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Database: PDB
Entry: 4B7W
LinkDB: 4B7W
Original site: 4B7W 
HEADER    RECEPTOR                                24-AUG-12   4B7W              
TITLE     LIGAND BINDING DOMAIN HUMAN HEPATOCYTE NUCLEAR FACTOR 4ALPHA: APO     
TITLE    2 FORM                                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEPATOCYTE NUCLEAR FACTOR 4-ALPHA;                         
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: LIGAND BINDING DOMAIN, RESIDUES 142-377;                   
COMPND   5 SYNONYM: HNF-4-ALPHA, NUCLEAR RECEPTOR SUBFAMILY 2 GROUP A MEMBER    
COMPND   6  1, TRANSCRIPTION FACTOR 14, TCF-14, TRANSCRIPTION FACTOR HNF-4;     
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PETM11                                     
KEYWDS    RECEPTOR, NUCLEAR RECEPTOR                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.DUDASOVA,M.OKVIST,M.KRETOVA,G.ONDROVICOVA,R.SKRABANA,R.LEGUEVEL,    
AUTHOR   2 G.SALBERT,G.LEONARD,S.MCSWEENEY,P.BARATH                             
REVDAT   1   11-SEP-13 4B7W    0                                                
JRNL        AUTH   Z.DUDASOVA,M.OKVIST,M.KRETOVA,G.ONDROVICOVA,R.SKRABANA,      
JRNL        AUTH 2 R.LEGUEVEL,G.SALBERT,G.LEONARD,S.MCSWEENEY,P.BARATH          
JRNL        TITL   FATTY ACIDS ARE NOT ESSENTIAL STRUCTURAL COMPONENTS OF       
JRNL        TITL 2 HEPATOCYTE NUCLEAR FACTOR 4ALPHA                             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 4.0                            
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.0                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 85.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 7987                           
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) : 0.2496                          
REMARK   3   FREE R VALUE                     : 0.2798                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 374                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 4.0                          
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 4.14                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 73.2                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 620                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.362                        
REMARK   3   BIN FREE R VALUE                    : 0.353                        
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.0                          
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 35                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6476                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
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) : -40.406                                              
REMARK   3    B22 (A**2) : -10.376                                              
REMARK   3    B33 (A**2) : 50.781                                               
REMARK   3    B12 (A**2) : 0.000                                                
REMARK   3    B13 (A**2) : 0.000                                                
REMARK   3    B23 (A**2) : 0.000                                                
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.002477                        
REMARK   3   BOND ANGLES            (DEGREES) : 0.65528                         
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) :  NULL ;  NULL                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) :  NULL ;  NULL                
REMARK   3   SIDE-CHAIN BOND              (A**2) :  NULL ;  NULL                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) :  NULL ;  NULL                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : 0.3                                                  
REMARK   3   BSOL        : 111.407                                              
REMARK   3                                                                      
REMARK   3  NCS MODEL : RESTRAINTS                                              
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  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: STRUCTURE REFINEMENT WAS CARRIED          
REMARK   3    OUT USING THE CNS-DEN METHODOLOGY. SEE SCHRODER, G. F.,           
REMARK   3    LEVITT, M. & BRUNGER, A. T. 2010. SUPER-RESOLUTION                
REMARK   3    BIOMOLECULAR CRYSTALLOGRAPHY WITH LOW-RESOLUTION DATA.            
