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Database: PDB
Entry: 2R46
LinkDB: 2R46
Original site: 2R46 
HEADER    OXIDOREDUCTASE                          30-AUG-07   2R46              
TITLE     CRYSTAL STRUCTURE OF ESCHERICHIA COLI GLYCEROL-3-PHOSPHATE            
TITLE    2 DEHYDROGENASE IN COMPLEX WITH 2-PHOSPHOPYRUVIC ACID.                 
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 2R46    1       VERSN                                    
REVDAT   1   29-APR-08 2R46    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)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 69138                          
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) : 0.193                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3671                            
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) : 4912                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2420                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 241                          
REMARK   3   BIN FREE R VALUE                    : 0.3080                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7924                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 349                                     
REMARK   3   SOLVENT ATOMS            : 385                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.58                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.52000                                              
REMARK   3    B22 (A**2) : 0.53000                                              
REMARK   3    B33 (A**2) : -1.05000                                             
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): 0.204         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.174         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.123         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.557         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.946                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8338 ; 0.024 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11313 ; 2.512 ; 1.972       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   999 ; 9.302 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   394 ;32.382 ;22.792       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1400 ;20.349 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    78 ;16.593 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1204 ; 0.208 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6350 ; 0.011 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4380 ; 0.282 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5517 ; 0.316 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   575 ; 0.227 ; 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):    35 ; 0.221 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     9 ; 0.227 ; 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):  5142 ; 1.345 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7967 ; 2.057 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3809 ; 3.028 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3346 ; 4.444 ; 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     495      4                      
REMARK   3           1     B      5       B     495      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   3929 ; 0.470 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   3929 ; 0.940 ; 2.000           
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 2R46 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-APR-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB044402.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-APR-07                          
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          : HKLL-2000                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 73532                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.890                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 9.900                              
REMARK 200  R MERGE                    (I) : 0.09900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50100                            
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   (%): 55.26                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M DI-AMMONIUM HYDROGEN               
REMARK 280  PHOSPHATE, 0.1 M 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       56.91150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       56.96850            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       96.37000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       56.91150            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       56.96850            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       96.37000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       56.91150            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       56.96850            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       96.37000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       56.91150            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       56.96850            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       96.37000            
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     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     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    GLN A  35      -97.78   -126.20                                   
REMARK 500    ALA A  40     -123.33   -109.85                                   
REMARK 500    ASP A 143     -176.09   -178.41                                   
REMARK 500    LYS A 162       50.08   -112.10                                   
REMARK 500    ASP A 263       -6.73     59.14                                   
REMARK 500    ASP A 321       99.58    -58.11                                   
REMARK 500    GLN A 374     -117.02    -18.29                                   
REMARK 500    TRP A 380      -23.29   -166.96                                   
REMARK 500    ILE A 391     -161.24   -113.52                                   
REMARK 500    ASP A 394      -75.35    112.97                                   
