Q 4 VAL D 119  THR D 123  0                                        
SHEET    2   Q 4 GLY D 285  TRP D 289 -1  O  TRP D 289   N  VAL D 119           
SHEET    3   Q 4 VAL D 267  SER D 273 -1  N  ILE D 270   O  ILE D 288           
SHEET    4   Q 4 MET D 240  ASP D 243  1  N  ILE D 242   O  SER D 271           
SHEET    1   R 3 GLU D 176  GLU D 179  0                                        
SHEET    2   R 3 ASN D 156  CYS D 159  1  N  LEU D 157   O  ARG D 178           
SHEET    3   R 3 THR D 202  VAL D 206  1  O  ILE D 203   N  ASN D 156           
SHEET    1   S 2 PHE D 301  VAL D 303  0                                        
SHEET    2   S 2 ILE D 310  THR D 312 -1  O  THR D 312   N  PHE D 301           
SHEET    1   T 4 TYR D 363  THR D 368  0                                        
SHEET    2   T 4 ALA D 377  LEU D 382 -1  O  LYS D 381   N  GLU D 364           
SHEET    3   T 4 VAL D 419  MET D 424 -1  O  ILE D 423   N  VAL D 378           
SHEET    4   T 4 ALA D 408  THR D 410 -1  N  PHE D 409   O  VAL D 420           
SHEET    1   U 2 LEU E  14  ASP E  15  0                                        
SHEET    2   U 2 ALA E  20  LYS E  21 -1  O  ALA E  20   N  ASP E  15           
SHEET    1   V 4 VAL E 119  THR E 123  0                                        
SHEET    2   V 4 GLY E 285  TRP E 289 -1  O  TRP E 289   N  VAL E 119           
SHEET    3   V 4 VAL E 267  SER E 273 -1  N  ILE E 270   O  ILE E 288           
SHEET    4   V 4 MET E 240  ASP E 243  1  N  ILE E 242   O  SER E 271           
SHEET    1   W 3 GLU E 176  GLU E 179  0                                        
SHEET    2   W 3 ASN E 156  CYS E 159  1  N  LEU E 157   O  ARG E 178           
SHEET    3   W 3 THR E 202  VAL E 206  1  O  ILE E 203   N  ASN E 156           
SHEET    1   X 2 PHE E 301  TYR E 305  0                                        
SHEET    2   X 2 GLY E 308  THR E 312 -1  O  THR E 312   N  PHE E 301           
SHEET    1   Y 4 TYR E 363  THR E 368  0                                        
SHEET    2   Y 4 ALA E 377  LEU E 382 -1  O  LYS E 381   N  GLU E 364           
SHEET    3   Y 4 VAL E 419  MET E 424 -1  O  ILE E 423   N  VAL E 378           
SHEET    4   Y 4 ALA E 408  THR E 410 -1  N  PHE E 409   O  VAL E 420           
SHEET    1   Z 2 LEU F  14  ASP F  15  0                                        
SHEET    2   Z 2 ALA F  20  LYS F  21 -1  O  ALA F  20   N  ASP F  15           
SHEET    1  AA 4 VAL F 119  THR F 123  0                                        
SHEET    2  AA 4 GLY F 285  TRP F 289 -1  O  TRP F 289   N  VAL F 119           
SHEET    3  AA 4 VAL F 267  SER F 273 -1  N  ILE F 270   O  ILE F 288           
SHEET    4  AA 4 MET F 240  ASP F 243  1  N  MET F 240   O  LYS F 268           
SHEET    1  AB 3 GLU F 176  GLU F 179  0                                        
SHEET    2  AB 3 ASN F 156  CYS F 159  1  N  LEU F 157   O  ARG F 178           
SHEET    3  AB 3 THR F 202  VAL F 206  1  O  ILE F 203   N  ASN F 156           
SHEET    1  AC 2 PHE F 301  VAL F 303  0                                        
SHEET    2  AC 2 ILE F 310  THR F 312 -1  O  THR F 312   N  PHE F 301           
SHEET    1  AD 4 TYR F 363  THR F 368  0                                        
SHEET    2  AD 4 ALA F 377  LEU F 382 -1  O  LYS F 381   N  GLU F 364           
SHEET    3  AD 4 VAL F 419  MET F 424 -1  O  ILE F 423   N  VAL F 378           
