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Database: PDB
Entry: 4ZPR
LinkDB: 4ZPR
Original site: 4ZPR 
HEADER    PROTEIN TRANSPORT/TRANSCRIPTION/DNA     08-MAY-15   4ZPR              
TITLE     CRYSTAL STRUCTURE OF THE HETERODIMERIC HIF-1A:ARNT COMPLEX WITH HRE   
TITLE    2 DNA                                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ARYL HYDROCARBON RECEPTOR NUCLEAR TRANSLOCATOR;            
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 82-464;                                       
COMPND   5 SYNONYM: ARNT PROTEIN, DIOXIN RECEPTOR, NUCLEAR TRANSLOCATOR,        
COMPND   6 HYPOXIA-INDUCIBLE FACTOR 1-BETA, HIF1-BETA;                          
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: HYPOXIA-INDUCIBLE FACTOR 1-ALPHA;                          
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 13-357;                                       
COMPND  12 SYNONYM: HIF1-ALPHA, ARNT-INTERACTING PROTEIN, HYPOXIA INDUCIBLE     
COMPND  13 FACTOR 1, ALPHA SUBUNIT;                                             
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: DNA (5'-                                                   
COMPND  17 D(*GP*GP*CP*TP*GP*CP*GP*TP*AP*CP*GP*TP*GP*CP*GP*GP*GP*TP*CP*GP*T)-   
COMPND  18 3');                                                                 
COMPND  19 CHAIN: C;                                                            
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 OTHER_DETAILS: HRE DNA SENSE STRAND;                                 
COMPND  22 MOL_ID: 4;                                                           
COMPND  23 MOLECULE: DNA (5'-                                                   
COMPND  24 D(*CP*AP*CP*GP*AP*CP*CP*CP*GP*CP*AP*CP*GP*TP*AP*CP*GP*CP*AP*GP*C)-   
COMPND  25 3');                                                                 
COMPND  26 CHAIN: D;                                                            
COMPND  27 ENGINEERED: YES;                                                     
COMPND  28 OTHER_DETAILS: HRE DNA ANTISENSE STRAND                              
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: ARNT;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PMKH;                                     
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  12 ORGANISM_COMMON: MOUSE;                                              
SOURCE  13 ORGANISM_TAXID: 10090;                                               
SOURCE  14 GENE: HIF1A;                                                         
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PSJ2;                                     
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 SYNTHETIC: YES;                                                      
SOURCE  21 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  22 ORGANISM_TAXID: 10090;                                               
SOURCE  23 MOL_ID: 4;                                                           
SOURCE  24 SYNTHETIC: YES;                                                      
SOURCE  25 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  26 ORGANISM_TAXID: 10090                                                
KEYWDS    ARNT, HIF-1A, HRE, BHLH-PAS, PROTEIN TRANSPORT-TRANSCRIPTION-DNA      
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.WU,N.POTLURI,J.LU,Y.KIM,F.RASTINEJAD                                
REVDAT   4   22-NOV-17 4ZPR    1       JRNL   REMARK                            
REVDAT   3   26-AUG-15 4ZPR    1       JRNL                                     
REVDAT   2   19-AUG-15 4ZPR    1       JRNL                                     
REVDAT   1   12-AUG-15 4ZPR    0                                                
JRNL        AUTH   D.WU,N.POTLURI,J.LU,Y.KIM,F.RASTINEJAD                       
JRNL        TITL   STRUCTURAL INTEGRATION IN HYPOXIA-INDUCIBLE FACTORS.         
