GenomeNet

Database: PDB
Entry: 2R4E
LinkDB: 2R4E
Original site: 2R4E 
HEADER    OXIDOREDUCTASE                          31-AUG-07   2R4E              
TITLE     CRYSTAL STRUCTURE OF ESCHERICHIA COLI GLYCEROL-3-PHOSPHATE            
TITLE    2 DEHYDROGENASE IN COMPLEX WITH DHAP                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE;                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.1.99.5;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: GLPD, GLYD;                                                    
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    GLPD, CYTOPLASM, FAD, FLAVOPROTEIN, GLYCEROL METABOLISM,              
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.I.YEH,S.DU,U.CHINTE                                                 
REVDAT   2   24-FEB-09 2R4E    1       VERSN                                    
REVDAT   1   29-APR-08 2R4E    0                                                
JRNL        AUTH   J.I.YEH,U.CHINTE,S.DU                                        
JRNL        TITL   STRUCTURE OF GLYCEROL-3-PHOSPHATE DEHYDROGENASE,             
JRNL        TITL 2 AN ESSENTIAL MONOTOPIC MEMBRANE ENZYME INVOLVED IN           
JRNL        TITL 3 RESPIRATION AND METABOLISM.                                  
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 105  3280 2008              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   18296637                                                     
JRNL        DOI    10.1073/PNAS.0712331105                                      
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 68832                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.201                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3628                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4809                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.81                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2660                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 268                          
REMARK   3   BIN FREE R VALUE                    : 0.3620                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7906                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 363                                     
REMARK   3   SOLVENT ATOMS            : 263                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.94                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.78000                                              
REMARK   3    B22 (A**2) : 0.60000                                              
REMARK   3    B33 (A**2) : -1.38000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.210         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.193         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.145         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.444         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.921                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8447 ; 0.023 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11420 ; 2.163 ; 1.993       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   986 ; 6.954 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   390 ;31.193 ;22.821       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1378 ;17.921 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    76 ;17.912 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1218 ; 0.147 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6278 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3813 ; 0.220 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5503 ; 0.313 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   452 ; 0.134 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    18 ; 0.231 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.114 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5059 ; 1.321 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7854 ; 2.054 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3998 ; 3.064 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3566 ; 4.494 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      5       A     494      4                      
REMARK   3           1     B      5       B     494      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   3920 ;  0.34 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   3920 ;  0.68 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2R4E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-DEC-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB044410.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9803                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 78152                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.07800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.12                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M DI-AMMONIUM HYDROGEN                
