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Database: PDB
Entry: 3F1O
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Original site: 3F1O 
HEADER    TRANSCRIPTION                           28-OCT-08   3F1O              
TITLE     CRYSTAL STRUCTURE OF THE HIGH AFFINITY HETERODIMER OF HIF2 ALPHA AND  
TITLE    2 ARNT C-TERMINAL PAS DOMAINS, WITH AN INTERNALLY-BOUND ARTIFICIAL     
TITLE    3 LIGAND                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDOTHELIAL PAS DOMAIN-CONTAINING PROTEIN 1;               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: HIF2 ALPHA C-TERMINAL PAS DOMAIN;                          
COMPND   5 SYNONYM: EPAS-1, MEMBER OF PAS PROTEIN 2, BASIC-HELIX-LOOP-HELIX-PAS 
COMPND   6 PROTEIN MOP2, HYPOXIA-INDUCIBLE FACTOR 2 ALPHA, HIF-2 ALPHA, HIF2    
COMPND   7 ALPHA, HIF-1 ALPHA-LIKE FACTOR, HLF;                                 
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: ARYL HYDROCARBON RECEPTOR NUCLEAR TRANSLOCATOR;            
COMPND  12 CHAIN: B;                                                            
COMPND  13 FRAGMENT: ARNT C-TERMINAL PAS DOMAIN;                                
COMPND  14 SYNONYM: ARNT PROTEIN, DIOXIN RECEPTOR, NUCLEAR TRANSLOCATOR,        
COMPND  15 HYPOXIA-INDUCIBLE FACTOR 1 BETA, HIF-1 BETA;                         
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: EPAS1, HIF2A, HYPOXIA INDUCIBLE FACTOR 2 ALPHA, MOP2;          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PHIS-GB1-PARALLEL;                    
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: ARNT, ARYL HYDROCARBON RECEPTOR NUCLEAR TRANSLOCATOR;          
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PHIS-PARALLEL                         
KEYWDS    PAS DOMAIN, HETERODIMER, INTERNAL CAVITY, ACTIVATOR, ANGIOGENESIS,    
KEYWDS   2 CONGENITAL ERYTHROCYTOSIS, DEVELOPMENTAL PROTEIN, DIFFERENTIATION,   
KEYWDS   3 DISEASE MUTATION, DNA-BINDING, HYDROXYLATION, NUCLEUS,               
KEYWDS   4 PHOSPHOPROTEIN, TRANSCRIPTION, TRANSCRIPTION REGULATION, UBL         
KEYWDS   5 CONJUGATION, ALTERNATIVE SPLICING, POLYMORPHISM                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.H.SCHEUERMANN,D.R.TOMCHICK,M.MACHIUS,Y.GUO,R.K.BRUICK,K.H.GARDNER   
REVDAT   4   25-OCT-17 3F1O    1       REMARK                                   
REVDAT   3   17-MAR-09 3F1O    1       AUTHOR                                   
REVDAT   2   17-FEB-09 3F1O    1       JRNL                                     
REVDAT   1   20-JAN-09 3F1O    0                                                
JRNL        AUTH   T.H.SCHEUERMANN,D.R.TOMCHICK,M.MACHIUS,Y.GUO,R.K.BRUICK,     
JRNL        AUTH 2 K.H.GARDNER                                                  
JRNL        TITL   ARTIFICIAL LIGAND BINDING WITHIN THE HIF2ALPHA PAS-B DOMAIN  
JRNL        TITL 2 OF THE HIF2 TRANSCRIPTION FACTOR.                            
