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Entry: 5YAK
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HEADER    OXIDOREDUCTASE                          01-SEP-17   5YAK              
TITLE     THE CRYSTAL STRUCTURE OF HUMAN IYD THR239 MUTANT WITH LIGAND 3-       
TITLE    2 FLUOROTYROSINE (F-TYR)                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: IODOTYROSINE DEIODINASE 1;                                 
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 FRAGMENT: UNP RESIDUES 32-289;                                       
COMPND   5 SYNONYM: IYD-1,IODOTYROSINE DEHALOGENASE 1;                          
COMPND   6 EC: 1.21.1.1;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 OTHER_DETAILS: FMN(FLAVIN MONONUCLEOTIDE) YOF(3-MONOFLUOROTYROSINE)  
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: IYD, C6ORF71, DEHAL1;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2(DE3);                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28-SUMO                                
KEYWDS    HIYD, FMN, MFT, T239A MUTANT, OXIDOREDUCTASE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.HU,S.E.ROKITA,J.SCHLESSMAN                                        
REVDAT   3   26-DEC-18 5YAK    1       JRNL                                     
REVDAT   2   15-AUG-18 5YAK    1       JRNL                                     
REVDAT   1   08-AUG-18 5YAK    0                                                
JRNL        AUTH   J.HU,Q.SU,J.L.SCHLESSMAN,S.E.ROKITA                          
JRNL        TITL   REDOX CONTROL OF IODOTYROSINE DEIODINASE                     
JRNL        REF    PROTEIN SCI.                  V.  28    68 2019              
JRNL        REFN                   ESSN 1469-896X                               
JRNL        PMID   30052294                                                     
JRNL        DOI    10.1002/PRO.3479                                             
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.M.HU,S.E.ROKITA                                            
REMARK   1  TITL   THE ROLE OF THR239 ON THE CATALYSIS OF HIYD                  
REMARK   1  REF    TO BE PUBLISHED                                              
REMARK   1  REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.52                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 78650                          
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) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4144                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5790                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.79                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2150                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 293                          
REMARK   3   BIN FREE R VALUE                    : 0.2940                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10536                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 270                                     
REMARK   3   SOLVENT ATOMS            : 297                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.41                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : -0.01000                                             
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): 0.244         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.199         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11058 ; 0.012 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 10958 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 15005 ; 1.544 ; 1.998       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 25229 ; 3.433 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1292 ; 6.456 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   459 ;34.989 ;23.333       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2006 ;16.129 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    78 ;17.714 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1685 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11900 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2402 ; 0.014 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  5219 ; 3.925 ; 4.510       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  5219 ; 3.925 ; 4.510       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6494 ; 5.228 ; 6.741       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  6495 ; 5.228 ; 6.741       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5839 ; 4.854 ; 5.024       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  5840 ; 4.854 ; 5.023       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  8512 ; 7.129 ; 7.295       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 13142 ; 8.465 ;36.449       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 13063 ; 8.479 ;36.434       
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 : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5YAK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-SEP-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300003521.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-FEB-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4-8.5                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X25                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
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 : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 82734                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.520                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 8.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 41.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.36                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.09300                            
REMARK 200  R SYM FOR SHELL            (I) : 0.08400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 4TTC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.17 M SODIUM ACETATE, 85 MM TRIS-HCL    
REMARK 280  (PH 8.5), 22.5 % W/V POLYETHYLENE GLYCOL 4,000 AND 15 %             
REMARK 280  GLYCEROL., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.15K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      100.06733            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      200.13467            
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      150.10100            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      250.16833            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       50.03367            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11330 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 18460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F                                  
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11820 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 18280 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11820 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 18190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E                                  
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     GLY A    32                                                      
REMARK 465     GLU A    33                                                      
REMARK 465     PRO A    34                                                      
REMARK 465     ARG A    35                                                      
REMARK 465     THR A    36                                                      