REMARK 280  PHOSPHATE, 0.1M TAPS, 12% W/V PEG 6000, PH 8.5, VAPOR               
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277.0K                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       56.92400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       56.91100            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       96.56650            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       56.92400            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       56.91100            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       96.56650            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       56.92400            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       56.91100            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       96.56650            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       56.92400            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       56.91100            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       96.56650            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLN A   495                                                      
REMARK 465     ARG A   496                                                      
REMARK 465     LEU A   497                                                      
REMARK 465     SER A   498                                                      
REMARK 465     LEU A   499                                                      
REMARK 465     ALA A   500                                                      
REMARK 465     SER A   501                                                      
REMARK 465     GLN B   495                                                      
REMARK 465     ARG B   496                                                      
REMARK 465     LEU B   497                                                      
REMARK 465     SER B   498                                                      
REMARK 465     LEU B   499                                                      
REMARK 465     ALA B   500                                                      
REMARK 465     SER B   501                                                      
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    GLU A   2      -34.15     76.76                                   
REMARK 500    GLN A  35      -96.54   -126.64                                   
REMARK 500    ALA A  38       16.84     55.59                                   
REMARK 500    ALA A  40     -118.74   -119.14                                   
REMARK 500    ALA A  78       58.91   -140.49                                   
REMARK 500    HIS A  94       -8.61    -59.22                                   
REMARK 500    LYS A 113      122.56     86.22                                   
REMARK 500    THR A 115      -23.58    -28.87                                   
REMARK 500    SER A 116      -25.35   -155.24                                   
REMARK 500    ASP A 263       -8.47     62.04                                   
REMARK 500    ASP A 321       88.23    -68.41                                   
REMARK 500    GLN A 374     -128.11     20.63                                   
REMARK 500    TRP A 380      -10.20   -159.64                                   
REMARK 500    THR A 420      -63.93   -103.45                                   
REMARK 500    TRP A 459       19.42     56.38                                   
REMARK 500    GLN B  35      -98.77   -126.46                                   
REMARK 500    ALA B  38       17.27     55.90                                   
REMARK 500    ALA B  40     -115.88   -115.69                                   
REMARK 500    LYS B 113      -97.17      9.64                                   
REMARK 500    SER B 116      -43.86   -150.06                                   
REMARK 500    PRO B 118     -160.90    -45.14                                   
REMARK 500    SER B 120      116.20     89.86                                   
REMARK 500    ILE B 226      122.20     51.18                                   
REMARK 500    ASP B 263      -10.84     61.52                                   
REMARK 500    THR B 270     -155.52   -130.21                                   
REMARK 500    ASP B 325      -58.27    110.10                                   