REMARK   3    NATURE 464, 1218-1222.                                            
REMARK   4                                                                      
REMARK   4 4B7W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-AUG-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-53064.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-APR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.873                              
REMARK 200  MONOCHROMATOR                  : SI (111)                           
REMARK 200  OPTICS                         : KB MIRRORS                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (MAR225)                       
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 8011                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 4.00                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.70                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.5                               
REMARK 200  DATA REDUNDANCY                : 4.6                                
REMARK 200  R MERGE                    (I) : 0.16                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.10                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.24                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.6                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.81                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.80                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1LV2                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.6                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.7 M AMMONIUM ACETATE, 0.1 M            
REMARK 280  SODIUM CITRATE, 10 MM DTT, 16% MPD IN 0.1 M TRIS, PH 8.0            
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       50.52400            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.64100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       50.52400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.64100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: OCTAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 20960 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 73520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -124.4 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   139                                                      
REMARK 465     ALA A   140                                                      
REMARK 465     MET A   141                                                      
REMARK 465     SER A   142                                                      
REMARK 465     SER A   143                                                      
REMARK 465     TYR A   144                                                      
REMARK 465     GLU A   145                                                      
REMARK 465     ASP A   146                                                      
REMARK 465     SER A   147                                                      
REMARK 465     SER A   148                                                      
REMARK 465     LEU A   149                                                      
REMARK 465     PRO A   150                                                      
REMARK 465     SER A   151                                                      
REMARK 465     ILE A   152                                                      
REMARK 465     ASN A   153                                                      
REMARK 465     ALA A   154                                                      
REMARK 465     LEU A   155                                                      
REMARK 465     LEU A   156                                                      
REMARK 465     GLN A   157                                                      
REMARK 465     ALA A   158                                                      
REMARK 465     GLU A   159                                                      
REMARK 465     VAL A   160                                                      
REMARK 465     LEU A   161                                                      
REMARK 465     SER A   162                                                      
REMARK 465     ARG A   163                                                      
REMARK 465     GLN A   164                                                      
REMARK 465     ILE A   165                                                      
REMARK 465     THR A   166                                                      
REMARK 465     SER A   167                                                      
REMARK 465     PRO A   168                                                      
REMARK 465     VAL A   169                                                      
REMARK 465     SER A   170                                                      
REMARK 465     GLY A   171                                                      
REMARK 465     ILE A   172                                                      
REMARK 465     ASN A   173                                                      
REMARK 465     GLY A   174                                                      