REMARK 465     ARG A    37                                                      
REMARK 465     ALA A    38                                                      
REMARK 465     GLU A    39                                                      
REMARK 465     ALA A    40                                                      
REMARK 465     ARG A    41                                                      
REMARK 465     PRO A    42                                                      
REMARK 465     TRP A    43                                                      
REMARK 465     VAL A    44                                                      
REMARK 465     ASP A    45                                                      
REMARK 465     GLU A    46                                                      
REMARK 465     ASP A    47                                                      
REMARK 465     LEU A    48                                                      
REMARK 465     LYS A    49                                                      
REMARK 465     ASP A    50                                                      
REMARK 465     SER A    51                                                      
REMARK 465     SER A    52                                                      
REMARK 465     ASP A    53                                                      
REMARK 465     LEU A    54                                                      
REMARK 465     HIS A    55                                                      
REMARK 465     GLN A    56                                                      
REMARK 465     ALA A    57                                                      
REMARK 465     GLU A    58                                                      
REMARK 465     GLU A    59                                                      
REMARK 465     ASP A    60                                                      
REMARK 465     ALA A    61                                                      
REMARK 465     ASP A    62                                                      
REMARK 465     GLU A    63                                                      
REMARK 465     TRP A    64                                                      
REMARK 465     GLN A    65                                                      
REMARK 465     GLU A    66                                                      
REMARK 465     SER A    67                                                      
REMARK 465     GLU A    68                                                      
REMARK 465     GLU A    69                                                      
REMARK 465     ASN A    70                                                      
REMARK 465     VAL A    71                                                      
REMARK 465     ALA A   203                                                      
REMARK 465     ASN A   204                                                      
REMARK 465     VAL A   289                                                      
REMARK 465     HIS A   290                                                      
REMARK 465     HIS A   291                                                      
REMARK 465     HIS A   292                                                      
REMARK 465     HIS A   293                                                      
REMARK 465     HIS A   294                                                      
REMARK 465     HIS A   295                                                      
REMARK 465     GLY B    32                                                      
REMARK 465     GLU B    33                                                      
REMARK 465     PRO B    34                                                      
REMARK 465     ARG B    35                                                      
REMARK 465     THR B    36                                                      
REMARK 465     ARG B    37                                                      
REMARK 465     ALA B    38                                                      
REMARK 465     GLU B    39                                                      
REMARK 465     ALA B    40                                                      
REMARK 465     ARG B    41                                                      
REMARK 465     PRO B    42                                                      
REMARK 465     TRP B    43                                                      
REMARK 465     VAL B    44                                                      
REMARK 465     ASP B    45                                                      
REMARK 465     GLU B    46                                                      
REMARK 465     ASP B    47                                                      
REMARK 465     LEU B    48                                                      
REMARK 465     LYS B    49                                                      
REMARK 465     ASP B    50                                                      
REMARK 465     SER B    51                                                      
REMARK 465     SER B    52                                                      
REMARK 465     ASP B    53                                                      
REMARK 465     LEU B    54                                                      
REMARK 465     HIS B    55                                                      
REMARK 465     GLN B    56                                                      
REMARK 465     ALA B    57                                                      
REMARK 465     GLU B    58                                                      
REMARK 465     GLU B    59                                                      
REMARK 465     ASP B    60                                                      
REMARK 465     ALA B    61                                                      
REMARK 465     ASP B    62                                                      
REMARK 465     GLU B    63                                                      
REMARK 465     TRP B    64                                                      
REMARK 465     GLN B    65                                                      
REMARK 465     GLU B    66                                                      
REMARK 465     SER B    67                                                      
REMARK 465     GLU B    68                                                      
REMARK 465     GLU B    69                                                      
REMARK 465     ASN B    70                                                      
REMARK 465     ALA B   203                                                      
REMARK 465     HIS B   290                                                      
REMARK 465     HIS B   291                                                      
REMARK 465     HIS B   292                                                      
REMARK 465     HIS B   293                                                      
REMARK 465     HIS B   294                                                      
REMARK 465     HIS B   295                                                      
REMARK 465     GLY C    32                                                      
REMARK 465     GLU C    33                                                      
REMARK 465     PRO C    34                                                      
REMARK 465     ARG C    35                                                      
