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Database: PDB
Entry: 2R45
LinkDB: 2R45
Original site: 2R45 
HEADER    OXIDOREDUCTASE                          30-AUG-07   2R45              
TITLE     CRYSTAL STRUCTURE OF ESCHERICHIA COLI GLYCEROL-3-PHOSPHATE            
TITLE    2 DEHYDROGENASE IN COMPLEX WITH 2-PHOSPHO-D-GLYCERIC 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;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    GLPD, OXIDOREDUCTASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.I.YEH,S.DU,U.CHINTE                                                 
REVDAT   2   24-FEB-09 2R45    1       VERSN                                    
REVDAT   1   15-APR-08 2R45    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.    2.30 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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 54271                          
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) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2754                            
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3122                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.76                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2400                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 171                          
REMARK   3   BIN FREE R VALUE                    : 0.3530                       
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          : 398                                     
REMARK   3   SOLVENT ATOMS            : 305                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.27                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.76000                                              
REMARK   3    B22 (A**2) : 0.77000                                              
REMARK   3    B33 (A**2) : -1.53000                                             
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): 0.314         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.259         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.181         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.337         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.908                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8340 ; 0.028 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11315 ; 2.747 ; 1.972       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   999 ;10.074 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   394 ;32.724 ;22.792       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1400 ;21.924 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    78 ;20.119 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1204 ; 0.206 ; 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):  4307 ; 0.293 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5421 ; 0.322 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   546 ; 0.239 ; 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):    37 ; 0.201 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.371 ; 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):  5153 ; 1.328 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7967 ; 2.143 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3823 ; 3.272 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3348 ; 4.952 ; 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 ; 0.480 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   3929 ; 0.970 ; 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 2R45 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-APR-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB044401.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-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          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55038                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
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     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : 0.09900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50500                            
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   (%): 55.29                                     
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 277K                           
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       56.87200            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       56.95400            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       96.53450            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       56.87200            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       56.95400            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       96.53450            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       56.87200            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       56.95400            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       96.53450            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       56.87200            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       56.95400            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       96.53450            
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 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 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    GLU A   2      -45.59     40.48                                   
REMARK 500    GLN A  35      -95.20   -126.48                                   
REMARK 500    ALA A  40     -116.93   -114.89                                   