JRNL        REF    NATURE                        V. 524   303 2015              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   26245371                                                     
JRNL        DOI    10.1038/NATURE14883                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.90 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) : 3.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.85                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.370                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 9578                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.272                           
REMARK   3   R VALUE            (WORKING SET) : 0.265                           
REMARK   3   FREE R VALUE                     : 0.341                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.040                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 962                             
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 29.8457 -  7.4310    0.95     1191   132  0.1846 0.2589        
REMARK   3     2  7.4310 -  5.9132    1.00     1256   130  0.3131 0.4049        
REMARK   3     3  5.9132 -  5.1702    1.00     1229   137  0.3366 0.4011        
REMARK   3     4  5.1702 -  4.6994    1.00     1235   139  0.3314 0.4042        
REMARK   3     5  4.6994 -  4.3637    1.00     1261   148  0.3364 0.4106        
REMARK   3     6  4.3637 -  4.1071    1.00     1236   128  0.3605 0.4609        
REMARK   3     7  4.1071 -  3.9019    1.00     1208   148  0.3872 0.4386        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.840            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 43.570           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 204.7                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 194.6                          
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      :  0.005           5229                                  
REMARK   3   ANGLE     :  0.843           7222                                  
REMARK   3   CHIRALITY :  0.033            812                                  
REMARK   3   PLANARITY :  0.003            767                                  
REMARK   3   DIHEDRAL  : 21.056           2002                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 4ZPR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAY-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000209675.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-AUG-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97929                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000, SCALEPACK                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9620                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.04500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.79000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4ZP4                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES, PH 6.0, 100 MM CALCIUM       
REMARK 280  ACETATE, 15% PEG400, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  289K                                                                
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      121.82200            
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      182.73300            
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       60.91100            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10480 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 34510 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.0 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    81                                                      
REMARK 465     SER A    82                                                      
REMARK 465     SER A    83                                                      
REMARK 465     ALA A    84                                                      
REMARK 465     ASP A    85                                                      
REMARK 465     LYS A    86                                                      
REMARK 465     CYS A   119                                                      
REMARK 465     SER A   120                                                      
REMARK 465     ARG A   143                                                      
REMARK 465     GLY A   144                                                      
REMARK 465     THR A   145                                                      
REMARK 465     GLY A   146                                                      
REMARK 465     ASN A   147                                                      
REMARK 465     THR A   148                                                      
REMARK 465     SER A   149                                                      
REMARK 465     THR A   150                                                      
REMARK 465     ASP A   151                                                      
REMARK 465     GLY A   152                                                      
REMARK 465     SER A   153                                                      
REMARK 465     TYR A   154                                                      
REMARK 465     LYS A   155                                                      
REMARK 465     PRO A   156                                                      
REMARK 465     SER A   157                                                      
REMARK 465     PHE A   158                                                      
REMARK 465     LEU A   159                                                      
REMARK 465     CYS A   181                                                      
