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Database: PDB
Entry: 3F5C
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Original site: 3F5C 
HEADER    TRANSCRIPTION                           03-NOV-08   3F5C              
TITLE     STRUCTURE OF DAX-1:LRH-1 COMPLEX                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NUCLEAR RECEPTOR SUBFAMILY 5 GROUP A MEMBER 2;             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 313-560;                                      
COMPND   5 SYNONYM: LIVER RECEPTOR HOMOLOG 1, LRH-1;                            
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: NUCLEAR RECEPTOR SUBFAMILY 0 GROUP B MEMBER 1;             
COMPND  10 CHAIN: B, C;                                                         
COMPND  11 FRAGMENT: UNP RESIDUES 205-472;                                      
COMPND  12 SYNONYM: NUCLEAR RECEPTOR DAX-1;                                     
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: NR5A2, LRH1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) STAR;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PACYCDUET-1;                              
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  13 ORGANISM_COMMON: MOUSE;                                              
SOURCE  14 ORGANISM_TAXID: 10090;                                               
SOURCE  15 GENE: NR0B1, AHCH, DAX1;                                             
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) STAR;                            
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PETDUET-1                                 
KEYWDS    NUCLEAR RECEPTOR, TRANSCRIPTIONAL COREPRESSOR, REGULATORY COMPLEX,    
KEYWDS   2 DNA-BINDING, LIPID-BINDING, METAL-BINDING, NUCLEUS, RECEPTOR,        
KEYWDS   3 TRANSCRIPTION, TRANSCRIPTION REGULATION, ZINC, ZINC-FINGER,          
KEYWDS   4 CYTOPLASM, REPRESSOR                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.J.FLETTERICK,E.P.SABLIN                                             
REVDAT   2   24-JUL-19 3F5C    1       REMARK                                   
REVDAT   1   23-DEC-08 3F5C    0                                                
JRNL        AUTH   E.P.SABLIN,A.WOODS,I.N.KRYLOVA,P.HWANG,H.A.INGRAHAM,         
JRNL        AUTH 2 R.J.FLETTERICK                                               
JRNL        TITL   THE STRUCTURE OF COREPRESSOR DAX-1 BOUND TO ITS TARGET       
JRNL        TITL 2 NUCLEAR RECEPTOR LRH-1.                                      
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 105 18390 2008              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   19015525                                                     
JRNL        DOI    10.1073/PNAS.0808936105                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.79                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.080                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 24366                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.279                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.870                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 700                             
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 24.7861 -  5.1182    1.00     4863   129  0.1873 0.2567        
REMARK   3     2  5.1182 -  4.0683    0.99     4745   174  0.1667 0.2342        
REMARK   3     3  4.0683 -  3.5558    0.99     4730   143  0.2202 0.2786        
REMARK   3     4  3.5558 -  3.2314    0.99     4749   139  0.3000 0.3393        
REMARK   3     5  3.2314 -  3.0000    0.95     4579   115  0.3827 0.4025        
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              : 0.27                                          
REMARK   3   B_SOL              : 60.49                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.590            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.860           
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      :  0.011           5036                                  
REMARK   3   ANGLE     :  1.253           6813                                  
REMARK   3   CHIRALITY :  0.073            781                                  
REMARK   3   PLANARITY :  0.006            861                                  
REMARK   3   DIHEDRAL  : 15.382           1863                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  84.9069  41.1261  69.0478              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4680 T22:   0.3151                                     
REMARK   3      T33:   0.4378 T12:   0.1362                                     
REMARK   3      T13:  -0.2337 T23:  -0.2672                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4661 L22:   5.5721                                     
REMARK   3      L33:   3.6729 L12:  -1.6936                                     
REMARK   3      L13:   1.4893 L23:  -0.0146                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2929 S12:  -0.4708 S13:   0.8802                       
REMARK   3      S21:   0.9052 S22:   0.1252 S23:  -0.5328                       
REMARK   3      S31:  -0.3866 S32:   0.1442 S33:   0.0845                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  56.0031  43.5002  47.5750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3606 T22:   0.3121                                     
REMARK   3      T33:   0.1429 T12:   0.1241                                     
REMARK   3      T13:  -0.1758 T23:   0.2193                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6963 L22:   3.4832                                     