REMARK 500    ALA A  78       58.19   -140.25                                   
REMARK 500    THR A 115      -84.43    -78.52                                   
REMARK 500    ASP A 143     -179.31   -171.93                                   
REMARK 500    ASP A 190      -61.06   -101.00                                   
REMARK 500    THR A 191      -71.85    -70.01                                   
REMARK 500    ASP A 263       -1.80     63.94                                   
REMARK 500    ASP A 321       91.87    -58.62                                   
REMARK 500    GLU A 323       20.85     48.75                                   
REMARK 500    PRO A 371      -35.34    -30.98                                   
REMARK 500    GLN A 374     -132.28     24.40                                   
REMARK 500    TRP A 380      -10.53   -154.28                                   
REMARK 500    GLU A 392       94.40     11.73                                   
REMARK 500    ASP A 394      -62.61     89.41                                   
REMARK 500    ASP A 396      -22.78    130.48                                   
REMARK 500    THR A 420      -66.40    -96.87                                   
REMARK 500    SER A 423       -9.89    -47.45                                   
REMARK 500    TRP A 459       19.41     58.94                                   
REMARK 500    GLN A 494      -81.49    -51.65                                   
REMARK 500    GLN B  35     -102.42   -122.24                                   
REMARK 500    ALA B  38       17.74     55.16                                   
REMARK 500    ALA B  40     -119.42   -122.31                                   
REMARK 500    SER B 116      -26.23   -142.66                                   
REMARK 500    SER B 120      131.98    106.15                                   
REMARK 500    SER B 129     -179.38    -67.16                                   
REMARK 500    ASP B 143     -169.95   -166.92                                   
REMARK 500    ASN B 179       32.67     76.53                                   
REMARK 500    ARG B 238      117.80    -30.89                                   
REMARK 500    ASP B 263       -5.30     57.74                                   
REMARK 500    ASP B 321       85.00    -60.47                                   
REMARK 500    ASP B 325      -62.10    120.83                                   
REMARK 500    LYS B 354      159.03    -48.46                                   
REMARK 500    PRO B 371      -27.50    -34.08                                   
REMARK 500    TRP B 380      -12.50   -158.48                                   
REMARK 500    GLU B 392       89.55      8.20                                   
REMARK 500    ASP B 394      177.77     64.57                                   
REMARK 500    ARG B 395      -11.30     69.28                                   
REMARK 500    ASP B 396      -63.39   -168.50                                   
REMARK 500    THR B 420      -66.58   -106.53                                   
REMARK 500    ARG B 469      -62.05   -120.22                                   
REMARK 500    THR B 493      -64.08    -93.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 TYR A  373     GLN A  374                  149.81                    
REMARK 500 ILE A  391     GLU A  392                 -147.54                    
REMARK 500 ASP A  394     ARG A  395                 -147.80                    
REMARK 500 ILE B  391     GLU B  392                 -148.70                    
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 B 800                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 800                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 900                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 900                 
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 PO4 A 1951                
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 901                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 902                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1952                
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 903                 
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1953                
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 904                 
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1954                
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1955                
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 600                 
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 600                 
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 905                 
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 1956                
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 906                 
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 907                 
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 908                 
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1957                
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 1958                
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1959                
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1960                
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 EDO B 909                 
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 910                 
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1963                