REMARK 500    ASN B 342       36.77     71.28                                   
REMARK 500    PRO B 371      -31.92    -38.51                                   
REMARK 500    GLN B 374      -97.71    -24.20                                   
REMARK 500    TRP B 380       -6.43   -158.78                                   
REMARK 500    ASP B 396      -59.13    101.50                                   
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 BOG A 1949                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 1950                
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 1949                
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 1950                
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 1951                
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 1952                
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 1951                
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 1952                
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 1953                
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1953                
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1954                
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 600                 
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 600                 
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 13P A 1955                
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1954                
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1955                
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1956                
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1957                
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1956                
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 1957                
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1958                
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1959                
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1960                
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1958                
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1959                
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1961                
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD B 1960                
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1962                
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1961                
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T3A A 7066                
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T3A B 7066                
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 13P B 7067                
DBREF  2R4E A    1   501  UNP    P13035   GLPD_ECOLI       1    501             
DBREF  2R4E B    1   501  UNP    P13035   GLPD_ECOLI       1    501             
SEQRES   1 A  501  MET GLU THR LYS ASP LEU ILE VAL ILE GLY GLY GLY ILE          
SEQRES   2 A  501  ASN GLY ALA GLY ILE ALA ALA ASP ALA ALA GLY ARG GLY          
SEQRES   3 A  501  LEU SER VAL LEU MET LEU GLU ALA GLN ASP LEU ALA CYS          
SEQRES   4 A  501  ALA THR SER SER ALA SER SER LYS LEU ILE HIS GLY GLY          
SEQRES   5 A  501  LEU ARG TYR LEU GLU HIS TYR GLU PHE ARG LEU VAL SER          
SEQRES   6 A  501  GLU ALA LEU ALA GLU ARG GLU VAL LEU LEU LYS MET ALA          
SEQRES   7 A  501  PRO HIS ILE ALA PHE PRO MET ARG PHE ARG LEU PRO HIS          
SEQRES   8 A  501  ARG PRO HIS LEU ARG PRO ALA TRP MET ILE ARG ILE GLY          
SEQRES   9 A  501  LEU PHE MET TYR ASP HIS LEU GLY LYS ARG THR SER LEU          
SEQRES  10 A  501  PRO GLY SER THR GLY LEU ARG PHE GLY ALA ASN SER VAL          
SEQRES  11 A  501  LEU LYS PRO GLU ILE LYS ARG GLY PHE GLU TYR SER ASP          
SEQRES  12 A  501  CYS TRP VAL ASP ASP ALA ARG LEU VAL LEU ALA ASN ALA          
SEQRES  13 A  501  GLN MET VAL VAL ARG LYS GLY GLY GLU VAL LEU THR ARG          
SEQRES  14 A  501  THR ARG ALA THR SER ALA ARG ARG GLU ASN GLY LEU TRP          
SEQRES  15 A  501  ILE VAL GLU ALA GLU ASP ILE ASP THR GLY LYS LYS TYR          
SEQRES  16 A  501  SER TRP GLN ALA ARG GLY LEU VAL ASN ALA THR GLY PRO          
SEQRES  17 A  501  TRP VAL LYS GLN PHE PHE ASP ASP GLY MET HIS LEU PRO          
SEQRES  18 A  501  SER PRO TYR GLY ILE ARG LEU ILE LYS GLY SER HIS ILE          
SEQRES  19 A  501  VAL VAL PRO ARG VAL HIS THR GLN LYS GLN ALA TYR ILE          
SEQRES  20 A  501  LEU GLN ASN GLU ASP LYS ARG ILE VAL PHE VAL ILE PRO          
SEQRES  21 A  501  TRP MET ASP GLU PHE SER ILE ILE GLY THR THR ASP VAL          