REMARK 465     THR C    36                                                      
REMARK 465     ARG C    37                                                      
REMARK 465     ALA C    38                                                      
REMARK 465     GLU C    39                                                      
REMARK 465     ALA C    40                                                      
REMARK 465     ARG C    41                                                      
REMARK 465     PRO C    42                                                      
REMARK 465     TRP C    43                                                      
REMARK 465     VAL C    44                                                      
REMARK 465     ASP C    45                                                      
REMARK 465     GLU C    46                                                      
REMARK 465     ASP C    47                                                      
REMARK 465     LEU C    48                                                      
REMARK 465     LYS C    49                                                      
REMARK 465     ASP C    50                                                      
REMARK 465     SER C    51                                                      
REMARK 465     SER C    52                                                      
REMARK 465     ASP C    53                                                      
REMARK 465     LEU C    54                                                      
REMARK 465     HIS C    55                                                      
REMARK 465     GLN C    56                                                      
REMARK 465     ALA C    57                                                      
REMARK 465     GLU C    58                                                      
REMARK 465     GLU C    59                                                      
REMARK 465     ASP C    60                                                      
REMARK 465     ALA C    61                                                      
REMARK 465     ASP C    62                                                      
REMARK 465     GLU C    63                                                      
REMARK 465     TRP C    64                                                      
REMARK 465     GLN C    65                                                      
REMARK 465     GLU C    66                                                      
REMARK 465     SER C    67                                                      
REMARK 465     GLU C    68                                                      
REMARK 465     GLU C    69                                                      
REMARK 465     ASN C    70                                                      
REMARK 465     ALA C   203                                                      
REMARK 465     ASN C   204                                                      
REMARK 465     HIS C   290                                                      
REMARK 465     HIS C   291                                                      
REMARK 465     HIS C   292                                                      
REMARK 465     HIS C   293                                                      
REMARK 465     HIS C   294                                                      
REMARK 465     HIS C   295                                                      
REMARK 465     GLY D    32                                                      
REMARK 465     GLU D    33                                                      
REMARK 465     PRO D    34                                                      
REMARK 465     ARG D    35                                                      
REMARK 465     THR D    36                                                      
REMARK 465     ARG D    37                                                      
REMARK 465     ALA D    38                                                      
REMARK 465     GLU D    39                                                      
REMARK 465     ALA D    40                                                      
REMARK 465     ARG D    41                                                      
REMARK 465     PRO D    42                                                      
REMARK 465     TRP D    43                                                      
REMARK 465     VAL D    44                                                      
REMARK 465     ASP D    45                                                      
REMARK 465     GLU D    46                                                      
REMARK 465     ASP D    47                                                      
REMARK 465     LEU D    48                                                      
REMARK 465     LYS D    49                                                      
REMARK 465     ASP D    50                                                      
REMARK 465     SER D    51                                                      
REMARK 465     SER D    52                                                      
REMARK 465     ASP D    53                                                      
REMARK 465     LEU D    54                                                      
REMARK 465     HIS D    55                                                      
REMARK 465     GLN D    56                                                      
REMARK 465     ALA D    57                                                      
REMARK 465     GLU D    58                                                      
REMARK 465     GLU D    59                                                      
REMARK 465     ASP D    60                                                      
REMARK 465     ALA D    61                                                      
REMARK 465     ASP D    62                                                      
REMARK 465     GLU D    63                                                      
REMARK 465     TRP D    64                                                      
REMARK 465     GLN D    65                                                      
REMARK 465     GLU D    66                                                      
REMARK 465     SER D    67                                                      
REMARK 465     GLU D    68                                                      
REMARK 465     GLU D    69                                                      
REMARK 465     ASN D    70                                                      
REMARK 465     ALA D   202                                                      
REMARK 465     ALA D   203                                                      
REMARK 465     ASN D   204                                                      
REMARK 465     LYS D   206                                                      
REMARK 465     HIS D   290                                                      
REMARK 465     HIS D   291                                                      
REMARK 465     HIS D   292                                                      
REMARK 465     HIS D   293                                                      
REMARK 465     HIS D   294                                                      
REMARK 465     HIS D   295                                                      
REMARK 465     GLY E    32                                                      
REMARK 465     GLU E    33                                                      
