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Database: PDB
Entry: 4EQ1
LinkDB: 4EQ1
Original site: 4EQ1 
HEADER    TRANSCRIPTION                           17-APR-12   4EQ1              
TITLE     CRYSTAL STRUCTURE OF THE ARNT PAS-B HOMODIMER                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ARYL HYDROCARBON RECEPTOR NUCLEAR TRANSLOCATOR;            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: PAS-B DOMAIN (UNP RESIDUES 357-464);                       
COMPND   5 SYNONYM: ARNT PROTEIN, CLASS E BASIC HELIX-LOOP-HELIX PROTEIN 2,     
COMPND   6 BHLHE2, DIOXIN RECEPTOR, NUCLEAR TRANSLOCATOR, HYPOXIA-INDUCIBLE     
COMPND   7 FACTOR 1-BETA, HIF-1-BETA, HIF1-BETA;                                
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ARNT, BHLHE2;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PER-ARNT-SIM, TRANSCRIPTION REGULATION, HOMODIMER, TRANSCRIPTION      
KEYWDS   2 FACTOR, DNA-BINDING, HIF1, HIF2, AHR, TRANSCRIPTION                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.H.GARDNER,J.M.KEY                                                   
REVDAT   2   15-NOV-17 4EQ1    1       REMARK                                   
REVDAT   1   17-APR-13 4EQ1    0                                                
JRNL        AUTH   Y.GUO,C.L.PARTCH,J.KEY,P.B.CARD,V.PASHKOV,A.PATEL,           
JRNL        AUTH 2 R.K.BRUICK,H.WURDAK,K.H.GARDNER                              
JRNL        TITL   REGULATING THE ARNT/TACC3 AXIS: MULTIPLE APPROACHES TO       
JRNL        TITL 2 MANIPULATING PROTEIN/PROTEIN INTERACTIONS WITH SMALL         
JRNL        TITL 3 MOLECULES.                                                   
JRNL        REF    ACS CHEM.BIOL.                V.   8   626 2013              
JRNL        REFN                   ISSN 1554-8929                               
JRNL        PMID   23240775                                                     
JRNL        DOI    10.1021/CB300604U                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.7.3_928                                     
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) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.05                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 34166                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.090                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1740                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 24.0494 -  3.6592    0.99     2774   130  0.2017 0.2061        
REMARK   3     2  3.6592 -  2.9060    1.00     2714   156  0.1889 0.2012        
REMARK   3     3  2.9060 -  2.5391    1.00     2686   161  0.1962 0.2473        
REMARK   3     4  2.5391 -  2.3072    1.00     2705   149  0.1945 0.2187        
REMARK   3     5  2.3072 -  2.1419    1.00     2690   147  0.2058 0.2388        
REMARK   3     6  2.1419 -  2.0157    1.00     2713   144  0.2025 0.2135        
REMARK   3     7  2.0157 -  1.9148    1.00     2662   161  0.1988 0.2225        
REMARK   3     8  1.9148 -  1.8315    1.00     2729   135  0.2025 0.2404        
REMARK   3     9  1.8315 -  1.7610    1.00     2676   152  0.2117 0.2804        
REMARK   3    10  1.7610 -  1.7002    1.00     2688   143  0.2180 0.2843        
REMARK   3    11  1.7002 -  1.6471    1.00     2683   128  0.2270 0.2417        
REMARK   3    12  1.6471 -  1.6000    1.00     2706   134  0.2454 0.3011        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.73                                          
REMARK   3   K_SOL              : 0.40                                          
REMARK   3   B_SOL              : 61.04                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.200            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.550           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.02                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.10810                                             
REMARK   3    B22 (A**2) : 0.07090                                              
REMARK   3    B33 (A**2) : 0.03710                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.11910                                             
REMARK   3    B23 (A**2) : 0.00000                                              
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      :  0.014           1885                                  
REMARK   3   ANGLE     :  1.448           2551                                  
REMARK   3   CHIRALITY :  0.086            275                                  
REMARK   3   PLANARITY :  0.008            330                                  
REMARK   3   DIHEDRAL  : 16.149            706                                  
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 4EQ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAY-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000071929.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-MAR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
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) : 0.97904                            
REMARK 200  MONOCHROMATOR                  : CUSTOM                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34166                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.047                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 4.550                              
REMARK 200  R MERGE                    (I) : 0.04700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 38.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: 3F1P CHAIN A                                         
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULFATE, 3% PEG400, 1%       
REMARK 280  PEI, 50MM TRIS PH 7.5, VAPOR DIFFUSION, HANGING DROP,               
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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       46.65750            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       30.83900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       46.65750            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       30.83900            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2500 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 701  LIES ON A SPECIAL POSITION.                          