SEQRES  22 A  501  GLU TYR LYS GLY ASP PRO LYS ALA VAL LYS ILE GLU GLU          
SEQRES  23 A  501  SER GLU ILE ASN TYR LEU LEU ASN VAL TYR ASN THR HIS          
SEQRES  24 A  501  PHE LYS LYS GLN LEU SER ARG ASP ASP ILE VAL TRP THR          
SEQRES  25 A  501  TYR SER GLY VAL ARG PRO LEU CYS ASP ASP GLU SER ASP          
SEQRES  26 A  501  SER PRO GLN ALA ILE THR ARG ASP TYR THR LEU ASP ILE          
SEQRES  27 A  501  HIS ASP GLU ASN GLY LYS ALA PRO LEU LEU SER VAL PHE          
SEQRES  28 A  501  GLY GLY LYS LEU THR THR TYR ARG LYS LEU ALA GLU HIS          
SEQRES  29 A  501  ALA LEU GLU LYS LEU THR PRO TYR TYR GLN GLY ILE GLY          
SEQRES  30 A  501  PRO ALA TRP THR LYS GLU SER VAL LEU PRO GLY GLY ALA          
SEQRES  31 A  501  ILE GLU GLY ASP ARG ASP ASP TYR ALA ALA ARG LEU ARG          
SEQRES  32 A  501  ARG ARG TYR PRO PHE LEU THR GLU SER LEU ALA ARG HIS          
SEQRES  33 A  501  TYR ALA ARG THR TYR GLY SER ASN SER GLU LEU LEU LEU          
SEQRES  34 A  501  GLY ASN ALA GLY THR VAL SER ASP LEU GLY GLU ASP PHE          
SEQRES  35 A  501  GLY HIS GLU PHE TYR GLU ALA GLU LEU LYS TYR LEU VAL          
SEQRES  36 A  501  ASP HIS GLU TRP VAL ARG ARG ALA ASP ASP ALA LEU TRP          
SEQRES  37 A  501  ARG ARG THR LYS GLN GLY MET TRP LEU ASN ALA ASP GLN          
SEQRES  38 A  501  GLN SER ARG VAL SER GLN TRP LEU VAL GLU TYR THR GLN          
SEQRES  39 A  501  GLN ARG LEU SER LEU ALA SER                                  
SEQRES   1 B  501  MET GLU THR LYS ASP LEU ILE VAL ILE GLY GLY GLY ILE          
SEQRES   2 B  501  ASN GLY ALA GLY ILE ALA ALA ASP ALA ALA GLY ARG GLY          
SEQRES   3 B  501  LEU SER VAL LEU MET LEU GLU ALA GLN ASP LEU ALA CYS          
SEQRES   4 B  501  ALA THR SER SER ALA SER SER LYS LEU ILE HIS GLY GLY          
SEQRES   5 B  501  LEU ARG TYR LEU GLU HIS TYR GLU PHE ARG LEU VAL SER          
SEQRES   6 B  501  GLU ALA LEU ALA GLU ARG GLU VAL LEU LEU LYS MET ALA          
SEQRES   7 B  501  PRO HIS ILE ALA PHE PRO MET ARG PHE ARG LEU PRO HIS          
SEQRES   8 B  501  ARG PRO HIS LEU ARG PRO ALA TRP MET ILE ARG ILE GLY          
SEQRES   9 B  501  LEU PHE MET TYR ASP HIS LEU GLY LYS ARG THR SER LEU          
SEQRES  10 B  501  PRO GLY SER THR GLY LEU ARG PHE GLY ALA ASN SER VAL          
SEQRES  11 B  501  LEU LYS PRO GLU ILE LYS ARG GLY PHE GLU TYR SER ASP          
SEQRES  12 B  501  CYS TRP VAL ASP ASP ALA ARG LEU VAL LEU ALA ASN ALA          
SEQRES  13 B  501  GLN MET VAL VAL ARG LYS GLY GLY GLU VAL LEU THR ARG          
SEQRES  14 B  501  THR ARG ALA THR SER ALA ARG ARG GLU ASN GLY LEU TRP          
SEQRES  15 B  501  ILE VAL GLU ALA GLU ASP ILE ASP THR GLY LYS LYS TYR          
SEQRES  16 B  501  SER TRP GLN ALA ARG GLY LEU VAL ASN ALA THR GLY PRO          
SEQRES  17 B  501  TRP VAL LYS GLN PHE PHE ASP ASP GLY MET HIS LEU PRO          
SEQRES  18 B  501  SER PRO TYR GLY ILE ARG LEU ILE LYS GLY SER HIS ILE          
SEQRES  19 B  501  VAL VAL PRO ARG VAL HIS THR GLN LYS GLN ALA TYR ILE          
SEQRES  20 B  501  LEU GLN ASN GLU ASP LYS ARG ILE VAL PHE VAL ILE PRO          
SEQRES  21 B  501  TRP MET ASP GLU PHE SER ILE ILE GLY THR THR ASP VAL          
SEQRES  22 B  501  GLU TYR LYS GLY ASP PRO LYS ALA VAL LYS ILE GLU GLU          
SEQRES  23 B  501  SER GLU ILE ASN TYR LEU LEU ASN VAL TYR ASN THR HIS          
SEQRES  24 B  501  PHE LYS LYS GLN LEU SER ARG ASP ASP ILE VAL TRP THR          
SEQRES  25 B  501  TYR SER GLY VAL ARG PRO LEU CYS ASP ASP GLU SER ASP          
SEQRES  26 B  501  SER PRO GLN ALA ILE THR ARG ASP TYR THR LEU ASP ILE          
SEQRES  27 B  501  HIS ASP GLU ASN GLY LYS ALA PRO LEU LEU SER VAL PHE          
SEQRES  28 B  501  GLY GLY LYS LEU THR THR TYR ARG LYS LEU ALA GLU HIS          
SEQRES  29 B  501  ALA LEU GLU LYS LEU THR PRO TYR TYR GLN GLY ILE GLY          
SEQRES  30 B  501  PRO ALA TRP THR LYS GLU SER VAL LEU PRO GLY GLY ALA          
SEQRES  31 B  501  ILE GLU GLY ASP ARG ASP ASP TYR ALA ALA ARG LEU ARG          
SEQRES  32 B  501  ARG ARG TYR PRO PHE LEU THR GLU SER LEU ALA ARG HIS          
SEQRES  33 B  501  TYR ALA ARG THR TYR GLY SER ASN SER GLU LEU LEU LEU          
SEQRES  34 B  501  GLY ASN ALA GLY THR VAL SER ASP LEU GLY GLU ASP PHE          
SEQRES  35 B  501  GLY HIS GLU PHE TYR GLU ALA GLU LEU LYS TYR LEU VAL          
SEQRES  36 B  501  ASP HIS GLU TRP VAL ARG ARG ALA ASP ASP ALA LEU TRP          
SEQRES  37 B  501  ARG ARG THR LYS GLN GLY MET TRP LEU ASN ALA ASP GLN          
SEQRES  38 B  501  GLN SER ARG VAL SER GLN TRP LEU VAL GLU TYR THR GLN          
SEQRES  39 B  501  GLN ARG LEU SER LEU ALA SER                                  
HET    BOG  A1949      20                                                       
