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Database: PDB
Entry: 2R0G
LinkDB: 2R0G
Original site: 2R0G 
HEADER    OXIDOREDUCTASE                          19-AUG-07   2R0G              
TITLE     CHROMOPYRROLIC ACID-SOAKED REBC WITH BOUND 7-CARBOXY-K252C            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: REBC;                                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PUTATIVE MONOOXYGENASE, PUTATIVE FAD-MONOOXYGENASE;         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LECHEVALIERIA AEROCOLONIGENES;                  
SOURCE   3 ORGANISM_TAXID: 68170;                                               
SOURCE   4 STRAIN: ATCC 39243;                                                  
SOURCE   5 GENE: RBMD, REBC;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    FLAVIN ADENINE DINUCLEOTIDE, CHROMOPYRROLIC ACID, 7-CARBOXY-K252C,    
KEYWDS   2 MONOOXYGENASE, OXIDOREDUCTASE                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.S.RYAN,C.L.DRENNAN                                                  
REVDAT   3   30-AUG-23 2R0G    1       REMARK SEQADV                            
REVDAT   2   24-FEB-09 2R0G    1       VERSN                                    
REVDAT   1   25-SEP-07 2R0G    0                                                
JRNL        AUTH   K.S.RYAN,A.R.HOWARD-JONES,M.J.HAMILL,S.J.ELLIOTT,C.T.WALSH,  
JRNL        AUTH 2 C.L.DRENNAN                                                  
JRNL        TITL   CRYSTALLOGRAPHIC TRAPPING IN THE REBECCAMYCIN BIOSYNTHETIC   
JRNL        TITL 2 ENZYME REBC                                                  
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 104 15311 2007              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   17873060                                                     
JRNL        DOI    10.1073/PNAS.0707190104                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.37 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.37                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 45763                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2283                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7965                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 160                                     
REMARK   3   SOLVENT ATOMS            : 353                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.32                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.33                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.41                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.41                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.304                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2R0G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-AUG-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000044271.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-MAR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 141.4                              
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46328                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.370                              
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     (%) : 90.8                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.37                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.45                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 61.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.27400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2R0C                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.48                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 MICROLITERS OF REBC (9 MG/ML IN      
REMARK 280  150 MM NACL, 10% GLYCEROL, 25 MM HEPES PH 7.5) WAS INCUBATED        