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    HOH A   695     O    HOH A   698              1.91            
REMARK 500   O    HOH A   706     O    HOH A   711              2.03            
REMARK 500   O    HOH A   667     O    HOH A   689              2.04            
REMARK 500   O    HOH B   579     O    HOH B   585              2.06            
REMARK 500   OD1  ASN A   463     O    HOH A   696              2.08            
REMARK 500   O    HOH A   665     O    HOH B   565              2.09            
REMARK 500   OE1  GLU A   435     O    HOH A   687              2.12            
REMARK 500   O    HOH A   708     O    HOH B   577              2.12            
REMARK 500   O    HOH A   668     O    HOH A   689              2.13            
REMARK 500   O    HOH B   538     O    HOH B   539              2.16            
REMARK 500   O    HOH A   672     O    HOH A   679              2.16            
REMARK 500   O    HOH A   669     O    HOH A   714              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NH1  ARG B   430     O    HOH B   557     4545     1.63            
REMARK 500   O    HOH A   646     O    HOH B   541     2656     2.00            
REMARK 500   NH1  ARG A   430     O    HOH A   679     4556     2.03            
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    THR B 361       22.71   -140.01                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PE5 A  501                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE5 A 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1X0O   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE HUMAN ARNT C-TERMINAL PAS DOMAIN DETERMINED BY NMR  
REMARK 900 RELATED ID: 2HV1   RELATED DB: PDB                                   
REMARK 900 HADDOCK STRUCTURE OF ARNT PAS-B HOMODIMER                            
REMARK 900 RELATED ID: 2K7S   RELATED DB: PDB                                   
REMARK 900 HUMAN ARNT C-TERMINAL PAS DOMAIN, 3 RESIDUE IB SLIP                  
REMARK 900 RELATED ID: 2B02   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ARNT PAS-B DOMAIN                               
REMARK 900 RELATED ID: 3F1P   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A HIGH AFFINITY HETERODIMER OF HIF2 ALPHA AND   
REMARK 900 ARNT C-TERMINAL PAS DOMAINS                                          
REMARK 900 RELATED ID: 3F1O   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HIGH AFFINITY HETERODIMER OF HIF2 HIF2-     
REMARK 900 ALPHA AND ARNT C-TERMINAL PAS DOMAINS, WITH AN INTERNALLY-BOUND      
REMARK 900 ARTIFICIAL LIGAND                                                    
REMARK 900 RELATED ID: 3H7W   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HIGH AFFINITY HETERODIMER OF HIF2 ALPHA     
REMARK 900 AND ARNT C-TERMINAL PAS DOMAINS WITH THE ARTIFICIAL LIGAND THS017    
REMARK 900 RELATED ID: 3H82   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HIGH AFFINITY HETERODIMER OF HIF2 ALPHA     
REMARK 900 AND ARNT C-TERMINAL PAS DOMAINS WITH THE ARTIFICIAL LIGAND THS020    
REMARK 900 RELATED ID: 3F1N   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A HIGH AFFINITY HETERODIMER OF HIF2 ALPHA AND   
REMARK 900 ARNT C-TERMINAL PAS DOMAINS, WITH INTERNALLY BOUND ETHYLENE GLYCOL.  