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 106   450 2009              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   19129502                                                     
JRNL        DOI    10.1073/PNAS.0808092106                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.3                                           
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) : 26.93                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 31173                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.168                           
REMARK   3   R VALUE            (WORKING SET) : 0.166                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1581                            
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 26.9336 -  3.5509    0.99     2758   166  0.1724 0.2158        
REMARK   3     2  3.5509 -  2.8195    0.99     2717   163  0.1613 0.1888        
REMARK   3     3  2.8195 -  2.4633    0.99     2700   166  0.1563 0.1933        
REMARK   3     4  2.4633 -  2.2382    0.99     2705   149  0.1601 0.1774        
REMARK   3     5  2.2382 -  2.0779    0.99     2726   126  0.1493 0.1862        
REMARK   3     6  2.0779 -  1.9554    0.98     2708   151  0.1541 0.2074        
REMARK   3     7  1.9554 -  1.8575    0.98     2662   140  0.1527 0.1775        
REMARK   3     8  1.8575 -  1.7767    0.98     2716   122  0.1666 0.2089        
REMARK   3     9  1.7767 -  1.7083    0.98     2671   123  0.1649 0.2041        
REMARK   3    10  1.7083 -  1.6493    0.98     2688   139  0.1808 0.2410        
REMARK   3    11  1.6493 -  1.5978    0.94     2541   136  0.2021 0.2368        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.41                                          
REMARK   3   B_SOL              : 49.91                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.93                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.21                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.43620                                              
REMARK   3    B22 (A**2) : -1.30440                                             
REMARK   3    B33 (A**2) : -3.13180                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.32780                                              
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      :  0.009           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  : 15.451           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  16.0554 -43.5747   9.9701              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1114 T22:   0.1308                                     
REMARK   3      T33:   0.1349 T12:  -0.0102                                     
REMARK   3      T13:  -0.0089 T23:  -0.0131                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.1787 L22:   1.6670                                     
REMARK   3      L33:   0.4414 L12:   0.3048                                     
REMARK   3      L13:  -0.0743 L23:   0.2294                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0247 S12:   0.0086 S13:  -0.0198                       
REMARK   3      S21:  -0.1277 S22:   0.0096 S23:  -0.0448                       
REMARK   3      S31:  -0.0603 S32:   0.0354 S33:   0.0087                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  18.4012 -18.9264  17.9199              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0913 T22:   0.0806                                     
REMARK   3      T33:   0.0866 T12:   0.0050                                     
REMARK   3      T13:   0.0050 T23:   0.0118                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2044 L22:   0.3909                                     
REMARK   3      L33:   0.9982 L12:  -0.1221                                     
REMARK   3      L13:  -0.0186 L23:   0.3725                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0351 S12:  -0.0388 S13:   0.0143                       
REMARK   3      S21:   0.0251 S22:   0.0303 S23:   0.0052                       
REMARK   3      S31:  -0.0365 S32:  -0.0231 S33:  -0.0540                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN C                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  12.1537 -41.5981  10.2748              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1699 T22:   0.2008                                     
REMARK   3      T33:   0.2055 T12:   0.0302                                     
REMARK   3      T13:   0.0179 T23:   0.0456                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7418 L22:  -0.1441                                     
REMARK   3      L33:   0.7616 L12:  -0.9901                                     
REMARK   3      L13:   1.0945 L23:   0.2796                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0239 S12:   0.0355 S13:  -0.0033                       
REMARK   3      S21:  -0.0076 S22:   0.0887 S23:   0.2030                       
REMARK   3      S31:   0.0025 S32:  -0.0569 S33:  -0.1068                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  THE DENSITY FOR THE N463 SIDE CHAIN IS RELATIVELY POOR, THAT ITS    
REMARK   3  CONFORMATION WAS INFORMED BY THAT OBSERVED IN THE HIGHER            
REMARK   3  RESOLUTION APO STRUCTURE (RCSB050035, 3F1P) AND MODELED WITH A      
