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Database: PDB
Entry: 2QCU
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Original site: 2QCU 
HEADER    OXIDOREDUCTASE                          19-JUN-07   2QCU              
TITLE     CRYSTAL STRUCTURE OF GLYCEROL-3-PHOSPHATE DEHYDROGENASE               
TITLE    2 FROM ESCHERICHIA COLI                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE;                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.1.99.5;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: GLPD, GLYD;                                                    
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    GLYCEROL-3-PHOSHATE DEHYDROGENASE, OXIDOREDUCTASE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.I.YEH,U.CHINTE,S.DU                                                 
REVDAT   2   24-FEB-09 2QCU    1       VERSN                                    
REVDAT   1   15-APR-08 2QCU    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.    1.75 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) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 118338                         
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) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6272                            
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) : 1.75                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.79                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8482                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.04                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2620                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 420                          
REMARK   3   BIN FREE R VALUE                    : 0.3360                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7997                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 419                                     
REMARK   3   SOLVENT ATOMS            : 476                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.65                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : 0.02000                                              
REMARK   3    B33 (A**2) : -0.03000                                             
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): 0.119         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.117         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.076         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.320         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.936                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8582 ; 0.011 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11552 ; 1.740 ; 1.995       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   998 ;14.085 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   393 ;32.356 ;22.774       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1395 ;18.183 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    78 ;17.041 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1233 ; 0.251 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6340 ; 0.019 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4272 ; 0.253 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5733 ; 0.326 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   552 ; 0.167 ; 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):    53 ; 0.288 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    11 ; 0.250 ; 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):  5079 ; 2.108 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7970 ; 3.034 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4042 ; 4.344 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3582 ; 6.223 ; 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     499      2                      
REMARK   3           1     B      5       B     499      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1980 ;  0.08 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1982 ;  0.56 ;  0.50           
REMARK   3   TIGHT THERMAL      1    A (A**2):   1980 ;  0.28 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1982 ;  1.19 ;  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 2QCU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUN-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB043437.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL; NULL                         
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : SLS; APS                           
REMARK 200  BEAMLINE                       : X10SA; 22-ID                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9803; 0.97928, 0.97947,          
REMARK 200                                   0.97181                            
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD;              
REMARK 200                                   MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 136571                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 9.000                              
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.71200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD                         
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE, PHASER                                         
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.30                                     
