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Database: PDB
Entry: 1OQC
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HEADER    OXIDOREDUCTASE                          07-MAR-03   1OQC              
TITLE     THE CRYSTAL STRUCTURE OF AUGMENTER OF LIVER REGENERATION: A MAMMALIAN 
TITLE    2 FAD DEPENDENT SULFHYDRYL OXIDASE                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AUGMENTER OF LIVER REGENERATION;                           
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: ALR;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: ALR;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET16                                     
KEYWDS    SULFHYDRYL OXIDASE, LIVER REGENERATION, ALR, HELIX-TURN-HELIX,        
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.P.ROSE,C.-K.WU,B.-C.WANG                                            
REVDAT   5   13-JUL-11 1OQC    1       VERSN                                    
REVDAT   4   24-FEB-09 1OQC    1       VERSN                                    
REVDAT   3   28-FEB-06 1OQC    1       REMARK                                   
REVDAT   2   27-APR-04 1OQC    1       JRNL                                     
REVDAT   1   15-APR-03 1OQC    0                                                
JRNL        AUTH   C.-K.WU,T.A.DAILEY,H.A.DAILEY,B.-C.WANG,J.P.ROSE             
JRNL        TITL   THE REFINED CRYSTAL STRUCTURE OF AUGMENTER OF LIVER          
JRNL        TITL 2 REGENERATION                                                 
JRNL        REF    INT.UNION CRYST.(MEETING)     V.   1   293 1999              
JRNL        REFN                   ISSN 1067-0696                               
JRNL        DOI    10.1109/ACC.1999.782787                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.-K.WU,T.A.DAILEY,H.A.DAILEY,B.C.WANG,J.P.ROSE              
REMARK   1  TITL   THE CRYSTAL STRUCTURE OF AUGMENTER OF LIVER REGENERATION: A  
REMARK   1  TITL 2 MAMMALIAN FAD-DEPENDENT SULFHYDRYL OXIDASE                   
REMARK   1  REF    PROTEIN SCI.                  V.  12  1109 2003              
REMARK   1  REFN                   ISSN 0961-8368                               
REMARK   1  PMID   12717032                                                     
REMARK   1  DOI    10.1110/PS.0238103                                           
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   C.-K.WU,T.DAILEY,H.DAILEY,A.FRANCAVILLA,T.E.STARZL,          
REMARK   1  AUTH 2 B.-C.WANG,J.P.ROSE                                           
REMARK   1  TITL   EXPRESSION, PURIFICATION, CRYSTALLIZATION AND PRELIMINARY    
REMARK   1  TITL 2 X-RAY ANALYSIS OF THE AUGMENTER OF LIVER REGENERATION        
REMARK   1  REF    PROTEIN PEPT.LETT.            V.   7    25 2000              
REMARK   1  REFN                   ISSN 0929-8665                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   J.P.ROSE,C.-K.WU,A.FRANCAVILLA,J.G.PRELICH,A.IACOBELLIS,     
REMARK   1  AUTH 2 M.HAGIYA,A.S.RAO,T.E.STARZL,B.C.WANG                         
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC DATA FOR    
REMARK   1  TITL 2 THE AUGMENTER OF LIVER REGENERATION                          
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  53   331 1997              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1  DOI    10.1107/S0907444996014084                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.65                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1754209.160                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 88.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 41788                          
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 SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2100                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.91                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 74.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5503                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2110                       
REMARK   3   BIN FREE R VALUE                    : 0.2680                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 279                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.016                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3728                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 212                                     
REMARK   3   SOLVENT ATOMS            : 623                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 10.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.94000                                              
REMARK   3    B22 (A**2) : -1.47000                                             