REMARK   3      L33:   2.9496 L12:   0.6719                                     
REMARK   3      L13:  -0.5944 L23:   1.1399                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1913 S12:   0.1125 S13:  -0.0504                       
REMARK   3      S21:  -0.1627 S22:  -0.1264 S23:   0.0886                       
REMARK   3      S31:   0.1419 S32:   0.1101 S33:  -0.0261                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN C                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  87.9032   3.9320  45.0439              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1947 T22:   0.3417                                     
REMARK   3      T33:   0.6514 T12:   0.0271                                     
REMARK   3      T13:  -0.0627 T23:  -0.2444                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3934 L22:   5.1570                                     
REMARK   3      L33:   6.1197 L12:   0.7796                                     
REMARK   3      L13:  -0.9765 L23:   4.4003                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2029 S12:  -0.1129 S13:  -0.1102                       
REMARK   3      S21:  -0.0806 S22:   0.1290 S23:  -0.4620                       
REMARK   3      S31:  -0.0185 S32:   0.2999 S33:  -0.0221                       
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 3F5C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-NOV-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000050165.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-NOV-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : KHOZU DOUBLE FLAT CRYSTAL          
REMARK 200                                   SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24366                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.07900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1PK5                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.51                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 20% PEG 8000, 1 MM DEOXY    
REMARK 280  -BIGCHAP, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE        
REMARK 280  298.0K                                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
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       58.72750            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       88.09125            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       29.36375            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLN A   313                                                      
REMARK 465     THR A   314                                                      
REMARK 465     ASN A   315                                                      
REMARK 465     SER A   316                                                      
REMARK 465     PRO A   317                                                      
REMARK 465     GLY B   205                                                      
REMARK 465     GLU B   206                                                      
REMARK 465     GLU B   207                                                      
REMARK 465     GLN B   208                                                      
REMARK 465     PRO B   209                                                      
REMARK 465     GLN B   210                                                      
REMARK 465     GLN B   211                                                      
REMARK 465     ILE B   212                                                      
REMARK 465     SER B   213                                                      
REMARK 465     VAL B   214                                                      
REMARK 465     ALA B   215                                                      
REMARK 465     SER B   216                                                      
REMARK 465     GLY B   217                                                      
REMARK 465     THR B   218                                                      
REMARK 465     PRO B   219                                                      
REMARK 465     VAL B   220                                                      
REMARK 465     SER B   221                                                      
REMARK 465     ALA B   222                                                      
REMARK 465     ASP B   223                                                      
REMARK 465     GLN B   224                                                      
REMARK 465     THR B   225                                                      
REMARK 465     PRO B   226                                                      
REMARK 465     ALA B   227                                                      
REMARK 465     THR B   228                                                      
REMARK 465     PRO B   229                                                      
REMARK 465     GLN B   230                                                      
REMARK 465     GLU B   231                                                      
REMARK 465     GLN B   232                                                      
REMARK 465     PRO B   233                                                      
REMARK 465     ARG B   234                                                      
REMARK 465     ALA B   235                                                      
REMARK 465     PRO B   236                                                      
REMARK 465     TRP B   237                                                      