REMARK 280  WITH 0.35 MICROLITERS OF GUANIDINE-HCL FOR 30 SECONDS, FOLLOWED     
REMARK 280  BY ADDITION OF 1.5 MICROLITERS OF PRECIPITANT SOLUTION (19% PEG-    
REMARK 280  8000, 0.1 M HEPES PH 7.4), WITHOUT MIXING, AT ROOM TEMPERATURE      
REMARK 280  AND SEALED OVER A PRECIPITANT WELL SOLUTION. IMMEDIATELY AFTER      
REMARK 280  SET UP, CRYSTAL TRAYS WERE PLACED ON A GEL SHAKER AND THEN,         
REMARK 280  AFTER 12 HOURS, TRANSFERRED TO A STORAGE SPACE IN VIBRATION-        
REMARK 280  ISOLATION. A CRYSTAL WAS THEN SOAKED IN 19% PEG-8000, 0.1 M         
REMARK 280  HEPES PH 7.4, AND 5 MM CHROMOPYRROLIC ACID FOR 1 WEEK. THE          
REMARK 280  CRYSTAL WAS THEN SOAKED FOR 5 SECONDS IN A CRYOGENIC SOLUTION       
REMARK 280  CONTAINING 19% PEG-8000, 0.1 M HEPES PH 7.4, 20% GLYCEROL, AND 5    
REMARK 280  MM CHROMOPYRROLIC ACID AND THEN FLASH-FROZEN IN LIQUID NITROGEN,    
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
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       39.21850            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
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     MET A   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     ASP A   246                                                      
REMARK 465     ALA A   247                                                      
REMARK 465     SER A   248                                                      
REMARK 465     LYS A   249                                                      
REMARK 465     SER A   250                                                      
REMARK 465     MET B   -19                                                      
REMARK 465     GLY B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     VAL B    -5                                                      
REMARK 465     PRO B    -4                                                      
REMARK 465     ARG B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ASN B     2                                                      
REMARK 465     ASP B   246                                                      
REMARK 465     ALA B   247                                                      
REMARK 465     SER B   248                                                      
REMARK 465     LYS B   249                                                      
REMARK 465     SER B   250                                                      
REMARK 465     GLU B   418                                                      
REMARK 465     THR B   419                                                      
REMARK 465     GLU B   420                                                      
REMARK 465     VAL B   421                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 161    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 245    CG   OD1  OD2                                       
REMARK 470     THR A 251    OG1  CG2                                            
REMARK 470     GLU A 418    CG   CD   OE1  OE2                                  
REMARK 470     THR A 419    OG1  CG2                                            
REMARK 470     GLU A 420    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 421    CG1  CG2                                            
REMARK 470     LEU B 370    CG   CD1  CD2                                       
REMARK 470     ARG B 379    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE B 380    CG1  CG2  CD1                                       
REMARK 470     GLU B 386    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 390    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 203   C   -  N   -  CA  ANGL. DEV. =  10.2 DEGREES          
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    ARG A  46      -63.76    -98.74                                   
REMARK 500    ARG A 131        1.07    -66.73                                   
REMARK 500    ARG A 144     -164.47   -103.29                                   