REMARK   3    B33 (A**2) : 0.53000                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.19                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.08                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 6.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.24                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.14                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 18.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.32                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.38                                                 
REMARK   3   BSOL        : 44.19                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  3  : FAD.PAR                                        
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : FAD.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1OQC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAR-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB018560.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-SEP-98; 25-JUN-98               
REMARK 200  TEMPERATURE           (KELVIN) : 120; 120                           
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : NSLS; APS                          
REMARK 200  BEAMLINE                       : X12C; 17-ID                        
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95, 0.979, 0.978; 0.979          
REMARK 200  MONOCHROMATOR                  : GRAPHITE CRYSTAL; GRAPHITE         
REMARK 200                                   CRYSTAL                            
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : CUSTOM-MADE; SIEMENS               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, SAINT                       
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, SAINT                   
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41788                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.650                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 76.5                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 40.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.02                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.17300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.880                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD; SINGLE WAVELENGTH                         
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: PHASING DATA (SE-MAD) WERE COLLECTED ON X12C, NSLS  TO 2.5   
REMARK 200  ANGSTROMS. REFINEMENT DATA WERE COLLECTED ON 17ID, APS TO 1.5       
REMARK 200  ANGSTROMS.                                                          
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, MAGNESIUM CHLORIDE, PH 6.5,    
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 300K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       53.49350            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.56500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       53.49350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       61.56500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: DISULFIDE LINKED HOMO DIMER                                  
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,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 5740 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 5580 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     LYS A     6                                                      
REMARK 465     ARG A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     ILE A     9                                                      
REMARK 465     LYS A    10                                                      
REMARK 465     PHE A    11                                                      
REMARK 465     ARG A    12                                                      
REMARK 465     ASP A   125                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ARG B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     GLN B     4                                                      
REMARK 465     GLN B     5                                                      
REMARK 465     LYS B     6                                                      
REMARK 465     ARG B     7                                                      
REMARK 465     ASP B     8                                                      
REMARK 465     ILE B     9                                                      
REMARK 465     LYS B    10                                                      
REMARK 465     PHE B    11                                                      
REMARK 465     ARG B    12                                                      
REMARK 465     GLU B    13                                                      
