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Database: PDB
Entry: 2R4J
LinkDB: 2R4J
Original site: 2R4J 
HEADER    OXIDOREDUCTASE                          31-AUG-07   2R4J              
TITLE     CRYSTAL STRUCTURE OF ESCHERICHIA COLI SEMET SUBSTITUTED               
TITLE    2 GLYCEROL-3-PHOSPHATE DEHYDROGENASE IN COMPLEX WITH DHAP              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE;                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.1.99.5;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 GENE: GLPD, GLYD;                                                    
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI                                  
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 2R4J    1       VERSN                                    
REVDAT   1   03-JUN-08 2R4J    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.    1.96 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) : 1.96                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 77725                          
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) : 0.214                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4086                            
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) : 1.96                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.01                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2841                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2800                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 149                          
REMARK   3   BIN FREE R VALUE                    : 0.3310                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7934                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 434                                     
REMARK   3   SOLVENT ATOMS            : 277                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.14                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.68000                                              
REMARK   3    B22 (A**2) : 1.56000                                              
REMARK   3    B33 (A**2) : -2.23000                                             
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): 0.188         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.175         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.152         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.472         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.926                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8534 ; 0.024 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11492 ; 2.354 ; 1.996       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   989 ; 6.943 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   392 ;32.529 ;22.806       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1385 ;20.095 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    77 ;18.437 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1219 ; 0.161 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6343 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3920 ; 0.250 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5657 ; 0.327 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   447 ; 0.173 ; 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):    47 ; 0.198 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.123 ; 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):  5049 ; 1.550 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7884 ; 2.305 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4068 ; 3.291 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3608 ; 4.923 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      5       A     494      4                      
REMARK   3           1     B      5       B     494      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   3920 ;  0.36 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   3920 ;  0.85 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2R4J COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-DEC-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB044415.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97928, 0.97947, 0.97181          
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 87054                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.960                              
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     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : 0.11300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.61400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M DI-AMMONIUM HYDROGEN                
REMARK 280  PHOSPHATE, 0.1M BICINE, 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       56.95800            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       57.07100            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       96.79550            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       56.95800            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       57.07100            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       96.79550            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       56.95800            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       57.07100            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       96.79550            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       56.95800            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       57.07100            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       96.79550            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLN A   495                                                      
REMARK 465     ARG A   496                                                      
REMARK 465     LEU A   497                                                      