REMARK 465     TRP B   238                                                      
REMARK 465     ASP B   239                                                      
REMARK 465     ALA B   240                                                      
REMARK 465     SER B   241                                                      
REMARK 465     PRO B   242                                                      
REMARK 465     GLY B   243                                                      
REMARK 465     VAL B   244                                                      
REMARK 465     GLN B   245                                                      
REMARK 465     ARG B   246                                                      
REMARK 465     LEU B   247                                                      
REMARK 465     ILE B   248                                                      
REMARK 465     THR B   249                                                      
REMARK 465     LEU B   250                                                      
REMARK 465     PRO B   314                                                      
REMARK 465     GLU B   315                                                      
REMARK 465     THR B   316                                                      
REMARK 465     ASN B   317                                                      
REMARK 465     THR B   318                                                      
REMARK 465     THR B   319                                                      
REMARK 465     GLN B   320                                                      
REMARK 465     GLU B   321                                                      
REMARK 465     MET B   322                                                      
REMARK 465     LEU B   323                                                      
REMARK 465     THR B   324                                                      
REMARK 465     THR B   325                                                      
REMARK 465     ARG B   326                                                      
REMARK 465     ARG B   327                                                      
REMARK 465     GLN B   328                                                      
REMARK 465     GLU B   329                                                      
REMARK 465     THR B   330                                                      
REMARK 465     GLU B   331                                                      
REMARK 465     GLY B   332                                                      
REMARK 465     PRO B   333                                                      
REMARK 465     GLU B   334                                                      
REMARK 465     PRO B   335                                                      
REMARK 465     ALA B   336                                                      
REMARK 465     GLU B   337                                                      
REMARK 465     PRO B   338                                                      
REMARK 465     GLN B   339                                                      
REMARK 465     ALA B   340                                                      
REMARK 465     THR B   341                                                      
REMARK 465     GLU B   342                                                      
REMARK 465     GLN B   343                                                      
REMARK 465     PRO B   344                                                      
REMARK 465     GLN B   345                                                      
REMARK 465     MET B   346                                                      
REMARK 465     VAL B   347                                                      
REMARK 465     SER B   348                                                      
REMARK 465     ALA B   349                                                      
REMARK 465     GLU B   350                                                      
REMARK 465     ALA B   351                                                      
REMARK 465     GLY B   352                                                      
REMARK 465     GLY C   205                                                      
REMARK 465     GLU C   206                                                      
REMARK 465     GLU C   207                                                      
REMARK 465     GLN C   208                                                      
REMARK 465     PRO C   209                                                      
REMARK 465     GLN C   210                                                      
REMARK 465     GLN C   211                                                      
REMARK 465     ILE C   212                                                      
REMARK 465     SER C   213                                                      
REMARK 465     VAL C   214                                                      
REMARK 465     ALA C   215                                                      
REMARK 465     SER C   216                                                      
REMARK 465     GLY C   217                                                      
REMARK 465     THR C   218                                                      
REMARK 465     PRO C   219                                                      
REMARK 465     VAL C   220                                                      
REMARK 465     SER C   221                                                      
REMARK 465     ALA C   222                                                      