REMARK 465     GLY A   377                                                      
REMARK 465     GLY B   139                                                      
REMARK 465     ALA B   140                                                      
REMARK 465     MET B   141                                                      
REMARK 465     SER B   142                                                      
REMARK 465     SER B   143                                                      
REMARK 465     TYR B   144                                                      
REMARK 465     GLU B   145                                                      
REMARK 465     ASP B   146                                                      
REMARK 465     SER B   147                                                      
REMARK 465     SER B   148                                                      
REMARK 465     LEU B   149                                                      
REMARK 465     PRO B   150                                                      
REMARK 465     SER B   151                                                      
REMARK 465     ILE B   152                                                      
REMARK 465     ASN B   153                                                      
REMARK 465     ALA B   154                                                      
REMARK 465     LEU B   155                                                      
REMARK 465     LEU B   156                                                      
REMARK 465     GLN B   157                                                      
REMARK 465     ALA B   158                                                      
REMARK 465     GLU B   159                                                      
REMARK 465     VAL B   160                                                      
REMARK 465     LEU B   161                                                      
REMARK 465     SER B   162                                                      
REMARK 465     ARG B   163                                                      
REMARK 465     GLN B   164                                                      
REMARK 465     ILE B   165                                                      
REMARK 465     THR B   166                                                      
REMARK 465     SER B   167                                                      
REMARK 465     PRO B   168                                                      
REMARK 465     VAL B   169                                                      
REMARK 465     SER B   170                                                      
REMARK 465     GLY B   171                                                      
REMARK 465     ILE B   172                                                      
REMARK 465     ASN B   173                                                      
REMARK 465     GLY B   174                                                      
REMARK 465     ASP B   175                                                      
REMARK 465     ILE B   176                                                      
REMARK 465     GLY B   377                                                      
REMARK 465     GLY C   139                                                      
REMARK 465     ALA C   140                                                      
REMARK 465     MET C   141                                                      
REMARK 465     SER C   142                                                      
REMARK 465     SER C   143                                                      
REMARK 465     TYR C   144                                                      
REMARK 465     GLU C   145                                                      
REMARK 465     ASP C   146                                                      
REMARK 465     SER C   147                                                      
REMARK 465     SER C   148                                                      
REMARK 465     LEU C   149                                                      
REMARK 465     PRO C   150                                                      
REMARK 465     SER C   151                                                      
REMARK 465     ILE C   152                                                      
REMARK 465     ASN C   153                                                      
REMARK 465     ALA C   154                                                      
REMARK 465     LEU C   155                                                      
REMARK 465     LEU C   156                                                      
REMARK 465     GLN C   157                                                      
REMARK 465     ALA C   158                                                      
REMARK 465     GLU C   159                                                      
REMARK 465     VAL C   160                                                      
REMARK 465     LEU C   161                                                      
REMARK 465     SER C   162                                                      
REMARK 465     ARG C   163                                                      
