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Database: PDB
Entry: 4TTC
LinkDB: 4TTC
Original site: 4TTC 
HEADER    OXIDOREDUCTASE                          20-JUN-14   4TTC              
TITLE     CRYSTAL STRUCTURE OF HOMO SAPIENS IODOTYROSINE DEIODINASE BOUND TO FMN
TITLE    2 AND MONO-IODOTYROSINE (MIT)                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: IODOTYROSINE DEHALOGENASE 1;                               
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 FRAGMENT: UNP RESIDUES 32-289;                                       
COMPND   5 SYNONYM: IYD-1;                                                      
COMPND   6 EC: 1.22.1.1;                                                        
COMPND   7 ENGINEERED: YES                                                      
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    OXIDOREDUCTASE, FLAVOPROTEIN, MEMBRANE, TRANSMEMBRANE, DEHALOGENASE,  
KEYWDS   2 IODIDE SALVAGE, MONO-IODOTYROSINE, MIT                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.CHUENCHOR,J.HU,S.ROKITA                                             
REVDAT   4   25-DEC-19 4TTC    1       REMARK                                   
REVDAT   3   20-SEP-17 4TTC    1       SOURCE JRNL   REMARK                     
REVDAT   2   14-JAN-15 4TTC    1       JRNL                                     
REVDAT   1   26-NOV-14 4TTC    0                                                
JRNL        AUTH   J.HU,W.CHUENCHOR,S.E.ROKITA                                  
JRNL        TITL   A SWITCH BETWEEN ONE- AND TWO-ELECTRON CHEMISTRY OF THE      
JRNL        TITL 2 HUMAN FLAVOPROTEIN IODOTYROSINE DEIODINASE IS CONTROLLED BY  
JRNL        TITL 3 SUBSTRATE.                                                   
JRNL        REF    J.BIOL.CHEM.                  V. 290   590 2015              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   25395621                                                     
JRNL        DOI    10.1074/JBC.M114.605964                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1692)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.86                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 54429                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.173                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.212                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2722                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 44.8645 -  7.0583    0.99     2740   137  0.1541 0.1613        
REMARK   3     2  7.0583 -  5.6058    1.00     2731   147  0.1697 0.1595        
REMARK   3     3  5.6058 -  4.8982    1.00     2713   143  0.1565 0.1992        
REMARK   3     4  4.8982 -  4.4508    1.00     2739   146  0.1287 0.1766        
REMARK   3     5  4.4508 -  4.1320    1.00     2733   137  0.1443 0.1761        
REMARK   3     6  4.1320 -  3.8886    1.00     2706   149  0.1632 0.2091        
REMARK   3     7  3.8886 -  3.6939    1.00     2731   143  0.1692 0.2008        
REMARK   3     8  3.6939 -  3.5332    1.00     2734   145  0.1765 0.2108        
REMARK   3     9  3.5332 -  3.3972    1.00     2705   145  0.1870 0.2633        
REMARK   3    10  3.3972 -  3.2800    1.00     2719   145  0.1851 0.2946        
REMARK   3    11  3.2800 -  3.1775    1.00     2699   142  0.1827 0.1861        
REMARK   3    12  3.1775 -  3.0867    1.00     2724   145  0.1983 0.2728        
REMARK   3    13  3.0867 -  3.0054    1.00     2739   140  0.1961 0.2758        
REMARK   3    14  3.0054 -  2.9321    1.00     2733   139  0.2128 0.2779        
REMARK   3    15  2.9321 -  2.8655    1.00     2742   143  0.2032 0.2773        
REMARK   3    16  2.8655 -  2.8045    1.00     2697   146  0.2067 0.2745        
REMARK   3    17  2.8045 -  2.7484    1.00     2703   141  0.2083 0.2764        
REMARK   3    18  2.7484 -  2.6966    1.00     2719   147  0.2023 0.2765        
REMARK   3    19  2.6966 -  2.6500    0.98     2700   142  0.1994 0.2630        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.290            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.940           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008          11214                                  
REMARK   3   ANGLE     :  1.280          15228                                  
REMARK   3   CHIRALITY :  0.047           1710                                  
REMARK   3   PLANARITY :  0.005           1884                                  