REMARK 465     PRO E    34                                                      
REMARK 465     ARG E    35                                                      
REMARK 465     THR E    36                                                      
REMARK 465     ARG E    37                                                      
REMARK 465     ALA E    38                                                      
REMARK 465     GLU E    39                                                      
REMARK 465     ALA E    40                                                      
REMARK 465     ARG E    41                                                      
REMARK 465     PRO E    42                                                      
REMARK 465     TRP E    43                                                      
REMARK 465     VAL E    44                                                      
REMARK 465     ASP E    45                                                      
REMARK 465     GLU E    46                                                      
REMARK 465     ASP E    47                                                      
REMARK 465     LEU E    48                                                      
REMARK 465     LYS E    49                                                      
REMARK 465     ASP E    50                                                      
REMARK 465     SER E    51                                                      
REMARK 465     SER E    52                                                      
REMARK 465     ASP E    53                                                      
REMARK 465     LEU E    54                                                      
REMARK 465     HIS E    55                                                      
REMARK 465     GLN E    56                                                      
REMARK 465     ALA E    57                                                      
REMARK 465     GLU E    58                                                      
REMARK 465     GLU E    59                                                      
REMARK 465     ASP E    60                                                      
REMARK 465     ALA E    61                                                      
REMARK 465     ASP E    62                                                      
REMARK 465     GLU E    63                                                      
REMARK 465     TRP E    64                                                      
REMARK 465     GLN E    65                                                      
REMARK 465     GLU E    66                                                      
REMARK 465     SER E    67                                                      
REMARK 465     GLU E    68                                                      
REMARK 465     GLU E    69                                                      
REMARK 465     ASN E    70                                                      
REMARK 465     HIS E   290                                                      
REMARK 465     HIS E   291                                                      
REMARK 465     HIS E   292                                                      
REMARK 465     HIS E   293                                                      
REMARK 465     HIS E   294                                                      
REMARK 465     HIS E   295                                                      
REMARK 465     GLY F    32                                                      
REMARK 465     GLU F    33                                                      
REMARK 465     PRO F    34                                                      
REMARK 465     ARG F    35                                                      
REMARK 465     THR F    36                                                      
REMARK 465     ARG F    37                                                      
REMARK 465     ALA F    38                                                      
REMARK 465     GLU F    39                                                      
REMARK 465     ALA F    40                                                      
REMARK 465     ARG F    41                                                      
REMARK 465     PRO F    42                                                      
REMARK 465     TRP F    43                                                      
REMARK 465     VAL F    44                                                      
REMARK 465     ASP F    45                                                      
REMARK 465     GLU F    46                                                      
REMARK 465     ASP F    47                                                      
REMARK 465     LEU F    48                                                      
REMARK 465     LYS F    49                                                      
REMARK 465     ASP F    50                                                      
REMARK 465     SER F    51                                                      
REMARK 465     SER F    52                                                      
REMARK 465     ASP F    53                                                      
REMARK 465     LEU F    54                                                      
REMARK 465     HIS F    55                                                      
REMARK 465     GLN F    56                                                      
REMARK 465     ALA F    57                                                      
REMARK 465     GLU F    58                                                      
REMARK 465     GLU F    59                                                      
REMARK 465     ASP F    60                                                      
REMARK 465     ALA F    61                                                      
REMARK 465     ASP F    62                                                      
REMARK 465     GLU F    63                                                      
REMARK 465     TRP F    64                                                      
REMARK 465     GLN F    65                                                      
REMARK 465     GLU F    66                                                      
REMARK 465     SER F    67                                                      
REMARK 465     GLU F    68                                                      
REMARK 465     GLU F    69                                                      
REMARK 465     ASN F    70                                                      
REMARK 465     HIS F   290                                                      
REMARK 465     HIS F   291                                                      
REMARK 465     HIS F   292                                                      
REMARK 465     HIS F   293                                                      
REMARK 465     HIS F   294                                                      
REMARK 465     HIS F   295                                                      
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    ALA A 130       34.76     38.44                                   
REMARK 500    PRO A 134       41.94    -87.58                                   
REMARK 500    ASN A 179     -157.46   -142.46                                   
REMARK 500    PRO B 134       49.01    -96.77                                   
REMARK 500    LYS B 163      -51.51   -129.23                                   
REMARK 500    ASN B 179     -159.76   -150.19                                   