REMARK 465     GLN C   164                                                      
REMARK 465     ILE C   165                                                      
REMARK 465     THR C   166                                                      
REMARK 465     SER C   167                                                      
REMARK 465     PRO C   168                                                      
REMARK 465     VAL C   169                                                      
REMARK 465     SER C   170                                                      
REMARK 465     GLY C   171                                                      
REMARK 465     ILE C   172                                                      
REMARK 465     ASN C   173                                                      
REMARK 465     GLY C   174                                                      
REMARK 465     GLY C   377                                                      
REMARK 465     GLY D   139                                                      
REMARK 465     ALA D   140                                                      
REMARK 465     MET D   141                                                      
REMARK 465     SER D   142                                                      
REMARK 465     SER D   143                                                      
REMARK 465     TYR D   144                                                      
REMARK 465     GLU D   145                                                      
REMARK 465     ASP D   146                                                      
REMARK 465     SER D   147                                                      
REMARK 465     SER D   148                                                      
REMARK 465     LEU D   149                                                      
REMARK 465     PRO D   150                                                      
REMARK 465     SER D   151                                                      
REMARK 465     ILE D   152                                                      
REMARK 465     ASN D   153                                                      
REMARK 465     ALA D   154                                                      
REMARK 465     LEU D   155                                                      
REMARK 465     LEU D   156                                                      
REMARK 465     GLN D   157                                                      
REMARK 465     ALA D   158                                                      
REMARK 465     GLU D   159                                                      
REMARK 465     VAL D   160                                                      
REMARK 465     LEU D   161                                                      
REMARK 465     SER D   162                                                      
REMARK 465     ARG D   163                                                      
REMARK 465     GLN D   164                                                      
REMARK 465     ILE D   165                                                      
REMARK 465     THR D   166                                                      
REMARK 465     SER D   167                                                      
REMARK 465     PRO D   168                                                      
REMARK 465     VAL D   169                                                      
REMARK 465     SER D   170                                                      
REMARK 465     GLY D   171                                                      
REMARK 465     ILE D   172                                                      
REMARK 465     ASN D   173                                                      
REMARK 465     GLY D   174                                                      
REMARK 465     ASP D   175                                                      
REMARK 465     ILE D   176                                                      
REMARK 465     GLY D   377                                                      
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    ILE A 176      -10.38   -143.27                                   
REMARK 500    ARG A 177      -72.68   -112.46                                   
REMARK 500    LYS A 180     -178.78     59.80                                   
REMARK 500    ALA A 222      -78.24    -95.98                                   
REMARK 500    ASN A 247       59.76   -162.04                                   
REMARK 500    ASP A 248     -148.92     60.43                                   
REMARK 500    TYR A 249       86.86     56.41                                   
REMARK 500    PRO A 252      164.38    -49.27                                   
REMARK 500    GLU A 257       28.03    -79.21                                   
REMARK 500    LEU A 258       55.97   -159.77                                   
REMARK 500    GLU A 260      -13.70     67.26                                   
REMARK 500    LEU A 272      -52.73   -136.05                                   
REMARK 500    ARG A 326       53.91   -169.70                                   