REMARK 500    ASP A 396      -36.89    -32.47                                   
REMARK 500    ASP A 397      -64.26   -139.96                                   
REMARK 500    TYR A 406       72.68   -115.80                                   
REMARK 500    THR A 420      -61.02   -109.22                                   
REMARK 500    ARG A 469      -57.03   -120.02                                   
REMARK 500    GLN A 494      -80.48    -73.59                                   
REMARK 500    GLU B   2      -42.24    -26.26                                   
REMARK 500    THR B   3      101.99    -48.84                                   
REMARK 500    GLN B  35     -107.69   -126.43                                   
REMARK 500    ALA B  40     -121.38   -113.80                                   
REMARK 500    LYS B 113      -72.21    -47.67                                   
REMARK 500    ARG B 114       86.84     62.85                                   
REMARK 500    SER B 116      -46.22   -139.25                                   
REMARK 500    ARG B 238      125.94    -34.80                                   
REMARK 500    ASP B 263       -9.51     59.71                                   
REMARK 500    THR B 270     -158.67   -129.66                                   
REMARK 500    ASP B 321       95.10    -58.41                                   
REMARK 500    GLU B 323       35.59     73.87                                   
REMARK 500    TRP B 380      -22.85   -162.90                                   
REMARK 500    ILE B 391     -106.10   -115.79                                   
REMARK 500    GLU B 392       49.07    140.33                                   
REMARK 500    ASP B 394      -91.88    120.74                                   
REMARK 500    ASP B 396       67.80    -40.65                                   
REMARK 500    ASP B 397      -12.43     67.11                                   
REMARK 500    TYR B 406       75.25   -113.02                                   
REMARK 500    SER B 423       -9.93    -59.13                                   
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 900                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 900                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 800                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 800                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 1949                
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 901                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 902                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 903                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 904                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1950                
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1951                
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 905                 
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1953                
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1954                
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1955                
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1956                
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 907                 
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 908                 
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1957                
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T3A A 7066                
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T3A B 7066                
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 7067                
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 7067                
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 7068                
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 7069                
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD B 7068                
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 600                 
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 600                 
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEP A 700                 
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEP B 700                 
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 7070                
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 7069                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2R45   RELATED DB: PDB                                   
DBREF  2R46 A    1   501  UNP    P13035   GLPD_ECOLI       1    501             
DBREF  2R46 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  A 900      20                                                       
HET    BOG  A 800      20                                                       
HET    BOG  A1949      20                                                       
HET    BOG  B 900      20                                                       
HET    BOG  B 800      20                                                       
HET    EDO  A1950       4                                                       
HET    EDO  A1951       4                                                       
HET    EDO  A1952       4                                                       
HET    EDO  A1953       4                                                       
HET    EDO  A1954       4                                                       
HET    EDO  A1955       4                                                       
HET    EDO  A1956       4                                                       
HET    EDO  A1957       4                                                       
HET    T3A  A7066      15                                                       
HET    EDO  A7067       4                                                       
HET    EDO  A7068       4                                                       
HET    EDO  A7069       4                                                       
HET    FAD  A 600      53                                                       
HET    PEP  A 700      10                                                       