REMARK 465     GLU A   182                                                      
REMARK 465     THR A   183                                                      
REMARK 465     THR A   227                                                      
REMARK 465     SER A   228                                                      
REMARK 465     GLU A   229                                                      
REMARK 465     ASN A   230                                                      
REMARK 465     ALA A   231                                                      
REMARK 465     LEU A   232                                                      
REMARK 465     THR A   233                                                      
REMARK 465     GLY A   234                                                      
REMARK 465     ARG A   235                                                      
REMARK 465     VAL A   236                                                      
REMARK 465     LEU A   237                                                      
REMARK 465     ASP A   238                                                      
REMARK 465     LEU A   239                                                      
REMARK 465     LYS A   240                                                      
REMARK 465     THR A   241                                                      
REMARK 465     GLY A   242                                                      
REMARK 465     THR A   243                                                      
REMARK 465     VAL A   244                                                      
REMARK 465     LYS A   245                                                      
REMARK 465     LYS A   246                                                      
REMARK 465     GLU A   247                                                      
REMARK 465     GLY A   248                                                      
REMARK 465     GLN A   249                                                      
REMARK 465     GLN A   250                                                      
REMARK 465     SER A   251                                                      
REMARK 465     SER A   252                                                      
REMARK 465     MET A   253                                                      
REMARK 465     ARG A   254                                                      
REMARK 465     MET A   255                                                      
REMARK 465     CYS A   256                                                      
REMARK 465     MET A   257                                                      
REMARK 465     GLY A   258                                                      
REMARK 465     SER A   259                                                      
REMARK 465     GLY A   270                                                      
REMARK 465     THR A   271                                                      
REMARK 465     SER A   272                                                      
REMARK 465     SER A   273                                                      
REMARK 465     VAL A   274                                                      
REMARK 465     ASP A   275                                                      
REMARK 465     PRO A   276                                                      
REMARK 465     VAL A   277                                                      
REMARK 465     SER A   278                                                      
REMARK 465     MET A   279                                                      
REMARK 465     ASN A   280                                                      
REMARK 465     ARG A   281                                                      
REMARK 465     LEU A   282                                                      
REMARK 465     SER A   283                                                      
REMARK 465     PHE A   284                                                      
REMARK 465     LEU A   285                                                      
REMARK 465     ARG A   286                                                      
REMARK 465     ASN A   287                                                      
REMARK 465     ARG A   288                                                      
REMARK 465     CYS A   289                                                      
REMARK 465     ARG A   290                                                      
REMARK 465     ASN A   291                                                      
REMARK 465     GLY A   292                                                      
REMARK 465     LEU A   293                                                      
REMARK 465     GLY A   294                                                      
REMARK 465     SER A   295                                                      
REMARK 465     VAL A   296                                                      
REMARK 465     LYS A   297                                                      
REMARK 465     GLU A   298                                                      
REMARK 465     GLY A   299                                                      
REMARK 465     GLU A   300                                                      
REMARK 465     PRO A   301                                                      
REMARK 465     HIS A   302                                                      
REMARK 465     PHE A   303                                                      
REMARK 465     VAL A   304                                                      
REMARK 465     VAL A   305                                                      