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 TRIS-HCL PH 8.5, 12 % W/V PEG MME 550, 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       56.89550            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       57.04850            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       96.40050            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       56.89550            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       57.04850            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       96.40050            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       56.89550            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       57.04850            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       96.40050            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       56.89550            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       57.04850            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       96.40050            
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 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 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     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LEU A   37   C                                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B  1036     O    HOH B  1037              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A  35      -94.41   -125.12                                   
REMARK 500    ALA A  40     -116.15   -117.23                                   
REMARK 500    ALA A  78       58.80   -144.50                                   
REMARK 500    LYS A 113       16.52     99.57                                   
REMARK 500    ARG A 114      141.27    -23.80                                   
REMARK 500    SER A 116      -17.58   -152.97                                   
REMARK 500    SER A 120      131.50    124.70                                   
REMARK 500    ASP A 143     -157.02   -149.76                                   
REMARK 500    ALA A 205       51.91   -110.94                                   
REMARK 500    LYS A 253       -1.83     81.38                                   
REMARK 500    ASP A 263      -14.21     64.60                                   
REMARK 500    LEU A 319      116.81     43.05                                   
REMARK 500    TRP A 380      -22.45   -153.82                                   
REMARK 500    ILE A 391     -140.43   -109.33                                   
REMARK 500    GLU A 392       58.76   -174.17                                   
REMARK 500    ASP A 396       17.43    132.25                                   
REMARK 500    THR A 420      -65.62   -109.60                                   
REMARK 500    TRP A 459       18.09     58.76                                   
REMARK 500    LEU A 497      -47.60   -161.49                                   
REMARK 500    LEU A 499      -83.25   -115.06                                   
REMARK 500    GLU B   2       -0.53   -163.83                                   
REMARK 500    GLN B  35      -94.21   -126.08                                   
REMARK 500    ALA B  40     -121.82   -114.86                                   
REMARK 500    HIS B  50      -61.73   -109.96                                   
REMARK 500    ALA B  78       58.39   -147.71                                   
REMARK 500    LYS B 113      -59.37    128.79                                   
REMARK 500    ARG B 114      124.97     54.03                                   
REMARK 500    SER B 116      -18.91   -149.60                                   
REMARK 500    ASP B 143     -159.89   -151.31                                   
REMARK 500    ALA B 205       51.44   -107.13                                   
REMARK 500    ILE B 226      109.74     55.70                                   
REMARK 500    LYS B 253       -1.46     77.29                                   
REMARK 500    ASP B 263      -12.43     64.07                                   
REMARK 500    THR B 270     -147.05   -126.46                                   
REMARK 500    LEU B 319      119.78     37.56                                   
REMARK 500    ILE B 376     -109.04    -52.26                                   
REMARK 500    ALA B 379      157.55    -34.24                                   
REMARK 500    TRP B 380      -21.13   -158.31                                   
REMARK 500    ILE B 391     -101.12   -122.15                                   
REMARK 500    GLU B 392       86.60    136.12                                   
REMARK 500    ASP B 394      -66.68    114.62                                   
REMARK 500    LEU B 497      -70.35   -161.87                                   
REMARK 500    ALA B 500      161.11    172.44                                   
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 ARG A  496     LEU A  497                  116.49                    
REMARK 500 LEU A  497     SER A  498                  146.84                    
REMARK 500 SER A  498     LEU A  499                 -124.81                    
REMARK 500 LEU A  499     ALA A  500                 -132.25                    
REMARK 500 ARG B  496     LEU B  497                  133.65                    
REMARK 500 LEU B  497     SER B  498                  146.20                    
REMARK 500 SER B  498     LEU B  499                 -139.55                    
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 701                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 800                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 801                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 700                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 800                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 802                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 803                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 801                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 802                 
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 804                 