REMARK 465     SER A   498                                                      
REMARK 465     LEU A   499                                                      
REMARK 465     ALA A   500                                                      
REMARK 465     SER A   501                                                      
REMARK 465     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      -17.39     60.90                                   
REMARK 500    GLN A  35      -96.34   -128.22                                   
REMARK 500    ALA A  40     -115.40   -126.83                                   
REMARK 500    GLU A  60       50.23    -94.23                                   
REMARK 500    LYS A 113      111.22     44.73                                   
REMARK 500    SER A 116      -45.55   -149.39                                   
REMARK 500    PRO A 118     -133.42    -56.51                                   
REMARK 500    GLU A 264      -32.11   -131.23                                   
REMARK 500    ASP A 321       97.44    -68.02                                   
REMARK 500    GLU A 341     -100.74   -112.99                                   
REMARK 500    ASN A 342       47.29    -84.12                                   
REMARK 500    LYS A 354      162.61    -46.91                                   
REMARK 500    PRO A 371      -27.22    -39.62                                   
REMARK 500    GLN A 374     -108.09    -78.76                                   
REMARK 500    ALA A 379      150.50    -48.71                                   
REMARK 500    TRP A 380       -1.60   -162.29                                   
REMARK 500    GLU A 392       49.49    -68.79                                   
REMARK 500    ASP A 397       36.96    -97.73                                   
REMARK 500    SER A 423       -9.22    -58.73                                   
REMARK 500    LYS B   4       86.46     81.50                                   
REMARK 500    GLN B  35      -96.30   -125.75                                   
REMARK 500    ALA B  40     -124.47   -126.91                                   
REMARK 500    TYR B  59       91.09     38.08                                   
REMARK 500    GLU B  60       55.29   -147.12                                   
REMARK 500    LYS B 113      -92.47      0.32                                   
REMARK 500    THR B 115      -45.88    -29.10                                   
REMARK 500    SER B 116      -43.24   -134.10                                   
REMARK 500    PRO B 118     -135.16    -64.34                                   
REMARK 500    ARG B 169       27.81     46.05                                   
REMARK 500    ASN B 179       31.38     74.93                                   
REMARK 500    THR B 270     -155.08   -126.72                                   
REMARK 500    GLU B 323     -169.89     63.57                                   
REMARK 500    SER B 324      -71.56    156.48                                   
REMARK 500    ASP B 325      -62.75    107.20                                   
REMARK 500    PRO B 371      -29.20    -36.88                                   
REMARK 500    GLN B 374      -94.40    -79.76                                   
REMARK 500    ALA B 379      152.68    -24.65                                   
REMARK 500    TRP B 380      -15.31   -169.22                                   
REMARK 500    GLU B 392       78.07   -150.27                                   
REMARK 500    ARG B 461      -31.90   -130.58                                   
REMARK 500    GLN B 495      -76.53   -177.44                                   
REMARK 500    ARG B 496       40.41    -63.65                                   
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 700                 
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 B 700                 
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 BOG A 1950                
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 801                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1951                
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 600                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 600                 
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 802                 
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 803                 
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 804                 
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 805                 
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 806                 
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1952                
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 807                 
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 808                 
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1953                
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1954                
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1955                
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1956                
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 809                 
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1957                
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 810                 
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 811                 
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1958                
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1959                
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 1960                
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAM B 812                 
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 1961                
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 813                 
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1962                