REMARK   3   DIHEDRAL  : 14.743           4200                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0538 109.0423  16.9982              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2034 T22:   0.1416                                     
REMARK   3      T33:   0.1453 T12:  -0.0193                                     
REMARK   3      T13:  -0.0128 T23:  -0.0688                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0340 L22:   0.4535                                     
REMARK   3      L33:  -0.0564 L12:   0.0226                                     
REMARK   3      L13:  -0.1859 L23:  -0.1158                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0576 S12:   0.0317 S13:   0.0105                       
REMARK   3      S21:   0.0538 S22:  -0.0693 S23:  -0.0081                       
REMARK   3      S31:  -0.0077 S32:   0.0749 S33:  -0.0520                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4TTC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUN-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000202210.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-DEC-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54565                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.650                              
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 9.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 27.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.900                              
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: D_1000202202                                         
REMARK 200                                                                      
REMARK 200 REMARK: NEEDLE-SHAPED CRYSTAL                                        
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15 M SODIUM ACETATE, 85 MM TRIS-HCL,   
REMARK 280  25.5 % W/V POLYETHYLENE GLYCOL 4,000 AND 15 % GLYCEROL, PH 8.5,     
REMARK 280  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      101.11267            
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      202.22533            
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      151.66900            
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      252.78167            
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       50.55633            
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: 11820 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 18540 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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: 11890 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 18450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -76.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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: 11880 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 18470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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 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     SER A    31                                                      
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     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     SER B    31                                                      
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     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     SER C    31                                                      
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     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     SER D    31                                                      
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     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     SER E    31                                                      
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   291                                                      
REMARK 465     HIS E   292                                                      
REMARK 465     HIS E   293                                                      
REMARK 465     HIS E   294                                                      
REMARK 465     HIS E   295                                                      
REMARK 465     SER F    31                                                      
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   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    PRO A 134       43.23    -83.27                                   
REMARK 500    LYS A 163      -52.82   -138.13                                   
REMARK 500    ASP A 283        0.61    -68.02                                   