REMARK 465     ASP B   125                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ARG C     2                                                      
REMARK 465     THR C     3                                                      
REMARK 465     GLN C     4                                                      
REMARK 465     GLN C     5                                                      
REMARK 465     LYS C     6                                                      
REMARK 465     ARG C     7                                                      
REMARK 465     ASP C     8                                                      
REMARK 465     ILE C     9                                                      
REMARK 465     LYS C    10                                                      
REMARK 465     PHE C    11                                                      
REMARK 465     ARG C    12                                                      
REMARK 465     ASP C   125                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ARG D     2                                                      
REMARK 465     THR D     3                                                      
REMARK 465     GLN D     4                                                      
REMARK 465     GLN D     5                                                      
REMARK 465     LYS D     6                                                      
REMARK 465     ARG D     7                                                      
REMARK 465     ASP D     8                                                      
REMARK 465     ILE D     9                                                      
REMARK 465     LYS D    10                                                      
REMARK 465     PHE D    11                                                      
REMARK 465     ARG D    12                                                      
REMARK 465     ASP D   125                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 120    CG   CD   CE   NZ                                   
REMARK 470     SER A 123    OG                                                  
REMARK 470     GLU C  13    CB   CG   CD   OE1  OE2                             
REMARK 470     GLU D  13    CB   CG   CD   OE1  OE2                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B  61   C   -  N   -  CA  ANGL. DEV. =  11.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A  61      -14.81    -41.21                                   
REMARK 500    ARG A 116      -58.50   -132.03                                   
REMARK 500    PRO B  61       13.91    -52.35                                   
REMARK 500    ARG B 116      -56.23   -126.54                                   
REMARK 500    ASP C  14       -8.66   -149.38                                   
REMARK 500    MET C  40       63.11   -119.74                                   
REMARK 500    CYS C  62      108.85    -58.26                                   
REMARK 500    ARG C 116      -55.42   -131.33                                   
REMARK 500    CYS D  62      109.29    -57.19                                   
REMARK 500    ARG D 116      -62.18   -124.97                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 273        DISTANCE =  5.20 ANGSTROMS                       
REMARK 525    HOH D 273        DISTANCE =  5.29 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: CTA                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: PUTATIVE CATALYTIC SITE                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CTB                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: PUTATIVE CATALYTIC SITE                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CTC                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: PUTATIVE CATALYTIC SITE                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CTD                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: PUTATIVE CATALYTIC SITE                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 126                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 126                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD C 126                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD D 126                 
DBREF  1OQC A    1   125  UNP    Q63042   ALR_RAT          1    125             
DBREF  1OQC B    1   125  UNP    Q63042   ALR_RAT          1    125             
DBREF  1OQC C    1   125  UNP    Q63042   ALR_RAT          1    125             
DBREF  1OQC D    1   125  UNP    Q63042   ALR_RAT          1    125             
SEQRES   1 A  125  MET ARG THR GLN GLN LYS ARG ASP ILE LYS PHE ARG GLU          
SEQRES   2 A  125  ASP CYS PRO GLN ASP ARG GLU GLU LEU GLY ARG ASN THR          
SEQRES   3 A  125  TRP ALA PHE LEU HIS THR LEU ALA ALA TYR TYR PRO ASP          