HET    BOG  A1950      20                                                       
HET    BOG  B1949      20                                                       
HET    BOG  B1950      20                                                       
HET    BOG  A1951      20                                                       
HET    BOG  A1952      20                                                       
HET    PO4  B1951       5                                                       
HET    PO4  B1952       5                                                       
HET    PO4  B1953       5                                                       
HET    PO4  A1953       5                                                       
HET    PO4  A1954       5                                                       
HET    FAD  A 600      53                                                       
HET    FAD  B 600      53                                                       
HET    13P  A1955      10                                                       
HET    EDO  B1954       4                                                       
HET    EDO  B1955       4                                                       
HET    EDO  B1956       4                                                       
HET    EDO  B1957       4                                                       
HET    EDO  A1956       4                                                       
HET    IMD  A1957       5                                                       
HET    EDO  A1958       4                                                       
HET    EDO  A1959       4                                                       
HET    EDO  A1960       4                                                       
HET    EDO  B1958       4                                                       
HET    EDO  B1959       4                                                       
HET    EDO  A1961       4                                                       
HET    IMD  B1960       5                                                       
HET    EDO  A1962       4                                                       
HET    EDO  B1961       4                                                       
HET    T3A  A7066      15                                                       
HET    T3A  B7066      15                                                       
HET    13P  B7067      10                                                       
HETNAM     BOG B-OCTYLGLUCOSIDE                                                 
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     13P 1,3-DIHYDROXYACETONEPHOSPHATE                                    
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     IMD IMIDAZOLE                                                        
HETNAM     T3A N-(TRIS(HYDROXYMETHYL)METHYL)-3-AMINOPROPANESULFONIC             
HETNAM   2 T3A  ACID                                                            
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  BOG    6(C14 H28 O6)                                                
FORMUL   9  PO4    5(O4 P 3-)                                                   
FORMUL  14  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL  16  13P    2(C3 H7 O6 P)                                                
FORMUL  17  EDO    13(C2 H6 O2)                                                 
FORMUL  22  IMD    2(C3 H5 N2 1+)                                               
FORMUL  32  T3A    2(C7 H17 N O6 S)                                             
FORMUL  35  HOH   *263(H2 O)                                                    
HELIX    1   1 GLY A   12  GLY A   24  1                                  13    
HELIX    2   2 ALA A   40  ALA A   44  5                                   5    
HELIX    3   3 GLY A   52  TYR A   59  5                                   8    
HELIX    4   4 GLU A   60  ALA A   78  1                                  19    
HELIX    5   5 PRO A   97  LEU A  111  1                                  15    
HELIX    6   6 ASP A  147  LYS A  162  1                                  16    
HELIX    7   7 THR A  206  PRO A  208  5                                   3    
HELIX    8   8 TRP A  209  GLY A  217  1                                   9    
HELIX    9   9 ASP A  278  VAL A  282  5                                   5    
HELIX   10  10 GLU A  285  PHE A  300  1                                  16    
HELIX   11  11 SER A  305  ILE A  309  5                                   5    
HELIX   12  12 SER A  326  ILE A  330  5                                   5    
HELIX   13  13 LYS A  354  THR A  356  5                                   3    