REMARK 500    PRO C 134       40.95    -88.37                                   
REMARK 500    LYS C 163      -56.55   -130.58                                   
REMARK 500    ALA D 130       27.73     48.55                                   
REMARK 500    PRO D 134       38.25    -87.16                                   
REMARK 500    LYS D 163      -49.51   -141.29                                   
REMARK 500    PRO E 134       41.23    -84.43                                   
REMARK 500    LYS E 163      -39.64   -142.92                                   
REMARK 500    ASN E 179     -157.53   -144.87                                   
REMARK 500    ASN E 204        4.62    -69.09                                   
REMARK 500    ASN E 242       17.44     59.84                                   
REMARK 500    PRO F 134       41.49    -83.58                                   
REMARK 500    LYS F 163      -50.59   -140.18                                   
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 FMN A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue YOF A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMN B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue YOF B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMN C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue YOF C 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMN D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue YOF D 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMN E 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue YOF E 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMN F 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue YOF F 502                 
DBREF  5YAK A   32   289  UNP    Q6PHW0   IYD1_HUMAN      32    289             
DBREF  5YAK B   32   289  UNP    Q6PHW0   IYD1_HUMAN      32    289             
DBREF  5YAK C   32   289  UNP    Q6PHW0   IYD1_HUMAN      32    289             
DBREF  5YAK D   32   289  UNP    Q6PHW0   IYD1_HUMAN      32    289             
DBREF  5YAK E   32   289  UNP    Q6PHW0   IYD1_HUMAN      32    289             
DBREF  5YAK F   32   289  UNP    Q6PHW0   IYD1_HUMAN      32    289             
SEQADV 5YAK ALA A  239  UNP  Q6PHW0    THR   239 ENGINEERED MUTATION            
SEQADV 5YAK HIS A  290  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS A  291  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS A  292  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS A  293  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS A  294  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS A  295  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK ALA B  239  UNP  Q6PHW0    THR   239 ENGINEERED MUTATION            
SEQADV 5YAK HIS B  290  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS B  291  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS B  292  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS B  293  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS B  294  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS B  295  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK ALA C  239  UNP  Q6PHW0    THR   239 ENGINEERED MUTATION            
SEQADV 5YAK HIS C  290  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS C  291  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS C  292  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS C  293  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS C  294  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS C  295  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK ALA D  239  UNP  Q6PHW0    THR   239 ENGINEERED MUTATION            
SEQADV 5YAK HIS D  290  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS D  291  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS D  292  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS D  293  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS D  294  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS D  295  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK ALA E  239  UNP  Q6PHW0    THR   239 ENGINEERED MUTATION            
SEQADV 5YAK HIS E  290  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS E  291  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS E  292  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS E  293  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS E  294  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS E  295  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK ALA F  239  UNP  Q6PHW0    THR   239 ENGINEERED MUTATION            
SEQADV 5YAK HIS F  290  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS F  291  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS F  292  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS F  293  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS F  294  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 5YAK HIS F  295  UNP  Q6PHW0              EXPRESSION TAG                 
SEQRES   1 A  264  GLY GLU PRO ARG THR ARG ALA GLU ALA ARG PRO TRP VAL          
SEQRES   2 A  264  ASP GLU ASP LEU LYS ASP SER SER ASP LEU HIS GLN ALA          
SEQRES   3 A  264  GLU GLU ASP ALA ASP GLU TRP GLN GLU SER GLU GLU ASN          
SEQRES   4 A  264  VAL GLU HIS ILE PRO PHE SER HIS ASN HIS TYR PRO GLU          
SEQRES   5 A  264  LYS GLU MET VAL LYS ARG SER GLN GLU PHE TYR GLU LEU          
SEQRES   6 A  264  LEU ASN LYS ARG ARG SER VAL ARG PHE ILE SER ASN GLU          
SEQRES   7 A  264  GLN VAL PRO MET GLU VAL ILE ASP ASN VAL ILE ARG THR          
SEQRES   8 A  264  ALA GLY THR ALA PRO SER GLY ALA HIS THR GLU PRO TRP          
SEQRES   9 A  264  THR PHE VAL VAL VAL LYS ASP PRO ASP VAL LYS HIS LYS          
SEQRES  10 A  264  ILE ARG LYS ILE ILE GLU GLU GLU GLU GLU ILE ASN TYR          
SEQRES  11 A  264  MET LYS ARG MET GLY HIS ARG TRP VAL THR ASP LEU LYS          
SEQRES  12 A  264  LYS LEU ARG THR ASN TRP ILE LYS GLU TYR LEU ASP THR          
SEQRES  13 A  264  ALA PRO ILE LEU ILE LEU ILE PHE LYS GLN VAL HIS GLY          
SEQRES  14 A  264  PHE ALA ALA ASN GLY LYS LYS LYS VAL HIS TYR TYR ASN          
SEQRES  15 A  264  GLU ILE SER VAL SER ILE ALA CYS GLY ILE LEU LEU ALA          
SEQRES  16 A  264  ALA LEU GLN ASN ALA GLY LEU VAL THR VAL THR THR ALA          
SEQRES  17 A  264  PRO LEU ASN CYS GLY PRO ARG LEU ARG VAL LEU LEU GLY          
SEQRES  18 A  264  ARG PRO ALA HIS GLU LYS LEU LEU MET LEU LEU PRO VAL          
SEQRES  19 A  264  GLY TYR PRO SER LYS GLU ALA THR VAL PRO ASP LEU LYS          
SEQRES  20 A  264  ARG LYS PRO LEU ASP GLN ILE MET VAL THR VAL HIS HIS          
SEQRES  21 A  264  HIS HIS HIS HIS                                              
SEQRES   1 B  264  GLY GLU PRO ARG THR ARG ALA GLU ALA ARG PRO TRP VAL          
SEQRES   2 B  264  ASP GLU ASP LEU LYS ASP SER SER ASP LEU HIS GLN ALA          
SEQRES   3 B  264  GLU GLU ASP ALA ASP GLU TRP GLN GLU SER GLU GLU ASN          
SEQRES   4 B  264  VAL GLU HIS ILE PRO PHE SER HIS ASN HIS TYR PRO GLU          
SEQRES   5 B  264  LYS GLU MET VAL LYS ARG SER GLN GLU PHE TYR GLU LEU          
SEQRES   6 B  264  LEU ASN LYS ARG ARG SER VAL ARG PHE ILE SER ASN GLU          
SEQRES   7 B  264  GLN VAL PRO MET GLU VAL ILE ASP ASN VAL ILE ARG THR          
SEQRES   8 B  264  ALA GLY THR ALA PRO SER GLY ALA HIS THR GLU PRO TRP          
SEQRES   9 B  264  THR PHE VAL VAL VAL LYS ASP PRO ASP VAL LYS HIS LYS          
SEQRES  10 B  264  ILE ARG LYS ILE ILE GLU GLU GLU GLU GLU ILE ASN TYR          
SEQRES  11 B  264  MET LYS ARG MET GLY HIS ARG TRP VAL THR ASP LEU LYS          