SEQRES   4 A  125  MET PRO THR PRO GLU GLN GLN GLN ASP MET ALA GLN PHE          
SEQRES   5 A  125  ILE HIS ILE PHE SER LYS PHE TYR PRO CYS GLU GLU CYS          
SEQRES   6 A  125  ALA GLU ASP ILE ARG LYS ARG ILE ASP ARG SER GLN PRO          
SEQRES   7 A  125  ASP THR SER THR ARG VAL SER PHE SER GLN TRP LEU CYS          
SEQRES   8 A  125  ARG LEU HIS ASN GLU VAL ASN ARG LYS LEU GLY LYS PRO          
SEQRES   9 A  125  ASP PHE ASP CYS SER ARG VAL ASP GLU ARG TRP ARG ASP          
SEQRES  10 A  125  GLY TRP LYS ASP GLY SER CYS ASP                              
SEQRES   1 B  125  MET ARG THR GLN GLN LYS ARG ASP ILE LYS PHE ARG GLU          
SEQRES   2 B  125  ASP CYS PRO GLN ASP ARG GLU GLU LEU GLY ARG ASN THR          
SEQRES   3 B  125  TRP ALA PHE LEU HIS THR LEU ALA ALA TYR TYR PRO ASP          
SEQRES   4 B  125  MET PRO THR PRO GLU GLN GLN GLN ASP MET ALA GLN PHE          
SEQRES   5 B  125  ILE HIS ILE PHE SER LYS PHE TYR PRO CYS GLU GLU CYS          
SEQRES   6 B  125  ALA GLU ASP ILE ARG LYS ARG ILE ASP ARG SER GLN PRO          
SEQRES   7 B  125  ASP THR SER THR ARG VAL SER PHE SER GLN TRP LEU CYS          
SEQRES   8 B  125  ARG LEU HIS ASN GLU VAL ASN ARG LYS LEU GLY LYS PRO          
SEQRES   9 B  125  ASP PHE ASP CYS SER ARG VAL ASP GLU ARG TRP ARG ASP          
SEQRES  10 B  125  GLY TRP LYS ASP GLY SER CYS ASP                              
SEQRES   1 C  125  MET ARG THR GLN GLN LYS ARG ASP ILE LYS PHE ARG GLU          
SEQRES   2 C  125  ASP CYS PRO GLN ASP ARG GLU GLU LEU GLY ARG ASN THR          
SEQRES   3 C  125  TRP ALA PHE LEU HIS THR LEU ALA ALA TYR TYR PRO ASP          
SEQRES   4 C  125  MET PRO THR PRO GLU GLN GLN GLN ASP MET ALA GLN PHE          
SEQRES   5 C  125  ILE HIS ILE PHE SER LYS PHE TYR PRO CYS GLU GLU CYS          
SEQRES   6 C  125  ALA GLU ASP ILE ARG LYS ARG ILE ASP ARG SER GLN PRO          
SEQRES   7 C  125  ASP THR SER THR ARG VAL SER PHE SER GLN TRP LEU CYS          
SEQRES   8 C  125  ARG LEU HIS ASN GLU VAL ASN ARG LYS LEU GLY LYS PRO          
SEQRES   9 C  125  ASP PHE ASP CYS SER ARG VAL ASP GLU ARG TRP ARG ASP          
SEQRES  10 C  125  GLY TRP LYS ASP GLY SER CYS ASP                              
SEQRES   1 D  125  MET ARG THR GLN GLN LYS ARG ASP ILE LYS PHE ARG GLU          
SEQRES   2 D  125  ASP CYS PRO GLN ASP ARG GLU GLU LEU GLY ARG ASN THR          
SEQRES   3 D  125  TRP ALA PHE LEU HIS THR LEU ALA ALA TYR TYR PRO ASP          
SEQRES   4 D  125  MET PRO THR PRO GLU GLN GLN GLN ASP MET ALA GLN PHE          
SEQRES   5 D  125  ILE HIS ILE PHE SER LYS PHE TYR PRO CYS GLU GLU CYS          
SEQRES   6 D  125  ALA GLU ASP ILE ARG LYS ARG ILE ASP ARG SER GLN PRO          
SEQRES   7 D  125  ASP THR SER THR ARG VAL SER PHE SER GLN TRP LEU CYS          
SEQRES   8 D  125  ARG LEU HIS ASN GLU VAL ASN ARG LYS LEU GLY LYS PRO          
SEQRES   9 D  125  ASP PHE ASP CYS SER ARG VAL ASP GLU ARG TRP ARG ASP          
SEQRES  10 D  125  GLY TRP LYS ASP GLY SER CYS ASP                              
HET    FAD  A 126      53                                                       
HET    FAD  B 126      53                                                       
HET    FAD  C 126      53                                                       
HET    FAD  D 126      53                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
FORMUL   5  FAD    4(C27 H33 N9 O15 P2)                                         
FORMUL   9  HOH   *623(H2 O)                                                    
HELIX    1   1 ASP A   18  TYR A   36  1                                  19    
HELIX    2   2 THR A   42  TYR A   60  1                                  19    
HELIX    3   3 CYS A   62  SER A   76  1                                  15    
HELIX    4   4 THR A   82  LEU A  101  1                                  20    
HELIX    5   5 ASP A  107  SER A  109  5                                   3    
HELIX    6   6 ARG A  110  ARG A  116  1                                   7    
HELIX    7   7 ASP B   18  TYR B   36  1                                  19    
HELIX    8   8 THR B   42  TYR B   60  1                                  19    
HELIX    9   9 CYS B   62  SER B   76  1                                  15    
HELIX   10  10 THR B   82  LEU B  101  1                                  20    
HELIX   11  11 ASP B  107  SER B  109  5                                   3    
HELIX   12  12 ARG B  110  ARG B  116  1                                   7    
HELIX   13  13 ASP C   18  TYR C   36  1                                  19    
HELIX   14  14 THR C   42  TYR C   60  1                                  19    
HELIX   15  15 CYS C   62  SER C   76  1                                  15    
HELIX   16  16 THR C   82  LEU C  101  1                                  20    