REMARK 465     ILE A   312                                                      
REMARK 465     LYS A   313                                                      
REMARK 465     ALA A   314                                                      
REMARK 465     TRP A   315                                                      
REMARK 465     PRO A   316                                                      
REMARK 465     PRO A   317                                                      
REMARK 465     ALA A   318                                                      
REMARK 465     GLY A   319                                                      
REMARK 465     VAL A   320                                                      
REMARK 465     SER A   321                                                      
REMARK 465     LEU A   322                                                      
REMARK 465     PRO A   323                                                      
REMARK 465     ASP A   324                                                      
REMARK 465     ASP A   325                                                      
REMARK 465     ASP A   326                                                      
REMARK 465     PRO A   327                                                      
REMARK 465     GLU A   328                                                      
REMARK 465     ALA A   329                                                      
REMARK 465     GLY A   330                                                      
REMARK 465     GLN A   331                                                      
REMARK 465     GLY A   332                                                      
REMARK 465     SER A   333                                                      
REMARK 465     LYS A   334                                                      
REMARK 465     PHE A   335                                                      
REMARK 465     CYS A   336                                                      
REMARK 465     LEU A   337                                                      
REMARK 465     VAL A   345                                                      
REMARK 465     THR A   346                                                      
REMARK 465     SER A   347                                                      
REMARK 465     SER A   348                                                      
REMARK 465     PRO A   349                                                      
REMARK 465     ASN A   350                                                      
REMARK 465     CYS A   351                                                      
REMARK 465     THR A   352                                                      
REMARK 465     ASP A   353                                                      
REMARK 465     MET A   354                                                      
REMARK 465     SER A   355                                                      
REMARK 465     ASN A   356                                                      
REMARK 465     ILE A   357                                                      
REMARK 465     CYS A   358                                                      
REMARK 465     GLN A   359                                                      
REMARK 465     PRO A   360                                                      
REMARK 465     ARG A   428                                                      
REMARK 465     PHE A   429                                                      
REMARK 465     ARG A   430                                                      
REMARK 465     SER A   431                                                      
REMARK 465     LYS A   432                                                      
REMARK 465     THR A   433                                                      
REMARK 465     ARG A   434                                                      
REMARK 465     GLU A   435                                                      
REMARK 465     TRP A   436                                                      
REMARK 465     LEU A   437                                                      
REMARK 465     MET B    13                                                      
REMARK 465     SER B    14                                                      
REMARK 465     ASP B    74                                                      
REMARK 465     ALA B    75                                                      
REMARK 465     GLY B    76                                                      
REMARK 465     GLY B    77                                                      
REMARK 465     LEU B    78                                                      
REMARK 465     ASP B    79                                                      
REMARK 465     SER B    80                                                      
REMARK 465     GLU B    81                                                      
REMARK 465     ASP B    82                                                      
REMARK 465     GLU B    83                                                      
REMARK 465     MET B    84                                                      
REMARK 465     LYS B    85                                                      
REMARK 465     ALA B    86                                                      
REMARK 465     GLN B    87                                                      
REMARK 465     MET B    88                                                      
REMARK 465     HIS B   150                                                      
REMARK 465     ARG B   151                                                      
REMARK 465     ASN B   152                                                      