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 803                 
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 600                 
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 600                 
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAM A 805                 
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 806                 
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 807                 
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 808                 
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 809                 
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 810                 
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 811                 
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 812                 
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 813                 
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 814                 
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 815                 
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 816                 
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 817                 
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 818                 
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 819                 
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 820                 
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 821                 
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 822                 
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAM A 823                 
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 804                 
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 805                 
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 806                 
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 807                 
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 808                 
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 809                 
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAM B 810                 
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 811                 
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 812                 
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 813                 
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 814                 
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 816                 
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 817                 
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 819                 
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 820                 
DBREF  2QCU A    1   501  UNP    P13035   GLPD_ECOLI       1    501             
DBREF  2QCU 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 700      20                                                       
HET    BOG  A 701      20                                                       
HET    BOG  A 800      20                                                       
HET    BOG  A 801      20                                                       
HET    BOG  B 700      20                                                       
HET    BOG  B 800      20                                                       
HET    SO4  A 802       5                                                       
HET    SO4  A 803       5                                                       
HET    SO4  B 801       5                                                       
HET    SO4  B 802       5                                                       
HET    PO4  A 804       5                                                       
HET    PO4  B 803       5                                                       
HET    FAD  A 600      53                                                       
HET    FAD  B 600      53                                                       
HET    TAM  A 805      11                                                       
HET    EDO  A 806       4                                                       
HET    IMD  A 807       5                                                       
HET    EDO  A 808       4                                                       
HET    EDO  A 809       4                                                       
HET    EDO  A 810       4                                                       
HET    EDO  A 811       4                                                       
HET    EDO  A 812       4                                                       
HET    EDO  A 813       4                                                       
HET    EDO  A 814       4                                                       
HET    EDO  A 815       4                                                       
HET    EDO  A 816       4                                                       
HET    EDO  A 817       4                                                       
HET    EDO  A 818       4                                                       
HET    EDO  A 819       4                                                       
HET    EDO  A 820       4                                                       
HET    IMD  A 821       5                                                       
HET    EDO  A 822       4                                                       
HET    TAM  A 823      11                                                       
HET    EDO  B 804       4                                                       
HET    EDO  B 805       4                                                       
HET    EDO  B 806       4                                                       