REMARK 500    PRO B 134       45.17    -81.31                                   
REMARK 500    LYS B 163      -53.16   -134.57                                   
REMARK 500    ASP B 283        2.28    -67.31                                   
REMARK 500    PRO C 134       42.33    -83.35                                   
REMARK 500    LYS C 163      -51.69   -134.99                                   
REMARK 500    ASP C 283        0.57    -66.22                                   
REMARK 500    PRO D 134       45.25    -83.00                                   
REMARK 500    LYS D 163      -54.18   -135.97                                   
REMARK 500    ASP D 283        0.06    -66.69                                   
REMARK 500    PRO E 134       44.99    -81.16                                   
REMARK 500    LYS E 163      -52.32   -135.12                                   
REMARK 500    ASP E 283        0.19    -67.33                                   
REMARK 500    PRO F 134       43.60    -83.66                                   
REMARK 500    LYS F 163      -51.48   -136.11                                   
REMARK 500    ASP F 283        1.48    -67.95                                   
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 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IYR A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMN B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IYR B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMN C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IYR C 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMN D 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IYR D 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMN E 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IYR E 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMN F 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IYR F 302                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4TTB   RELATED DB: PDB                                   
DBREF  4TTC A   32   289  UNP    Q6PHW0   IYD1_HUMAN      32    289             
DBREF  4TTC B   32   289  UNP    Q6PHW0   IYD1_HUMAN      32    289             
DBREF  4TTC C   32   289  UNP    Q6PHW0   IYD1_HUMAN      32    289             
DBREF  4TTC D   32   289  UNP    Q6PHW0   IYD1_HUMAN      32    289             
DBREF  4TTC E   32   289  UNP    Q6PHW0   IYD1_HUMAN      32    289             
DBREF  4TTC F   32   289  UNP    Q6PHW0   IYD1_HUMAN      32    289             
SEQADV 4TTC SER A   31  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS A  290  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS A  291  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS A  292  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS A  293  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS A  294  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS A  295  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC SER B   31  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS B  290  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS B  291  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS B  292  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS B  293  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS B  294  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS B  295  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC SER C   31  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS C  290  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS C  291  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS C  292  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS C  293  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS C  294  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS C  295  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC SER D   31  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS D  290  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS D  291  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS D  292  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS D  293  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS D  294  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS D  295  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC SER E   31  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS E  290  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS E  291  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS E  292  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS E  293  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS E  294  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS E  295  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC SER F   31  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS F  290  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS F  291  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS F  292  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS F  293  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS F  294  UNP  Q6PHW0              EXPRESSION TAG                 