REMARK 500    CYS A 171       54.98   -118.92                                   
REMARK 500    SER A 176      106.62    -33.45                                   
REMARK 500    ALA A 186       75.82   -117.00                                   
REMARK 500    LEU A 225       68.21   -114.16                                   
REMARK 500    ARG A 235       31.58   -152.15                                   
REMARK 500    ALA A 263       46.84    -81.31                                   
REMARK 500    ALA A 288      109.92   -163.67                                   
REMARK 500    PRO A 368      -75.77    -38.46                                   
REMARK 500    PRO A 375      -16.29    -47.16                                   
REMARK 500    ASP A 398       78.12   -156.05                                   
REMARK 500    ALA A 399       58.95   -114.11                                   
REMARK 500    GLU A 418      115.28    -25.08                                   
REMARK 500    VAL A 421       95.80   -160.39                                   
REMARK 500    ARG A 453      -93.39    -98.24                                   
REMARK 500    ALA A 487      102.80    -16.83                                   
REMARK 500    GLU A 495      -43.77     72.49                                   
REMARK 500    GLN B  29       53.64     38.72                                   
REMARK 500    ARG B  46      -66.61   -101.67                                   
REMARK 500    SER B 176      106.00    -33.40                                   
REMARK 500    GLU B 211        9.65    -68.72                                   
REMARK 500    MET B 220       55.37   -142.68                                   
REMARK 500    LEU B 225       66.92   -101.49                                   
REMARK 500    MET B 252     -137.80    -98.13                                   
REMARK 500    SER B 254      -78.14    -36.94                                   
REMARK 500    PHE B 264      144.76    -38.74                                   
REMARK 500    ALA B 288      102.25   -164.99                                   
REMARK 500    SER B 304       92.19    -64.98                                   
REMARK 500    ASP B 398       80.28   -155.30                                   
REMARK 500    ALA B 399       66.35   -117.25                                   
REMARK 500    ARG B 409       72.99   -116.39                                   
REMARK 500    THR B 423     -151.87    -72.71                                   
REMARK 500    ARG B 453      -99.80   -104.15                                   
REMARK 500    GLU B 495       -1.93     57.84                                   
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 FAD A 1354                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 7CK A 1355                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 1356                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 7CK B 1357                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2R0C   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE SUBSTRATE-FREE FORM OF THE REBECCAMYCIN             
REMARK 900 BIOSYNTHETIC ENZYME REBC                                             
REMARK 900 RELATED ID: 2R0P   RELATED DB: PDB                                   
REMARK 900 K252C-SOAKED REBC                                                    
DBREF  2R0G A    1   529  UNP    Q8KI25   Q8KI25_NOCAE     1    529             
DBREF  2R0G B    1   529  UNP    Q8KI25   Q8KI25_NOCAE     1    529             