REMARK 500    GLN A 327      179.74     61.08                                   
REMARK 500    TYR A 328     -177.37     59.56                                   
REMARK 500    MET A 373      -44.77   -141.25                                   
REMARK 500    LYS B 179      -14.07     65.06                                   
REMARK 500    LYS B 180      142.83     65.26                                   
REMARK 500    SER B 236       19.20   -150.78                                   
REMARK 500    ASP B 248     -140.75     62.61                                   
REMARK 500    TYR B 249       83.08     54.33                                   
REMARK 500    PRO B 252      159.93    -45.26                                   
REMARK 500    GLU B 257       22.36    -70.62                                   
REMARK 500    LEU B 258       36.56   -150.78                                   
REMARK 500    GLU B 260       18.00     56.05                                   
REMARK 500    MET B 261      -11.90   -156.53                                   
REMARK 500    LEU B 272      -59.89   -144.48                                   
REMARK 500    GLN B 280       70.79     50.94                                   
REMARK 500    ASP B 282     -160.01    -77.53                                   
REMARK 500    ASP B 329      179.59     59.26                                   
REMARK 500    SER B 330        7.74   -175.83                                   
REMARK 500    MET B 363      -78.73    -48.45                                   
REMARK 500    ILE C 176      -10.07   -143.61                                   
REMARK 500    ARG C 177      -72.43   -112.74                                   
REMARK 500    LYS C 180     -179.13     58.95                                   
REMARK 500    ALA C 222      -78.53    -95.77                                   
REMARK 500    ASN C 247       59.60   -162.44                                   
REMARK 500    ASP C 248     -149.05     60.65                                   
REMARK 500    TYR C 249       86.53     56.53                                   
REMARK 500    PRO C 252      164.73    -49.24                                   
REMARK 500    GLU C 257       28.19    -79.16                                   
REMARK 500    LEU C 258       55.95   -159.82                                   
REMARK 500    GLU C 260      -13.79     67.03                                   
REMARK 500    LEU C 272      -52.84   -136.11                                   
REMARK 500    ARG C 326       53.69   -169.64                                   
REMARK 500    GLN C 327      179.59     61.16                                   
REMARK 500    TYR C 328     -177.25     59.82                                   
REMARK 500    MET C 373      -44.65   -141.28                                   
REMARK 500    LYS D 179      -14.15     64.84                                   
REMARK 500    LYS D 180      143.00     65.76                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      64 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1PZL   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HNF4A LBD IN COMPLEX WITH THE                  
REMARK 900  LIGANDAND THE COACTIVATOR SRC-1 PEPTIDE                             
DBREF  4B7W A  142   377  UNP    P41235   HNF4A_HUMAN    142    377             
DBREF  4B7W B  142   377  UNP    P41235   HNF4A_HUMAN    142    377             
DBREF  4B7W C  142   377  UNP    P41235   HNF4A_HUMAN    142    377             
DBREF  4B7W D  142   377  UNP    P41235   HNF4A_HUMAN    142    377             
SEQADV 4B7W GLY A  139  UNP  P41235              EXPRESSION TAG                 
SEQADV 4B7W ALA A  140  UNP  P41235              EXPRESSION TAG                 
SEQADV 4B7W MET A  141  UNP  P41235              EXPRESSION TAG                 
SEQADV 4B7W GLY B  139  UNP  P41235              EXPRESSION TAG                 
SEQADV 4B7W ALA B  140  UNP  P41235              EXPRESSION TAG                 
SEQADV 4B7W MET B  141  UNP  P41235              EXPRESSION TAG                 
SEQADV 4B7W GLY C  139  UNP  P41235              EXPRESSION TAG                 
SEQADV 4B7W ALA C  140  UNP  P41235              EXPRESSION TAG                 
SEQADV 4B7W MET C  141  UNP  P41235              EXPRESSION TAG                 
SEQADV 4B7W GLY D  139  UNP  P41235              EXPRESSION TAG                 
SEQADV 4B7W ALA D  140  UNP  P41235              EXPRESSION TAG                 
SEQADV 4B7W MET D  141  UNP  P41235              EXPRESSION TAG                 
SEQRES   1 A  239  GLY ALA MET SER SER TYR GLU ASP SER SER LEU PRO SER          
SEQRES   2 A  239  ILE ASN ALA LEU LEU GLN ALA GLU VAL LEU SER ARG GLN          
SEQRES   3 A  239  ILE THR SER PRO VAL SER GLY ILE ASN GLY ASP ILE ARG          
SEQRES   4 A  239  ALA LYS LYS ILE ALA SER ILE ALA ASP VAL CYS GLU SER          
SEQRES   5 A  239  MET LYS GLU GLN LEU LEU VAL LEU VAL GLU TRP ALA LYS          
SEQRES   6 A  239  TYR ILE PRO ALA PHE CYS GLU LEU PRO LEU ASP ASP GLN          
SEQRES   7 A  239  VAL ALA LEU LEU ARG ALA HIS ALA GLY GLU HIS LEU LEU          
SEQRES   8 A  239  LEU GLY ALA THR LYS ARG SER MET VAL PHE LYS ASP VAL          
SEQRES   9 A  239  LEU LEU LEU GLY ASN ASP TYR ILE VAL PRO ARG HIS CYS          