REMARK   3  HEAVY WEIGHTING TOWARD GEOMETRIC IDEALITY AT THE EXPENSE OF A BEST  
REMARK   3  FIT AGAINST POOR                                                    
REMARK   3  DENSITY                                                             
REMARK   4                                                                      
REMARK   4 3F1O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-OCT-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000050034.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-JUN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97934                            
REMARK 200  MONOCHROMATOR                  : CUSTOM                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : SBC-2                              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31184                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 26.930                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.61                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
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 2B02                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 3350, 0.1M BISTRIS, 0.05M        
REMARK 280  TRIS, 0.017M NACL, 0.005M DTT , PH 6.5, VAPOR DIFFUSION COMBINED    
REMARK 280  WITH MICROSEEDING, TEMPERATURE 293K                                 
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       36.88050            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.50950            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       36.88050            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       41.50950            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1960 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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 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   234                                                      
REMARK 465     GLU A   235                                                      
REMARK 465     PRO A   329                                                      
REMARK 465     ARG A   330                                                      
REMARK 465     ASN A   331                                                      
REMARK 465     LEU A   332                                                      
REMARK 465     GLN A   333                                                      
REMARK 465     ASN A   350                                                      
REMARK 465     GLY B   350                                                      
REMARK 465     GLU B   351                                                      
REMARK 465     PHE B   352                                                      
REMARK 465     LYS B   353                                                      
REMARK 465     GLY B   354                                                      
REMARK 465     LEU B   355                                                      
REMARK 465     ASN B   356                                                      
REMARK 465     GLN B   469                                                      
REMARK 465     GLU B   470                                                      
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    ARG A 260   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ASP B 410   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A 313       41.85   -104.64                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED                              
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2XY A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 351                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1X0O   RELATED DB: PDB                                   
REMARK 900 NMR STRUCTURE OF THE ARNT C-TERMINAL PAS DOMAIN                      
REMARK 900 RELATED ID: 1P97   RELATED DB: PDB                                   
REMARK 900 NMR STRUCTURE OF THE HIF2 ALPHA C-TERMINAL PAS DOMAIN                
REMARK 900 RELATED ID: 2B02   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE ARNT C-TERMINAL PAS DOMAIN                  
REMARK 900 RELATED ID: 2A24   RELATED DB: PDB                                   
REMARK 900 NMR-GUIDED MODEL OF THE HETERODIMER OF THE WILD-TYPE HIF2 ALPHA AND  
REMARK 900 ARNT C-TERMINAL PAS DOMAINS                                          
REMARK 900 RELATED ID: 3F1N   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3F1P   RELATED DB: PDB                                   
DBREF  3F1O A  239   350  UNP    Q99814   EPAS1_HUMAN    239    350             
DBREF  3F1O B  356   470  UNP    P27540   ARNT_HUMAN     356    470             
SEQADV 3F1O GLY A  234  UNP  Q99814              EXPRESSION TAG                 
SEQADV 3F1O GLU A  235  UNP  Q99814              EXPRESSION TAG                 
SEQADV 3F1O PHE A  236  UNP  Q99814              EXPRESSION TAG                 
SEQADV 3F1O LYS A  237  UNP  Q99814              EXPRESSION TAG                 
SEQADV 3F1O GLY A  238  UNP  Q99814              EXPRESSION TAG                 
SEQADV 3F1O GLU A  247  UNP  Q99814    ARG   247 ENGINEERED                     
SEQADV 3F1O GLY B  350  UNP  P27540              EXPRESSION TAG                 