SEQADV 2R0G MET A  -19  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G GLY A  -18  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G SER A  -17  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G SER A  -16  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G HIS A  -15  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G HIS A  -14  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G HIS A  -13  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G HIS A  -12  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G HIS A  -11  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G HIS A  -10  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G SER A   -9  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G SER A   -8  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G GLY A   -7  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G LEU A   -6  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G VAL A   -5  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G PRO A   -4  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G ARG A   -3  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G GLY A   -2  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G SER A   -1  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G HIS A    0  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G MET B  -19  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G GLY B  -18  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G SER B  -17  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G SER B  -16  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G HIS B  -15  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G HIS B  -14  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G HIS B  -13  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G HIS B  -12  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G HIS B  -11  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G HIS B  -10  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G SER B   -9  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G SER B   -8  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G GLY B   -7  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G LEU B   -6  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G VAL B   -5  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G PRO B   -4  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G ARG B   -3  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G GLY B   -2  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G SER B   -1  UNP  Q8KI25              EXPRESSION TAG                 
SEQADV 2R0G HIS B    0  UNP  Q8KI25              EXPRESSION TAG                 
SEQRES   1 A  549  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  549  LEU VAL PRO ARG GLY SER HIS MET ASN ALA PRO ILE GLU          
SEQRES   3 A  549  THR ASP VAL LEU ILE LEU GLY GLY GLY PRO VAL GLY MET          
SEQRES   4 A  549  ALA LEU ALA LEU ASP LEU ALA HIS ARG GLN VAL GLY HIS          
SEQRES   5 A  549  LEU VAL VAL GLU GLN THR ASP GLY THR ILE THR HIS PRO          
SEQRES   6 A  549  ARG VAL GLY THR ILE GLY PRO ARG SER MET GLU LEU PHE          
SEQRES   7 A  549  ARG ARG TRP GLY VAL ALA LYS GLN ILE ARG THR ALA GLY          
SEQRES   8 A  549  TRP PRO GLY ASP HIS PRO LEU ASP ALA ALA TRP VAL THR          
SEQRES   9 A  549  ARG VAL GLY GLY HIS GLU VAL TYR ARG ILE PRO LEU GLY          
SEQRES  10 A  549  THR ALA ASP THR ARG ALA THR PRO GLU HIS THR PRO GLU          
SEQRES  11 A  549  PRO ASP ALA ILE CYS PRO GLN HIS TRP LEU ALA PRO LEU          
SEQRES  12 A  549  LEU ALA GLU ALA VAL GLY GLU ARG LEU ARG THR ARG SER          
SEQRES  13 A  549  ARG LEU ASP SER PHE GLU GLN ARG ASP ASP HIS VAL ARG          
SEQRES  14 A  549  ALA THR ILE THR ASP LEU ARG THR GLY ALA THR ARG ALA          
SEQRES  15 A  549  VAL HIS ALA ARG TYR LEU VAL ALA CYS ASP GLY ALA SER          
SEQRES  16 A  549  SER PRO THR ARG LYS ALA LEU GLY ILE ASP ALA PRO PRO          
SEQRES  17 A  549  ARG HIS ARG THR GLN VAL PHE ARG ASN ILE LEU PHE ARG          
SEQRES  18 A  549  ALA PRO GLU LEU ARG SER LEU LEU GLY GLU ARG ALA ALA          
SEQRES  19 A  549  LEU PHE PHE PHE LEU MET LEU SER SER SER LEU ARG PHE          
SEQRES  20 A  549  PRO LEU ARG ALA LEU ASP GLY ARG GLY LEU TYR ARG LEU          