REMARK 465     GLY B   153                                                      
REMARK 465     PRO B   154                                                      
REMARK 465     VAL B   155                                                      
REMARK 465     ARG B   156                                                      
REMARK 465     LYS B   157                                                      
REMARK 465     GLY B   158                                                      
REMARK 465     LYS B   159                                                      
REMARK 465     GLU B   160                                                      
REMARK 465     LEU B   161                                                      
REMARK 465     ASN B   162                                                      
REMARK 465     SER B   177                                                      
REMARK 465     ARG B   178                                                      
REMARK 465     GLY B   179                                                      
REMARK 465     VAL B   200                                                      
REMARK 465     TYR B   201                                                      
REMARK 465     ASP B   202                                                      
REMARK 465     THR B   203                                                      
REMARK 465     ASN B   204                                                      
REMARK 465     SER B   205                                                      
REMARK 465     ASN B   206                                                      
REMARK 465     GLN B   207                                                      
REMARK 465     PRO B   208                                                      
REMARK 465     GLN B   209                                                      
REMARK 465     CYS B   210                                                      
REMARK 465     GLY B   211                                                      
REMARK 465     TYR B   212                                                      
REMARK 465     LYS B   213                                                      
REMARK 465     LYS B   214                                                      
REMARK 465     PRO B   215                                                      
REMARK 465     PRO B   216                                                      
REMARK 465     MET B   217                                                      
REMARK 465     THR B   218                                                      
REMARK 465     ILE B   235                                                      
REMARK 465     PRO B   236                                                      
REMARK 465     LEU B   237                                                      
REMARK 465     ASP B   238                                                      
REMARK 465     GLU B   257                                                      
REMARK 465     ARG B   258                                                      
REMARK 465     LEU B   350                                                      
REMARK 465     ILE B   351                                                      
REMARK 465     PHE B   352                                                      
REMARK 465     SER B   353                                                      
REMARK 465     LEU B   354                                                      
REMARK 465     GLN B   355                                                      
REMARK 465     GLN B   356                                                      
REMARK 465     THR B   357                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ILE A   109     OG   SER A   113              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    LYS A 125   N   -  CA  -  C   ANGL. DEV. =  19.0 DEGREES          
REMARK 500    PRO A 388   C   -  N   -  CA  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    TYR B 305   CB  -  CA  -  C   ANGL. DEV. = -15.0 DEGREES          
REMARK 500     DC D   1   O4' -  C1' -  N1  ANGL. DEV. =   2.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A 125       64.92     38.08                                   
REMARK 500    SER A 192        3.14    -62.66                                   
REMARK 500    ASN A 198     -133.58     56.51                                   
REMARK 500    GLN A 199       65.23     29.18                                   
REMARK 500    SER A 202      -67.93    -91.85                                   
REMARK 500    TRP A 204     -113.20   -122.91                                   
REMARK 500    PHE A 205     -122.45     54.62                                   
REMARK 500    ASP A 211       43.86    -86.01                                   
REMARK 500    GLN A 212      -17.45   -159.03                                   
REMARK 500    ASP A 217       66.38   -100.73                                   
REMARK 500    LEU A 225       49.04   -146.95                                   
REMARK 500    HIS A 367     -169.43   -117.40                                   
REMARK 500    THR A 374      -32.44   -156.18                                   
REMARK 500    PRO A 388      -50.66    -28.23                                   
REMARK 500    LYS A 419      107.07    -55.51                                   
REMARK 500    LEU A 423      110.90   -165.57                                   
REMARK 500    SER A 442       72.12   -106.11                                   
REMARK 500    ASN A 448      108.46    -55.50                                   
REMARK 500    PRO A 449      -35.02    -37.65                                   
REMARK 500    GLU A 455      -17.28   -154.35                                   