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 814                 
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 1963                
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1964                
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1965                
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 1966                
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 815                 
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 1967                
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 13P A 1968                
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 13P B 816                 
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 817                 
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 818                 
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD B 819                 
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCN B 820                 
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCN B 821                 
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCN A 1969                
DBREF  2R4J A    1   501  UNP    P13035   GLPD_ECOLI       1    501             
DBREF  2R4J 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 MSE 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 MSE ALA          
SEQRES   7 A  501  PRO HIS ILE ALA PHE PRO MSE 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE ALA          
SEQRES   7 B  501  PRO HIS ILE ALA PHE PRO MSE 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 MSE 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 MSE 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 MSE 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 MSE 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                                  
MODRES 2R4J MSE A   31  MET  SELENOMETHIONINE                                   
MODRES 2R4J MSE A   77  MET  SELENOMETHIONINE                                   
MODRES 2R4J MSE A   85  MET  SELENOMETHIONINE                                   
MODRES 2R4J MSE A  158  MET  SELENOMETHIONINE                                   
MODRES 2R4J MSE A  218  MET  SELENOMETHIONINE                                   
MODRES 2R4J MSE A  262  MET  SELENOMETHIONINE                                   
MODRES 2R4J MSE A  475  MET  SELENOMETHIONINE                                   
MODRES 2R4J MSE B   31  MET  SELENOMETHIONINE                                   
MODRES 2R4J MSE B   77  MET  SELENOMETHIONINE                                   
MODRES 2R4J MSE B   85  MET  SELENOMETHIONINE                                   
MODRES 2R4J MSE B  158  MET  SELENOMETHIONINE                                   
MODRES 2R4J MSE B  218  MET  SELENOMETHIONINE                                   
MODRES 2R4J MSE B  262  MET  SELENOMETHIONINE                                   
MODRES 2R4J MSE B  475  MET  SELENOMETHIONINE                                   
HET    MSE  A  31       8                                                       
HET    MSE  A  77       8                                                       
HET    MSE  A  85       8                                                       
HET    MSE  A 158       8                                                       
HET    MSE  A 218       8                                                       
HET    MSE  A 262       8                                                       
HET    MSE  A 475       8                                                       
HET    MSE  B  31       8                                                       
HET    MSE  B  77       8                                                       
HET    MSE  B  85       8                                                       
HET    MSE  B 158       8                                                       
HET    MSE  B 218       8                                                       
HET    MSE  B 262       8                                                       
HET    MSE  B 475       8                                                       
HET    BOG  A 700      20                                                       
HET    BOG  A 800      20                                                       
HET    BOG  B 700      20                                                       
HET    BOG  B 800      20                                                       
HET    BOG  A1949      20                                                       
HET    BOG  A1950      20                                                       
HET    PO4  B 801       5                                                       
HET    PO4  A1951       5                                                       
HET    FAD  A 600      53                                                       
HET    FAD  B 600      53                                                       
HET    EDO  B 802       4                                                       
HET    EDO  B 803       4                                                       
HET    EDO  B 804       4                                                       
HET    EDO  B 805       4                                                       
HET    EDO  B 806       4                                                       
HET    EDO  A1952       4                                                       
HET    EDO  B 807       4                                                       
HET    EDO  B 808       4                                                       
HET    EDO  A1953       4                                                       
HET    EDO  A1954       4                                                       
HET    EDO  A1955       4                                                       
HET    EDO  A1956       4                                                       
HET    EDO  B 809       4                                                       