SEQRES  21 A  549  THR VAL GLY VAL ASP ASP ALA SER LYS SER THR MET ASP          
SEQRES  22 A  549  SER PHE GLU LEU VAL ARG ARG ALA VAL ALA PHE ASP THR          
SEQRES  23 A  549  GLU ILE GLU VAL LEU SER ASP SER GLU TRP HIS LEU THR          
SEQRES  24 A  549  HIS ARG VAL ALA ASP SER PHE SER ALA GLY ARG VAL PHE          
SEQRES  25 A  549  LEU THR GLY ASP ALA ALA HIS THR LEU SER PRO SER GLY          
SEQRES  26 A  549  GLY PHE GLY MET ASN THR GLY ILE GLY SER ALA ALA ASP          
SEQRES  27 A  549  LEU GLY TRP LYS LEU ALA ALA THR LEU ARG GLY TRP ALA          
SEQRES  28 A  549  GLY PRO GLY LEU LEU ALA THR TYR GLU GLU GLU ARG ARG          
SEQRES  29 A  549  PRO VAL ALA ILE THR SER LEU GLU GLU ALA ASN VAL ASN          
SEQRES  30 A  549  LEU ARG ARG THR MET ASP ARG GLU LEU PRO PRO GLY LEU          
SEQRES  31 A  549  HIS ASP ASP GLY PRO ARG GLY GLU ARG ILE ARG ALA ALA          
SEQRES  32 A  549  VAL ALA GLU LYS LEU GLU ARG SER GLY ALA ARG ARG GLU          
SEQRES  33 A  549  PHE ASP ALA PRO GLY ILE HIS PHE GLY HIS THR TYR ARG          
SEQRES  34 A  549  SER SER ILE VAL CYS GLY GLU PRO GLU THR GLU VAL ALA          
SEQRES  35 A  549  THR GLY GLY TRP ARG PRO SER ALA ARG PRO GLY ALA ARG          
SEQRES  36 A  549  ALA PRO HIS ALA TRP LEU THR PRO THR THR SER THR LEU          
SEQRES  37 A  549  ASP LEU PHE GLY ARG GLY PHE VAL LEU LEU SER PHE GLY          
SEQRES  38 A  549  THR THR ASP GLY VAL GLU ALA VAL THR ARG ALA PHE ALA          
SEQRES  39 A  549  ASP ARG HIS VAL PRO LEU GLU THR VAL THR CYS HIS ALA          
SEQRES  40 A  549  PRO GLU ILE HIS ALA LEU TYR GLU ARG ALA HIS VAL LEU          
SEQRES  41 A  549  VAL ARG PRO ASP GLY HIS VAL ALA TRP ARG GLY ASP HIS          
SEQRES  42 A  549  LEU PRO ALA GLU LEU GLY GLY LEU VAL ASP LYS VAL ARG          
SEQRES  43 A  549  GLY ALA ALA                                                  
SEQRES   1 B  549  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  549  LEU VAL PRO ARG GLY SER HIS MET ASN ALA PRO ILE GLU          
SEQRES   3 B  549  THR ASP VAL LEU ILE LEU GLY GLY GLY PRO VAL GLY MET          
SEQRES   4 B  549  ALA LEU ALA LEU ASP LEU ALA HIS ARG GLN VAL GLY HIS          
SEQRES   5 B  549  LEU VAL VAL GLU GLN THR ASP GLY THR ILE THR HIS PRO          
SEQRES   6 B  549  ARG VAL GLY THR ILE GLY PRO ARG SER MET GLU LEU PHE          
SEQRES   7 B  549  ARG ARG TRP GLY VAL ALA LYS GLN ILE ARG THR ALA GLY          
SEQRES   8 B  549  TRP PRO GLY ASP HIS PRO LEU ASP ALA ALA TRP VAL THR          
SEQRES   9 B  549  ARG VAL GLY GLY HIS GLU VAL TYR ARG ILE PRO LEU GLY          
SEQRES  10 B  549  THR ALA ASP THR ARG ALA THR PRO GLU HIS THR PRO GLU          
SEQRES  11 B  549  PRO ASP ALA ILE CYS PRO GLN HIS TRP LEU ALA PRO LEU          
SEQRES  12 B  549  LEU ALA GLU ALA VAL GLY GLU ARG LEU ARG THR ARG SER          
SEQRES  13 B  549  ARG LEU ASP SER PHE GLU GLN ARG ASP ASP HIS VAL ARG          
SEQRES  14 B  549  ALA THR ILE THR ASP LEU ARG THR GLY ALA THR ARG ALA          
SEQRES  15 B  549  VAL HIS ALA ARG TYR LEU VAL ALA CYS ASP GLY ALA SER          
SEQRES  16 B  549  SER PRO THR ARG LYS ALA LEU GLY ILE ASP ALA PRO PRO          
SEQRES  17 B  549  ARG HIS ARG THR GLN VAL PHE ARG ASN ILE LEU PHE ARG          
SEQRES  18 B  549  ALA PRO GLU LEU ARG SER LEU LEU GLY GLU ARG ALA ALA          
SEQRES  19 B  549  LEU PHE PHE PHE LEU MET LEU SER SER SER LEU ARG PHE          
SEQRES  20 B  549  PRO LEU ARG ALA LEU ASP GLY ARG GLY LEU TYR ARG LEU          
SEQRES  21 B  549  THR VAL GLY VAL ASP ASP ALA SER LYS SER THR MET ASP          
SEQRES  22 B  549  SER PHE GLU LEU VAL ARG ARG ALA VAL ALA PHE ASP THR          
SEQRES  23 B  549  GLU ILE GLU VAL LEU SER ASP SER GLU TRP HIS LEU THR          
SEQRES  24 B  549  HIS ARG VAL ALA ASP SER PHE SER ALA GLY ARG VAL PHE          
SEQRES  25 B  549  LEU THR GLY ASP ALA ALA HIS THR LEU SER PRO SER GLY          
SEQRES  26 B  549  GLY PHE GLY MET ASN THR GLY ILE GLY SER ALA ALA ASP          