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD B 912                 
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T3A B 7066                
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T3A A 7066                
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 7067                
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 7067                
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2PG B 700                 
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2PG A 700                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2R46   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN IN COMPLEX WITH 2-PHOSPHOPYRUVIC ACID                   
DBREF  2R45 A    1   501  UNP    P13035   GLPD_ECOLI       1    501             
DBREF  2R45 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 800      20                                                       
HET    BOG  A 900      20                                                       
HET    BOG  A1949      20                                                       
HET    BOG  A1950      20                                                       
HET    BOG  B 800      20                                                       
HET    BOG  B 900      20                                                       
HET    PO4  A1951       5                                                       
HET    PO4  A1952       5                                                       
HET    PO4  A1953       5                                                       
HET    PO4  A1954       5                                                       
HET    PO4  A1955       5                                                       
HET    PO4  B 901       5                                                       
HET    PO4  B 902       5                                                       
HET    PO4  B 903       5                                                       
HET    PO4  B 904       5                                                       
HET    FAD  A 600      53                                                       
HET    IMD  A1956       5                                                       
HET    EDO  A1957       4                                                       
HET    IMD  A1958       5                                                       
HET    EDO  A1959       4                                                       
HET    EDO  A1960       4                                                       
HET    EDO  A1961       4                                                       
HET    EDO  A1962       4                                                       
HET    EDO  A1963       4                                                       
HET    T3A  A7066      15                                                       
HET    EDO  A7067       4                                                       
HET    2PG  A 700      11                                                       
HET    FAD  B 600      53                                                       
HET    EDO  B 905       4                                                       
HET    EDO  B 906       4                                                       
HET    EDO  B 907       4                                                       
HET    EDO  B 908       4                                                       
HET    EDO  B 909       4                                                       
HET    EDO  B 910       4                                                       
HET    EDO  B 911       4                                                       
HET    IMD  B 912       5                                                       
HET    T3A  B7066      15                                                       
HET    EDO  B7067       4                                                       
HET    2PG  B 700      11                                                       
HETNAM     BOG B-OCTYLGLUCOSIDE                                                 
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     IMD IMIDAZOLE                                                        
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     T3A N-(TRIS(HYDROXYMETHYL)METHYL)-3-AMINOPROPANESULFONIC             
HETNAM   2 T3A  ACID                                                            
HETNAM     2PG 2-PHOSPHOGLYCERIC ACID                                           
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  BOG    6(C14 H28 O6)                                                
FORMUL   9  PO4    9(O4 P 3-)                                                   
FORMUL  18  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL  19  IMD    3(C3 H5 N2 1+)                                               
FORMUL  20  EDO    15(C2 H6 O2)                                                 
FORMUL  27  T3A    2(C7 H17 N O6 S)                                             
FORMUL  29  2PG    2(C3 H7 O7 P)                                                
FORMUL  42  HOH   *305(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 LYS A  354  THR A  356  5                                   3    
HELIX   13  13 THR A  357  THR A  370  1                                  14    
HELIX   14  14 PRO A  371  TYR A  373  5                                   3    
HELIX   15  15 TRP A  380  SER A  384  5                                   5    
HELIX   16  16 ASP A  396  TYR A  406  1                                  11    
HELIX   17  17 THR A  410  TYR A  421  1                                  12    
HELIX   18  18 ASN A  424  GLY A  430  1                                   7    