SEQRES  10 A  239  PRO GLU LEU ALA GLU MET SER ARG VAL SER ILE ARG ILE          
SEQRES  11 A  239  LEU ASP GLU LEU VAL LEU PRO PHE GLN GLU LEU GLN ILE          
SEQRES  12 A  239  ASP ASP ASN GLU TYR ALA TYR LEU LYS ALA ILE ILE PHE          
SEQRES  13 A  239  PHE ASP PRO ASP ALA LYS GLY LEU SER ASP PRO GLY LYS          
SEQRES  14 A  239  ILE LYS ARG LEU ARG SER GLN VAL GLN VAL SER LEU GLU          
SEQRES  15 A  239  ASP TYR ILE ASN ASP ARG GLN TYR ASP SER ARG GLY ARG          
SEQRES  16 A  239  PHE GLY GLU LEU LEU LEU LEU LEU PRO THR LEU GLN SER          
SEQRES  17 A  239  ILE THR TRP GLN MET ILE GLU GLN ILE GLN PHE ILE LYS          
SEQRES  18 A  239  LEU PHE GLY MET ALA LYS ILE ASP ASN LEU LEU GLN GLU          
SEQRES  19 A  239  MET LEU LEU GLY GLY                                          
SEQRES   1 B  239  GLY ALA MET SER SER TYR GLU ASP SER SER LEU PRO SER          
SEQRES   2 B  239  ILE ASN ALA LEU LEU GLN ALA GLU VAL LEU SER ARG GLN          
SEQRES   3 B  239  ILE THR SER PRO VAL SER GLY ILE ASN GLY ASP ILE ARG          
SEQRES   4 B  239  ALA LYS LYS ILE ALA SER ILE ALA ASP VAL CYS GLU SER          
SEQRES   5 B  239  MET LYS GLU GLN LEU LEU VAL LEU VAL GLU TRP ALA LYS          
SEQRES   6 B  239  TYR ILE PRO ALA PHE CYS GLU LEU PRO LEU ASP ASP GLN          
SEQRES   7 B  239  VAL ALA LEU LEU ARG ALA HIS ALA GLY GLU HIS LEU LEU          
SEQRES   8 B  239  LEU GLY ALA THR LYS ARG SER MET VAL PHE LYS ASP VAL          
SEQRES   9 B  239  LEU LEU LEU GLY ASN ASP TYR ILE VAL PRO ARG HIS CYS          
SEQRES  10 B  239  PRO GLU LEU ALA GLU MET SER ARG VAL SER ILE ARG ILE          
SEQRES  11 B  239  LEU ASP GLU LEU VAL LEU PRO PHE GLN GLU LEU GLN ILE          
SEQRES  12 B  239  ASP ASP ASN GLU TYR ALA TYR LEU LYS ALA ILE ILE PHE          
SEQRES  13 B  239  PHE ASP PRO ASP ALA LYS GLY LEU SER ASP PRO GLY LYS          
SEQRES  14 B  239  ILE LYS ARG LEU ARG SER GLN VAL GLN VAL SER LEU GLU          
SEQRES  15 B  239  ASP TYR ILE ASN ASP ARG GLN TYR ASP SER ARG GLY ARG          
SEQRES  16 B  239  PHE GLY GLU LEU LEU LEU LEU LEU PRO THR LEU GLN SER          
SEQRES  17 B  239  ILE THR TRP GLN MET ILE GLU GLN ILE GLN PHE ILE LYS          
SEQRES  18 B  239  LEU PHE GLY MET ALA LYS ILE ASP ASN LEU LEU GLN GLU          
SEQRES  19 B  239  MET LEU LEU GLY GLY                                          
SEQRES   1 C  239  GLY ALA MET SER SER TYR GLU ASP SER SER LEU PRO SER          
SEQRES   2 C  239  ILE ASN ALA LEU LEU GLN ALA GLU VAL LEU SER ARG GLN          
SEQRES   3 C  239  ILE THR SER PRO VAL SER GLY ILE ASN GLY ASP ILE ARG          
SEQRES   4 C  239  ALA LYS LYS ILE ALA SER ILE ALA ASP VAL CYS GLU SER          
SEQRES   5 C  239  MET LYS GLU GLN LEU LEU VAL LEU VAL GLU TRP ALA LYS          
SEQRES   6 C  239  TYR ILE PRO ALA PHE CYS GLU LEU PRO LEU ASP ASP GLN          
SEQRES   7 C  239  VAL ALA LEU LEU ARG ALA HIS ALA GLY GLU HIS LEU LEU          
SEQRES   8 C  239  LEU GLY ALA THR LYS ARG SER MET VAL PHE LYS ASP VAL          
SEQRES   9 C  239  LEU LEU LEU GLY ASN ASP TYR ILE VAL PRO ARG HIS CYS          
SEQRES  10 C  239  PRO GLU LEU ALA GLU MET SER ARG VAL SER ILE ARG ILE          
SEQRES  11 C  239  LEU ASP GLU LEU VAL LEU PRO PHE GLN GLU LEU GLN ILE          
SEQRES  12 C  239  ASP ASP ASN GLU TYR ALA TYR LEU LYS ALA ILE ILE PHE          
SEQRES  13 C  239  PHE ASP PRO ASP ALA LYS GLY LEU SER ASP PRO GLY LYS          
SEQRES  14 C  239  ILE LYS ARG LEU ARG SER GLN VAL GLN VAL SER LEU GLU          
SEQRES  15 C  239  ASP TYR ILE ASN ASP ARG GLN TYR ASP SER ARG GLY ARG          
SEQRES  16 C  239  PHE GLY GLU LEU LEU LEU LEU LEU PRO THR LEU GLN SER          
SEQRES  17 C  239  ILE THR TRP GLN MET ILE GLU GLN ILE GLN PHE ILE LYS          
SEQRES  18 C  239  LEU PHE GLY MET ALA LYS ILE ASP ASN LEU LEU GLN GLU          
SEQRES  19 C  239  MET LEU LEU GLY GLY                                          
SEQRES   1 D  239  GLY ALA MET SER SER TYR GLU ASP SER SER LEU PRO SER          
SEQRES   2 D  239  ILE ASN ALA LEU LEU GLN ALA GLU VAL LEU SER ARG GLN          
SEQRES   3 D  239  ILE THR SER PRO VAL SER GLY ILE ASN GLY ASP ILE ARG          
SEQRES   4 D  239  ALA LYS LYS ILE ALA SER ILE ALA ASP VAL CYS GLU SER          
SEQRES   5 D  239  MET LYS GLU GLN LEU LEU VAL LEU VAL GLU TRP ALA LYS          
SEQRES   6 D  239  TYR ILE PRO ALA PHE CYS GLU LEU PRO LEU ASP ASP GLN          
SEQRES   7 D  239  VAL ALA LEU LEU ARG ALA HIS ALA GLY GLU HIS LEU LEU          
SEQRES   8 D  239  LEU GLY ALA THR LYS ARG SER MET VAL PHE LYS ASP VAL          
SEQRES   9 D  239  LEU LEU LEU GLY ASN ASP TYR ILE VAL PRO ARG HIS CYS          
SEQRES  10 D  239  PRO GLU LEU ALA GLU MET SER ARG VAL SER ILE ARG ILE          
SEQRES  11 D  239  LEU ASP GLU LEU VAL LEU PRO PHE GLN GLU LEU GLN ILE          
SEQRES  12 D  239  ASP ASP ASN GLU TYR ALA TYR LEU LYS ALA ILE ILE PHE          
SEQRES  13 D  239  PHE ASP PRO ASP ALA LYS GLY LEU SER ASP PRO GLY LYS          
SEQRES  14 D  239  ILE LYS ARG LEU ARG SER GLN VAL GLN VAL SER LEU GLU          
SEQRES  15 D  239  ASP TYR ILE ASN ASP ARG GLN TYR ASP SER ARG GLY ARG          
SEQRES  16 D  239  PHE GLY GLU LEU LEU LEU LEU LEU PRO THR LEU GLN SER          