HELIX   17  17 ASP C  107  SER C  109  5                                   3    
HELIX   18  18 ARG C  110  ARG C  116  1                                   7    
HELIX   19  19 ASP D   18  TYR D   36  1                                  19    
HELIX   20  20 THR D   42  TYR D   60  1                                  19    
HELIX   21  21 CYS D   62  SER D   76  1                                  15    
HELIX   22  22 THR D   82  LEU D  101  1                                  20    
HELIX   23  23 ASP D  107  SER D  109  5                                   3    
HELIX   24  24 ARG D  110  ARG D  116  1                                   7    
SSBOND   1 CYS A   15    CYS C  124                          1555   1555  2.02  
SSBOND   2 CYS A   62    CYS A   65                          1555   1555  2.03  
SSBOND   3 CYS A   91    CYS A  108                          1555   1555  2.03  
SSBOND   4 CYS A  124    CYS C   15                          1555   1555  2.03  
SSBOND   5 CYS B   15    CYS D  124                          1555   1555  2.03  
SSBOND   6 CYS B   62    CYS B   65                          1555   1555  2.03  
SSBOND   7 CYS B   91    CYS B  108                          1555   1555  2.03  
SSBOND   8 CYS B  124    CYS D   15                          1555   1555  2.03  
SSBOND   9 CYS C   62    CYS C   65                          1555   1555  2.03  
SSBOND  10 CYS C   91    CYS C  108                          1555   1555  2.03  
SSBOND  11 CYS D   62    CYS D   65                          1555   1555  2.03  
SSBOND  12 CYS D   91    CYS D  108                          1555   1555  2.03  
SITE     1 CTA  3 CYS A  62  CYS A  65  FAD A 126                               
SITE     1 CTB  3 CYS B  62  CYS B  65  FAD B 126                               
SITE     1 CTC  3 CYS C  62  CYS C  65  FAD C 126                               
SITE     1 CTD  3 CYS D  62  CYS D  65  FAD D 126                               
SITE     1 AC1 30 ARG A  19  GLU A  20  GLY A  23  ARG A  24                    
SITE     2 AC1 30 TRP A  27  HIS A  31  PHE A  56  TYR A  60                    
SITE     3 AC1 30 CYS A  65  ILE A  69  CYS A  91  HIS A  94                    
SITE     4 AC1 30 ASN A  95  VAL A  97  ASN A  98  LYS A 100                    
SITE     5 AC1 30 LEU A 101  LYS A 103  PHE A 106  ARG A 114                    
SITE     6 AC1 30 TRP A 115  HOH A 131  HOH A 148  HOH A 150                    
SITE     7 AC1 30 HOH A 165  HOH A 195  HOH A 201  HOH A 203                    
SITE     8 AC1 30 HOH A 252  HOH A 266                                          
SITE     1 AC2 29 ARG B  19  GLU B  20  GLY B  23  ARG B  24                    
SITE     2 AC2 29 TRP B  27  HIS B  31  PHE B  56  TYR B  60                    
SITE     3 AC2 29 CYS B  65  CYS B  91  HIS B  94  ASN B  95                    
SITE     4 AC2 29 VAL B  97  ASN B  98  LYS B 100  LEU B 101                    
SITE     5 AC2 29 LYS B 103  PHE B 106  ARG B 114  TRP B 115                    
SITE     6 AC2 29 HOH B 135  HOH B 152  HOH B 167  HOH B 174                    
SITE     7 AC2 29 HOH B 192  HOH B 198  HOH B 215  HOH B 232                    
SITE     8 AC2 29 HOH B 276                                                     
SITE     1 AC3 29 ARG C  19  GLU C  20  GLY C  23  ARG C  24                    
SITE     2 AC3 29 TRP C  27  HIS C  31  PHE C  56  TYR C  60                    
SITE     3 AC3 29 CYS C  65  ILE C  69  CYS C  91  HIS C  94                    
SITE     4 AC3 29 ASN C  95  VAL C  97  ASN C  98  LYS C 100                    
SITE     5 AC3 29 LEU C 101  LYS C 103  PHE C 106  ARG C 114                    
SITE     6 AC3 29 TRP C 115  HOH C 139  HOH C 162  HOH C 179                    
SITE     7 AC3 29 HOH C 185  HOH C 189  HOH C 233  HOH C 263                    
SITE     8 AC3 29 HOH C 274                                                     
SITE     1 AC4 32 ARG D  19  GLU D  20  GLY D  23  ARG D  24                    
SITE     2 AC4 32 TRP D  27  HIS D  31  PHE D  56  TYR D  60                    
SITE     3 AC4 32 CYS D  65  ASP D  68  ILE D  69  CYS D  91                    
SITE     4 AC4 32 HIS D  94  ASN D  95  VAL D  97  ASN D  98                    
SITE     5 AC4 32 LYS D 100  LEU D 101  LYS D 103  PHE D 106                    
SITE     6 AC4 32 ARG D 114  TRP D 115  HOH D 144  HOH D 148                    
SITE     7 AC4 32 HOH D 159  HOH D 162  HOH D 164  HOH D 183                    
SITE     8 AC4 32 HOH D 187  HOH D 193  HOH D 261  HOH D 269                    
CRYST1  106.987  123.130   37.930  90.00  90.00  90.00 P 21 21 2    16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009347  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008121  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.026364        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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