HET    EDO  A1957       4                                                       
HET    EDO  B 810       4                                                       
HET    EDO  B 811       4                                                       
HET    EDO  A1958       4                                                       
HET    EDO  A1959       4                                                       
HET    IMD  A1960       5                                                       
HET    TAM  B 812      11                                                       
HET    IMD  A1961       5                                                       
HET    EDO  B 813       4                                                       
HET    EDO  A1962       4                                                       
HET    EDO  B 814       4                                                       
HET    IMD  A1963       5                                                       
HET    EDO  A1964       4                                                       
HET    EDO  A1965       4                                                       
HET    IMD  A1966       5                                                       
HET    EDO  B 815       4                                                       
HET    IMD  A1967       5                                                       
HET    13P  A1968      10                                                       
HET    13P  B 816      10                                                       
HET    EDO  B 817       4                                                       
HET    EDO  B 818       4                                                       
HET    IMD  B 819       5                                                       
HET    BCN  B 820      11                                                       
HET    BCN  B 821      11                                                       
HET    BCN  A1969      11                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     BOG B-OCTYLGLUCOSIDE                                                 
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     IMD IMIDAZOLE                                                        
HETNAM     TAM TRIS(HYDROXYETHYL)AMINOMETHANE                                   
HETNAM     13P 1,3-DIHYDROXYACETONEPHOSPHATE                                    
HETNAM     BCN BICINE                                                           
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  MSE    14(C5 H11 N O2 SE)                                           
FORMUL   3  BOG    6(C14 H28 O6)                                                
FORMUL   9  PO4    2(O4 P 3-)                                                   
FORMUL  11  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL  13  EDO    26(C2 H6 O2)                                                 
FORMUL  31  IMD    6(C3 H5 N2 1+)                                               
FORMUL  32  TAM    C7 H17 N O3                                                  
FORMUL  43  13P    2(C3 H7 O6 P)                                                
FORMUL  48  BCN    3(C6 H13 N O4)                                               
FORMUL  51  HOH   *277(H2 O)                                                    
HELIX    1   1 GLY A   12  GLY A   24  1                                  13    
HELIX    2   2 ALA A   40  ALA A   44  5                                   5    
HELIX    3   3 GLY A   52  TYR A   59  5                                   8    
HELIX    4   4 GLU A   60  ALA A   78  1                                  19    
HELIX    5   5 PRO A   97  LEU A  111  1                                  15    
HELIX    6   6 ASP A  147  LYS A  162  1                                  16    
HELIX    7   7 THR A  206  PRO A  208  5                                   3    
HELIX    8   8 TRP A  209  GLY A  217  1                                   9    
HELIX    9   9 ASP A  278  VAL A  282  5                                   5    
HELIX   10  10 GLU A  285  THR A  298  1                                  14    
HELIX   11  11 SER A  305  ILE A  309  5                                   5    
HELIX   12  12 SER A  326  ILE A  330  5                                   5    
HELIX   13  13 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 ARG A  395  TYR A  406  1                                  12    
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  THR A  493  1                                  16    
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  TYR B   59  5                                   8    
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 ASP B  278  VAL B  282  5                                   5    
HELIX   33  33 GLU B  285  PHE B  300  1                                  16    
HELIX   34  34 SER B  305  ILE B  309  5                                   5    
HELIX   35  35 SER B  326  ILE B  330  5                                   5    
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  394  TYR B  406  1                                  13    
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 VAL B  435  GLY B  439  5                                   5    
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 6 GLU A 165  LEU A 167  0                                        
SHEET    2   A 6 VAL A  29  LEU A  32  1  N  MSE A  31   O  LEU A 167           
SHEET    3   A 6 THR A   3  ILE A   9  1  N  VAL A   8   O  LEU A  32           
SHEET    4   A 6 LYS A 194  ASN A 204  1  O  VAL A 203   N  ILE A   7           
SHEET    5   A 6 LEU A 181  ASP A 188 -1  N  TRP A 182   O  ALA A 199           
SHEET    6   A 6 THR A 170  GLU A 178 -1  N  GLU A 178   O  LEU A 181           
SHEET    1   B 6 GLU A 165  LEU A 167  0                                        
SHEET    2   B 6 VAL A  29  LEU A  32  1  N  MSE A  31   O  LEU A 167           
SHEET    3   B 6 THR A   3  ILE A   9  1  N  VAL A   8   O  LEU A  32           