HELIX   19  19 THR A  434  GLY A  439  5                                   6    
HELIX   20  20 TYR A  447  GLU A  458  1                                  12    
HELIX   21  21 ARG A  462  ARG A  469  1                                   8    
HELIX   22  22 LYS A  472  TRP A  476  5                                   5    
HELIX   23  23 ASN A  478  GLN A  494  1                                  17    
HELIX   24  24 GLY B   12  GLY B   24  1                                  13    
HELIX   25  25 ALA B   40  ALA B   44  5                                   5    
HELIX   26  26 GLY B   52  LEU B   56  5                                   5    
HELIX   27  27 GLU B   60  ALA B   78  1                                  19    
HELIX   28  28 PRO B   97  LEU B  111  1                                  15    
HELIX   29  29 ASP B  147  LYS B  162  1                                  16    
HELIX   30  30 THR B  206  PRO B  208  5                                   3    
HELIX   31  31 TRP B  209  GLY B  217  1                                   9    
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 THR B  357  LEU B  369  1                                  13    
HELIX   36  36 THR B  370  TYR B  373  5                                   4    
HELIX   37  37 TRP B  380  SER B  384  5                                   5    
HELIX   38  38 ASP B  396  TYR B  406  1                                  11    
HELIX   39  39 THR B  410  TYR B  421  1                                  12    
HELIX   40  40 ASN B  424  GLY B  430  1                                   7    
HELIX   41  41 THR B  434  GLY B  439  5                                   6    
HELIX   42  42 TYR B  447  TRP B  459  1                                  13    
HELIX   43  43 ARG B  462  ARG B  469  1                                   8    
HELIX   44  44 LYS B  472  TRP B  476  5                                   5    
HELIX   45  45 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 LEU A   6  ILE A   9  1  N  VAL A   8   O  LEU A  32           
SHEET    4   A 6 LEU A 202  ASN A 204  1  O  VAL A 203   N  ILE A   7           
SHEET    5   A 6 LYS A 344  PHE A 351  1  O  LEU A 348   N  ASN A 204           
SHEET    6   A 6 THR A 335  GLU A 341 -1  N  THR A 335   O  PHE A 351           
SHEET    1   B 8 LEU A  48  ILE A  49  0                                        
SHEET    2   B 8 ARG A 137  VAL A 146 -1  O  CYS A 144   N  ILE A  49           
SHEET    3   B 8 ALA A  82  PRO A  90 -1  N  MET A  85   O  ASP A 143           
SHEET    4   B 8 ALA A 245  GLN A 249  1  O  ALA A 245   N  ARG A  88           
SHEET    5   B 8 ILE A 255  TRP A 261 -1  O  VAL A 256   N  LEU A 248           
SHEET    6   B 8 PHE A 265  GLY A 269 -1  O  PHE A 265   N  TRP A 261           
SHEET    7   B 8 ILE A 226  PRO A 237 -1  N  ILE A 234   O  ILE A 268           
SHEET    8   B 8 VAL A 273  GLU A 274 -1  O  VAL A 273   N  LYS A 230           
SHEET    1   C 8 THR A 121  ARG A 124  0                                        
SHEET    2   C 8 ARG A 137  VAL A 146 -1  O  GLU A 140   N  THR A 121           
SHEET    3   C 8 ALA A  82  PRO A  90 -1  N  MET A  85   O  ASP A 143           
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  PHE A 265   N  TRP A 261           
SHEET    7   C 8 ILE A 226  PRO A 237 -1  N  ILE A 234   O  ILE A 268           
SHEET    8   C 8 TRP A 311  CYS A 320 -1  O  LEU A 319   N  ARG A 227           
SHEET    1   D 3 THR A 170  GLU A 178  0                                        
SHEET    2   D 3 LEU A 181  ASP A 188 -1  O  GLU A 185   N  THR A 173           
SHEET    3   D 3 LYS A 194  ALA A 199 -1  O  ALA A 199   N  TRP A 182           
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 LEU B   6  ILE B   9  1  N  VAL B   8   O  LEU B  32           
SHEET    4   E 6 LEU B 202  ASN B 204  1  O  VAL B 203   N  ILE B   7           
SHEET    5   E 6 LYS B 344  PHE B 351  1  O  LEU B 348   N  LEU B 202           
SHEET    6   E 6 THR B 335  GLU B 341 -1  N  ASP B 337   O  SER B 349           
SHEET    1   F 8 LEU B  48  ILE B  49  0                                        
SHEET    2   F 8 ARG B 137  VAL B 146 -1  O  CYS B 144   N  ILE B  49           
SHEET    3   F 8 ALA B  82  PRO B  90 -1  N  PHE B  87   O  TYR B 141           
SHEET    4   F 8 ALA B 245  GLN B 249  1  O  ALA B 245   N  ARG B  88           
SHEET    5   F 8 ILE B 255  TRP B 261 -1  O  VAL B 256   N  LEU B 248           
SHEET    6   F 8 PHE B 265  GLY B 269 -1  O  PHE B 265   N  TRP B 261           
SHEET    7   F 8 ILE B 226  PRO B 237 -1  N  ILE B 234   O  ILE B 268           
SHEET    8   F 8 VAL B 273  TYR B 275 -1  O  TYR B 275   N  LEU B 228           
SHEET    1   G 8 THR B 121  ARG B 124  0                                        
SHEET    2   G 8 ARG B 137  VAL B 146 -1  O  GLU B 140   N  THR B 121           
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  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  PHE B 265   N  TRP B 261           
SHEET    7   G 8 ILE B 226  PRO B 237 -1  N  ILE B 234   O  ILE B 268           
SHEET    8   G 8 TRP B 311  CYS B 320 -1  O  TRP B 311   N  VAL B 235           
SHEET    1   H 3 THR B 170  GLU B 178  0                                        
SHEET    2   H 3 LEU B 181  ASP B 188 -1  O  GLU B 185   N  THR B 173           
SHEET    3   H 3 LYS B 194  ALA B 199 -1  O  ALA B 199   N  TRP B 182           
CISPEP   1 MET A    1    GLU A    2          0        22.48                     
CISPEP   2 GLY A  269    THR A  270          0         2.35                     
CISPEP   3 GLN A  374    GLY A  375          0        18.09                     