SHEET    4  AD 4 ALA F 408  THR F 410 -1  N  PHE F 409   O  VAL F 420           
SITE     1 AC1 16 GLY A 125  SER A 126  SER A 127  GLN A 163                    
SITE     2 AC1 16 THR A 212  ASP A 243  ALA A 245  HIS A 275                    
SITE     3 AC1 16 LYS A 276  HIS A 465  THR A 466  HOH A3266                    
SITE     4 AC1 16 HOH A3314  HOH A3427  PHE B 317  SER B 318                    
SITE     1 AC2 16 PHE A 317  SER A 318  HOH A3307  GLY B 125                    
SITE     2 AC2 16 SER B 126  SER B 127  GLN B 163  THR B 212                    
SITE     3 AC2 16 ASP B 243  ALA B 245  SER B 273  HIS B 275                    
SITE     4 AC2 16 LYS B 276  HIS B 465  HOH B3316  HOH B3425                    
SITE     1 AC3 18 GLY C 125  SER C 126  SER C 127  GLN C 163                    
SITE     2 AC3 18 THR C 208  THR C 212  ASP C 243  ALA C 245                    
SITE     3 AC3 18 SER C 273  HIS C 275  LYS C 276  HIS C 465                    
SITE     4 AC3 18 THR C 466  HOH C3317  HOH C3326  PHE D 317                    
SITE     5 AC3 18 SER D 318  HOH D3310                                          
SITE     1 AC4 17 PHE C 317  SER C 318  HOH C3364  GLY D 125                    
SITE     2 AC4 17 SER D 126  SER D 127  GLN D 163  THR D 212                    
SITE     3 AC4 17 ASP D 243  ALA D 245  SER D 273  HIS D 275                    
SITE     4 AC4 17 LYS D 276  HIS D 465  THR D 466  HOH D3328                    
SITE     5 AC4 17 HOH D3422                                                     
SITE     1 AC5 16 SER E 126  SER E 127  GLN E 163  THR E 212                    
SITE     2 AC5 16 ASP E 243  ALA E 245  SER E 273  HIS E 275                    
SITE     3 AC5 16 LYS E 276  HIS E 465  THR E 466  HOH E3315                    
SITE     4 AC5 16 HOH E3319  PHE F 317  SER F 318  HOH F3295                    
SITE     1 AC6 17 PHE E 317  SER E 318  GLY F 125  SER F 126                    
SITE     2 AC6 17 SER F 127  GLN F 163  THR F 212  ASP F 243                    
SITE     3 AC6 17 ALA F 245  SER F 273  HIS F 275  LYS F 276                    
SITE     4 AC6 17 HIS F 465  THR F 466  HOH F3267  HOH F3313                    
SITE     5 AC6 17 HOH F3318                                                     
SITE     1 AC7 15 GLN A  65  THR A  66  TRP A  67  ASP A  69                    
SITE     2 AC7 15 VAL A  72  LEU A 279  ALA A 280  PRO A 281                    
SITE     3 AC7 15 GLU A 330  ARG A 427  HOH A3255  HOH A3305                    
SITE     4 AC7 15 HOH A3437  ILE B  80  ASN B  81                               
SITE     1 AC8 10 ILE A  80  ASN A  81  GLN B  65  TRP B  67                    
SITE     2 AC8 10 VAL B  72  LEU B 279  ALA B 280  PRO B 281                    
SITE     3 AC8 10 GLU B 330  ARG B 427                                          
SITE     1 AC9  9 ASN C  81  GLN D  65  TRP D  67  ASP D  69                    
SITE     2 AC9  9 VAL D  72  LEU D 279  GLU D 330  ARG D 427                    
SITE     3 AC9  9 HOH D3363                                                     
SITE     1 BC1 11 GLN E  65  THR E  66  TRP E  67  ASP E  69                    
SITE     2 BC1 11 VAL E  72  LEU E 279  ALA E 280  ARG E 427                    
SITE     3 BC1 11 HOH E3380  HOH E3437  ASN F  81                               