SHEET    4   B 6 LYS A 194  ASN A 204  1  O  VAL A 203   N  ILE A   7           
SHEET    5   B 6 LEU A 347  PHE A 351  1  O  LEU A 348   N  ASN A 204           
SHEET    6   B 6 THR A 335  HIS A 339 -1  N  THR A 335   O  PHE A 351           
SHEET    1   C 8 LEU A  48  ILE A  49  0                                        
SHEET    2   C 8 ARG A 137  VAL A 146 -1  O  CYS A 144   N  ILE A  49           
SHEET    3   C 8 ALA A  82  PRO A  90 -1  N  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  GLU A 140   N  THR A 121           
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  MSE B  31   O  LEU B 167           
SHEET    3   E 6 LEU B   6  ILE B   9  1  N  VAL B   8   O  LEU B  32           
SHEET    4   E 6 GLY B 201  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  ASN B 204           
SHEET    6   E 6 THR B 335  GLU B 341 -1  N  THR B 335   O  PHE B 351           
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  ILE B 267   N  ILE B 259           
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  GLU B 274 -1  O  VAL B 273   N  LYS B 230           
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  ILE B 267   N  ILE B 259           
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  LEU B 181   N  GLU B 178           
SHEET    3   H 3 LYS B 194  ALA B 199 -1  O  ALA B 199   N  TRP B 182           
LINK         C   LEU A  30                 N   MSE A  31     1555   1555  1.33  
LINK         C   MSE A  31                 N   LEU A  32     1555   1555  1.35  
LINK         C   LYS A  76                 N   MSE A  77     1555   1555  1.32  
LINK         C   MSE A  77                 N   ALA A  78     1555   1555  1.34  
LINK         C   PRO A  84                 N   MSE A  85     1555   1555  1.33  
LINK         C   MSE A  85                 N   ARG A  86     1555   1555  1.33  
LINK         C   GLN A 157                 N   MSE A 158     1555   1555  1.31  
LINK         C   MSE A 158                 N   VAL A 159     1555   1555  1.33  
LINK         C   GLY A 217                 N   MSE A 218     1555   1555  1.33  
LINK         C   MSE A 218                 N   HIS A 219     1555   1555  1.34  
LINK         C   TRP A 261                 N   MSE A 262     1555   1555  1.32  
LINK         C   MSE A 262                 N   ASP A 263     1555   1555  1.33  
LINK         C   GLY A 474                 N   MSE A 475     1555   1555  1.32  
LINK         C   MSE A 475                 N   TRP A 476     1555   1555  1.34  
LINK         C   LEU B  30                 N   MSE B  31     1555   1555  1.32  
LINK         C   MSE B  31                 N   LEU B  32     1555   1555  1.35  
LINK         C   LYS B  76                 N   MSE B  77     1555   1555  1.33  
LINK         C   MSE B  77                 N   ALA B  78     1555   1555  1.33  
LINK         C   PRO B  84                 N   MSE B  85     1555   1555  1.34  
LINK         C   MSE B  85                 N   ARG B  86     1555   1555  1.33  
LINK         C   GLN B 157                 N   MSE B 158     1555   1555  1.32  
LINK         C   MSE B 158                 N   VAL B 159     1555   1555  1.33  
LINK         C   GLY B 217                 N   MSE B 218     1555   1555  1.32  
LINK         C   MSE B 218                 N   HIS B 219     1555   1555  1.34  
LINK         C   TRP B 261                 N   MSE B 262     1555   1555  1.33  
LINK         C   MSE B 262                 N   ASP B 263     1555   1555  1.33  
LINK         C   GLY B 474                 N   MSE B 475     1555   1555  1.32  
LINK         C   MSE B 475                 N   TRP B 476     1555   1555  1.35  
CISPEP   1 MET A    1    GLU A    2          0        20.42                     
CISPEP   2 GLY A  269    THR A  270          0         6.63                     
CISPEP   3 GLN A  374    GLY A  375          0        14.16                     
CISPEP   4 THR B    3    LYS B    4          0        20.04                     
CISPEP   5 LYS B  113    ARG B  114          0        -7.39                     
CISPEP   6 GLY B  269    THR B  270          0        -0.37                     
CISPEP   7 GLN B  374    GLY B  375          0         3.49                     
SITE     1 AC1  6 TRP A  99  ARG A 102  ARG A 137  BOG A1949                    
SITE     2 AC1  6 BOG A1950  TYR B  59                                          
SITE     1 AC2  9 LEU A  53  ARG A  54  LEU A  56  GLU A  57                    
SITE     2 AC2  9 TYR A  59  PHE A  61  LEU A  89  ARG A  96                    
SITE     3 AC2  9 GLN A 249                                                     
SITE     1 AC3  4 TRP B  99  ARG B 102  ILE B 103  ARG B 137                    
SITE     1 AC4 12 LEU B  53  ARG B  54  LEU B  56  GLU B  57                    
SITE     2 AC4 12 TYR B  59  PHE B  61  ARG B  96  MET B 100                    
SITE     3 AC4 12 ILE B 101  GLY B 104  LEU B 105  ILE B 255                    
SITE     1 AC5  2 TRP A  99  BOG A 700                                          
SITE     1 AC6  5 HIS A  91  PRO A  93  ALA A  98  ARG A 137                    
SITE     2 AC6  5 BOG A 700                                                     
SITE     1 AC7  5 ARG A 161  TYR B 398  ARG B 401  ARG B 405                    
SITE     2 AC7  5 HOH B 894                                                     
SITE     1 AC8  4 ILE A 183  SER A 196  TRP A 197  GLN A 198                    
SITE     1 AC9 31 ILE A   9  GLY A  12  ILE A  13  ASN A  14                    
SITE     2 AC9 31 LEU A  32  GLU A  33  ALA A  34  CYS A  39                    
SITE     3 AC9 31 THR A  41  SER A  42  ALA A  44  SER A  45                    
SITE     4 AC9 31 SER A  46  LYS A  47  LEU A  48  ALA A 172                    
SITE     5 AC9 31 THR A 206  GLY A 207  GLY A 231  THR A 270                    
SITE     6 AC9 31 ARG A 317  GLY A 353  LYS A 354  LEU A 355                    
SITE     7 AC9 31 THR A 356  EDO A1952  HOH A1972  HOH A1986                    