CISPEP   4 GLN A  494    GLN A  495          0       -20.43                     
CISPEP   5 LYS B  113    ARG B  114          0        -4.95                     
CISPEP   6 GLY B  269    THR B  270          0         9.07                     
SITE     1 AC1  3 TRP B  99  ARG B 102  ARG B 137                               
SITE     1 AC2  4 TRP A  99  ARG A 102  ARG A 137  TYR B  59                    
SITE     1 AC3  9 LEU A  53  ARG A  54  LEU A  56  GLU A  57                    
SITE     2 AC3  9 LEU A  89  ARG A  96  MET A 100  ILE A 101                    
SITE     3 AC3  9 GLY A 104                                                     
SITE     1 AC4  7 LEU B  53  ARG B  54  LEU B  56  GLU B  57                    
SITE     2 AC4  7 ARG B  96  ILE B 101  LEU B 105                               
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 TRP A 468  GLY A 474                                          
SITE     1 AC7  4 ARG A 161  TYR B 398  ARG B 401  ARG B 405                    
SITE     1 AC8  5 PRO B 208  GLN B 212  LEU B 228  GLY B 277                    
SITE     2 AC8  5 PRO B 279                                                     
SITE     1 AC9  3 ARG A 462  ALA A 463  ASP A 464                               
SITE     1 BC1  3 ARG B 462  ALA B 463  ASP B 464                               
SITE     1 BC2  3 ARG A  92  PRO A  93  HIS A  94                               
SITE     1 BC3  3 ARG B  92  PRO B  93  HIS B  94                               
SITE     1 BC4  4 TYR A 398  ARG A 401  ARG A 405  ARG B 161                    
SITE     1 BC5  5 PRO A 208  GLN A 212  LEU A 228  GLY A 277                    
SITE     2 BC5  5 PRO A 279                                                     
SITE     1 BC6 30 ILE A   9  GLY A  10  GLY A  11  GLY A  12                    
SITE     2 BC6 30 ILE A  13  ASN A  14  GLU A  33  ALA A  34                    
SITE     3 BC6 30 CYS A  39  ALA A  40  THR A  41  SER A  42                    
SITE     4 BC6 30 ALA A  44  SER A  45  SER A  46  LYS A  47                    
SITE     5 BC6 30 LEU A  48  ALA A 172  THR A 206  GLY A 207                    
SITE     6 BC6 30 PRO A 208  TRP A 209  PHE A 213  GLY A 231                    
SITE     7 BC6 30 THR A 270  ARG A 317  GLY A 353  LYS A 354                    
SITE     8 BC6 30 LEU A 355  THR A 356                                          
SITE     1 BC7 31 ILE B   9  GLY B  10  GLY B  12  ILE B  13                    
SITE     2 BC7 31 ASN B  14  LEU B  32  GLU B  33  ALA B  34                    
SITE     3 BC7 31 CYS B  39  ALA B  40  THR B  41  SER B  42                    
SITE     4 BC7 31 ALA B  44  SER B  45  SER B  46  LYS B  47                    
SITE     5 BC7 31 LEU B  48  HIS B  50  ARG B 171  ALA B 172                    
SITE     6 BC7 31 THR B 206  GLY B 207  PRO B 208  GLY B 231                    
SITE     7 BC7 31 HIS B 233  THR B 270  ARG B 317  GLY B 353                    
SITE     8 BC7 31 LYS B 354  LEU B 355  THR B 356                               
SITE     1 BC8  3 ARG B 254  THR B 271  ASP B 272                               
SITE     1 BC9  4 HIS A  80  PHE A  83  ASP A 394  ARG A 419                    
SITE     1 CC1  3 ALA B  34  ARG B 171  TRP B 209                               
SITE     1 CC2  2 TRP B 311  TRP B 468                                          
SITE     1 CC3  4 SER B  43  TRP B 311  TRP B 468  ARG B 469                    
SITE     1 CC4  3 ALA A  34  ARG A 171  TRP A 209                               
SITE     1 CC5  4 HIS A 416  HIS A 444  GLU A 445  GLN A 473                    
SITE     1 CC6  3 SER A  43  TRP A 311  ARG A 469                               
SITE     1 CC7  1 TRP A 311                                                     
SITE     1 CC8  3 ASN A 294  SER B 305  ARG B 306                               
SITE     1 CC9  5 SER B 412  HIS B 416  HIS B 444  GLU B 445                    
SITE     2 CC9  5 GLN B 473                                                     
SITE     1 DC1  4 ARG A 254  THR A 271  ASP A 272  SER B 287                    
SITE     1 DC2  2 LYS B 162  SER B 384                                          
SITE     1 DC3  3 ARG A 161  TRP A 380  SER A 384                               
SITE     1 DC4  3 TRP B 488  GLU B 491  TYR B 492                               
SITE     1 DC5  5 GLN B 157  ASP B 456  HIS B 457  GLU B 458                    
SITE     2 DC5  5 TRP B 459                                                     
SITE     1 DC6  6 GLN A 157  ASP A 456  HIS A 457  GLU A 458                    
SITE     2 DC6  6 TRP A 459  ARG B 405                                          
SITE     1 DC7  4 GLN A 157  ARG A 161  ASN A 424  GLU B 426                    
SITE     1 DC8  5 ARG A 405  GLN B 157  ARG B 161  PRO B 387                    
SITE     2 DC8  5 ASN B 424                                                     
SITE     1 DC9 10 ARG B  54  TYR B  55  ARG B 254  ILE B 255                    
SITE     2 DC9 10 PHE B 257  THR B 270  ASP B 272  ARG B 317                    
SITE     3 DC9 10 ARG B 332  LYS B 354                                          
SITE     1 EC1  8 ARG A  54  TYR A  55  ARG A 254  ILE A 255                    
SITE     2 EC1  8 PHE A 257  THR A 270  ARG A 317  ARG A 332                    
CRYST1  113.744  113.908  193.069  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      0.008792  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008779  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005179        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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