SEQRES  27 B  549  LEU GLY TRP LYS LEU ALA ALA THR LEU ARG GLY TRP ALA          
SEQRES  28 B  549  GLY PRO GLY LEU LEU ALA THR TYR GLU GLU GLU ARG ARG          
SEQRES  29 B  549  PRO VAL ALA ILE THR SER LEU GLU GLU ALA ASN VAL ASN          
SEQRES  30 B  549  LEU ARG ARG THR MET ASP ARG GLU LEU PRO PRO GLY LEU          
SEQRES  31 B  549  HIS ASP ASP GLY PRO ARG GLY GLU ARG ILE ARG ALA ALA          
SEQRES  32 B  549  VAL ALA GLU LYS LEU GLU ARG SER GLY ALA ARG ARG GLU          
SEQRES  33 B  549  PHE ASP ALA PRO GLY ILE HIS PHE GLY HIS THR TYR ARG          
SEQRES  34 B  549  SER SER ILE VAL CYS GLY GLU PRO GLU THR GLU VAL ALA          
SEQRES  35 B  549  THR GLY GLY TRP ARG PRO SER ALA ARG PRO GLY ALA ARG          
SEQRES  36 B  549  ALA PRO HIS ALA TRP LEU THR PRO THR THR SER THR LEU          
SEQRES  37 B  549  ASP LEU PHE GLY ARG GLY PHE VAL LEU LEU SER PHE GLY          
SEQRES  38 B  549  THR THR ASP GLY VAL GLU ALA VAL THR ARG ALA PHE ALA          
SEQRES  39 B  549  ASP ARG HIS VAL PRO LEU GLU THR VAL THR CYS HIS ALA          
SEQRES  40 B  549  PRO GLU ILE HIS ALA LEU TYR GLU ARG ALA HIS VAL LEU          
SEQRES  41 B  549  VAL ARG PRO ASP GLY HIS VAL ALA TRP ARG GLY ASP HIS          
SEQRES  42 B  549  LEU PRO ALA GLU LEU GLY GLY LEU VAL ASP LYS VAL ARG          
SEQRES  43 B  549  GLY ALA ALA                                                  
HET    FAD  A1354      53                                                       
HET    7CK  A1355      27                                                       
HET    FAD  B1356      53                                                       
HET    7CK  B1357      27                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     7CK 7-CARBOXY-5-HYDROXY-12,13-DIHYDRO-6H-INDOLO[2,3-                 
HETNAM   2 7CK  A]PYRROLO[3,4-C]CARBAZOLE                                       
HETSYN     7CK 7-HYDROXY-12,13-DIHYDRO-6H-INDOLO[2,3-A]PYRROLO[3,4-             
HETSYN   2 7CK  C]CARBAZOLE-5-CARBOXYLIC ACID                                   
FORMUL   3  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL   4  7CK    2(C21 H13 N3 O3)                                             
FORMUL   7  HOH   *353(H2 O)                                                    
HELIX    1   1 GLY A   15  HIS A   27  1                                  13    
HELIX    2   2 GLY A   51  TRP A   61  1                                  11    
HELIX    3   3 VAL A   63  THR A   69  1                                   7    
HELIX    4   4 PRO A  116  GLY A  129  1                                  14    
HELIX    5   5 SER A  176  LEU A  182  1                                   7    
HELIX    6   6 GLU A  204  GLY A  210  1                                   7    
HELIX    7   7 GLU A  211  ALA A  213  5                                   3    
HELIX    8   8 ASP A  253  VAL A  262  1                                  10    
HELIX    9   9 GLY A  295  ALA A  298  5                                   4    
HELIX   10  10 PHE A  307  GLY A  329  1                                  23    
HELIX   11  11 ALA A  337  ASP A  363  1                                  27    
HELIX   12  12 GLY A  374  SER A  391  1                                  18    
HELIX   13  13 GLY A  392  PHE A  397  5                                   6    
HELIX   14  14 ALA A  399  GLY A  405  1                                   7    
HELIX   15  15 LEU A  448  PHE A  451  5                                   4    
HELIX   16  16 GLY A  465  ASP A  475  1                                  11    
HELIX   17  17 ALA A  487  GLU A  495  1                                   9    
HELIX   18  18 GLU A  517  ARG A  526  1                                  10    
HELIX   19  19 GLY B   15  HIS B   27  1                                  13    
HELIX   20  20 GLY B   51  TRP B   61  1                                  11    
HELIX   21  21 VAL B   63  THR B   69  1                                   7    