HELIX   14  14 THR A  357  THR A  370  1                                  14    
HELIX   15  15 PRO A  371  TYR A  373  5                                   3    
HELIX   16  16 TRP A  380  SER A  384  5                                   5    
HELIX   17  17 ASP A  394  TYR A  406  1                                  13    
HELIX   18  18 THR A  410  TYR A  421  1                                  12    
HELIX   19  19 ASN A  424  GLY A  430  1                                   7    
HELIX   20  20 VAL A  435  GLY A  439  5                                   5    
HELIX   21  21 TYR A  447  GLU A  458  1                                  12    
HELIX   22  22 ARG A  462  ARG A  469  1                                   8    
HELIX   23  23 LYS A  472  TRP A  476  5                                   5    
HELIX   24  24 ASN A  478  THR A  493  1                                  16    
HELIX   25  25 GLY B   12  GLY B   24  1                                  13    
HELIX   26  26 ALA B   40  ALA B   44  5                                   5    
HELIX   27  27 GLY B   52  TYR B   59  5                                   8    
HELIX   28  28 GLU B   60  ALA B   78  1                                  19    
HELIX   29  29 PRO B   97  LEU B  111  1                                  15    
HELIX   30  30 ASP B  147  LYS B  162  1                                  16    
HELIX   31  31 THR B  206  PRO B  208  5                                   3    
HELIX   32  32 TRP B  209  GLY B  217  1                                   9    
HELIX   33  33 ASP B  278  VAL B  282  5                                   5    
HELIX   34  34 GLU B  285  PHE B  300  1                                  16    
HELIX   35  35 SER B  305  ILE B  309  5                                   5    
HELIX   36  36 SER B  326  ILE B  330  5                                   5    
HELIX   37  37 LYS B  354  THR B  356  5                                   3    
HELIX   38  38 THR B  357  THR B  370  1                                  14    
HELIX   39  39 PRO B  371  TYR B  373  5                                   3    
HELIX   40  40 TRP B  380  SER B  384  5                                   5    
HELIX   41  41 ASP B  396  TYR B  406  1                                  11    
HELIX   42  42 THR B  410  TYR B  421  1                                  12    
HELIX   43  43 ASN B  424  GLY B  430  1                                   7    
HELIX   44  44 VAL B  435  GLY B  439  5                                   5    
HELIX   45  45 TYR B  447  GLU B  458  1                                  12    
HELIX   46  46 ARG B  462  ARG B  469  1                                   8    
HELIX   47  47 LYS B  472  TRP B  476  5                                   5    
HELIX   48  48 ASN B  478  GLN B  494  1                                  17    
SHEET    1   A 6 GLU A 165  LEU A 167  0                                        
SHEET    2   A 6 VAL A  29  LEU A  32  1  N  VAL A  29   O  GLU A 165           
SHEET    3   A 6 THR A   3  ILE A   9  1  N  VAL A   8   O  LEU A  32           
SHEET    4   A 6 LYS A 194  ASN A 204  1  O  VAL A 203   N  ILE A   7           
SHEET    5   A 6 LEU A 181  ASP A 188 -1  N  TRP A 182   O  ALA A 199           
SHEET    6   A 6 THR A 170  GLU A 178 -1  N  GLU A 178   O  LEU A 181           
SHEET    1   B 6 GLU A 165  LEU A 167  0                                        
SHEET    2   B 6 VAL A  29  LEU A  32  1  N  VAL A  29   O  GLU A 165           
SHEET    3   B 6 THR A   3  ILE A   9  1  N  VAL A   8   O  LEU A  32           
SHEET    4   B 6 LYS A 194  ASN A 204  1  O  VAL A 203   N  ILE A   7           
SHEET    5   B 6 LYS A 344  PHE A 351  1  O  LEU A 348   N  ASN A 204           
SHEET    6   B 6 THR A 335  GLU A 341 -1  N  THR A 335   O  PHE A 351           
SHEET    1   C 8 LEU A  48  ILE A  49  0                                        
SHEET    2   C 8 ARG A 137  VAL A 146 -1  O  CYS A 144   N  ILE A  49           
SHEET    3   C 8 ALA A  82  PRO A  90 -1  N  PHE A  83   O  TRP A 145           
SHEET    4   C 8 ALA A 245  GLN A 249  1  O  ALA A 245   N  ARG A  88           
SHEET    5   C 8 ILE A 255  TRP A 261 -1  O  VAL A 256   N  LEU A 248           
SHEET    6   C 8 PHE A 265  GLY A 269 -1  O  ILE A 267   N  ILE A 259           
SHEET    7   C 8 ILE A 226  PRO A 237 -1  N  ILE A 234   O  ILE A 268           
SHEET    8   C 8 VAL A 273  GLU A 274 -1  O  VAL A 273   N  LYS A 230           
SHEET    1   D 8 THR A 121  ARG A 124  0                                        
SHEET    2   D 8 ARG A 137  VAL A 146 -1  O  GLU A 140   N  THR A 121           
SHEET    3   D 8 ALA A  82  PRO A  90 -1  N  PHE A  83   O  TRP A 145           