SEQADV 3F1O GLU B  351  UNP  P27540              EXPRESSION TAG                 
SEQADV 3F1O PHE B  352  UNP  P27540              EXPRESSION TAG                 
SEQADV 3F1O LYS B  353  UNP  P27540              EXPRESSION TAG                 
SEQADV 3F1O GLY B  354  UNP  P27540              EXPRESSION TAG                 
SEQADV 3F1O LEU B  355  UNP  P27540              EXPRESSION TAG                 
SEQADV 3F1O ARG B  362  UNP  P27540    GLU   362 ENGINEERED                     
SEQRES   1 A  117  GLY GLU PHE LYS GLY LEU ASP SER LYS THR PHE LEU SER          
SEQRES   2 A  117  GLU HIS SER MET ASP MET LYS PHE THR TYR CYS ASP ASP          
SEQRES   3 A  117  ARG ILE THR GLU LEU ILE GLY TYR HIS PRO GLU GLU LEU          
SEQRES   4 A  117  LEU GLY ARG SER ALA TYR GLU PHE TYR HIS ALA LEU ASP          
SEQRES   5 A  117  SER GLU ASN MET THR LYS SER HIS GLN ASN LEU CYS THR          
SEQRES   6 A  117  LYS GLY GLN VAL VAL SER GLY GLN TYR ARG MET LEU ALA          
SEQRES   7 A  117  LYS HIS GLY GLY TYR VAL TRP LEU GLU THR GLN GLY THR          
SEQRES   8 A  117  VAL ILE TYR ASN PRO ARG ASN LEU GLN PRO GLN CYS ILE          
SEQRES   9 A  117  MET CYS VAL ASN TYR VAL LEU SER GLU ILE GLU LYS ASN          
SEQRES   1 B  121  GLY GLU PHE LYS GLY LEU ASN VAL CYS GLN PRO THR ARG          
SEQRES   2 B  121  PHE ILE SER ARG HIS ASN ILE GLU GLY ILE PHE THR PHE          
SEQRES   3 B  121  VAL ASP HIS ARG CYS VAL ALA THR VAL GLY TYR GLN PRO          
SEQRES   4 B  121  GLN GLU LEU LEU GLY LYS ASN ILE VAL GLU PHE CYS HIS          
SEQRES   5 B  121  PRO GLU ASP GLN GLN LEU LEU ARG ASP SER PHE GLN GLN          
SEQRES   6 B  121  VAL VAL LYS LEU LYS GLY GLN VAL LEU SER VAL MET PHE          
SEQRES   7 B  121  ARG PHE ARG SER LYS ASN GLN GLU TRP LEU TRP MET ARG          
SEQRES   8 B  121  THR SER SER PHE THR PHE GLN ASN PRO TYR SER ASP GLU          
SEQRES   9 B  121  ILE GLU TYR ILE ILE CYS THR ASN THR ASN VAL LYS ASN          
SEQRES  10 B  121  SER SER GLN GLU                                              
HET    2XY  A   1      20                                                       
HET    EDO  A 351      10                                                       
HETNAM     2XY N-[2-NITRO-4-(TRIFLUOROMETHYL)PHENYL]MORPHOLIN-4-AMINE           
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  2XY    C11 H12 F3 N3 O3                                             
FORMUL   4  EDO    C2 H6 O2                                                     
FORMUL   5  HOH   *185(H2 O)                                                    
HELIX    1   1 LEU A  239  SER A  241  5                                   3    
HELIX    2   2 ARG A  260  ILE A  265  1                                   6    
HELIX    3   3 PRO A  269  LEU A  272  1                                   4    
HELIX    4   4 ALA A  277  PHE A  280  5                                   4    
HELIX    5   5 LEU A  284  LYS A  299  1                                  16    
HELIX    6   6 ARG B  379  VAL B  384  1                                   6    
HELIX    7   7 PRO B  388  LEU B  392  1                                   5    
HELIX    8   8 ILE B  396  CYS B  400  5                                   5    
HELIX    9   9 ASP B  404  LYS B  417  1                                  14    
SHEET    1   A 5 PHE A 254  CYS A 257  0                                        
SHEET    2   A 5 THR A 243  HIS A 248 -1  N  GLU A 247   O  THR A 255           
SHEET    3   A 5 CYS A 336  VAL A 343 -1  O  CYS A 339   N  SER A 246           
SHEET    4   A 5 TYR A 316  ILE A 326 -1  N  THR A 324   O  MET A 338           
SHEET    5   A 5 GLN A 301  LEU A 310 -1  N  VAL A 302   O  LEU A 319           
SHEET    1   B 5 PHE A 254  CYS A 257  0                                        
SHEET    2   B 5 THR A 243  HIS A 248 -1  N  GLU A 247   O  THR A 255           
SHEET    3   B 5 CYS A 336  VAL A 343 -1  O  CYS A 339   N  SER A 246           
SHEET    4   B 5 TYR A 316  ILE A 326 -1  N  THR A 324   O  MET A 338           
SHEET    1   C 5 PHE B 373  VAL B 376  0                                        
SHEET    2   C 5 ARG B 362  HIS B 367 -1  N  ARG B 366   O  THR B 374           
SHEET    3   C 5 TYR B 456  ASN B 463 -1  O  CYS B 459   N  SER B 365           
SHEET    4   C 5 TRP B 436  PHE B 446 -1  N  PHE B 444   O  ILE B 458           
SHEET    5   C 5 LEU B 423  ARG B 430 -1  N  PHE B 427   O  MET B 439           
SITE     1 AC1 16 SER A 246  HIS A 248  MET A 252  PHE A 254                    
SITE     2 AC1 16 ALA A 277  TYR A 281  MET A 289  SER A 292                    
SITE     3 AC1 16 HIS A 293  VAL A 302  SER A 304  TYR A 307                    
SITE     4 AC1 16 MET A 309  THR A 321  CYS A 339  ASN A 341                    
SITE     1 AC2  9 HOH A 161  TYR A 278  TYR A 281  SER A 286                    
SITE     2 AC2  9 GLU B 398  CYS B 400  PRO B 402  GLN B 405                    
SITE     3 AC2  9 ARG B 430                                                     
CRYST1   73.761   83.019   41.553  90.00 106.36  90.00 C 1 2 1       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      0.013557  0.000000  0.003980        0.00000                         
SCALE2      0.000000  0.012045  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.025081        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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