SEQADV 4TTC HIS F  295  UNP  Q6PHW0              EXPRESSION TAG                 
SEQRES   1 A  265  SER GLY GLU PRO ARG THR ARG ALA GLU ALA ARG PRO TRP          
SEQRES   2 A  265  VAL ASP GLU ASP LEU LYS ASP SER SER ASP LEU HIS GLN          
SEQRES   3 A  265  ALA GLU GLU ASP ALA ASP GLU TRP GLN GLU SER GLU GLU          
SEQRES   4 A  265  ASN VAL GLU HIS ILE PRO PHE SER HIS ASN HIS TYR PRO          
SEQRES   5 A  265  GLU LYS GLU MET VAL LYS ARG SER GLN GLU PHE TYR GLU          
SEQRES   6 A  265  LEU LEU ASN LYS ARG ARG SER VAL ARG PHE ILE SER ASN          
SEQRES   7 A  265  GLU GLN VAL PRO MET GLU VAL ILE ASP ASN VAL ILE ARG          
SEQRES   8 A  265  THR ALA GLY THR ALA PRO SER GLY ALA HIS THR GLU PRO          
SEQRES   9 A  265  TRP THR PHE VAL VAL VAL LYS ASP PRO ASP VAL LYS HIS          
SEQRES  10 A  265  LYS ILE ARG LYS ILE ILE GLU GLU GLU GLU GLU ILE ASN          
SEQRES  11 A  265  TYR MET LYS ARG MET GLY HIS ARG TRP VAL THR ASP LEU          
SEQRES  12 A  265  LYS LYS LEU ARG THR ASN TRP ILE LYS GLU TYR LEU ASP          
SEQRES  13 A  265  THR ALA PRO ILE LEU ILE LEU ILE PHE LYS GLN VAL HIS          
SEQRES  14 A  265  GLY PHE ALA ALA ASN GLY LYS LYS LYS VAL HIS TYR TYR          
SEQRES  15 A  265  ASN GLU ILE SER VAL SER ILE ALA CYS GLY ILE LEU LEU          
SEQRES  16 A  265  ALA ALA LEU GLN ASN ALA GLY LEU VAL THR VAL THR THR          
SEQRES  17 A  265  THR PRO LEU ASN CYS GLY PRO ARG LEU ARG VAL LEU LEU          
SEQRES  18 A  265  GLY ARG PRO ALA HIS GLU LYS LEU LEU MET LEU LEU PRO          
SEQRES  19 A  265  VAL GLY TYR PRO SER LYS GLU ALA THR VAL PRO ASP LEU          
SEQRES  20 A  265  LYS ARG LYS PRO LEU ASP GLN ILE MET VAL THR VAL HIS          
SEQRES  21 A  265  HIS HIS HIS HIS HIS                                          
SEQRES   1 B  265  SER GLY GLU PRO ARG THR ARG ALA GLU ALA ARG PRO TRP          
SEQRES   2 B  265  VAL ASP GLU ASP LEU LYS ASP SER SER ASP LEU HIS GLN          
SEQRES   3 B  265  ALA GLU GLU ASP ALA ASP GLU TRP GLN GLU SER GLU GLU          
SEQRES   4 B  265  ASN VAL GLU HIS ILE PRO PHE SER HIS ASN HIS TYR PRO          
SEQRES   5 B  265  GLU LYS GLU MET VAL LYS ARG SER GLN GLU PHE TYR GLU          
SEQRES   6 B  265  LEU LEU ASN LYS ARG ARG SER VAL ARG PHE ILE SER ASN          
SEQRES   7 B  265  GLU GLN VAL PRO MET GLU VAL ILE ASP ASN VAL ILE ARG          
SEQRES   8 B  265  THR ALA GLY THR ALA PRO SER GLY ALA HIS THR GLU PRO          
SEQRES   9 B  265  TRP THR PHE VAL VAL VAL LYS ASP PRO ASP VAL LYS HIS          
SEQRES  10 B  265  LYS ILE ARG LYS ILE ILE GLU GLU GLU GLU GLU ILE ASN          
SEQRES  11 B  265  TYR MET LYS ARG MET GLY HIS ARG TRP VAL THR ASP LEU          
SEQRES  12 B  265  LYS LYS LEU ARG THR ASN TRP ILE LYS GLU TYR LEU ASP          
SEQRES  13 B  265  THR ALA PRO ILE LEU ILE LEU ILE PHE LYS GLN VAL HIS          
SEQRES  14 B  265  GLY PHE ALA ALA ASN GLY LYS LYS LYS VAL HIS TYR TYR          
SEQRES  15 B  265  ASN GLU ILE SER VAL SER ILE ALA CYS GLY ILE LEU LEU          
SEQRES  16 B  265  ALA ALA LEU GLN ASN ALA GLY LEU VAL THR VAL THR THR          
SEQRES  17 B  265  THR PRO LEU ASN CYS GLY PRO ARG LEU ARG VAL LEU LEU          
SEQRES  18 B  265  GLY ARG PRO ALA HIS GLU LYS LEU LEU MET LEU LEU PRO          
SEQRES  19 B  265  VAL GLY TYR PRO SER LYS GLU ALA THR VAL PRO ASP LEU          
SEQRES  20 B  265  LYS ARG LYS PRO LEU ASP GLN ILE MET VAL THR VAL HIS          
SEQRES  21 B  265  HIS HIS HIS HIS HIS                                          
SEQRES   1 C  265  SER GLY GLU PRO ARG THR ARG ALA GLU ALA ARG PRO TRP          
SEQRES   2 C  265  VAL ASP GLU ASP LEU LYS ASP SER SER ASP LEU HIS GLN          
SEQRES   3 C  265  ALA GLU GLU ASP ALA ASP GLU TRP GLN GLU SER GLU GLU          
SEQRES   4 C  265  ASN VAL GLU HIS ILE PRO PHE SER HIS ASN HIS TYR PRO          
SEQRES   5 C  265  GLU LYS GLU MET VAL LYS ARG SER GLN GLU PHE TYR GLU          
SEQRES   6 C  265  LEU LEU ASN LYS ARG ARG SER VAL ARG PHE ILE SER ASN          
SEQRES   7 C  265  GLU GLN VAL PRO MET GLU VAL ILE ASP ASN VAL ILE ARG          
SEQRES   8 C  265  THR ALA GLY THR ALA PRO SER GLY ALA HIS THR GLU PRO          