HET    EDO  B 807       4                                                       
HET    EDO  B 808       4                                                       
HET    EDO  B 809       4                                                       
HET    TAM  B 810      11                                                       
HET    EDO  B 811       4                                                       
HET    EDO  B 812       4                                                       
HET    EDO  B 813       4                                                       
HET    EDO  B 814       4                                                       
HET    EDO  B 815       4                                                       
HET    EDO  B 816       4                                                       
HET    EDO  B 817       4                                                       
HET    EDO  B 819       4                                                       
HET    EDO  B 820       4                                                       
HETNAM     BOG B-OCTYLGLUCOSIDE                                                 
HETNAM     SO4 SULFATE ION                                                      
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     TAM TRIS(HYDROXYETHYL)AMINOMETHANE                                   
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     IMD IMIDAZOLE                                                        
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  BOG    6(C14 H28 O6)                                                
FORMUL   9  SO4    4(O4 S 2-)                                                   
FORMUL  13  PO4    2(O4 P 3-)                                                   
FORMUL  15  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL  17  TAM    3(C7 H17 N O3)                                               
FORMUL  18  EDO    30(C2 H6 O2)                                                 
FORMUL  19  IMD    2(C3 H5 N2 1+)                                               
FORMUL  52  HOH   *476(H2 O)                                                    
HELIX    1   1 GLY A   12  ARG A   25  1                                  14    
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  HIS A  110  1                                  14    
HELIX    6   6 ASP A  147  LYS A  162  1                                  16    
HELIX    7   7 THR A  206  PRO A  208  5                                   3    
HELIX    8   8 TRP A  209  GLY A  217  1                                   9    
HELIX    9   9 ASP A  278  VAL A  282  5                                   5    
HELIX   10  10 GLU A  285  PHE A  300  1                                  16    
HELIX   11  11 SER A  305  ILE A  309  5                                   5    
HELIX   12  12 SER A  326  ILE A  330  5                                   5    
HELIX   13  13 LYS A  354  THR A  356  5                                   3    
HELIX   14  14 THR A  357  THR A  370  1                                  14    
HELIX   15  15 PRO A  371  TYR A  373  5                                   3    
HELIX   16  16 TRP A  380  SER A  384  5                                   5    
HELIX   17  17 ASP A  397  TYR A  406  1                                  10    
HELIX   18  18 THR A  410  TYR A  421  1                                  12    
HELIX   19  19 ASN A  424  GLY A  430  1                                   7    
HELIX   20  20 THR A  434  GLY A  439  5                                   6    
HELIX   21  21 TYR A  447  GLU A  458  1                                  12    
HELIX   22  22 ARG A  462  ARG A  469  1                                   8    
HELIX   23  23 LYS A  472  TRP A  476  5                                   5    
HELIX   24  24 ASN A  478  GLN A  495  1                                  18    
HELIX   25  25 GLY B   12  ARG B   25  1                                  14    
HELIX   26  26 ALA B   40  ALA B   44  5                                   5    
HELIX   27  27 GLY B   52  TYR B   59  5                                   8    
HELIX   28  28 GLU B   60  ALA B   78  1                                  19    
HELIX   29  29 PRO B   97  HIS B  110  1                                  14    
HELIX   30  30 ASP B  147  LYS B  162  1                                  16    
HELIX   31  31 THR B  206  PRO B  208  5                                   3    
HELIX   32  32 TRP B  209  GLY B  217  1                                   9    
HELIX   33  33 ASP B  278  VAL B  282  5                                   5    
HELIX   34  34 GLU B  285  PHE B  300  1                                  16    
HELIX   35  35 SER B  305  ILE B  309  5                                   5    
HELIX   36  36 SER B  326  ILE B  330  5                                   5    
HELIX   37  37 THR B  357  THR B  370  1                                  14    
HELIX   38  38 PRO B  371  TYR B  373  5                                   3    
HELIX   39  39 TRP B  380  SER B  384  5                                   5    
HELIX   40  40 ASP B  397  TYR B  406  1                                  10    
HELIX   41  41 THR B  410  TYR B  421  1                                  12    
HELIX   42  42 ASN B  424  GLY B  430  1                                   7    
HELIX   43  43 THR B  434  GLY B  439  5                                   6    
HELIX   44  44 TYR B  447  GLU B  458  1                                  12    
HELIX   45  45 ARG B  462  ARG B  469  1                                   8    
HELIX   46  46 LYS B  472  TRP B  476  5                                   5    
HELIX   47  47 ASN B  478  GLN B  495  1                                  18    
SHEET    1   A 6 GLU A 165  LEU A 167  0                                        
SHEET    2   A 6 VAL A  29  LEU A  32  1  N  MET A  31   O  GLU A 165           