REMARK 500    SER B  51      -76.27    -65.12                                   
REMARK 500    ASP B 108       97.18    -65.05                                   
REMARK 500    MET B 109       89.54    -66.38                                   
REMARK 500    MET B 120      -57.87     53.11                                   
REMARK 500    LEU B 127       34.14   -145.86                                   
REMARK 500    ASP B 140      -14.11   -148.05                                   
REMARK 500    MET B 171     -168.38    -68.04                                   
REMARK 500    LEU B 175      -31.27   -138.45                                   
REMARK 500    MET B 182     -158.88   -136.28                                   
REMARK 500    LYS B 185      -27.27     70.82                                   
REMARK 500    PRO B 230        0.79    -57.27                                   
REMARK 500    SER B 247     -168.58    -74.50                                   
REMARK 500    MET B 250       67.06     65.70                                   
REMARK 500    SER B 253      -32.98   -137.71                                   
REMARK 500    MET B 263      -84.06   -111.65                                   
REMARK 500    LEU B 270      -93.80    -85.73                                   
REMARK 500    LEU B 271      -87.32     64.99                                   
REMARK 500    LYS B 297     -141.96    -97.63                                   
REMARK 500    GLN B 299     -168.93   -106.99                                   
REMARK 500    THR B 302     -171.17    -66.94                                   
REMARK 500    ASN B 326      106.69    -52.05                                   
REMARK 500    LYS B 328      102.43    -56.09                                   
REMARK 500    SER B 330       64.63     39.73                                   
REMARK 500    PRO B 332      107.51    -50.08                                   
REMARK 500    GLN B 347       62.21     64.54                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4ZP4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ZPH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ZPK   RELATED DB: PDB                                   
DBREF  4ZPR A   82   464  UNP    P53762   ARNT_MOUSE      82    464             
DBREF  4ZPR B   13   357  UNP    Q61221   HIF1A_MOUSE     13    357             
DBREF  4ZPR C    1    21  PDB    4ZPR     4ZPR             1     21             
DBREF  4ZPR D    1    21  PDB    4ZPR     4ZPR             1     21             
SEQADV 4ZPR MET A   81  UNP  P53762              INITIATING METHIONINE          
SEQRES   1 A  384  MET SER SER ALA ASP LYS GLU ARG LEU ALA ARG GLU ASN          
SEQRES   2 A  384  HIS SER GLU ILE GLU ARG ARG ARG ARG ASN LYS MET THR          
SEQRES   3 A  384  ALA TYR ILE THR GLU LEU SER ASP MET VAL PRO THR CYS          
SEQRES   4 A  384  SER ALA LEU ALA ARG LYS PRO ASP LYS LEU THR ILE LEU          
SEQRES   5 A  384  ARG MET ALA VAL SER HIS MET LYS SER LEU ARG GLY THR          
SEQRES   6 A  384  GLY ASN THR SER THR ASP GLY SER TYR LYS PRO SER PHE          
SEQRES   7 A  384  LEU THR ASP GLN GLU LEU LYS HIS LEU ILE LEU GLU ALA          
SEQRES   8 A  384  ALA ASP GLY PHE LEU PHE ILE VAL SER CYS GLU THR GLY          
SEQRES   9 A  384  ARG VAL VAL TYR VAL SER ASP SER VAL THR PRO VAL LEU          
SEQRES  10 A  384  ASN GLN PRO GLN SER GLU TRP PHE GLY SER THR LEU TYR          
SEQRES  11 A  384  ASP GLN VAL HIS PRO ASP ASP VAL ASP LYS LEU ARG GLU          
SEQRES  12 A  384  GLN LEU SER THR SER GLU ASN ALA LEU THR GLY ARG VAL          
SEQRES  13 A  384  LEU ASP LEU LYS THR GLY THR VAL LYS LYS GLU GLY GLN          
SEQRES  14 A  384  GLN SER SER MET ARG MET CYS MET GLY SER ARG ARG SER          
SEQRES  15 A  384  PHE ILE CYS ARG MET ARG CYS GLY THR SER SER VAL ASP          
SEQRES  16 A  384  PRO VAL SER MET ASN ARG LEU SER PHE LEU ARG ASN ARG          
SEQRES  17 A  384  CYS ARG ASN GLY LEU GLY SER VAL LYS GLU GLY GLU PRO          
SEQRES  18 A  384  HIS PHE VAL VAL VAL HIS CYS THR GLY TYR ILE LYS ALA          
SEQRES  19 A  384  TRP PRO PRO ALA GLY VAL SER LEU PRO ASP ASP ASP PRO          
SEQRES  20 A  384  GLU ALA GLY GLN GLY SER LYS PHE CYS LEU VAL ALA ILE          
SEQRES  21 A  384  GLY ARG LEU GLN VAL THR SER SER PRO ASN CYS THR ASP          
SEQRES  22 A  384  MET SER ASN ILE CYS GLN PRO THR GLU PHE ILE SER ARG          
SEQRES  23 A  384  HIS ASN ILE GLU GLY ILE PHE THR PHE VAL ASP HIS ARG          
SEQRES  24 A  384  CYS VAL ALA THR VAL GLY TYR GLN PRO GLN GLU LEU LEU          
SEQRES  25 A  384  GLY LYS ASN ILE VAL GLU PHE CYS HIS PRO GLU ASP GLN          
SEQRES  26 A  384  GLN LEU LEU ARG ASP SER PHE GLN GLN VAL VAL LYS LEU          
SEQRES  27 A  384  LYS GLY GLN VAL LEU SER VAL MET PHE ARG PHE ARG SER          
SEQRES  28 A  384  LYS THR ARG GLU TRP LEU TRP MET ARG THR SER SER PHE          
SEQRES  29 A  384  THR PHE GLN ASN PRO TYR SER ASP GLU ILE GLU TYR ILE          
SEQRES  30 A  384  ILE CYS THR ASN THR ASN VAL                                  
SEQRES   1 B  345  MET SER SER GLU ARG ARG LYS GLU LYS SER ARG ASP ALA          
SEQRES   2 B  345  ALA ARG SER ARG ARG SER LYS GLU SER GLU VAL PHE TYR          
SEQRES   3 B  345  GLU LEU ALA HIS GLN LEU PRO LEU PRO HIS ASN VAL SER          
SEQRES   4 B  345  SER HIS LEU ASP LYS ALA SER VAL MET ARG LEU THR ILE          
SEQRES   5 B  345  SER TYR LEU ARG VAL ARG LYS LEU LEU ASP ALA GLY GLY          
SEQRES   6 B  345  LEU ASP SER GLU ASP GLU MET LYS ALA GLN MET ASP CYS          
SEQRES   7 B  345  PHE TYR LEU LYS ALA LEU ASP GLY PHE VAL MET VAL LEU          
SEQRES   8 B  345  THR ASP ASP GLY ASP MET VAL TYR ILE SER ASP ASN VAL          