HET    EDO  A7070       4                                                       
HET    EDO  B 901       4                                                       
HET    EDO  B 902       4                                                       
HET    EDO  B 903       4                                                       
HET    EDO  B 904       4                                                       
HET    EDO  B 905       4                                                       
HET    EDO  B 906       4                                                       
HET    EDO  B 907       4                                                       
HET    EDO  B 908       4                                                       
HET    T3A  B7066      15                                                       
HET    EDO  B7067       4                                                       
HET    IMD  B7068       5                                                       
HET    FAD  B 600      53                                                       
HET    PEP  B 700      10                                                       
HET    EDO  B7069       4                                                       
HETNAM     BOG B-OCTYLGLUCOSIDE                                                 
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     T3A N-(TRIS(HYDROXYMETHYL)METHYL)-3-AMINOPROPANESULFONIC             
HETNAM   2 T3A  ACID                                                            
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     PEP PHOSPHOENOLPYRUVATE                                              
HETNAM     IMD IMIDAZOLE                                                        
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  BOG    5(C14 H28 O6)                                                
FORMUL   8  EDO    22(C2 H6 O2)                                                 
FORMUL  16  T3A    2(C7 H17 N O6 S)                                             
FORMUL  20  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL  21  PEP    2(C3 H5 O6 P)                                                
FORMUL  33  IMD    C3 H5 N2 1+                                                  
FORMUL  37  HOH   *385(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 GLU A  285  PHE A  300  1                                  16    
HELIX   10  10 SER A  305  ILE A  309  5                                   5    
HELIX   11  11 SER A  326  ILE A  330  5                                   5    
HELIX   12  12 THR A  357  THR A  370  1                                  14    
HELIX   13  13 PRO A  371  TYR A  373  5                                   3    
HELIX   14  14 TRP A  380  SER A  384  5                                   5    
HELIX   15  15 ASP A  397  TYR A  406  1                                  10    
HELIX   16  16 THR A  410  TYR A  421  1                                  12    
HELIX   17  17 ASN A  424  GLY A  430  1                                   7    
HELIX   18  18 THR A  434  GLY A  439  5                                   6    
HELIX   19  19 TYR A  447  GLU A  458  1                                  12    
HELIX   20  20 ARG A  462  ARG A  469  1                                   8    
HELIX   21  21 LYS A  472  TRP A  476  5                                   5    
HELIX   22  22 ASN A  478  GLN A  495  1                                  18    
HELIX   23  23 GLY B   12  GLY B   24  1                                  13    
HELIX   24  24 ALA B   40  ALA B   44  5                                   5    
HELIX   25  25 GLY B   52  TYR B   59  5                                   8    
HELIX   26  26 GLU B   60  ALA B   78  1                                  19    
HELIX   27  27 PRO B   97  LEU B  111  1                                  15    
HELIX   28  28 ASP B  147  LYS B  162  1                                  16    
HELIX   29  29 THR B  206  PRO B  208  5                                   3    
HELIX   30  30 TRP B  209  GLY B  217  1                                   9    
HELIX   31  31 ASP B  278  VAL B  282  5                                   5    
HELIX   32  32 GLU B  285  PHE B  300  1                                  16    
HELIX   33  33 SER B  305  ILE B  309  5                                   5    
HELIX   34  34 SER B  326  ILE B  330  5                                   5    
HELIX   35  35 LYS B  354  THR B  356  5                                   3    
HELIX   36  36 THR B  357  THR B  370  1                                  14    
HELIX   37  37 PRO B  371  TYR B  373  5                                   3    
HELIX   38  38 TRP B  380  SER B  384  5                                   5    
HELIX   39  39 ASP B  397  TYR B  406  1                                  10    
HELIX   40  40 THR B  410  TYR B  421  1                                  12    
HELIX   41  41 ASN B  424  GLY B  430  1                                   7    
HELIX   42  42 THR B  434  GLY B  439  5                                   6    
HELIX   43  43 TYR B  447  GLU B  458  1                                  12    
HELIX   44  44 ARG B  462  ARG B  469  1                                   8    
HELIX   45  45 LYS B  472  TRP B  476  5                                   5    
HELIX   46  46 ASN B  478  GLN B  494  1                                  17    
SHEET    1   A 4 THR A   3  LYS A   4  0                                        
SHEET    2   A 4 LYS A 194  ALA A 199  1  O  GLN A 198   N  LYS A   4           
SHEET    3   A 4 LEU A 181  ASP A 188 -1  N  TRP A 182   O  ALA A 199           
SHEET    4   A 4 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  MET A  31   O  LEU A 167           
SHEET    3   B 6 LEU A   6  ILE A   9  1  N  VAL A   8   O  LEU A  32           
SHEET    4   B 6 LEU A 202  ASN A 204  1  O  VAL A 203   N  ILE A   9           
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  GLU A 341   O  LYS A 344           
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  LEU A  89   O  PHE A 139           
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  GLY A 269   N  PHE A 257           
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  GLY A 138   N  LEU A 123           
SHEET    3   D 8 ALA A  82  PRO A  90 -1  N  LEU A  89   O  PHE A 139           