DBREF  4EQ1 A  357   464  UNP    P27540   ARNT_HUMAN     357    464             
DBREF  4EQ1 B  357   464  UNP    P27540   ARNT_HUMAN     357    464             
SEQADV 4EQ1 GLY A  356  UNP  P27540              EXPRESSION TAG                 
SEQADV 4EQ1 GLY B  356  UNP  P27540              EXPRESSION TAG                 
SEQRES   1 A  109  GLY VAL CYS GLN PRO THR GLU PHE ILE SER ARG HIS ASN          
SEQRES   2 A  109  ILE GLU GLY ILE PHE THR PHE VAL ASP HIS ARG CYS VAL          
SEQRES   3 A  109  ALA THR VAL GLY TYR GLN PRO GLN GLU LEU LEU GLY LYS          
SEQRES   4 A  109  ASN ILE VAL GLU PHE CYS HIS PRO GLU ASP GLN GLN LEU          
SEQRES   5 A  109  LEU ARG ASP SER PHE GLN GLN VAL VAL LYS LEU LYS GLY          
SEQRES   6 A  109  GLN VAL LEU SER VAL MET PHE ARG PHE ARG SER LYS ASN          
SEQRES   7 A  109  GLN GLU TRP LEU TRP MET ARG THR SER SER PHE THR PHE          
SEQRES   8 A  109  GLN ASN PRO TYR SER ASP GLU ILE GLU TYR ILE ILE CYS          
SEQRES   9 A  109  THR ASN THR ASN VAL                                          
SEQRES   1 B  109  GLY VAL CYS GLN PRO THR GLU PHE ILE SER ARG HIS ASN          
SEQRES   2 B  109  ILE GLU GLY ILE PHE THR PHE VAL ASP HIS ARG CYS VAL          
SEQRES   3 B  109  ALA THR VAL GLY TYR GLN PRO GLN GLU LEU LEU GLY LYS          
SEQRES   4 B  109  ASN ILE VAL GLU PHE CYS HIS PRO GLU ASP GLN GLN LEU          
SEQRES   5 B  109  LEU ARG ASP SER PHE GLN GLN VAL VAL LYS LEU LYS GLY          
SEQRES   6 B  109  GLN VAL LEU SER VAL MET PHE ARG PHE ARG SER LYS ASN          
SEQRES   7 B  109  GLN GLU TRP LEU TRP MET ARG THR SER SER PHE THR PHE          
SEQRES   8 B  109  GLN ASN PRO TYR SER ASP GLU ILE GLU TYR ILE ILE CYS          
SEQRES   9 B  109  THR ASN THR ASN VAL                                          
HET    PE5  A 501      14                                                       
HETNAM     PE5 3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL                       
HETSYN     PE5 2-(2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-           
HETSYN   2 PE5  ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL, POLYETHYLENE           
HETSYN   3 PE5  GLYCOL PEG400                                                   
FORMUL   3  PE5    C18 H38 O9                                                   
FORMUL   4  HOH   *206(H2 O)                                                    
HELIX    1   1 HIS A  378  GLY A  385  1                                   8    
HELIX    2   2 GLN A  387  LEU A  392  1                                   6    
HELIX    3   3 ASN A  395  CYS A  400  5                                   6    
HELIX    4   4 HIS A  401  GLU A  403  5                                   3    
HELIX    5   5 ASP A  404  LEU A  418  1                                  15    
HELIX    6   6 ARG B  379  GLY B  385  1                                   7    
HELIX    7   7 GLN B  387  LEU B  392  1                                   6    
HELIX    8   8 ASN B  395  CYS B  400  5                                   6    
HELIX    9   9 HIS B  401  GLU B  403  5                                   3    
HELIX   10  10 ASP B  404  LEU B  418  1                                  15    
SHEET    1   A 6 VAL A 357  CYS A 358  0                                        
SHEET    2   A 6 VAL B 422  ARG B 430 -1  O  VAL B 422   N  CYS A 358           
SHEET    3   A 6 TRP B 436  GLN B 447 -1  O  MET B 439   N  PHE B 427           
SHEET    4   A 6 ILE B 454  ASN B 463 -1  O  ILE B 458   N  PHE B 444           
SHEET    5   A 6 GLU B 362  HIS B 367 -1  N  SER B 365   O  CYS B 459           
SHEET    6   A 6 PHE B 373  VAL B 376 -1  O  THR B 374   N  ARG B 366           
SHEET    1   B 6 PHE A 373  VAL A 376  0                                        
SHEET    2   B 6 GLU A 362  HIS A 367 -1  N  ARG A 366   O  THR A 374           
SHEET    3   B 6 ILE A 454  ASN A 463 -1  O  CYS A 459   N  SER A 365           
SHEET    4   B 6 TRP A 436  GLN A 447 -1  N  PHE A 444   O  ILE A 458           
SHEET    5   B 6 VAL A 422  ARG A 430 -1  N  VAL A 425   O  THR A 441           
SHEET    6   B 6 VAL B 357  CYS B 358 -1  O  CYS B 358   N  VAL A 422           
SITE     1 AC1  8 ARG A 366  PHE A 375  TYR A 456  ILE A 458                    
SITE     2 AC1  8 ARG B 366  PHE B 375  TYR B 456  ILE B 458                    
CRYST1   93.315   61.678   55.514  90.00 124.60  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010716  0.000000  0.007391        0.00000                         
SCALE2      0.000000  0.016213  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021883        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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