SEQRES   9 C  265  TRP THR PHE VAL VAL VAL LYS ASP PRO ASP VAL LYS HIS          
SEQRES  10 C  265  LYS ILE ARG LYS ILE ILE GLU GLU GLU GLU GLU ILE ASN          
SEQRES  11 C  265  TYR MET LYS ARG MET GLY HIS ARG TRP VAL THR ASP LEU          
SEQRES  12 C  265  LYS LYS LEU ARG THR ASN TRP ILE LYS GLU TYR LEU ASP          
SEQRES  13 C  265  THR ALA PRO ILE LEU ILE LEU ILE PHE LYS GLN VAL HIS          
SEQRES  14 C  265  GLY PHE ALA ALA ASN GLY LYS LYS LYS VAL HIS TYR TYR          
SEQRES  15 C  265  ASN GLU ILE SER VAL SER ILE ALA CYS GLY ILE LEU LEU          
SEQRES  16 C  265  ALA ALA LEU GLN ASN ALA GLY LEU VAL THR VAL THR THR          
SEQRES  17 C  265  THR PRO LEU ASN CYS GLY PRO ARG LEU ARG VAL LEU LEU          
SEQRES  18 C  265  GLY ARG PRO ALA HIS GLU LYS LEU LEU MET LEU LEU PRO          
SEQRES  19 C  265  VAL GLY TYR PRO SER LYS GLU ALA THR VAL PRO ASP LEU          
SEQRES  20 C  265  LYS ARG LYS PRO LEU ASP GLN ILE MET VAL THR VAL HIS          
SEQRES  21 C  265  HIS HIS HIS HIS HIS                                          
SEQRES   1 D  265  SER GLY GLU PRO ARG THR ARG ALA GLU ALA ARG PRO TRP          
SEQRES   2 D  265  VAL ASP GLU ASP LEU LYS ASP SER SER ASP LEU HIS GLN          
SEQRES   3 D  265  ALA GLU GLU ASP ALA ASP GLU TRP GLN GLU SER GLU GLU          
SEQRES   4 D  265  ASN VAL GLU HIS ILE PRO PHE SER HIS ASN HIS TYR PRO          
SEQRES   5 D  265  GLU LYS GLU MET VAL LYS ARG SER GLN GLU PHE TYR GLU          
SEQRES   6 D  265  LEU LEU ASN LYS ARG ARG SER VAL ARG PHE ILE SER ASN          
SEQRES   7 D  265  GLU GLN VAL PRO MET GLU VAL ILE ASP ASN VAL ILE ARG          
SEQRES   8 D  265  THR ALA GLY THR ALA PRO SER GLY ALA HIS THR GLU PRO          
SEQRES   9 D  265  TRP THR PHE VAL VAL VAL LYS ASP PRO ASP VAL LYS HIS          
SEQRES  10 D  265  LYS ILE ARG LYS ILE ILE GLU GLU GLU GLU GLU ILE ASN          
SEQRES  11 D  265  TYR MET LYS ARG MET GLY HIS ARG TRP VAL THR ASP LEU          
SEQRES  12 D  265  LYS LYS LEU ARG THR ASN TRP ILE LYS GLU TYR LEU ASP          
SEQRES  13 D  265  THR ALA PRO ILE LEU ILE LEU ILE PHE LYS GLN VAL HIS          
SEQRES  14 D  265  GLY PHE ALA ALA ASN GLY LYS LYS LYS VAL HIS TYR TYR          
SEQRES  15 D  265  ASN GLU ILE SER VAL SER ILE ALA CYS GLY ILE LEU LEU          
SEQRES  16 D  265  ALA ALA LEU GLN ASN ALA GLY LEU VAL THR VAL THR THR          
SEQRES  17 D  265  THR PRO LEU ASN CYS GLY PRO ARG LEU ARG VAL LEU LEU          
SEQRES  18 D  265  GLY ARG PRO ALA HIS GLU LYS LEU LEU MET LEU LEU PRO          
SEQRES  19 D  265  VAL GLY TYR PRO SER LYS GLU ALA THR VAL PRO ASP LEU          
SEQRES  20 D  265  LYS ARG LYS PRO LEU ASP GLN ILE MET VAL THR VAL HIS          
SEQRES  21 D  265  HIS HIS HIS HIS HIS                                          
SEQRES   1 E  265  SER GLY GLU PRO ARG THR ARG ALA GLU ALA ARG PRO TRP          
SEQRES   2 E  265  VAL ASP GLU ASP LEU LYS ASP SER SER ASP LEU HIS GLN          
SEQRES   3 E  265  ALA GLU GLU ASP ALA ASP GLU TRP GLN GLU SER GLU GLU          
SEQRES   4 E  265  ASN VAL GLU HIS ILE PRO PHE SER HIS ASN HIS TYR PRO          
SEQRES   5 E  265  GLU LYS GLU MET VAL LYS ARG SER GLN GLU PHE TYR GLU          
SEQRES   6 E  265  LEU LEU ASN LYS ARG ARG SER VAL ARG PHE ILE SER ASN          
SEQRES   7 E  265  GLU GLN VAL PRO MET GLU VAL ILE ASP ASN VAL ILE ARG          
SEQRES   8 E  265  THR ALA GLY THR ALA PRO SER GLY ALA HIS THR GLU PRO          
SEQRES   9 E  265  TRP THR PHE VAL VAL VAL LYS ASP PRO ASP VAL LYS HIS          
SEQRES  10 E  265  LYS ILE ARG LYS ILE ILE GLU GLU GLU GLU GLU ILE ASN          
SEQRES  11 E  265  TYR MET LYS ARG MET GLY HIS ARG TRP VAL THR ASP LEU          
SEQRES  12 E  265  LYS LYS LEU ARG THR ASN TRP ILE LYS GLU TYR LEU ASP          
SEQRES  13 E  265  THR ALA PRO ILE LEU ILE LEU ILE PHE LYS GLN VAL HIS          
SEQRES  14 E  265  GLY PHE ALA ALA ASN GLY LYS LYS LYS VAL HIS TYR TYR          
SEQRES  15 E  265  ASN GLU ILE SER VAL SER ILE ALA CYS GLY ILE LEU LEU          
SEQRES  16 E  265  ALA ALA LEU GLN ASN ALA GLY LEU VAL THR VAL THR THR          
SEQRES  17 E  265  THR PRO LEU ASN CYS GLY PRO ARG LEU ARG VAL LEU LEU          
SEQRES  18 E  265  GLY ARG PRO ALA HIS GLU LYS LEU LEU MET LEU LEU PRO          
SEQRES  19 E  265  VAL GLY TYR PRO SER LYS GLU ALA THR VAL PRO ASP LEU          
SEQRES  20 E  265  LYS ARG LYS PRO LEU ASP GLN ILE MET VAL THR VAL HIS          
SEQRES  21 E  265  HIS HIS HIS HIS HIS                                          
SEQRES   1 F  265  SER GLY GLU PRO ARG THR ARG ALA GLU ALA ARG PRO TRP          
SEQRES   2 F  265  VAL ASP GLU ASP LEU LYS ASP SER SER ASP LEU HIS GLN          