HELIX   22  22 PRO B  116  GLY B  129  1                                  14    
HELIX   23  23 SER B  176  LEU B  182  1                                   7    
HELIX   24  24 GLU B  204  GLY B  210  1                                   7    
HELIX   25  25 GLU B  211  ALA B  213  5                                   3    
HELIX   26  26 ASP B  253  VAL B  262  1                                  10    
HELIX   27  27 GLY B  295  ALA B  298  5                                   4    
HELIX   28  28 PHE B  307  GLY B  329  1                                  23    
HELIX   29  29 ALA B  337  ARG B  364  1                                  28    
HELIX   30  30 GLY B  374  GLY B  392  1                                  19    
HELIX   31  31 ALA B  393  ASP B  398  5                                   6    
HELIX   32  32 ALA B  399  GLY B  405  1                                   7    
HELIX   33  33 LEU B  448  PHE B  451  5                                   4    
HELIX   34  34 GLY B  465  ARG B  476  1                                  12    
HELIX   35  35 ALA B  487  GLU B  495  1                                   9    
HELIX   36  36 GLU B  517  ARG B  526  1                                  10    
SHEET    1   A 6 LEU A 132  THR A 134  0                                        
SHEET    2   A 6 HIS A  32  GLU A  36  1  N  VAL A  34   O  ARG A 133           
SHEET    3   A 6 ILE A   5  LEU A  12  1  N  ILE A  11   O  LEU A  33           
SHEET    4   A 6 THR A 160  ALA A 170  1  O  VAL A 169   N  LEU A  12           
SHEET    5   A 6 VAL A 148  ASP A 154 -1  N  VAL A 148   O  ALA A 165           
SHEET    6   A 6 SER A 136  GLN A 143 -1  N  ARG A 137   O  THR A 153           
SHEET    1   B 6 LEU A 132  THR A 134  0                                        
SHEET    2   B 6 HIS A  32  GLU A  36  1  N  VAL A  34   O  ARG A 133           
SHEET    3   B 6 ILE A   5  LEU A  12  1  N  ILE A  11   O  LEU A  33           
SHEET    4   B 6 THR A 160  ALA A 170  1  O  VAL A 169   N  LEU A  12           
SHEET    5   B 6 VAL A 291  LEU A 293  1  O  PHE A 292   N  ALA A 170           
SHEET    6   B 6 SER A 287  ALA A 288 -1  N  ALA A 288   O  VAL A 291           
SHEET    1   C 2 THR A  49  ILE A  50  0                                        
SHEET    2   C 2 ALA A 113  ILE A 114 -1  O  ALA A 113   N  ILE A  50           
SHEET    1   D 7 GLU A  90  ILE A  94  0                                        
SHEET    2   D 7 ALA A  80  VAL A  83 -1  N  TRP A  82   O  TYR A  92           
SHEET    3   D 7 PHE A 216  LEU A 219  1  O  PHE A 218   N  ALA A  81           
SHEET    4   D 7 PRO A 228  ALA A 231 -1  O  LEU A 229   N  PHE A 217           
SHEET    5   D 7 LEU A 237  GLY A 243 -1  O  ARG A 239   N  ARG A 230           
SHEET    6   D 7 GLN A 193  ARG A 201 -1  N  ARG A 196   O  VAL A 242           
SHEET    7   D 7 GLU A 269  LEU A 278 -1  O  LEU A 271   N  LEU A 199           
SHEET    1   E 2 TRP A 440  THR A 442  0                                        
SHEET    2   E 2 THR A 445  SER A 446 -1  O  THR A 445   N  LEU A 441           
SHEET    1   F 4 LEU A 480  THR A 484  0                                        
SHEET    2   F 4 PHE A 455  SER A 459  1  N  LEU A 457   O  GLU A 481           
SHEET    3   F 4 HIS A 498  VAL A 501 -1  O  VAL A 501   N  VAL A 456           
SHEET    4   F 4 VAL A 507  GLY A 511 -1  O  ALA A 508   N  LEU A 500           
SHEET    1   G 6 LEU B 132  ARG B 133  0                                        
SHEET    2   G 6 HIS B  32  VAL B  35  1  N  VAL B  34   O  ARG B 133           
SHEET    3   G 6 ILE B   5  LEU B  12  1  N  ILE B  11   O  LEU B  33           
SHEET    4   G 6 THR B 160  ALA B 170  1  O  TYR B 167   N  LEU B  10           
SHEET    5   G 6 VAL B 148  ASP B 154 -1  N  ILE B 152   O  ARG B 161           
SHEET    6   G 6 SER B 136  GLN B 143 -1  N  GLU B 142   O  ARG B 149           
SHEET    1   H 6 LEU B 132  ARG B 133  0                                        