SEQRES  12 B  264  LYS LEU ARG THR ASN TRP ILE LYS GLU TYR LEU ASP THR          
SEQRES  13 B  264  ALA PRO ILE LEU ILE LEU ILE PHE LYS GLN VAL HIS GLY          
SEQRES  14 B  264  PHE ALA ALA ASN GLY LYS LYS LYS VAL HIS TYR TYR ASN          
SEQRES  15 B  264  GLU ILE SER VAL SER ILE ALA CYS GLY ILE LEU LEU ALA          
SEQRES  16 B  264  ALA LEU GLN ASN ALA GLY LEU VAL THR VAL THR THR ALA          
SEQRES  17 B  264  PRO LEU ASN CYS GLY PRO ARG LEU ARG VAL LEU LEU GLY          
SEQRES  18 B  264  ARG PRO ALA HIS GLU LYS LEU LEU MET LEU LEU PRO VAL          
SEQRES  19 B  264  GLY TYR PRO SER LYS GLU ALA THR VAL PRO ASP LEU LYS          
SEQRES  20 B  264  ARG LYS PRO LEU ASP GLN ILE MET VAL THR VAL HIS HIS          
SEQRES  21 B  264  HIS HIS HIS HIS                                              
SEQRES   1 C  264  GLY GLU PRO ARG THR ARG ALA GLU ALA ARG PRO TRP VAL          
SEQRES   2 C  264  ASP GLU ASP LEU LYS ASP SER SER ASP LEU HIS GLN ALA          
SEQRES   3 C  264  GLU GLU ASP ALA ASP GLU TRP GLN GLU SER GLU GLU ASN          
SEQRES   4 C  264  VAL GLU HIS ILE PRO PHE SER HIS ASN HIS TYR PRO GLU          
SEQRES   5 C  264  LYS GLU MET VAL LYS ARG SER GLN GLU PHE TYR GLU LEU          
SEQRES   6 C  264  LEU ASN LYS ARG ARG SER VAL ARG PHE ILE SER ASN GLU          
SEQRES   7 C  264  GLN VAL PRO MET GLU VAL ILE ASP ASN VAL ILE ARG THR          
SEQRES   8 C  264  ALA GLY THR ALA PRO SER GLY ALA HIS THR GLU PRO TRP          
SEQRES   9 C  264  THR PHE VAL VAL VAL LYS ASP PRO ASP VAL LYS HIS LYS          
SEQRES  10 C  264  ILE ARG LYS ILE ILE GLU GLU GLU GLU GLU ILE ASN TYR          
SEQRES  11 C  264  MET LYS ARG MET GLY HIS ARG TRP VAL THR ASP LEU LYS          
SEQRES  12 C  264  LYS LEU ARG THR ASN TRP ILE LYS GLU TYR LEU ASP THR          
SEQRES  13 C  264  ALA PRO ILE LEU ILE LEU ILE PHE LYS GLN VAL HIS GLY          
SEQRES  14 C  264  PHE ALA ALA ASN GLY LYS LYS LYS VAL HIS TYR TYR ASN          
SEQRES  15 C  264  GLU ILE SER VAL SER ILE ALA CYS GLY ILE LEU LEU ALA          
SEQRES  16 C  264  ALA LEU GLN ASN ALA GLY LEU VAL THR VAL THR THR ALA          
SEQRES  17 C  264  PRO LEU ASN CYS GLY PRO ARG LEU ARG VAL LEU LEU GLY          
SEQRES  18 C  264  ARG PRO ALA HIS GLU LYS LEU LEU MET LEU LEU PRO VAL          
SEQRES  19 C  264  GLY TYR PRO SER LYS GLU ALA THR VAL PRO ASP LEU LYS          
SEQRES  20 C  264  ARG LYS PRO LEU ASP GLN ILE MET VAL THR VAL HIS HIS          
SEQRES  21 C  264  HIS HIS HIS HIS                                              
SEQRES   1 D  264  GLY GLU PRO ARG THR ARG ALA GLU ALA ARG PRO TRP VAL          
SEQRES   2 D  264  ASP GLU ASP LEU LYS ASP SER SER ASP LEU HIS GLN ALA          
SEQRES   3 D  264  GLU GLU ASP ALA ASP GLU TRP GLN GLU SER GLU GLU ASN          
SEQRES   4 D  264  VAL GLU HIS ILE PRO PHE SER HIS ASN HIS TYR PRO GLU          
SEQRES   5 D  264  LYS GLU MET VAL LYS ARG SER GLN GLU PHE TYR GLU LEU          
SEQRES   6 D  264  LEU ASN LYS ARG ARG SER VAL ARG PHE ILE SER ASN GLU          
SEQRES   7 D  264  GLN VAL PRO MET GLU VAL ILE ASP ASN VAL ILE ARG THR          
SEQRES   8 D  264  ALA GLY THR ALA PRO SER GLY ALA HIS THR GLU PRO TRP          
SEQRES   9 D  264  THR PHE VAL VAL VAL LYS ASP PRO ASP VAL LYS HIS LYS          
SEQRES  10 D  264  ILE ARG LYS ILE ILE GLU GLU GLU GLU GLU ILE ASN TYR          
SEQRES  11 D  264  MET LYS ARG MET GLY HIS ARG TRP VAL THR ASP LEU LYS          
SEQRES  12 D  264  LYS LEU ARG THR ASN TRP ILE LYS GLU TYR LEU ASP THR          
SEQRES  13 D  264  ALA PRO ILE LEU ILE LEU ILE PHE LYS GLN VAL HIS GLY          
SEQRES  14 D  264  PHE ALA ALA ASN GLY LYS LYS LYS VAL HIS TYR TYR ASN          
SEQRES  15 D  264  GLU ILE SER VAL SER ILE ALA CYS GLY ILE LEU LEU ALA          
SEQRES  16 D  264  ALA LEU GLN ASN ALA GLY LEU VAL THR VAL THR THR ALA          
SEQRES  17 D  264  PRO LEU ASN CYS GLY PRO ARG LEU ARG VAL LEU LEU GLY          
SEQRES  18 D  264  ARG PRO ALA HIS GLU LYS LEU LEU MET LEU LEU PRO VAL          
SEQRES  19 D  264  GLY TYR PRO SER LYS GLU ALA THR VAL PRO ASP LEU LYS          
SEQRES  20 D  264  ARG LYS PRO LEU ASP GLN ILE MET VAL THR VAL HIS HIS          
SEQRES  21 D  264  HIS HIS HIS HIS                                              
SEQRES   1 E  264  GLY GLU PRO ARG THR ARG ALA GLU ALA ARG PRO TRP VAL          
SEQRES   2 E  264  ASP GLU ASP LEU LYS ASP SER SER ASP LEU HIS GLN ALA          
SEQRES   3 E  264  GLU GLU ASP ALA ASP GLU TRP GLN GLU SER GLU GLU ASN          
SEQRES   4 E  264  VAL GLU HIS ILE PRO PHE SER HIS ASN HIS TYR PRO GLU          
SEQRES   5 E  264  LYS GLU MET VAL LYS ARG SER GLN GLU PHE TYR GLU LEU          
SEQRES   6 E  264  LEU ASN LYS ARG ARG SER VAL ARG PHE ILE SER ASN GLU          
SEQRES   7 E  264  GLN VAL PRO MET GLU VAL ILE ASP ASN VAL ILE ARG THR          
SEQRES   8 E  264  ALA GLY THR ALA PRO SER GLY ALA HIS THR GLU PRO TRP          
SEQRES   9 E  264  THR PHE VAL VAL VAL LYS ASP PRO ASP VAL LYS HIS LYS          
SEQRES  10 E  264  ILE ARG LYS ILE ILE GLU GLU GLU GLU GLU ILE ASN TYR          
SEQRES  11 E  264  MET LYS ARG MET GLY HIS ARG TRP VAL THR ASP LEU LYS          
SEQRES  12 E  264  LYS LEU ARG THR ASN TRP ILE LYS GLU TYR LEU ASP THR          
SEQRES  13 E  264  ALA PRO ILE LEU ILE LEU ILE PHE LYS GLN VAL HIS GLY          
SEQRES  14 E  264  PHE ALA ALA ASN GLY LYS LYS LYS VAL HIS TYR TYR ASN          
SEQRES  15 E  264  GLU ILE SER VAL SER ILE ALA CYS GLY ILE LEU LEU ALA          
SEQRES  16 E  264  ALA LEU GLN ASN ALA GLY LEU VAL THR VAL THR THR ALA          
SEQRES  17 E  264  PRO LEU ASN CYS GLY PRO ARG LEU ARG VAL LEU LEU GLY          
SEQRES  18 E  264  ARG PRO ALA HIS GLU LYS LEU LEU MET LEU LEU PRO VAL          
SEQRES  19 E  264  GLY TYR PRO SER LYS GLU ALA THR VAL PRO ASP LEU LYS          
SEQRES  20 E  264  ARG LYS PRO LEU ASP GLN ILE MET VAL THR VAL HIS HIS          
SEQRES  21 E  264  HIS HIS HIS HIS                                              
SEQRES   1 F  264  GLY GLU PRO ARG THR ARG ALA GLU ALA ARG PRO TRP VAL          
SEQRES   2 F  264  ASP GLU ASP LEU LYS ASP SER SER ASP LEU HIS GLN ALA          
SEQRES   3 F  264  GLU GLU ASP ALA ASP GLU TRP GLN GLU SER GLU GLU ASN          
SEQRES   4 F  264  VAL GLU HIS ILE PRO PHE SER HIS ASN HIS TYR PRO GLU          
SEQRES   5 F  264  LYS GLU MET VAL LYS ARG SER GLN GLU PHE TYR GLU LEU          
SEQRES   6 F  264  LEU ASN LYS ARG ARG SER VAL ARG PHE ILE SER ASN GLU          
SEQRES   7 F  264  GLN VAL PRO MET GLU VAL ILE ASP ASN VAL ILE ARG THR          
SEQRES   8 F  264  ALA GLY THR ALA PRO SER GLY ALA HIS THR GLU PRO TRP          
SEQRES   9 F  264  THR PHE VAL VAL VAL LYS ASP PRO ASP VAL LYS HIS LYS          
SEQRES  10 F  264  ILE ARG LYS ILE ILE GLU GLU GLU GLU GLU ILE ASN TYR          
SEQRES  11 F  264  MET LYS ARG MET GLY HIS ARG TRP VAL THR ASP LEU LYS          
SEQRES  12 F  264  LYS LEU ARG THR ASN TRP ILE LYS GLU TYR LEU ASP THR          
SEQRES  13 F  264  ALA PRO ILE LEU ILE LEU ILE PHE LYS GLN VAL HIS GLY          
SEQRES  14 F  264  PHE ALA ALA ASN GLY LYS LYS LYS VAL HIS TYR TYR ASN          
SEQRES  15 F  264  GLU ILE SER VAL SER ILE ALA CYS GLY ILE LEU LEU ALA          
SEQRES  16 F  264  ALA LEU GLN ASN ALA GLY LEU VAL THR VAL THR THR ALA          
SEQRES  17 F  264  PRO LEU ASN CYS GLY PRO ARG LEU ARG VAL LEU LEU GLY          
SEQRES  18 F  264  ARG PRO ALA HIS GLU LYS LEU LEU MET LEU LEU PRO VAL          
SEQRES  19 F  264  GLY TYR PRO SER LYS GLU ALA THR VAL PRO ASP LEU LYS          
SEQRES  20 F  264  ARG LYS PRO LEU ASP GLN ILE MET VAL THR VAL HIS HIS          
SEQRES  21 F  264  HIS HIS HIS HIS                                              