SHEET    3   A 6 LEU A   6  ILE A   9  1  N  VAL A   8   O  LEU A  30           
SHEET    4   A 6 LEU A 202  ASN A 204  1  O  VAL A 203   N  ILE A   9           
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  HIS A 339   O  LEU A 347           
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  PHE A  87   O  TYR A 141           
SHEET    4   B 8 ALA A 245  GLN A 249  1  O  ALA A 245   N  ARG A  86           
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  GLY A 269   N  PHE A 257           
SHEET    7   B 8 ILE A 229  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  PHE A  87   O  TYR A 141           
SHEET    4   C 8 ALA A 245  GLN A 249  1  O  ALA A 245   N  ARG A  86           
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 229  PRO A 237 -1  N  ILE A 234   O  ILE A 268           
SHEET    8   C 8 TRP A 311  ARG A 317 -1  O  TRP A 311   N  VAL A 235           
SHEET    1   D 3 THR A 170  GLU A 178  0                                        
SHEET    2   D 3 LEU A 181  ASP A 188 -1  O  LEU A 181   N  GLU A 178           
SHEET    3   D 3 LYS A 194  ALA A 199 -1  O  TRP A 197   N  VAL A 184           
SHEET    1   E 4 THR B   3  LYS B   4  0                                        
SHEET    2   E 4 LYS B 194  ALA B 199  1  O  GLN B 198   N  LYS B   4           
SHEET    3   E 4 LEU B 181  ASP B 188 -1  N  TRP B 182   O  ALA B 199           
SHEET    4   E 4 THR B 170  GLU B 178 -1  N  GLU B 178   O  LEU B 181           
SHEET    1   F 6 GLU B 165  LEU B 167  0                                        
SHEET    2   F 6 VAL B  29  LEU B  32  1  N  MET B  31   O  GLU B 165           
SHEET    3   F 6 LEU B   6  ILE B   9  1  N  VAL B   8   O  LEU B  30           
SHEET    4   F 6 LEU B 202  ASN B 204  1  O  VAL B 203   N  ILE B   9           
SHEET    5   F 6 LYS B 344  PHE B 351  1  O  LEU B 348   N  ASN B 204           
SHEET    6   F 6 THR B 335  GLU B 341 -1  N  THR B 335   O  PHE B 351           
SHEET    1   G 8 LEU B  48  ILE B  49  0                                        
SHEET    2   G 8 ARG B 137  VAL B 146 -1  O  CYS B 144   N  ILE B  49           
SHEET    3   G 8 ALA B  82  PRO B  90 -1  N  LEU B  89   O  PHE B 139           
SHEET    4   G 8 ALA B 245  GLN B 249  1  O  ALA B 245   N  ARG B  86           
SHEET    5   G 8 ILE B 255  TRP B 261 -1  O  VAL B 256   N  LEU B 248           
SHEET    6   G 8 PHE B 265  GLY B 269 -1  O  GLY B 269   N  PHE B 257           
SHEET    7   G 8 ILE B 229  PRO B 237 -1  N  ILE B 234   O  ILE B 268           
SHEET    8   G 8 VAL B 273  GLU B 274 -1  O  VAL B 273   N  LYS B 230           
SHEET    1   H 8 THR B 121  ARG B 124  0                                        
SHEET    2   H 8 ARG B 137  VAL B 146 -1  O  GLU B 140   N  THR B 121           
SHEET    3   H 8 ALA B  82  PRO B  90 -1  N  LEU B  89   O  PHE B 139           
SHEET    4   H 8 ALA B 245  GLN B 249  1  O  ALA B 245   N  ARG B  86           
SHEET    5   H 8 ILE B 255  TRP B 261 -1  O  VAL B 256   N  LEU B 248           
SHEET    6   H 8 PHE B 265  GLY B 269 -1  O  GLY B 269   N  PHE B 257           
SHEET    7   H 8 ILE B 229  PRO B 237 -1  N  ILE B 234   O  ILE B 268           
SHEET    8   H 8 TRP B 311  ARG B 317 -1  O  TRP B 311   N  VAL B 235           
CISPEP   1 GLY A  269    THR A  270          0        26.14                     
CISPEP   2 ARG A  395    ASP A  396          0        -1.63                     
CISPEP   3 ASP A  396    ASP A  397          0        -1.27                     
CISPEP   4 GLY B  269    THR B  270          0         0.93                     
CISPEP   5 ASP B  396    ASP B  397          0         1.32                     
SITE     1 AC1  1 TRP A  99                                                     
SITE     1 AC2  4 TRP A  99  ARG A 102  ARG A 137  BOG A 800                    
SITE     1 AC3  7 HIS A  91  PRO A  93  PRO A  97  ALA A  98                    
SITE     2 AC3  7 GLU A 134  LYS A 136  BOG A 701                               
SITE     1 AC4  9 LEU A  53  ARG A  54  LEU A  56  GLU A  57                    
SITE     2 AC4  9 TYR A  59  ARG A  96  ILE A 101  GLY A 104                    
SITE     3 AC4  9 MET A 107                                                     
SITE     1 AC5  6 ALA B  98  TRP B  99  ILE B 103  ARG B 137                    
SITE     2 AC5  6 BOG B 800  EDO B 820                                          
SITE     1 AC6  6 TYR A  59  ARG A  62  ARG B 102  THR B 121                    
SITE     2 AC6  6 GLY B 122  BOG B 700                                          
SITE     1 AC7  5 VAL A 310  TRP A 311  TRP A 468  GLY A 474                    
SITE     2 AC7  5 MET A 475                                                     
SITE     1 AC8  5 HIS A  80  PHE A  83  ASP A 394  ARG A 419                    
SITE     2 AC8  5 HOH A1031                                                     
SITE     1 AC9  4 VAL B 310  TRP B 468  GLY B 474  MET B 475                    
SITE     1 BC1  7 ARG A 161  HOH A 942  TYR B 398  ARG B 401                    
SITE     2 BC1  7 LEU B 402  ARG B 405  GLU B 426                               
SITE     1 BC2  9 ARG A  54  TYR A  55  ARG A 317  ARG A 332                    
SITE     2 BC2  9 LYS A 354  HOH A 897  HOH A 973  HOH A 989                    
SITE     3 BC2  9 HOH A1057                                                     
SITE     1 BC3  9 ARG B  54  TYR B  55  ARG B 317  ARG B 332                    
SITE     2 BC3  9 HOH B 908  HOH B 922  HOH B 943  HOH B1005                    
SITE     3 BC3  9 HOH B1038                                                     
SITE     1 BC4 34 ILE A   9  GLY A  10  GLY A  11  GLY A  12                    
SITE     2 BC4 34 ILE A  13  ASN A  14  GLU A  33  ALA A  34                    
SITE     3 BC4 34 CYS A  39  ALA A  40  THR A  41  SER A  42                    