REMARK 465     ASP C   223                                                      
REMARK 465     GLN C   224                                                      
REMARK 465     THR C   225                                                      
REMARK 465     PRO C   226                                                      
REMARK 465     ALA C   227                                                      
REMARK 465     THR C   228                                                      
REMARK 465     PRO C   229                                                      
REMARK 465     GLN C   230                                                      
REMARK 465     GLU C   231                                                      
REMARK 465     GLN C   232                                                      
REMARK 465     PRO C   233                                                      
REMARK 465     ARG C   234                                                      
REMARK 465     ALA C   235                                                      
REMARK 465     PRO C   236                                                      
REMARK 465     TRP C   237                                                      
REMARK 465     TRP C   238                                                      
REMARK 465     ASP C   239                                                      
REMARK 465     ALA C   240                                                      
REMARK 465     SER C   241                                                      
REMARK 465     PRO C   242                                                      
REMARK 465     GLY C   243                                                      
REMARK 465     VAL C   244                                                      
REMARK 465     GLN C   245                                                      
REMARK 465     ARG C   246                                                      
REMARK 465     LEU C   247                                                      
REMARK 465     ILE C   248                                                      
REMARK 465     THR C   249                                                      
REMARK 465     LEU C   250                                                      
REMARK 465     LYS C   251                                                      
REMARK 465     ILE C   313                                                      
REMARK 465     PRO C   314                                                      
REMARK 465     GLU C   315                                                      
REMARK 465     THR C   316                                                      
REMARK 465     ASN C   317                                                      
REMARK 465     THR C   318                                                      
REMARK 465     THR C   319                                                      
REMARK 465     GLN C   320                                                      
REMARK 465     GLU C   321                                                      
REMARK 465     MET C   322                                                      
REMARK 465     LEU C   323                                                      
REMARK 465     THR C   324                                                      
REMARK 465     THR C   325                                                      
REMARK 465     ARG C   326                                                      
REMARK 465     ARG C   327                                                      
REMARK 465     GLN C   328                                                      
REMARK 465     GLU C   329                                                      
REMARK 465     THR C   330                                                      
REMARK 465     GLU C   331                                                      
REMARK 465     GLY C   332                                                      
REMARK 465     PRO C   333                                                      
REMARK 465     GLU C   334                                                      
REMARK 465     PRO C   335                                                      
REMARK 465     ALA C   336                                                      
REMARK 465     GLU C   337                                                      
REMARK 465     PRO C   338                                                      
REMARK 465     GLN C   339                                                      
REMARK 465     ALA C   340                                                      
REMARK 465     THR C   341                                                      
REMARK 465     GLU C   342                                                      
REMARK 465     GLN C   343                                                      
REMARK 465     PRO C   344                                                      
REMARK 465     GLN C   345                                                      
REMARK 465     MET C   346                                                      
REMARK 465     VAL C   347                                                      
REMARK 465     SER C   348                                                      
REMARK 465     ALA C   349                                                      
REMARK 465     GLU C   350                                                      
REMARK 465     ALA C   351                                                      
REMARK 465     GLY C   352                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 509   C   -  N   -  CA  ANGL. DEV. =  14.4 DEGREES          