SHEET    4   D 8 ALA A 245  GLN A 249  1  O  ALA A 245   N  ARG A  88           
SHEET    5   D 8 ILE A 255  TRP A 261 -1  O  VAL A 256   N  LEU A 248           
SHEET    6   D 8 PHE A 265  GLY A 269 -1  O  ILE A 267   N  ILE A 259           
SHEET    7   D 8 ILE A 226  PRO A 237 -1  N  ILE A 234   O  ILE A 268           
SHEET    8   D 8 TRP A 311  CYS A 320 -1  O  LEU A 319   N  ARG A 227           
SHEET    1   E 6 GLU B 165  LEU B 167  0                                        
SHEET    2   E 6 VAL B  29  LEU B  32  1  N  MET B  31   O  LEU B 167           
SHEET    3   E 6 THR B   3  ILE B   9  1  N  VAL B   8   O  LEU B  32           
SHEET    4   E 6 LYS B 194  ASN B 204  1  O  VAL B 203   N  ILE B   7           
SHEET    5   E 6 LEU B 181  ASP B 188 -1  N  TRP B 182   O  ALA B 199           
SHEET    6   E 6 THR B 170  GLU B 178 -1  N  GLU B 178   O  LEU B 181           
SHEET    1   F 6 GLU B 165  LEU B 167  0                                        
SHEET    2   F 6 VAL B  29  LEU B  32  1  N  MET B  31   O  LEU B 167           
SHEET    3   F 6 THR B   3  ILE B   9  1  N  VAL B   8   O  LEU B  32           
SHEET    4   F 6 LYS B 194  ASN B 204  1  O  VAL B 203   N  ILE B   7           
SHEET    5   F 6 LYS B 344  PHE B 351  1  O  LEU B 348   N  ASN B 204           
SHEET    6   F 6 THR B 335  GLU B 341 -1  N  THR B 335   O  PHE B 351           
SHEET    1   G 8 LEU B  48  ILE B  49  0                                        
SHEET    2   G 8 ARG B 137  VAL B 146 -1  O  CYS B 144   N  ILE B  49           
SHEET    3   G 8 ALA B  82  PRO B  90 -1  N  PHE B  87   O  TYR B 141           
SHEET    4   G 8 ALA B 245  GLN B 249  1  O  ILE B 247   N  ARG B  88           
SHEET    5   G 8 ILE B 255  TRP B 261 -1  O  VAL B 256   N  LEU B 248           
SHEET    6   G 8 PHE B 265  GLY B 269 -1  O  PHE B 265   N  TRP B 261           
SHEET    7   G 8 ARG B 227  PRO B 237 -1  N  ILE B 234   O  ILE B 268           
SHEET    8   G 8 VAL B 273  GLU B 274 -1  O  VAL B 273   N  LYS B 230           
SHEET    1   H 8 THR B 121  ARG B 124  0                                        
SHEET    2   H 8 ARG B 137  VAL B 146 -1  O  GLU B 140   N  THR B 121           
SHEET    3   H 8 ALA B  82  PRO B  90 -1  N  PHE B  87   O  TYR B 141           
SHEET    4   H 8 ALA B 245  GLN B 249  1  O  ILE B 247   N  ARG B  88           
SHEET    5   H 8 ILE B 255  TRP B 261 -1  O  VAL B 256   N  LEU B 248           
SHEET    6   H 8 PHE B 265  GLY B 269 -1  O  PHE B 265   N  TRP B 261           
SHEET    7   H 8 ARG B 227  PRO B 237 -1  N  ILE B 234   O  ILE B 268           
SHEET    8   H 8 TRP B 311  LEU B 319 -1  O  LEU B 319   N  ARG B 227           
CISPEP   1 MET A    1    GLU A    2          0        10.92                     
CISPEP   2 GLY A  269    THR A  270          0         8.72                     
CISPEP   3 LYS B  113    ARG B  114          0       -10.40                     
CISPEP   4 PRO B  118    GLY B  119          0         0.84                     
CISPEP   5 GLY B  269    THR B  270          0        -3.12                     
CISPEP   6 GLY B  377    PRO B  378          0        -1.15                     
CISPEP   7 GLU B  392    GLY B  393          0         3.31                     
SITE     1 AC1  5 TRP A  99  ARG A 102  ARG A 137  BOG A1952                    
SITE     2 AC1  5 HIS B  58                                                     
SITE     1 AC2  8 LEU A  53  ARG A  54  GLU A  57  ARG A  96                    
SITE     2 AC2  8 ILE A 101  GLY A 104  LEU A 105  MET A 107                    
SITE     1 AC3  3 TRP B  99  ARG B 102  ARG B 137                               
SITE     1 AC4 10 LEU B  53  ARG B  54  LEU B  56  GLU B  57                    
SITE     2 AC4 10 TYR B  59  PHE B  61  LEU B  89  ARG B  96                    
SITE     3 AC4 10 ILE B 101  LEU B 105                                          
SITE     1 AC5  1 TRP A  99                                                     
SITE     1 AC6  6 HIS A  91  PRO A  93  ALA A  98  ARG A 137                    
SITE     2 AC6  6 BOG A1949  ASP B 322                                          
SITE     1 AC7  5 ARG A 161  TYR B 398  ARG B 401  LEU B 402                    
SITE     2 AC7  5 ARG B 405                                                     
SITE     1 AC8  6 PRO B 208  GLN B 212  LEU B 228  GLY B 277                    
SITE     2 AC8  6 PRO B 279  HOH B7152                                          
SITE     1 AC9  3 ARG B  92  PRO B  93  HIS B  94                               
SITE     1 BC1  5 TYR A 398  ARG A 401  LEU A 402  ARG A 405                    
SITE     2 BC1  5 ARG B 161                                                     
SITE     1 BC2  8 PRO A 208  TRP A 209  GLN A 212  LEU A 228                    