SEQRES  17 D  239  ILE THR TRP GLN MET ILE GLU GLN ILE GLN PHE ILE LYS          
SEQRES  18 D  239  LEU PHE GLY MET ALA LYS ILE ASP ASN LEU LEU GLN GLU          
SEQRES  19 D  239  MET LEU LEU GLY GLY                                          
HELIX    1   1 ALA A  185  LEU A  198  1                                  14    
HELIX    2   2 LEU A  198  LYS A  203  1                                   6    
HELIX    3   3 ILE A  205  GLU A  210  1                                   6    
HELIX    4   4 PRO A  212  VAL A  217  1                                   6    
HELIX    5   5 HIS A  223  ARG A  235  1                                  13    
HELIX    6   6 CYS A  255  ALA A  259  5                                   5    
HELIX    7   7 MET A  261  LEU A  272  1                                  12    
HELIX    8   8 LEU A  272  LEU A  279  1                                   8    
HELIX    9   9 ASP A  282  ILE A  293  1                                  12    
HELIX   10  10 ASP A  304  ASP A  325  1                                  22    
HELIX   11  11 GLY A  332  LEU A  339  1                                   8    
HELIX   12  12 LEU A  340  PHE A  361  1                                  22    
HELIX   13  13 ASP A  367  GLU A  372  1                                   6    
HELIX   14  14 SER B  183  GLN B  194  1                                  12    
HELIX   15  15 LEU B  195  TYR B  204  1                                  10    
HELIX   16  16 ILE B  205  GLU B  210  1                                   6    
HELIX   17  17 PRO B  212  ARG B  221  1                                  10    
HELIX   18  18 HIS B  223  ARG B  235  1                                  13    
HELIX   19  19 CYS B  255  ALA B  259  5                                   5    
HELIX   20  20 MET B  261  LEU B  272  1                                  12    
HELIX   21  21 LEU B  272  GLN B  280  1                                   9    
HELIX   22  22 ASP B  283  PHE B  295  1                                  13    
HELIX   23  23 ASP B  304  ASN B  324  1                                  21    
HELIX   24  24 PHE B  334  LEU B  339  1                                   6    
HELIX   25  25 LEU B  340  LEU B  375  1                                  36    
HELIX   26  26 ALA C  185  LEU C  198  1                                  14    
HELIX   27  27 LEU C  198  LYS C  203  1                                   6    
HELIX   28  28 ILE C  205  GLU C  210  1                                   6    
HELIX   29  29 PRO C  212  VAL C  217  1                                   6    
HELIX   30  30 HIS C  223  ARG C  235  1                                  13    
HELIX   31  31 CYS C  255  ALA C  259  5                                   5    
HELIX   32  32 MET C  261  LEU C  272  1                                  12    
HELIX   33  33 LEU C  272  LEU C  279  1                                   8    
HELIX   34  34 ASP C  282  ILE C  293  1                                  12    
HELIX   35  35 ASP C  304  ASP C  325  1                                  22    
HELIX   36  36 GLY C  332  LEU C  339  1                                   8    
HELIX   37  37 LEU C  340  PHE C  361  1                                  22    
HELIX   38  38 ASP C  367  GLU C  372  1                                   6    
HELIX   39  39 SER D  183  GLN D  194  1                                  12    
HELIX   40  40 LEU D  195  TYR D  204  1                                  10    
HELIX   41  41 ILE D  205  GLU D  210  1                                   6    
HELIX   42  42 PRO D  212  ARG D  221  1                                  10    
HELIX   43  43 HIS D  223  ARG D  235  1                                  13    
HELIX   44  44 CYS D  255  ALA D  259  5                                   5    
HELIX   45  45 MET D  261  LEU D  272  1                                  12    
HELIX   46  46 LEU D  272  GLN D  280  1                                   9    
HELIX   47  47 ASP D  283  PHE D  295  1                                  13    
HELIX   48  48 ASP D  304  ASN D  324  1                                  21    
HELIX   49  49 PHE D  334  LEU D  339  1                                   6    
HELIX   50  50 LEU D  340  LEU D  375  1                                  36    
SHEET    1  DA 2 LEU D 244  LEU D 245  0                                        
SHEET    2  DA 2 ASP D 248  ILE D 250 -1  O  ASP D 248   N  LEU D 245           
CRYST1  101.048  105.282   98.322  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      0.009896  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009498  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010171        0.00000                         
MTRIX1   1 -0.265440  0.964130 -0.001020        0.16176    1                    
MTRIX2   1  0.964040  0.265430  0.012940       -0.84988    1                    
MTRIX3   1  0.012740  0.002450 -0.999920       52.36674    1                    
MTRIX1   2 -0.248810  0.968550 -0.002500        0.25932    1                    
MTRIX2   2  0.968200  0.248790  0.026350       -1.20403    1                    
MTRIX3   2  0.026140  0.004140 -0.999650       52.34188    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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