SEQRES   3 F  265  ALA GLU GLU ASP ALA ASP GLU TRP GLN GLU SER GLU GLU          
SEQRES   4 F  265  ASN VAL GLU HIS ILE PRO PHE SER HIS ASN HIS TYR PRO          
SEQRES   5 F  265  GLU LYS GLU MET VAL LYS ARG SER GLN GLU PHE TYR GLU          
SEQRES   6 F  265  LEU LEU ASN LYS ARG ARG SER VAL ARG PHE ILE SER ASN          
SEQRES   7 F  265  GLU GLN VAL PRO MET GLU VAL ILE ASP ASN VAL ILE ARG          
SEQRES   8 F  265  THR ALA GLY THR ALA PRO SER GLY ALA HIS THR GLU PRO          
SEQRES   9 F  265  TRP THR PHE VAL VAL VAL LYS ASP PRO ASP VAL LYS HIS          
SEQRES  10 F  265  LYS ILE ARG LYS ILE ILE GLU GLU GLU GLU GLU ILE ASN          
SEQRES  11 F  265  TYR MET LYS ARG MET GLY HIS ARG TRP VAL THR ASP LEU          
SEQRES  12 F  265  LYS LYS LEU ARG THR ASN TRP ILE LYS GLU TYR LEU ASP          
SEQRES  13 F  265  THR ALA PRO ILE LEU ILE LEU ILE PHE LYS GLN VAL HIS          
SEQRES  14 F  265  GLY PHE ALA ALA ASN GLY LYS LYS LYS VAL HIS TYR TYR          
SEQRES  15 F  265  ASN GLU ILE SER VAL SER ILE ALA CYS GLY ILE LEU LEU          
SEQRES  16 F  265  ALA ALA LEU GLN ASN ALA GLY LEU VAL THR VAL THR THR          
SEQRES  17 F  265  THR PRO LEU ASN CYS GLY PRO ARG LEU ARG VAL LEU LEU          
SEQRES  18 F  265  GLY ARG PRO ALA HIS GLU LYS LEU LEU MET LEU LEU PRO          
SEQRES  19 F  265  VAL GLY TYR PRO SER LYS GLU ALA THR VAL PRO ASP LEU          
SEQRES  20 F  265  LYS ARG LYS PRO LEU ASP GLN ILE MET VAL THR VAL HIS          
SEQRES  21 F  265  HIS HIS HIS HIS HIS                                          
HET    FMN  A 301      31                                                       
HET    IYR  A 302      14                                                       
HET    FMN  B 301      31                                                       
HET    IYR  B 302      14                                                       
HET    FMN  C 301      31                                                       
HET    IYR  C 302      14                                                       
HET    FMN  D 301      31                                                       
HET    IYR  D 302      14                                                       
HET    FMN  E 301      31                                                       
HET    IYR  E 302      14                                                       
HET    FMN  F 301      31                                                       
HET    IYR  F 302      14                                                       
HETNAM     FMN FLAVIN MONONUCLEOTIDE                                            
HETNAM     IYR 3-IODO-TYROSINE                                                  
HETSYN     FMN RIBOFLAVIN MONOPHOSPHATE                                         
FORMUL   7  FMN    6(C17 H21 N4 O9 P)                                           
FORMUL   8  IYR    6(C9 H10 I N O3)                                             
FORMUL  19  HOH   *221(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  LEU A  173  1                                   8    
HELIX    6 AA6 LYS A  174  ARG A  177  5                                   4    
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 ASP C  142  LYS C  163  1                                  22    
HELIX   24 AC6 GLY C  166  LEU C  173  1                                   8    
HELIX   25 AC7 LYS C  174  ARG C  177  5                                   4    
HELIX   26 AC8 GLU C  183  ALA C  188  1                                   6    
HELIX   27 AC9 TYR C  212  ALA C  231  1                                  20    
HELIX   28 AD1 CYS C  243  LEU C  251  1                                   9    
HELIX   29 AD2 PRO C  281  GLN C  284  5                                   4    
HELIX   30 AD3 PRO D   82  LYS D   99  1                                  18    
HELIX   31 AD4 PRO D  112  GLY D  124  1                                  13    
HELIX   32 AD5 SER D  128  THR D  132  5                                   5    
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  LEU D  251  1                                   9    
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  LYS E  174  1                                   9    
HELIX   45 AE9 LYS E  175  ARG E  177  5                                   3    
HELIX   46 AF1 GLU E  183  ALA E  188  1                                   6    
HELIX   47 AF2 TYR E  212  ALA E  231  1                                  20    
HELIX   48 AF3 CYS E  243  LEU E  251  1                                   9    
HELIX   49 AF4 PRO E  281  GLN E  284  5                                   4    