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  GLY A 269   N  PHE A 257           
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  TRP A 311   N  VAL A 235           
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  GLU B 165           
SHEET    3   E 6 LYS B   4  ILE B   9  1  N  VAL B   8   O  LEU B  30           
SHEET    4   E 6 LYS B 194  ASN B 204  1  O  GLN B 198   N  LYS B   4           
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  GLU B 165           
SHEET    3   F 6 LYS B   4  ILE B   9  1  N  VAL B   8   O  LEU B  30           
SHEET    4   F 6 LYS B 194  ASN B 204  1  O  GLN B 198   N  LYS B   4           
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  GLU B 341   O  LYS B 344           
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  LEU B  89   O  PHE B 139           
SHEET    4   G 8 ALA B 245  GLN B 249  1  O  ALA B 245   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  GLY B 269   N  PHE B 257           
SHEET    7   G 8 ILE B 226  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  LEU B  89   O  PHE B 139           
SHEET    4   H 8 ALA B 245  GLN B 249  1  O  ALA B 245   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  GLY B 269   N  PHE B 257           
SHEET    7   H 8 ILE B 226  PRO B 237 -1  N  ILE B 234   O  ILE B 268           
SHEET    8   H 8 TRP B 311  CYS B 320 -1  O  LEU B 319   N  ARG B 227           
CISPEP   1 GLY A  269    THR A  270          0         3.96                     
CISPEP   2 GLY B  269    THR B  270          0         3.62                     
SITE     1 AC1  7 LEU A  53  ARG A  54  GLU A  57  LEU A  89                    
SITE     2 AC1  7 ARG A  96  ILE A 101  GLY A 104                               
SITE     1 AC2  7 LEU B  53  ARG B  54  GLU B  57  ARG B  96                    
SITE     2 AC2  7 ILE B 101  GLY B 104  LEU B 105                               
SITE     1 AC3  4 ALA A  98  TRP A  99  ARG A 102  ARG A 137                    
SITE     1 AC4  4 ALA B  98  TRP B  99  ARG B 102  ARG B 137                    
SITE     1 AC5  5 HIS A  91  PRO A  93  ALA A  98  ARG A 137                    
SITE     2 AC5  5 ASP B 322                                                     
SITE     1 AC6  2 THR B 271  ASP B 272                                          
SITE     1 AC7  2 ALA B  34  TRP B 209                                          
SITE     1 AC8  2 TRP B 311  TRP B 468                                          
SITE     1 AC9  3 SER B  43  TRP B 468  ARG B 469                               
SITE     1 BC1  2 ALA A  34  LYS A 280                                          
SITE     1 BC2  3 SER A  43  TRP A 468  ARG A 469                               
SITE     1 BC3  1 ILE B 309                                                     
SITE     1 BC4  4 GLN A 157  ARG A 161  PRO A 387  ARG B 405                    
SITE     1 BC5  3 ARG A 254  THR A 271  ASP A 272                               
SITE     1 BC6  2 LEU A 438  GLU A 448                                          
SITE     1 BC7  4 ARG A 405  GLN B 157  ARG B 161  PRO B 387                    
SITE     1 BC8  5 ARG B  88  PHE B 125  SER B 129  GLN B 242                    
SITE     2 BC8  5 TYR B 246                                                     
SITE     1 BC9  4 PRO B 208  GLN B 212  LEU B 228  PRO B 279                    
SITE     1 CC1  2 ALA A 400  ARG A 404                                          
SITE     1 CC2  6 GLN A 157  ASP A 456  HIS A 457  GLU A 458                    
SITE     2 CC2  6 TRP A 459  ARG B 405                                          
SITE     1 CC3  6 ARG A 405  GLN B 157  ASP B 456  HIS B 457                    
SITE     2 CC3  6 GLU B 458  TRP B 459                                          
SITE     1 CC4  1 GLU A 165                                                     
SITE     1 CC5  2 GLU B 165  TRP B 459                                          
SITE     1 CC6  4 SER A 174  ASP A 216  GLY A 217  HIS A 219                    
SITE     1 CC7  2 TRP A 311  THR A 312                                          
SITE     1 CC8  2 ALA B 463  ASP B 464                                          
SITE     1 CC9 28 ILE A   9  GLY A  10  GLY A  12  ILE A  13                    
SITE     2 CC9 28 ASN A  14  LEU A  32  GLU A  33  ALA A  34                    
SITE     3 CC9 28 CYS A  39  ALA A  40  THR A  41  SER A  42                    
SITE     4 CC9 28 ALA A  44  SER A  45  SER A  46  LYS A  47                    
SITE     5 CC9 28 LEU A  48  ALA A 172  THR A 206  GLY A 207                    
SITE     6 CC9 28 PRO A 208  GLY A 231  THR A 270  ARG A 317                    
SITE     7 CC9 28 GLY A 353  LYS A 354  LEU A 355  THR A 356                    
SITE     1 DC1 28 ILE B   9  GLY B  10  GLY B  12  ILE B  13                    
SITE     2 DC1 28 ASN B  14  LEU B  32  GLU B  33  ALA B  34                    
SITE     3 DC1 28 CYS B  39  ALA B  40  THR B  41  SER B  42                    
SITE     4 DC1 28 ALA B  44  SER B  45  SER B  46  LYS B  47                    
SITE     5 DC1 28 LEU B  48  HIS B  50  ALA B 172  THR B 206                    
SITE     6 DC1 28 PRO B 208  GLY B 231  THR B 270  ARG B 317                    
SITE     7 DC1 28 GLY B 353  LYS B 354  LEU B 355  THR B 356                    
SITE     1 DC2  9 ARG A  54  TYR A  55  ARG A 254  ILE A 255                    
SITE     2 DC2  9 PHE A 257  THR A 270  ASP A 272  ARG A 317                    
SITE     3 DC2  9 ARG A 332                                                     
SITE     1 DC3 10 ARG B  54  TYR B  55  ARG B 254  ILE B 255                    
SITE     2 DC3 10 PHE B 257  THR B 270  ASP B 272  ARG B 317                    
SITE     3 DC3 10 ARG B 332  LYS B 354                                          
SITE     1 DC4  5 PRO A 208  TRP A 209  GLN A 212  LEU A 228                    
SITE     2 DC4  5 PRO A 279                                                     
SITE     1 DC5  3 TRP B 468  GLY B 474  MET B 475                               
CRYST1  113.823  113.937  192.740  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      0.008786  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008777  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005188        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system