SITE     1 BC2 10 ASN E  81  GLN F  65  TRP F  67  VAL F  72                    
SITE     2 BC2 10 LEU F 279  ALA F 280  PRO F 281  GLU F 330                    
SITE     3 BC2 10 ARG F 427  HOH F3286                                          
SITE     1 BC3  9 VAL A 119  GLY A 120  THR A 121  VAL A 300                    
SITE     2 BC3  9 GLY A 311  PHE A 313  TRS A3251  HOH A3372                    
SITE     3 BC3  9 HOH A3438                                                     
SITE     1 BC4  8 TRP B  84  LYS B  87  ASP B  97  LEU B  98                    
SITE     2 BC4  8 GLY B 120  THR B 121  ASN B 122  HOH B3390                    
SITE     1 BC5  8 TRP C  84  LYS C  87  ASP C  97  GLY C 120                    
SITE     2 BC5  8 THR C 121  ASN C 122  THR C 312  HOH C3442                    
SITE     1 BC6 10 TRP D  84  ASP D  97  LEU D  98  VAL D 101                    
SITE     2 BC6 10 GLY D 120  THR D 121  ASN D 122  THR D 312                    
SITE     3 BC6 10 TRS D3245  HOH D3359                                          
SITE     1 BC7  7 VAL D 119  GLY D 120  THR D 121  GLY D 311                    
SITE     2 BC7  7 THR D 312  PHE D 313  TRS D3244                               
SITE     1 BC8 10 TRP E  84  LYS E  87  ASP E  97  LEU E  98                    
SITE     2 BC8 10 VAL E 101  GLY E 120  THR E 121  ASN E 122                    
SITE     3 BC8 10 THR E 312  TRS E3247                                          
SITE     1 BC9 10 VAL E 119  GLY E 120  LEU E 295  VAL E 300                    
SITE     2 BC9 10 GLY E 311  THR E 312  PHE E 313  TRS E3246                    
SITE     3 BC9 10 HOH E3342  HOH E3410                                          
SITE     1 CC1 10 TRP F  84  ASP F  97  LEU F  98  VAL F 101                    
SITE     2 CC1 10 GLY F 120  THR F 121  ASN F 122  GLY F 311                    
SITE     3 CC1 10 THR F 312  TRS F3249                                          
SITE     1 CC2 10 VAL F 119  GLY F 120  THR F 121  LEU F 295                    
SITE     2 CC2 10 GLY F 311  THR F 312  PHE F 313  TRS F3248                    
SITE     3 CC2 10 HOH F3423  HOH F3438                                          
SITE     1 CC3 10 GLN C  65  TRP C  67  ASP C  69  VAL C  72                    
SITE     2 CC3 10 LEU C 279  ALA C 280  PRO C 281  GLU C 330                    
SITE     3 CC3 10 HOH C3399  ASN D  81                                          
SITE     1 CC4 10 TRP A  84  ASP A  97  LEU A  98  VAL A 101                    
SITE     2 CC4 10 GLY A 120  THR A 121  ASN A 122  TRS A3241                    
SITE     3 CC4 10 HOH A3288  HOH A3439                                          
SITE     1 CC5  8 PRO A  91  GLN A  92  LEU B  52  GLN C  58                    
SITE     2 CC5  8 ARG C 402  LEU C 436  ASP C 440  HOH C3407                    
SITE     1 CC6  6 PRO E 184  GLY E 185  LEU E 187  GLU E 364                    
SITE     2 CC6  6 LYS E 381  ILE E 418                                          
CRYST1  115.995  115.995  207.350  90.00  90.00 120.00 P 32         18          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008621  0.004977  0.000000        0.00000                         
SCALE2      0.000000  0.009955  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004823        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system