HET    FMN  A 501      31                                                       
HET    YOF  A 502      14                                                       
HET    FMN  B 501      31                                                       
HET    YOF  B 502      14                                                       
HET    FMN  C 501      31                                                       
HET    YOF  C 502      14                                                       
HET    FMN  D 501      31                                                       
HET    YOF  D 502      14                                                       
HET    FMN  E 501      31                                                       
HET    YOF  E 502      14                                                       
HET    FMN  F 501      31                                                       
HET    YOF  F 502      14                                                       
HETNAM     FMN FLAVIN MONONUCLEOTIDE                                            
HETNAM     YOF 3-FLUOROTYROSINE                                                 
HETSYN     FMN RIBOFLAVIN MONOPHOSPHATE                                         
FORMUL   7  FMN    6(C17 H21 N4 O9 P)                                           
FORMUL   8  YOF    6(C9 H10 F N O3)                                             
FORMUL  19  HOH   *297(H2 O)                                                    
HELIX    1 AA1 PRO A   82  LYS A   99  1                                  18    
HELIX    2 AA2 PRO A  112  GLY A  124  1                                  13    
HELIX    3 AA3 SER A  128  THR A  132  5                                   5    
HELIX    4 AA4 ASP A  142  LYS A  163  1                                  22    
HELIX    5 AA5 GLY A  166  LYS A  174  1                                   9    
HELIX    6 AA6 LYS A  175  ARG A  177  5                                   3    
HELIX    7 AA7 GLU A  183  ALA A  188  1                                   6    
HELIX    8 AA8 TYR A  212  ALA A  231  1                                  20    
HELIX    9 AA9 CYS A  243  LEU A  251  1                                   9    
HELIX   10 AB1 PRO A  281  GLN A  284  5                                   4    
HELIX   11 AB2 PRO B   82  LYS B   99  1                                  18    
HELIX   12 AB3 PRO B  112  GLY B  124  1                                  13    
HELIX   13 AB4 SER B  128  THR B  132  5                                   5    
HELIX   14 AB5 ASP B  142  LYS B  163  1                                  22    
HELIX   15 AB6 GLY B  166  LEU B  173  1                                   8    
HELIX   16 AB7 LYS B  174  ARG B  177  5                                   4    
HELIX   17 AB8 GLU B  183  ALA B  188  1                                   6    
HELIX   18 AB9 TYR B  212  ALA B  231  1                                  20    
HELIX   19 AC1 CYS B  243  LEU B  251  1                                   9    
HELIX   20 AC2 PRO B  281  GLN B  284  5                                   4    
HELIX   21 AC3 PRO C   82  LYS C   99  1                                  18    
HELIX   22 AC4 PRO C  112  GLY C  124  1                                  13    
HELIX   23 AC5 SER C  128  THR C  132  5                                   5    
HELIX   24 AC6 ASP C  142  LYS C  163  1                                  22    
HELIX   25 AC7 GLY C  166  LEU C  173  1                                   8    
HELIX   26 AC8 LYS C  174  ARG C  177  5                                   4    
HELIX   27 AC9 GLU C  183  ALA C  188  1                                   6    
HELIX   28 AD1 TYR C  212  GLY C  232  1                                  21    
HELIX   29 AD2 CYS C  243  GLY C  252  1                                  10    
HELIX   30 AD3 PRO C  281  ILE C  285  1                                   5    
HELIX   31 AD4 PRO D   82  LYS D   99  1                                  18    
HELIX   32 AD5 PRO D  112  GLY D  124  1                                  13    
HELIX   33 AD6 ASP D  142  LYS D  163  1                                  22    
HELIX   34 AD7 GLY D  166  LEU D  173  1                                   8    
HELIX   35 AD8 LYS D  174  ARG D  177  5                                   4    
HELIX   36 AD9 GLU D  183  ALA D  188  1                                   6    
HELIX   37 AE1 TYR D  212  ALA D  231  1                                  20    
HELIX   38 AE2 CYS D  243  GLY D  252  1                                  10    
HELIX   39 AE3 PRO D  281  GLN D  284  5                                   4    
HELIX   40 AE4 PRO E   82  LYS E   99  1                                  18    
HELIX   41 AE5 PRO E  112  GLY E  124  1                                  13    
HELIX   42 AE6 SER E  128  THR E  132  5                                   5    
HELIX   43 AE7 ASP E  142  LYS E  163  1                                  22    
HELIX   44 AE8 GLY E  166  LEU E  173  1                                   8    
HELIX   45 AE9 LYS E  174  ARG E  177  5                                   4    
HELIX   46 AF1 GLU E  183  ALA E  188  1                                   6    
HELIX   47 AF2 TYR E  212  GLY E  232  1                                  21    
HELIX   48 AF3 CYS E  243  LEU E  251  1                                   9    
HELIX   49 AF4 PRO E  281  ILE E  285  1                                   5    
HELIX   50 AF5 PRO F   82  LYS F   99  1                                  18    
HELIX   51 AF6 PRO F  112  GLY F  124  1                                  13    
HELIX   52 AF7 SER F  128  THR F  132  5                                   5    
HELIX   53 AF8 ASP F  142  LYS F  163  1                                  22    
HELIX   54 AF9 GLY F  166  LEU F  173  1                                   8    
HELIX   55 AG1 LYS F  174  ARG F  177  5                                   4    
HELIX   56 AG2 GLU F  183  ALA F  188  1                                   6    
HELIX   57 AG3 TYR F  212  ASN F  230  1                                  19    
HELIX   58 AG4 CYS F  243  LEU F  251  1                                   9    
HELIX   59 AG5 PRO F  281  GLN F  284  5                                   4    
SHEET    1 AA1 2 HIS A  73  PRO A  75  0                                        
SHEET    2 AA1 2 THR F 273  PRO F 275 -1  O  VAL F 274   N  ILE A  74           
SHEET    1 AA2 5 VAL A 234  THR A 235  0                                        
SHEET    2 AA2 5 GLU A 257  GLY A 266 -1  O  GLY A 266   N  VAL A 234           
SHEET    3 AA2 5 ILE A 190  GLN A 197 -1  N  ILE A 194   O  MET A 261           
SHEET    4 AA2 5 TRP A 135  VAL A 140 -1  N  VAL A 138   O  LEU A 193           
SHEET    5 AA2 5 MET F 286  VAL F 289  1  O  VAL F 287   N  VAL A 139           
SHEET    1 AA3 2 GLY A 200  PHE A 201  0                                        
SHEET    2 AA3 2 LYS A 207  LYS A 208 -1  O  LYS A 208   N  GLY A 200           
SHEET    1 AA4 2 THR A 273  PRO A 275  0                                        
SHEET    2 AA4 2 HIS F  73  PRO F  75 -1  O  ILE F  74   N  VAL A 274           
SHEET    1 AA5 4 MET A 286  VAL A 287  0                                        
SHEET    2 AA5 4 TRP F 135  VAL F 140  1  O  VAL F 139   N  VAL A 287           
SHEET    3 AA5 4 ILE F 190  GLN F 197 -1  O  LEU F 193   N  VAL F 138           
SHEET    4 AA5 4 GLU F 257  VAL F 265 -1  O  VAL F 265   N  ILE F 190           
SHEET    1 AA6 2 HIS B  73  PRO B  75  0                                        
SHEET    2 AA6 2 THR C 273  PRO C 275 -1  O  VAL C 274   N  ILE B  74           