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 ASP F  142  LYS F  163  1                                  22    
HELIX   53 AF8 MET F  165  LEU F  173  1                                   9    
HELIX   54 AF9 LYS F  174  ARG F  177  5                                   4    
HELIX   55 AG1 GLU F  183  ALA F  188  1                                   6    
HELIX   56 AG2 TYR F  212  ALA F  231  1                                  20    
HELIX   57 AG3 CYS F  243  LEU F  251  1                                   9    
HELIX   58 AG4 PRO F  281  GLN F  284  5                                   4    
SHEET    1 AA1 2 HIS A  73  PRO A  75  0                                        
SHEET    2 AA1 2 THR B 273  PRO B 275 -1  O  VAL B 274   N  ILE A  74           
SHEET    1 AA2 2 SER A  77  ASN A  79  0                                        
SHEET    2 AA2 2 SER D  77  ASN D  79 -1  O  HIS D  78   N  HIS A  78           
SHEET    1 AA3 4 GLU A 257  VAL A 265  0                                        
SHEET    2 AA3 4 ILE A 190  GLN A 197 -1  N  ILE A 194   O  LEU A 260           
SHEET    3 AA3 4 TRP A 135  VAL A 140 -1  N  VAL A 138   O  LEU A 193           
SHEET    4 AA3 4 MET B 286  VAL B 289  1  O  VAL B 287   N  VAL A 139           
SHEET    1 AA4 2 HIS A 199  PHE A 201  0                                        
SHEET    2 AA4 2 LYS A 207  VAL A 209 -1  O  LYS A 208   N  GLY A 200           
SHEET    1 AA5 2 THR A 273  PRO A 275  0                                        
SHEET    2 AA5 2 HIS B  73  PRO B  75 -1  O  ILE B  74   N  VAL A 274           
SHEET    1 AA6 4 MET A 286  VAL A 289  0                                        
SHEET    2 AA6 4 TRP B 135  VAL B 140  1  O  VAL B 139   N  VAL A 287           
SHEET    3 AA6 4 ILE B 190  GLN B 197 -1  O  LEU B 193   N  VAL B 138           
SHEET    4 AA6 4 GLU B 257  VAL B 265 -1  O  VAL B 265   N  ILE B 190           
SHEET    1 AA7 2 HIS B 199  PHE B 201  0                                        
SHEET    2 AA7 2 LYS B 207  VAL B 209 -1  O  LYS B 208   N  GLY B 200           
SHEET    1 AA8 2 HIS C  73  PRO C  75  0                                        
SHEET    2 AA8 2 THR D 273  PRO D 275 -1  O  VAL D 274   N  ILE C  74           
SHEET    1 AA9 4 GLU C 257  VAL C 265  0                                        
SHEET    2 AA9 4 ILE C 190  GLN C 197 -1  N  ILE C 190   O  VAL C 265           
SHEET    3 AA9 4 TRP C 135  VAL C 140 -1  N  THR C 136   O  PHE C 195           
SHEET    4 AA9 4 MET D 286  VAL D 289  1  O  VAL D 287   N  VAL C 139           
SHEET    1 AB1 2 HIS C 199  PHE C 201  0                                        
SHEET    2 AB1 2 LYS C 207  VAL C 209 -1  O  LYS C 208   N  GLY C 200           
SHEET    1 AB2 2 THR C 273  PRO C 275  0                                        
SHEET    2 AB2 2 HIS D  73  PRO D  75 -1  O  ILE D  74   N  VAL C 274           
SHEET    1 AB3 4 MET C 286  VAL C 289  0                                        
SHEET    2 AB3 4 TRP D 135  VAL D 140  1  O  VAL D 139   N  VAL C 287           
SHEET    3 AB3 4 ILE D 190  GLN D 197 -1  O  LEU D 193   N  VAL D 138           
SHEET    4 AB3 4 GLU D 257  VAL D 265 -1  O  VAL D 265   N  ILE D 190           
SHEET    1 AB4 2 HIS D 199  PHE D 201  0                                        
SHEET    2 AB4 2 LYS D 207  VAL D 209 -1  O  LYS D 208   N  GLY D 200           
SHEET    1 AB5 2 HIS E  73  PRO E  75  0                                        
SHEET    2 AB5 2 THR F 273  PRO F 275 -1  O  VAL F 274   N  ILE E  74           
SHEET    1 AB6 4 GLU E 257  VAL E 265  0                                        
SHEET    2 AB6 4 ILE E 190  GLN E 197 -1  N  ILE E 190   O  VAL E 265           
SHEET    3 AB6 4 TRP E 135  VAL E 140 -1  N  VAL E 138   O  LEU E 193           
SHEET    4 AB6 4 MET F 286  VAL F 289  1  O  VAL F 287   N  VAL E 139           
SHEET    1 AB7 2 HIS E 199  PHE E 201  0                                        
SHEET    2 AB7 2 LYS E 207  VAL E 209 -1  O  LYS E 208   N  GLY E 200           
SHEET    1 AB8 2 THR E 273  PRO E 275  0                                        
SHEET    2 AB8 2 HIS F  73  PRO F  75 -1  O  ILE F  74   N  VAL E 274           
SHEET    1 AB9 4 MET E 286  VAL E 289  0                                        
SHEET    2 AB9 4 TRP F 135  VAL F 140  1  O  VAL F 139   N  VAL E 287           
SHEET    3 AB9 4 ILE F 190  GLN F 197 -1  O  PHE F 195   N  THR F 136           
SHEET    4 AB9 4 GLU F 257  VAL F 265 -1  O  VAL F 265   N  ILE F 190           
SHEET    1 AC1 2 HIS F 199  PHE F 201  0                                        
SHEET    2 AC1 2 LYS F 207  VAL F 209 -1  O  LYS F 208   N  GLY F 200           