SITE     8 AC9 31 HOH A1988  HOH A2075  HOH A2076                               
SITE     1 BC1 33 ILE B   9  GLY B  10  GLY B  12  ILE B  13                    
SITE     2 BC1 33 ASN B  14  GLU B  33  ALA B  34  CYS B  39                    
SITE     3 BC1 33 ALA B  40  THR B  41  SER B  42  ALA B  44                    
SITE     4 BC1 33 SER B  45  SER B  46  LYS B  47  LEU B  48                    
SITE     5 BC1 33 ALA B 172  THR B 206  GLY B 207  PRO B 208                    
SITE     6 BC1 33 TRP B 209  GLY B 231  THR B 270  ARG B 317                    
SITE     7 BC1 33 GLY B 353  LYS B 354  LEU B 355  THR B 356                    
SITE     8 BC1 33 EDO B 804  HOH B 827  HOH B 831  HOH B 924                    
SITE     9 BC1 33 HOH B 948                                                     
SITE     1 BC2  5 ARG B 254  THR B 271  ASP B 272  HOH B 909                    
SITE     2 BC2  5 HOH B 919                                                     
SITE     1 BC3  5 LEU B 293  ASN B 294  ASN B 297  EDO B 817                    
SITE     2 BC3  5 HOH B 822                                                     
SITE     1 BC4  5 ALA B  34  ARG B 171  FAD B 600  HOH B 924                    
SITE     2 BC4  5 HOH B 937                                                     
SITE     1 BC5  2 TRP B 311  TRP B 468                                          
SITE     1 BC6  5 SER B  43  TRP B 468  ARG B 469  HOH B 843                    
SITE     2 BC6  5 HOH B 958                                                     
SITE     1 BC7  2 ALA A  34  FAD A 600                                          
SITE     1 BC8  6 MSE B 262  HIS B 416  LYS B 472  GLN B 473                    
SITE     2 BC8  6 EDO B 808  HOH B 853                                          
SITE     1 BC9  4 HIS B 444  GLU B 445  GLN B 473  EDO B 807                    
SITE     1 CC1  5 SER A  43  TRP A 468  ARG A 469  EDO A1954                    
SITE     2 CC1  5 EDO A1965                                                     
SITE     1 CC2  2 TRP A 311  EDO A1953                                          
SITE     1 CC3  3 ASN A 294  THR A 298  EDO B 817                               
SITE     1 CC4  6 ASN A 290  LEU A 293  ASN A 294  ASN B 294                    
SITE     2 CC4  6 HOH B 822  HOH B 856                                          
SITE     1 CC5  2 ILE B 289  ARG B 306                                          
SITE     1 CC6  7 MSE A 262  HIS A 416  LYS A 472  GLN A 473                    
SITE     2 CC6  7 TRP A 476  IMD A1960  HOH A1995                               
SITE     1 CC7  5 PRO B 208  GLN B 212  LEU B 228  PRO B 279                    
SITE     2 CC7  5 HOH B 838                                                     
SITE     1 CC8  6 VAL B 455  ASP B 456  HIS B 457  GLU B 458                    
SITE     2 CC8  6 TRP B 459  TAM B 812                                          
SITE     1 CC9  6 THR A  41  PRO A 279  LYS A 280  GLY A 315                    
SITE     2 CC9  6 VAL A 316  HOH A2097                                          
SITE     1 DC1  4 HIS A 457  IMD A1961  IMD A1963  ARG B 405                    
SITE     1 DC2  5 HIS A 416  HIS A 444  GLU A 445  GLN A 473                    
SITE     2 DC2  5 EDO A1957                                                     
SITE     1 DC3  6 ARG A 405  GLN B 157  VAL B 160  ARG B 161                    
SITE     2 DC3  6 HIS B 457  EDO B 811                                          
SITE     1 DC4  4 ASN A 424  LEU A 427  EDO A1959  HOH A2058                    
SITE     1 DC5  7 ALA B  40  THR B  41  PRO B 279  LYS B 280                    
SITE     2 DC5  7 GLY B 315  VAL B 316  HOH B 869                               
SITE     1 DC6  2 ARG A 405  ARG B 161                                          
SITE     1 DC7  2 MSE B 475  HOH B 896                                          
SITE     1 DC8  6 VAL A 455  ASP A 456  HIS A 457  GLU A 458                    
SITE     2 DC8  6 TRP A 459  EDO A1959                                          
SITE     1 DC9  1 PHE A 106                                                     
SITE     1 EC1  9 CYS A  39  ALA A  40  SER A  43  ALA A  44                    
SITE     2 EC1  9 TYR A 313  SER A 314  EDO A1953  HOH A2092                    
SITE     3 EC1  9 HOH A2097                                                     
SITE     1 EC2  2 PRO A 237  VAL A 310                                          
SITE     1 EC3  4 ARG B 171  ALA B 172  GLY B 217  HOH B 937                    
SITE     1 EC4  4 PRO A 208  LEU A 228  PRO A 279  HOH A2002                    
SITE     1 EC5  9 ARG A  54  TYR A  55  ARG A 254  ILE A 255                    
SITE     2 EC5  9 THR A 270  ASP A 272  ARG A 317  ARG A 332                    
SITE     3 EC5  9 HOH A2100                                                     
SITE     1 EC6  8 ARG B  54  TYR B  55  ARG B 254  ILE B 255                    
SITE     2 EC6  8 THR B 270  ASP B 272  ARG B 317  ARG B 332                    
SITE     1 EC7  3 EDO A1955  GLN B 303  EDO B 803                               
SITE     1 EC8  1 GLU B 383                                                     
SITE     1 EC9  3 TRP B 488  GLU B 491  TYR B 492                               
SITE     1 FC1  7 GLU A 274  GLU A 285  SER A 287  ASP B 272                    
SITE     2 FC1  7 VAL B 273  GLU B 274  BCN B 821                               
SITE     1 FC2  7 ASP A 272  VAL A 273  SER A 287  GLU B 285                    
SITE     2 FC2  7 SER B 287  BCN B 820  HOH B 910                               
SITE     1 FC3  3 GLY A  26  LYS A 162  ARG B 404                               
CRYST1  113.916  114.142  193.591  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      0.008778  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008761  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005166        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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