SHEET    1 AA7 5 VAL B 234  THR B 235  0                                        
SHEET    2 AA7 5 GLU B 257  GLY B 266 -1  O  GLY B 266   N  VAL B 234           
SHEET    3 AA7 5 ILE B 190  GLN B 197 -1  N  ILE B 190   O  VAL B 265           
SHEET    4 AA7 5 TRP B 135  VAL B 140 -1  N  VAL B 140   O  LEU B 191           
SHEET    5 AA7 5 MET C 286  VAL C 289  1  O  VAL C 289   N  VAL B 139           
SHEET    1 AA8 2 HIS B 199  PHE B 201  0                                        
SHEET    2 AA8 2 LYS B 207  VAL B 209 -1  O  LYS B 208   N  GLY B 200           
SHEET    1 AA9 2 THR B 273  PRO B 275  0                                        
SHEET    2 AA9 2 HIS C  73  PRO C  75 -1  O  ILE C  74   N  VAL B 274           
SHEET    1 AB1 4 MET B 286  VAL B 289  0                                        
SHEET    2 AB1 4 TRP C 135  VAL C 140  1  O  VAL C 139   N  VAL B 287           
SHEET    3 AB1 4 ILE C 190  GLN C 197 -1  O  LEU C 193   N  VAL C 138           
SHEET    4 AB1 4 GLU C 257  VAL C 265 -1  O  VAL C 265   N  ILE C 190           
SHEET    1 AB2 2 SER C  77  ASN C  79  0                                        
SHEET    2 AB2 2 SER E  77  ASN E  79 -1  O  HIS E  78   N  HIS C  78           
SHEET    1 AB3 2 HIS C 199  PHE C 201  0                                        
SHEET    2 AB3 2 LYS C 207  VAL C 209 -1  O  LYS C 208   N  GLY C 200           
SHEET    1 AB4 2 HIS D  73  PRO D  75  0                                        
SHEET    2 AB4 2 THR E 273  PRO E 275 -1  O  VAL E 274   N  ILE D  74           
SHEET    1 AB5 4 GLU D 257  VAL D 265  0                                        
SHEET    2 AB5 4 ILE D 190  GLN D 197 -1  N  ILE D 190   O  VAL D 265           
SHEET    3 AB5 4 TRP D 135  VAL D 140 -1  N  THR D 136   O  PHE D 195           
SHEET    4 AB5 4 MET E 286  VAL E 289  1  O  VAL E 289   N  VAL D 139           
SHEET    1 AB6 2 THR D 273  PRO D 275  0                                        
SHEET    2 AB6 2 HIS E  73  PRO E  75 -1  O  ILE E  74   N  VAL D 274           
SHEET    1 AB7 5 MET D 286  VAL D 289  0                                        
SHEET    2 AB7 5 TRP E 135  VAL E 140  1  O  VAL E 139   N  VAL D 287           
SHEET    3 AB7 5 ILE E 190  GLN E 197 -1  O  LEU E 193   N  VAL E 138           
SHEET    4 AB7 5 GLU E 257  GLY E 266 -1  O  MET E 261   N  ILE E 194           
SHEET    5 AB7 5 VAL E 234  THR E 235 -1  N  VAL E 234   O  GLY E 266           
SHEET    1 AB8 2 HIS E 199  PHE E 201  0                                        
SHEET    2 AB8 2 LYS E 207  VAL E 209 -1  O  LYS E 208   N  GLY E 200           
SHEET    1 AB9 2 HIS F 199  PHE F 201  0                                        
SHEET    2 AB9 2 LYS F 207  VAL F 209 -1  O  LYS F 208   N  GLY F 200           
SITE     1 AC1 22 ARG A 100  ARG A 101  SER A 102  ARG A 104                    
SITE     2 AC1 22 LEU A 176  THR A 178  THR A 237  THR A 238                    
SITE     3 AC1 22 ALA A 239  ARG A 279  YOF A 502  HOH A 602                    
SITE     4 AC1 22 HOH A 605  HOH A 619  HOH A 620  HOH A 624                    
SITE     5 AC1 22 PRO F 127  SER F 128  GLY F 129  HIS F 131                    
SITE     6 AC1 22 TYR F 212  SER F 216                                          
SITE     1 AC2 14 GLU A 157  TYR A 161  TRP A 169  LEU A 173                    
SITE     2 AC2 14 THR A 178  ASN A 179  LYS A 182  ALA A 239                    
SITE     3 AC2 14 FMN A 501  HOH A 626  GLY F 129  ALA F 130                    
SITE     4 AC2 14 TYR F 212  HOH F 627                                          
SITE     1 AC3 23 ARG B 100  ARG B 101  SER B 102  ARG B 104                    
SITE     2 AC3 23 LEU B 176  THR B 178  VAL B 236  THR B 237                    
SITE     3 AC3 23 THR B 238  ALA B 239  ARG B 279  YOF B 502                    
SITE     4 AC3 23 HOH B 603  HOH B 609  HOH B 615  HOH B 624                    
SITE     5 AC3 23 PRO C 127  SER C 128  GLY C 129  HIS C 131                    
SITE     6 AC3 23 TYR C 212  SER C 216  HOH C 608                               
SITE     1 AC4 12 GLU B 157  TYR B 161  LEU B 173  LEU B 176                    
SITE     2 AC4 12 LYS B 182  ALA B 239  FMN B 501  HOH B 612                    
SITE     3 AC4 12 GLY C 129  ALA C 130  TYR C 212  HOH C 619                    
SITE     1 AC5 24 PRO B 127  SER B 128  GLY B 129  HIS B 131                    
SITE     2 AC5 24 TYR B 212  ILE B 215  SER B 216  HOH B 631                    
SITE     3 AC5 24 ARG C 100  ARG C 101  SER C 102  ARG C 104                    
SITE     4 AC5 24 LEU C 176  THR C 178  VAL C 236  THR C 237                    
SITE     5 AC5 24 ALA C 239  LEU C 277  ARG C 279  YOF C 502                    
SITE     6 AC5 24 HOH C 603  HOH C 610  HOH C 629  HOH C 634                    
SITE     1 AC6 11 GLY B 129  ALA B 130  HOH B 630  GLU C 157                    
SITE     2 AC6 11 TYR C 161  LEU C 173  THR C 178  LYS C 182                    
SITE     3 AC6 11 ALA C 239  FMN C 501  HOH C 640                               
SITE     1 AC7 23 ARG D 100  ARG D 101  SER D 102  ARG D 104                    
SITE     2 AC7 23 LEU D 176  THR D 178  THR D 237  THR D 238                    
SITE     3 AC7 23 ALA D 239  ARG D 279  YOF D 502  HOH D 603                    
SITE     4 AC7 23 HOH D 606  HOH D 621  HOH D 624  PRO E 127                    
SITE     5 AC7 23 SER E 128  GLY E 129  HIS E 131  TYR E 212                    
SITE     6 AC7 23 ILE E 215  SER E 216  HOH E 628                               
SITE     1 AC8 11 GLU D 157  TYR D 161  LEU D 173  LYS D 182                    
SITE     2 AC8 11 ALA D 239  FMN D 501  HOH D 618  GLY E 129                    
SITE     3 AC8 11 ALA E 130  TYR E 212  HOH E 602                               
SITE     1 AC9 22 PRO D 127  SER D 128  GLY D 129  HIS D 131                    
SITE     2 AC9 22 TYR D 212  SER D 216  HOH D 619  ARG E 100                    
SITE     3 AC9 22 ARG E 101  SER E 102  ARG E 104  LEU E 176                    
SITE     4 AC9 22 VAL E 236  THR E 237  THR E 238  ALA E 239                    
SITE     5 AC9 22 ARG E 279  YOF E 502  HOH E 609  HOH E 611                    
SITE     6 AC9 22 HOH E 621  HOH E 626                                          
SITE     1 AD1 10 GLY D 129  ALA D 130  HOH D 631  GLU E 157                    
SITE     2 AD1 10 TYR E 161  LEU E 173  LYS E 182  ALA E 239                    
SITE     3 AD1 10 FMN E 501  HOH E 622                                          
SITE     1 AD2 23 PRO A 127  SER A 128  GLY A 129  HIS A 131                    
SITE     2 AD2 23 TYR A 212  ILE A 215  SER A 216  ARG F 100                    
SITE     3 AD2 23 ARG F 101  SER F 102  ARG F 104  LEU F 176                    
SITE     4 AD2 23 THR F 178  VAL F 236  THR F 237  THR F 238                    
SITE     5 AD2 23 ALA F 239  ARG F 279  YOF F 502  HOH F 609                    
SITE     6 AD2 23 HOH F 610  HOH F 621  HOH F 636                               
SITE     1 AD3 11 GLY A 129  ALA A 130  HOH A 628  GLU F 157                    
SITE     2 AD3 11 TYR F 161  LEU F 173  ASN F 179  LYS F 182                    
SITE     3 AD3 11 ALA F 239  FMN F 501  HOH F 605                               
CRYST1  105.079  105.079  300.202  90.00  90.00 120.00 P 61         36          
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      0.009517  0.005494  0.000000        0.00000                         
SCALE2      0.000000  0.010989  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003331        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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