SITE     2 BC2  8 GLY A 277  PRO A 279  HOH A7121  HOH A7123                    
SITE     1 BC3 34 ILE A   9  GLY A  10  GLY A  11  GLY A  12                    
SITE     2 BC3 34 ILE A  13  ASN A  14  LEU A  32  GLU A  33                    
SITE     3 BC3 34 ALA A  34  CYS A  39  ALA A  40  THR A  41                    
SITE     4 BC3 34 SER A  42  ALA A  44  SER A  45  SER A  46                    
SITE     5 BC3 34 LYS A  47  LEU A  48  ALA A 172  THR A 206                    
SITE     6 BC3 34 GLY A 207  PRO A 208  TRP A 209  GLY A 231                    
SITE     7 BC3 34 THR A 270  ARG A 317  GLY A 353  LYS A 354                    
SITE     8 BC3 34 LEU A 355  THR A 356  EDO A1956  HOH A7067                    
SITE     9 BC3 34 HOH A7071  HOH A7159                                          
SITE     1 BC4 33 ILE B   9  GLY B  10  GLY B  11  GLY B  12                    
SITE     2 BC4 33 ILE B  13  ASN B  14  GLU B  33  ALA B  34                    
SITE     3 BC4 33 CYS B  39  ALA B  40  THR B  41  SER B  42                    
SITE     4 BC4 33 ALA B  44  SER B  45  SER B  46  LYS B  47                    
SITE     5 BC4 33 LEU B  48  HIS B  50  ALA B 172  ALA B 205                    
SITE     6 BC4 33 THR B 206  GLY B 207  PRO B 208  PHE B 213                    
SITE     7 BC4 33 GLY B 231  ARG B 317  GLY B 353  LYS B 354                    
SITE     8 BC4 33 LEU B 355  THR B 356  HOH B7068  HOH B7072                    
SITE     9 BC4 33 HOH B7158                                                     
SITE     1 BC5  9 ARG A  54  TYR A  55  ARG A 254  ILE A 255                    
SITE     2 BC5  9 THR A 270  ASP A 272  ARG A 317  ARG A 332                    
SITE     3 BC5  9 HOH A7138                                                     
SITE     1 BC6  5 HOH A7115  ARG B 254  THR B 271  ASP B 272                    
SITE     2 BC6  5 HOH B7123                                                     
SITE     1 BC7  3 ALA B  34  ARG B 171  TRP B 209                               
SITE     1 BC8  1 TRP B 311                                                     
SITE     1 BC9  6 SER B  43  TRP B 311  TRP B 468  ARG B 469                    
SITE     2 BC9  6 HOH B7083  HOH B7156                                          
SITE     1 CC1  4 ALA A  34  CYS A  39  LYS A 280  FAD A 600                    
SITE     1 CC2  4 HIS A 416  HIS A 444  GLU A 445  GLN A 473                    
SITE     1 CC3  5 SER A  43  TRP A 468  ARG A 469  HOH A7080                    
SITE     2 CC3  5 HOH A7165                                                     
SITE     1 CC4  2 TRP A 311  TRP A 468                                          
SITE     1 CC5  6 ARG A 254  THR A 271  ASP A 272  VAL A 273                    
SITE     2 CC5  6 TYR A 291  SER B 287                                          
SITE     1 CC6  1 VAL B 385                                                     
SITE     1 CC7  2 VAL B 310  HOH B7168                                          
SITE     1 CC8  5 LYS A 162  TRP A 380  SER A 384  VAL A 385                    
SITE     2 CC8  5 GLU B 392                                                     
SITE     1 CC9  3 TRP B 488  GLU B 491  TYR B 492                               
SITE     1 DC1  5 GLN A 157  ARG A 161  ASN A 424  T3A A7066                    
SITE     2 DC1  5 ARG B 405                                                     
SITE     1 DC2  7 ARG A 405  GLU A 426  GLN B 157  ARG B 161                    
SITE     2 DC2  7 PRO B 387  ASN B 424  T3A B7066                               
SITE     1 DC3  9 GLN A 157  VAL A 160  VAL A 455  ASP A 456                    
SITE     2 DC3  9 HIS A 457  GLU A 458  TRP A 459  EDO A1962                    
SITE     3 DC3  9 ARG B 405                                                     
SITE     1 DC4  9 ARG A 405  GLN B 157  VAL B 160  VAL B 455                    
SITE     2 DC4  9 ASP B 456  HIS B 457  GLU B 458  TRP B 459                    
SITE     3 DC4  9 EDO B1961                                                     
SITE     1 DC5 10 ARG B  54  TYR B  55  ARG B 254  ILE B 255                    
SITE     2 DC5 10 THR B 270  ASP B 272  ARG B 317  ARG B 332                    
SITE     3 DC5 10 HOH B7139  HOH B7169                                          
CRYST1  113.848  113.822  193.133  90.00  90.00  90.00 I 2 2 2      16          
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      0.008784  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008786  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005178        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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