SEQRES   9 B  345  ASN LYS TYR MET GLY LEU THR GLN PHE GLU LEU THR GLY          
SEQRES  10 B  345  HIS SER VAL PHE ASP PHE THR HIS PRO CYS ASP HIS GLU          
SEQRES  11 B  345  GLU MET ARG GLU MET LEU THR HIS ARG ASN GLY PRO VAL          
SEQRES  12 B  345  ARG LYS GLY LYS GLU LEU ASN THR GLN ARG SER PHE PHE          
SEQRES  13 B  345  LEU ARG MET LYS CYS THR LEU THR SER ARG GLY ARG THR          
SEQRES  14 B  345  MET ASN ILE LYS SER ALA THR TRP LYS VAL LEU HIS CYS          
SEQRES  15 B  345  THR GLY HIS ILE HIS VAL TYR ASP THR ASN SER ASN GLN          
SEQRES  16 B  345  PRO GLN CYS GLY TYR LYS LYS PRO PRO MET THR CYS LEU          
SEQRES  17 B  345  VAL LEU ILE CYS GLU PRO ILE PRO HIS PRO SER ASN ILE          
SEQRES  18 B  345  GLU ILE PRO LEU ASP SER LYS THR PHE LEU SER ARG HIS          
SEQRES  19 B  345  SER LEU ASP MET LYS PHE SER TYR CYS ASP GLU ARG ILE          
SEQRES  20 B  345  THR GLU LEU MET GLY TYR GLU PRO GLU GLU LEU LEU GLY          
SEQRES  21 B  345  ARG SER ILE TYR GLU TYR TYR HIS ALA LEU ASP SER ASP          
SEQRES  22 B  345  HIS LEU THR LYS THR HIS HIS ASP MET PHE THR LYS GLY          
SEQRES  23 B  345  GLN VAL THR THR GLY GLN TYR ARG MET LEU ALA LYS ARG          
SEQRES  24 B  345  GLY GLY TYR VAL TRP VAL GLU THR GLN ALA THR VAL ILE          
SEQRES  25 B  345  TYR ASN THR LYS ASN SER GLN PRO GLN CYS ILE VAL CYS          
SEQRES  26 B  345  VAL ASN TYR VAL VAL SER GLY ILE ILE GLN HIS ASP LEU          
SEQRES  27 B  345  ILE PHE SER LEU GLN GLN THR                                  
SEQRES   1 C   21   DG  DG  DC  DT  DG  DC  DG  DT  DA  DC  DG  DT  DG          
SEQRES   2 C   21   DC  DG  DG  DG  DT  DC  DG  DT                              
SEQRES   1 D   21   DC  DA  DC  DG  DA  DC  DC  DC  DG  DC  DA  DC  DG          
SEQRES   2 D   21   DT  DA  DC  DG  DC  DA  DG  DC                              
HELIX    1 AA1 GLU A   87  VAL A  116  1                                  30    
HELIX    2 AA2 ASP A  127  LYS A  140  1                                  14    
HELIX    3 AA3 ASP A  161  ASP A  173  1                                  13    
HELIX    4 AA4 VAL A  193  ASN A  198  1                                   6    
HELIX    5 AA5 THR A  208  VAL A  213  5                                   6    
HELIX    6 AA6 VAL A  218  GLN A  224  1                                   7    
HELIX    7 AA7 ARG A  379  VAL A  384  1                                   6    
HELIX    8 AA8 GLN A  387  LEU A  391  5                                   5    
HELIX    9 AA9 HIS A  401  GLU A  403  5                                   3    
HELIX   10 AB1 ASP A  404  VAL A  416  1                                  13    
HELIX   11 AB2 GLU B   16  GLN B   43  1                                  28    
HELIX   12 AB3 ASP B   55  LEU B   73  1                                  19    
HELIX   13 AB4 CYS B   90  LEU B   96  1                                   7    
HELIX   14 AB5 ASP B  114  TYR B  119  5                                   6    
HELIX   15 AB6 THR B  123  LEU B  127  5                                   5    
HELIX   16 AB7 ASP B  140  MET B  147  1                                   8    
HELIX   17 AB8 HIS B  229  ILE B  233  5                                   5    
HELIX   18 AB9 HIS B  280  LYS B  297  1                                  18    
HELIX   19 AC1 THR B  327  SER B  330  5                                   4    
SHEET    1 AA1 5 VAL A 186  VAL A 189  0                                        
SHEET    2 AA1 5 PHE A 175  VAL A 179 -1  N  ILE A 178   O  VAL A 187           
SHEET    3 AA1 5 ALA A 339  ARG A 342 -1  O  GLY A 341   N  PHE A 175           
SHEET    4 AA1 5 HIS A 307  GLY A 310 -1  N  HIS A 307   O  ARG A 342           
SHEET    5 AA1 5 ARG A 261  ILE A 264 -1  N  PHE A 263   O  CYS A 308           
SHEET    1 AA2 4 GLU A 362  PHE A 363  0                                        
SHEET    2 AA2 4 ILE A 454  THR A 462 -1  O  ASN A 461   N  PHE A 363           
SHEET    3 AA2 4 SER A 365  HIS A 367 -1  N  SER A 365   O  CYS A 459           
SHEET    4 AA2 4 PHE A 373  VAL A 376 -1  O  PHE A 375   N  ARG A 366           
SHEET    1 AA3 4 GLU A 362  PHE A 363  0                                        
SHEET    2 AA3 4 ILE A 454  THR A 462 -1  O  ASN A 461   N  PHE A 363           
SHEET    3 AA3 4 ARG A 440  GLN A 447 -1  N  ARG A 440   O  THR A 462           
SHEET    4 AA3 4 SER A 424  MET A 426 -1  N  VAL A 425   O  THR A 441           
SHEET    1 AA4 5 TYR B 111  ILE B 112  0                                        
SHEET    2 AA4 5 PHE B  99  LEU B 103 -1  N  VAL B 102   O  TYR B 111           
SHEET    3 AA4 5 LEU B 220  GLU B 225 -1  O  CYS B 224   N  PHE B  99           
SHEET    4 AA4 5 LEU B 192  HIS B 197 -1  N  HIS B 197   O  VAL B 221           
SHEET    5 AA4 5 ARG B 165  LEU B 169 -1  N  LEU B 169   O  LEU B 192           
SHEET    1 AA5 2 LYS B 172  CYS B 173  0                                        
SHEET    2 AA5 2 THR B 188  TRP B 189 -1  O  THR B 188   N  CYS B 173           
SHEET    1 AA6 5 PHE B 252  TYR B 254  0                                        
SHEET    2 AA6 5 PHE B 242  HIS B 246 -1  N  ARG B 245   O  SER B 253           
SHEET    3 AA6 5 GLN B 331  VAL B 341 -1  O  ASN B 339   N  PHE B 242           
SHEET    4 AA6 5 TYR B 314  ASN B 326 -1  N  ILE B 324   O  CYS B 334           
SHEET    5 AA6 5 TYR B 305  LEU B 308 -1  N  TYR B 305   O  VAL B 317           
CRYST1   66.735   66.735  243.644  90.00  90.00  90.00 P 43          4          
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      0.014985  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014985  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004104        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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