REMARK 500    PRO A 509   C   -  N   -  CD  ANGL. DEV. = -13.8 DEGREES          
REMARK 500    PRO B 356   C   -  N   -  CA  ANGL. DEV. =  10.5 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    ASP A 333     -101.09    104.50                                   
REMARK 500    GLU A 334      -29.44    130.37                                   
REMARK 500    GLN A 355     -165.08   -104.01                                   
REMARK 500    LEU A 358      -84.95    100.44                                   
REMARK 500    SER A 359      -67.59   -122.22                                   
REMARK 500    LEU A 388      117.39     73.56                                   
REMARK 500    LYS A 418      -70.26   -145.25                                   
REMARK 500    ASN A 445       -4.32    -51.54                                   
REMARK 500    GLU A 452      -34.05    -34.69                                   
REMARK 500    VAL A 480     -119.20   -107.27                                   
REMARK 500    LYS A 481      -95.93   -169.04                                   
REMARK 500    THR A 512      -57.31     68.50                                   
REMARK 500    LEU B 355      139.35   -170.44                                   
REMARK 500    GLU B 423      -77.39    109.45                                   
REMARK 500    TYR B 424       -7.00     76.67                                   
REMARK 500    ASN B 442      -43.80    122.22                                   
REMARK 500    SER B 443        3.72     83.32                                   
REMARK 500    LYS B 471     -123.27     43.39                                   
REMARK 500    PRO C 281        8.13    -64.46                                   
REMARK 500    LEU C 282      -57.38     75.74                                   
REMARK 500    SER C 291      -53.89   -128.70                                   
REMARK 500    MET C 420      -82.97   -151.87                                   
REMARK 500    ARG C 439      -35.00    -32.76                                   
REMARK 500    PHE C 440       63.96   -104.20                                   
REMARK 500    ASN C 442      -54.42     70.14                                   
REMARK 500    SER C 443       -3.79     79.18                                   
REMARK 500    ALA C 457        6.74     85.57                                   
REMARK 500    SER C 459      164.99     81.27                                   
REMARK 500    ASP C 461      -54.00   -126.89                                   
REMARK 500    ALA C 470      -70.80    -49.25                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3F5C A  313   560  UNP    P45448   NR5A2_MOUSE    313    560             
DBREF  3F5C B  205   472  UNP    Q61066   NR0B1_MOUSE    205    472             
DBREF  3F5C C  205   472  UNP    Q61066   NR0B1_MOUSE    205    472             
SEQADV 3F5C LEU A  525  UNP  P45448    ILE   525 ENGINEERED                     
SEQRES   1 A  248  GLN THR ASN SER PRO ALA SER ILE PRO HIS LEU ILE LEU          
SEQRES   2 A  248  GLU LEU LEU LYS CYS GLU PRO ASP GLU PRO GLN VAL GLN          
SEQRES   3 A  248  ALA LYS ILE MET ALA TYR LEU GLN GLN GLU GLN SER ASN          
SEQRES   4 A  248  ARG ASN ARG GLN GLU LYS LEU SER ALA PHE GLY LEU LEU          
SEQRES   5 A  248  CYS LYS MET ALA ASP GLN THR LEU PHE SER ILE VAL GLU          
SEQRES   6 A  248  TRP ALA ARG SER SER ILE PHE PHE ARG GLU LEU LYS VAL          
SEQRES   7 A  248  ASP ASP GLN MET LYS LEU LEU GLN ASN CYS TRP SER GLU          
SEQRES   8 A  248  LEU LEU ILE LEU ASP HIS ILE TYR ARG GLN VAL ALA HIS          
SEQRES   9 A  248  GLY LYS GLU GLY THR ILE PHE LEU VAL THR GLY GLU HIS          
SEQRES  10 A  248  VAL ASP TYR SER THR ILE ILE SER HIS THR GLU VAL ALA          
SEQRES  11 A  248  PHE ASN ASN LEU LEU SER LEU ALA GLN GLU LEU VAL VAL          
SEQRES  12 A  248  ARG LEU ARG SER LEU GLN PHE ASP GLN ARG GLU PHE VAL          
SEQRES  13 A  248  CYS LEU LYS PHE LEU VAL LEU PHE SER SER ASP VAL LYS          
SEQRES  14 A  248  ASN LEU GLU ASN LEU GLN LEU VAL GLU GLY VAL GLN GLU          
SEQRES  15 A  248  GLN VAL ASN ALA ALA LEU LEU ASP TYR THR VAL CYS ASN          
SEQRES  16 A  248  TYR PRO GLN GLN THR GLU LYS PHE GLY GLN LEU LEU LEU          
SEQRES  17 A  248  ARG LEU PRO GLU LEU ARG ALA ILE SER LYS GLN ALA GLU          
SEQRES  18 A  248  ASP TYR LEU TYR TYR LYS HIS VAL ASN GLY ASP VAL PRO          
SEQRES  19 A  248  TYR ASN ASN LEU LEU ILE GLU MET LEU HIS ALA LYS ARG          
SEQRES  20 A  248  ALA                                                          
SEQRES   1 B  268  GLY GLU GLU GLN PRO GLN GLN ILE SER VAL ALA SER GLY          
SEQRES   2 B  268  THR PRO VAL SER ALA ASP GLN THR PRO ALA THR PRO GLN          
SEQRES   3 B  268  GLU GLN PRO ARG ALA PRO TRP TRP ASP ALA SER PRO GLY          
SEQRES   4 B  268  VAL GLN ARG LEU ILE THR LEU LYS ASP PRO GLN VAL VAL          
SEQRES   5 B  268  CYS GLU ALA ALA SER ALA GLY LEU LEU LYS THR LEU ARG          
SEQRES   6 B  268  PHE VAL LYS TYR LEU PRO CYS PHE GLN ILE LEU PRO LEU          
SEQRES   7 B  268  ASP GLN GLN LEU VAL LEU VAL ARG SER CYS TRP ALA PRO          
SEQRES   8 B  268  LEU LEU MET LEU GLU LEU ALA GLN ASP HIS LEU HIS PHE          
SEQRES   9 B  268  GLU MET MET GLU ILE PRO GLU THR ASN THR THR GLN GLU          
SEQRES  10 B  268  MET LEU THR THR ARG ARG GLN GLU THR GLU GLY PRO GLU          
SEQRES  11 B  268  PRO ALA GLU PRO GLN ALA THR GLU GLN PRO GLN MET VAL          
SEQRES  12 B  268  SER ALA GLU ALA GLY HIS LEU LEU PRO ALA ALA ALA VAL          
SEQRES  13 B  268  GLN ALA ILE LYS SER PHE PHE PHE LYS CYS TRP SER LEU          