SITE     4 BC4 34 ALA A  44  SER A  45  SER A  46  LYS A  47                    
SITE     5 BC4 34 LEU A  48  HIS A  50  ALA A 172  THR A 206                    
SITE     6 BC4 34 GLY A 207  PRO A 208  PHE A 213  GLY A 231                    
SITE     7 BC4 34 THR A 270  ARG A 317  GLY A 353  LYS A 354                    
SITE     8 BC4 34 LEU A 355  THR A 356  EDO A 806  HOH A 824                    
SITE     9 BC4 34 HOH A 825  HOH A1052                                          
SITE     1 BC5 32 ILE B   9  GLY B  10  GLY B  12  ILE B  13                    
SITE     2 BC5 32 ASN B  14  LEU B  32  GLU B  33  ALA B  34                    
SITE     3 BC5 32 CYS B  39  ALA B  40  THR B  41  SER B  42                    
SITE     4 BC5 32 ALA B  44  SER B  45  SER B  46  LYS B  47                    
SITE     5 BC5 32 LEU B  48  HIS B  50  ALA B 172  THR B 206                    
SITE     6 BC5 32 GLY B 207  PRO B 208  GLY B 231  ARG B 317                    
SITE     7 BC5 32 GLY B 353  LYS B 354  LEU B 355  THR B 356                    
SITE     8 BC5 32 EDO B 806  HOH B 821  HOH B 822  HOH B1050                    
SITE     1 BC6  8 ALA A  23  GLY A  24  LYS A 162  HOH A 942                    
SITE     2 BC6  8 HOH A1056  ARG B 401  ARG B 404  HOH B 971                    
SITE     1 BC7  4 ALA A  34  ARG A 171  LYS A 280  FAD A 600                    
SITE     1 BC8  4 HIS A 444  GLU A 445  GLN A 473  EDO A 811                    
SITE     1 BC9  8 SER A  43  TRP A 311  TRP A 468  EDO A 812                    
SITE     2 BC9  8 HOH A 826  HOH A 832  HOH A1034  HOH A1035                    
SITE     1 CC1  5 GLN A 303  EDO A 815  HOH A 964  HOH A1039                    
SITE     2 CC1  5 EDO B 805                                                     
SITE     1 CC2  2 ARG A 306  ILE A 309                                          
SITE     1 CC3  7 HIS A 416  THR A 471  LYS A 472  GLN A 473                    
SITE     2 CC3  7 TRP A 476  IMD A 807  HOH A 872                               
SITE     1 CC4  3 TRP A 311  TRP A 468  EDO A 808                               
SITE     1 CC5  1 GLU A 448                                                     
SITE     1 CC6  2 GLU A 440  ASP A 441                                          
SITE     1 CC7  5 ASN A 294  ASN A 297  THR A 298  EDO A 809                    
SITE     2 CC7  5 HOH A 928                                                     
SITE     1 CC8  5 ASN A 294  HOH A 947  SER B 305  ARG B 306                    
SITE     2 CC8  5 HOH B 839                                                     
SITE     1 CC9  4 ARG A 254  THR A 271  ASP A 272  TAM A 823                    
SITE     1 DC1  8 ALA A  40  THR A  41  PRO A 279  LYS A 280                    
SITE     2 DC1  8 VAL A 282  GLY A 315  VAL A 316  HOH A1043                    
SITE     1 DC2  4 ARG A 404  ALA B  23  GLY B  24  HOH B1025                    
SITE     1 DC3  4 ASP A 397  ARG A 404  HOH A 939  HOH A 969                    
SITE     1 DC4  7 GLN A 157  ASN A 424  LEU A 427  TYR A 453                    
SITE     2 DC4  7 EDO A 822  HOH A1066  HOH B 957                               
SITE     1 DC5  6 GLN A 157  HIS A 457  TRP A 459  IMD A 821                    
SITE     2 DC5  6 HOH A1063  ARG B 405                                          
SITE     1 DC6 10 ASP A 272  VAL A 273  GLU A 274  GLU A 285                    
SITE     2 DC6 10 SER A 287  GLU A 288  EDO A 817  GLU B 285                    
SITE     3 DC6 10 SER B 287  HOH B 924                                          
SITE     1 DC7  3 ARG B 254  THR B 271  ASP B 272                               
SITE     1 DC8  5 EDO A 809  LEU B 293  ASN B 294  ASN B 297                    
SITE     2 DC8  5 HOH B 860                                                     
SITE     1 DC9  4 ALA B  34  TRP B 209  LYS B 280  FAD B 600                    
SITE     1 EC1  3 TRP B 311  TRP B 468  EDO B 811                               
SITE     1 EC2  4 MET B 262  EDO B 817  HOH B1030  HOH B1033                    
SITE     1 EC3  2 ILE B 289  ARG B 306                                          
SITE     1 EC4  9 ARG A 405  GLU A 426  GLN B 157  VAL B 160                    
SITE     2 EC4  9 ARG B 161  PRO B 387  ASN B 424  HIS B 457                    
SITE     3 EC4  9 HOH B1054                                                     
SITE     1 EC5  7 SER B  43  ALA B  44  TRP B 311  TRP B 468                    
SITE     2 EC5  7 EDO B 807  HOH B 830  HOH B 833                               
SITE     1 EC6  7 ARG B  88  ARG B 124  PHE B 125  SER B 129                    
SITE     2 EC6  7 VAL B 130  GLN B 242  HOH B1000                               
SITE     1 EC7  4 PRO B 208  GLN B 212  LEU B 228  PRO B 279                    
SITE     1 EC8  5 VAL B 455  ASP B 456  HIS B 457  GLU B 458                    
SITE     2 EC8  5 TRP B 459                                                     
SITE     1 EC9  1 ILE B 101                                                     
SITE     1 FC1  5 HIS B 416  EDO B 808  EDO B 819  HOH B 826                    
SITE     2 FC1  5 HOH B1028                                                     
SITE     1 FC2  5 HIS B 444  GLU B 445  GLN B 473  EDO B 817                    
SITE     2 FC2  5 HOH B 866                                                     
SITE     1 FC3  5 HIS B  91  PRO B  93  PRO B  97  ALA B  98                    
SITE     2 FC3  5 BOG B 700                                                     
CRYST1  113.791  114.097  192.801  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      0.008788  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008764  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005187        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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