SHEET    2   H 6 HIS B  32  VAL B  35  1  N  VAL B  34   O  ARG B 133           
SHEET    3   H 6 ILE B   5  LEU B  12  1  N  ILE B  11   O  LEU B  33           
SHEET    4   H 6 THR B 160  ALA B 170  1  O  TYR B 167   N  LEU B  10           
SHEET    5   H 6 VAL B 291  LEU B 293  1  O  PHE B 292   N  ALA B 170           
SHEET    6   H 6 SER B 287  ALA B 288 -1  N  ALA B 288   O  VAL B 291           
SHEET    1   I 2 THR B  49  ILE B  50  0                                        
SHEET    2   I 2 ALA B 113  ILE B 114 -1  O  ALA B 113   N  ILE B  50           
SHEET    1   J 7 GLU B  90  ILE B  94  0                                        
SHEET    2   J 7 ALA B  80  VAL B  83 -1  N  TRP B  82   O  TYR B  92           
SHEET    3   J 7 PHE B 216  LEU B 219  1  O  PHE B 218   N  VAL B  83           
SHEET    4   J 7 PRO B 228  ALA B 231 -1  O  LEU B 229   N  PHE B 217           
SHEET    5   J 7 LEU B 237  VAL B 244 -1  O  ARG B 239   N  ARG B 230           
SHEET    6   J 7 GLN B 193  ARG B 201 -1  N  ARG B 196   O  VAL B 242           
SHEET    7   J 7 GLU B 269  LEU B 278 -1  O  SER B 274   N  ASN B 197           
SHEET    1   K 2 TRP B 440  THR B 442  0                                        
SHEET    2   K 2 THR B 445  SER B 446 -1  O  THR B 445   N  LEU B 441           
SHEET    1   L 4 LEU B 480  THR B 484  0                                        
SHEET    2   L 4 PHE B 455  SER B 459  1  N  LEU B 457   O  GLU B 481           
SHEET    3   L 4 HIS B 498  VAL B 501 -1  O  VAL B 501   N  VAL B 456           
SHEET    4   L 4 VAL B 507  GLY B 511 -1  O  TRP B 509   N  LEU B 500           
SITE     1 AC1 34 LEU A  12  GLY A  13  PRO A  16  VAL A  17                    
SITE     2 AC1 34 VAL A  35  GLU A  36  GLN A  37  THR A  38                    
SITE     3 AC1 34 ARG A  46  VAL A  47  GLY A  48  THR A  49                    
SITE     4 AC1 34 SER A 136  ARG A 137  LEU A 138  CYS A 171                    
SITE     5 AC1 34 ASP A 172  GLY A 173  ASN A 197  TRP A 276                    
SITE     6 AC1 34 GLY A 295  ASP A 296  GLY A 306  GLY A 308                    
SITE     7 AC1 34 MET A 309  ASN A 310  HOH A1050  HOH A1051                    
SITE     8 AC1 34 HOH A1059  HOH A1149  HOH A1224  HOH A1271                    
SITE     9 AC1 34 HOH A1291  7CK A1355                                          
SITE     1 AC2 13 THR A  49  PHE A 216  PHE A 227  ARG A 230                    
SITE     2 AC2 13 ARG A 239  PRO A 303  SER A 304  GLY A 305                    
SITE     3 AC2 13 LEU A 358  GLU A 396  PHE A 397  HOH A1224                    
SITE     4 AC2 13 FAD A1354                                                     
SITE     1 AC3 31 LEU B  12  GLY B  13  PRO B  16  VAL B  17                    
SITE     2 AC3 31 VAL B  35  GLU B  36  GLN B  37  ARG B  46                    
SITE     3 AC3 31 VAL B  47  GLY B  48  THR B  49  SER B 136                    
SITE     4 AC3 31 ARG B 137  LEU B 138  CYS B 171  ASN B 197                    
SITE     5 AC3 31 TRP B 276  GLY B 295  ASP B 296  GLY B 308                    
SITE     6 AC3 31 MET B 309  ASN B 310  HOH B1018  HOH B1092                    
SITE     7 AC3 31 HOH B1100  HOH B1195  HOH B1219  HOH B1243                    
SITE     8 AC3 31 HOH B1314  HOH B1315  7CK B1357                               
SITE     1 AC4 12 PHE B 216  PHE B 227  ARG B 230  ARG B 239                    
SITE     2 AC4 12 THR B 241  PRO B 303  SER B 304  GLY B 305                    
SITE     3 AC4 12 GLU B 396  PHE B 397  HOH B1195  FAD B1356                    
CRYST1   64.892   78.437  123.625  90.00  99.61  90.00 P 1 21 1      4          
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      0.015410  0.000000  0.002609        0.00000                         
SCALE2      0.000000  0.012749  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008204        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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