SEQRES  14 B  268  ASN ILE ASP THR LYS GLU TYR ALA TYR LEU LYS GLY THR          
SEQRES  15 B  268  VAL LEU PHE ASN PRO ASP LEU PRO GLY LEU GLN CYS VAL          
SEQRES  16 B  268  LYS TYR ILE GLU GLY LEU GLN TRP ARG THR GLN GLN ILE          
SEQRES  17 B  268  LEU THR GLU HIS ILE ARG MET MET GLN ARG GLU TYR GLN          
SEQRES  18 B  268  ILE ARG SER ALA GLU LEU ASN SER ALA LEU PHE LEU LEU          
SEQRES  19 B  268  ARG PHE ILE ASN SER ASP VAL VAL THR GLU LEU PHE PHE          
SEQRES  20 B  268  ARG PRO ILE ILE GLY ALA VAL SER MET ASP ASP MET MET          
SEQRES  21 B  268  LEU GLU MET LEU CYS ALA LYS LEU                              
SEQRES   1 C  268  GLY GLU GLU GLN PRO GLN GLN ILE SER VAL ALA SER GLY          
SEQRES   2 C  268  THR PRO VAL SER ALA ASP GLN THR PRO ALA THR PRO GLN          
SEQRES   3 C  268  GLU GLN PRO ARG ALA PRO TRP TRP ASP ALA SER PRO GLY          
SEQRES   4 C  268  VAL GLN ARG LEU ILE THR LEU LYS ASP PRO GLN VAL VAL          
SEQRES   5 C  268  CYS GLU ALA ALA SER ALA GLY LEU LEU LYS THR LEU ARG          
SEQRES   6 C  268  PHE VAL LYS TYR LEU PRO CYS PHE GLN ILE LEU PRO LEU          
SEQRES   7 C  268  ASP GLN GLN LEU VAL LEU VAL ARG SER CYS TRP ALA PRO          
SEQRES   8 C  268  LEU LEU MET LEU GLU LEU ALA GLN ASP HIS LEU HIS PHE          
SEQRES   9 C  268  GLU MET MET GLU ILE PRO GLU THR ASN THR THR GLN GLU          
SEQRES  10 C  268  MET LEU THR THR ARG ARG GLN GLU THR GLU GLY PRO GLU          
SEQRES  11 C  268  PRO ALA GLU PRO GLN ALA THR GLU GLN PRO GLN MET VAL          
SEQRES  12 C  268  SER ALA GLU ALA GLY HIS LEU LEU PRO ALA ALA ALA VAL          
SEQRES  13 C  268  GLN ALA ILE LYS SER PHE PHE PHE LYS CYS TRP SER LEU          
SEQRES  14 C  268  ASN ILE ASP THR LYS GLU TYR ALA TYR LEU LYS GLY THR          
SEQRES  15 C  268  VAL LEU PHE ASN PRO ASP LEU PRO GLY LEU GLN CYS VAL          
SEQRES  16 C  268  LYS TYR ILE GLU GLY LEU GLN TRP ARG THR GLN GLN ILE          
SEQRES  17 C  268  LEU THR GLU HIS ILE ARG MET MET GLN ARG GLU TYR GLN          
SEQRES  18 C  268  ILE ARG SER ALA GLU LEU ASN SER ALA LEU PHE LEU LEU          
SEQRES  19 C  268  ARG PHE ILE ASN SER ASP VAL VAL THR GLU LEU PHE PHE          
SEQRES  20 C  268  ARG PRO ILE ILE GLY ALA VAL SER MET ASP ASP MET MET          
SEQRES  21 C  268  LEU GLU MET LEU CYS ALA LYS LEU                              
HELIX    1   1 PRO A  321  LEU A  328  1                                   8    
HELIX    2   2 LYS A  329  GLU A  331  5                                   3    
HELIX    3   3 PRO A  335  ASN A  351  1                                  17    
HELIX    4   4 ALA A  360  SER A  381  1                                  22    
HELIX    5   5 SER A  382  GLU A  387  1                                   6    
HELIX    6   6 LYS A  389  HIS A  416  1                                  28    
HELIX    7   7 TYR A  432  THR A  439  1                                   8    
HELIX    8   8 GLU A  440  SER A  459  1                                  20    
HELIX    9   9 ASP A  463  PHE A  476  1                                  14    
HELIX   10  10 ASN A  485  ASN A  507  1                                  23    
HELIX   11  11 GLU A  513  LEU A  519  1                                   7    
HELIX   12  12 LEU A  522  VAL A  541  1                                  20    
HELIX   13  13 ASN A  549  ALA A  560  1                                  12    
HELIX   14  14 ASP B  252  TYR B  273  1                                  22    
HELIX   15  15 LEU B  274  ILE B  279  1                                   6    
HELIX   16  16 PRO B  281  ASP B  304  1                                  24    
HELIX   17  17 ALA B  358  LEU B  373  1                                  16    
HELIX   18  18 ASP B  376  PHE B  389  1                                  14    
HELIX   19  19 CYS B  398  GLN B  421  1                                  24    
HELIX   20  20 GLN B  425  ARG B  439  1                                  15    
HELIX   21  21 ASP B  444  PHE B  451  1                                   8    
HELIX   22  22 PHE B  451  GLY B  456  1                                   6    
HELIX   23  23 SER B  459  LEU B  468  1                                  10    
HELIX   24  24 ASP C  252  TYR C  273  1                                  22    
HELIX   25  25 LEU C  274  ILE C  279  1                                   6    
HELIX   26  26 LEU C  282  ASP C  304  1                                  23    
HELIX   27  27 PRO C  356  LEU C  373  1                                  18    
HELIX   28  28 ASP C  376  PHE C  389  1                                  14    
HELIX   29  29 CYS C  398  MET C  419  1                                  22    
HELIX   30  30 GLU C  423  ARG C  439  1                                  17    
HELIX   31  31 SER C  443  PHE C  451  1                                   9    
HELIX   32  32 PHE C  451  GLY C  456  1                                   6    
HELIX   33  33 ASP C  461  LYS C  471  1                                  11    
SHEET    1   A 2 THR A 421  PHE A 423  0                                        
SHEET    2   A 2 HIS A 429  ASP A 431 -1  O  VAL A 430   N  ILE A 422           
CISPEP   1 LEU A  358    SER A  359          0        -2.71                     
CRYST1  103.355  103.355  117.455  90.00  90.00  90.00 P 43          8          
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      0.009675  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009675  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008514        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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