SITE     1 AC1 21 ARG A 100  ARG A 101  SER A 102  ARG A 104                    
SITE     2 AC1 21 LEU A 176  THR A 178  THR A 237  THR A 238                    
SITE     3 AC1 21 THR A 239  ARG A 279  IYR A 302  HOH A 425                    
SITE     4 AC1 21 HOH A 426  HOH A 427  PRO B 127  SER B 128                    
SITE     5 AC1 21 GLY B 129  HIS B 131  TYR B 212  ILE B 215                    
SITE     6 AC1 21 SER B 216                                                     
SITE     1 AC2 10 GLU A 157  TYR A 161  LEU A 173  LEU A 176                    
SITE     2 AC2 10 THR A 178  ASN A 179  LYS A 182  FMN A 301                    
SITE     3 AC2 10 HOH A 437  ALA B 130                                          
SITE     1 AC3 20 PRO A 127  SER A 128  GLY A 129  TYR A 212                    
SITE     2 AC3 20 SER A 216  ARG B 100  ARG B 101  SER B 102                    
SITE     3 AC3 20 ARG B 104  LEU B 176  VAL B 236  THR B 237                    
SITE     4 AC3 20 THR B 238  THR B 239  LEU B 277  ARG B 279                    
SITE     5 AC3 20 IYR B 302  HOH B 404  HOH B 413  HOH B 424                    
SITE     1 AC4 10 ALA A 130  GLU B 157  TYR B 161  LEU B 173                    
SITE     2 AC4 10 LEU B 176  THR B 178  ASN B 179  LYS B 182                    
SITE     3 AC4 10 FMN B 301  HOH B 435                                          
SITE     1 AC5 21 ARG C 100  ARG C 101  SER C 102  ARG C 104                    
SITE     2 AC5 21 LEU C 176  THR C 178  VAL C 236  THR C 237                    
SITE     3 AC5 21 THR C 238  THR C 239  ARG C 279  IYR C 302                    
SITE     4 AC5 21 HOH C 409  HOH C 411  HOH C 415  HOH C 416                    
SITE     5 AC5 21 PRO D 127  SER D 128  GLY D 129  TYR D 212                    
SITE     6 AC5 21 SER D 216                                                     
SITE     1 AC6 10 GLU C 157  TYR C 161  TRP C 169  LEU C 173                    
SITE     2 AC6 10 LEU C 176  THR C 178  LYS C 182  FMN C 301                    
SITE     3 AC6 10 ALA D 130  TYR D 211                                          
SITE     1 AC7 19 PRO C 127  SER C 128  GLY C 129  HIS C 131                    
SITE     2 AC7 19 TYR C 212  SER C 216  ARG D 100  ARG D 101                    
SITE     3 AC7 19 SER D 102  ARG D 104  LEU D 176  VAL D 236                    
SITE     4 AC7 19 THR D 237  THR D 238  THR D 239  ARG D 279                    
SITE     5 AC7 19 IYR D 302  HOH D 410  HOH D 416                               
SITE     1 AC8 10 ALA C 130  GLU D 157  TYR D 161  LEU D 173                    
SITE     2 AC8 10 LEU D 176  ASN D 179  LYS D 182  THR D 239                    
SITE     3 AC8 10 FMN D 301  HOH D 412                                          
SITE     1 AC9 22 ARG E 100  ARG E 101  SER E 102  ARG E 104                    
SITE     2 AC9 22 LEU E 176  THR E 178  VAL E 236  THR E 237                    
SITE     3 AC9 22 THR E 238  THR E 239  ARG E 279  IYR E 302                    
SITE     4 AC9 22 HOH E 406  HOH E 410  HOH E 420  PRO F 127                    
SITE     5 AC9 22 SER F 128  GLY F 129  HIS F 131  TYR F 212                    
SITE     6 AC9 22 SER F 216  HOH F 405                                          
SITE     1 AD1 10 GLU E 157  TYR E 161  LEU E 173  LEU E 176                    
SITE     2 AD1 10 THR E 178  ASN E 179  LYS E 182  THR E 239                    
SITE     3 AD1 10 FMN E 301  ALA F 130                                          
SITE     1 AD2 21 PRO E 127  SER E 128  GLY E 129  TYR E 212                    
SITE     2 AD2 21 ILE E 215  SER E 216  ARG F 100  ARG F 101                    
SITE     3 AD2 21 SER F 102  ARG F 104  LEU F 176  THR F 178                    
SITE     4 AD2 21 VAL F 236  THR F 237  THR F 238  THR F 239                    
SITE     5 AD2 21 ARG F 279  IYR F 302  HOH F 404  HOH F 406                    
SITE     6 AD2 21 HOH F 409                                                     
SITE     1 AD3  9 ALA E 130  GLU F 157  TYR F 161  LEU F 173                    
SITE     2 AD3  9 LEU F 176  THR F 178  ASN F 179  LYS F 182                    
SITE     3 AD3  9 FMN F 301                                                     
CRYST1  104.747  104.747  303.338  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      0.009547  0.005512  0.000000        0.00000                         
SCALE2      0.000000  0.011024  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003297        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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