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Database: PDB
Entry: 5UFP
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HEADER    TRANSCRIPTION                           05-JAN-17   5UFP              
TITLE     CRYSTAL STRUCTURE OF PT2399 BOUND TO HIF2A-B*:ARNT-B* COMPLEX         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDOTHELIAL PAS DOMAIN-CONTAINING PROTEIN 1;               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 239-348;                                      
COMPND   5 SYNONYM: EPAS-1,BASIC-HELIX-LOOP-HELIX-PAS PROTEIN MOP2,CLASS E BASIC
COMPND   6 HELIX-LOOP-HELIX PROTEIN 73,BHLHE73,HIF-1-ALPHA-LIKE FACTOR,HLF,     
COMPND   7 HYPOXIA-INDUCIBLE FACTOR 2-ALPHA,HIF2-ALPHA,MEMBER OF PAS PROTEIN 2, 
COMPND   8 PAS DOMAIN-CONTAINING PROTEIN 2;                                     
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: ARYL HYDROCARBON RECEPTOR NUCLEAR TRANSLOCATOR;            
COMPND  12 CHAIN: B;                                                            
COMPND  13 FRAGMENT: UNP RESIDUES 342-453;                                      
COMPND  14 SYNONYM: ARNT PROTEIN,CLASS E BASIC HELIX-LOOP-HELIX PROTEIN 2,      
COMPND  15 BHLHE2,DIOXIN RECEPTOR,NUCLEAR TRANSLOCATOR,HYPOXIA-INDUCIBLE FACTOR 
COMPND  16 1-BETA,HIF1-BETA;                                                    
COMPND  17 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: EPAS1, BHLHE73, HIF2A, MOP2, PASD2;                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';        
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 866768;                                     
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: ARNT, BHLHE2;                                                  
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';        
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 866768                                      
KEYWDS    HIF2 INHIBITOR HIF2 LIGAND PAS-B HYPOXIA INDUCIBLE FACTOR 2 EPAS1,    
KEYWDS   2 TRANSCRIPTION                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.DU                                                                  
REVDAT   2   22-NOV-17 5UFP    1       REMARK                                   
REVDAT   1   25-JAN-17 5UFP    0                                                
SPRSDE     25-JAN-17 5UFP      5T0T                                             
JRNL        AUTH   H.CHO,X.DU,J.P.RIZZI,E.LIBERZON,A.A.CHAKRABORTY,W.GAO,       
JRNL        AUTH 2 I.CARVO,S.SIGNORETTI,R.K.BRUICK,J.A.JOSEY,E.M.WALLACE,       
JRNL        AUTH 3 W.G.KAELIN                                                   
JRNL        TITL   ON-TARGET EFFICACY OF A HIF-2 ALPHA ANTAGONIST IN            
JRNL        TITL 2 PRECLINICAL KIDNEY CANCER MODELS.                            
JRNL        REF    NATURE                        V. 539   107 2016              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   27595393                                                     
JRNL        DOI    10.1038/NATURE19795                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.89                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 18032                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.221                           
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 975                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1283                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.90                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3440                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 66                           
REMARK   3   BIN FREE R VALUE                    : 0.4020                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1756                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 60                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.04                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.69000                                              
REMARK   3    B22 (A**2) : -0.98000                                             
REMARK   3    B33 (A**2) : -1.85000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.23000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.176         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.168         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.149         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.307         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1838 ; 0.020 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2490 ; 2.140 ; 1.950       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   213 ; 7.381 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    95 ;39.381 ;24.211       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   315 ;16.603 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;19.147 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   265 ; 0.150 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1399 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 5UFP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JAN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000225734.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUL-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 5.4                                
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) : 0.97                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000, DENZO                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18032                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.890                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.07700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.99                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 50.00                    
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.03200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 49.00                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: RECTANGULAR RODS                                             
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: COMPLEX OF HIF2-B*:ARNT-B* 10-12 MG/ML   
REMARK 280  IN 10 MM TRIS-HCL, PH8.0 AND 50 MM KCL; CRYSTALLIZATION BUFFER      
REMARK 280  OF 50 MM BIS-TRIS, PH5.4 AND 16% PEG3350., VAPOR DIFFUSION,         
REMARK 280  HANGING DROP, 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       36.68950            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.02850            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       36.68950            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       42.02850            
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 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     PHE A   236                                                      
REMARK 465     LEU A   237                                                      
REMARK 465     GLY A   238                                                      
REMARK 465     ARG A   330                                                      
REMARK 465     ASN A   331                                                      
REMARK 465     LEU A   332                                                      
REMARK 465     GLN A   333                                                      
REMARK 465     ILE A   347                                                      
REMARK 465     GLU A   348                                                      
REMARK 465     GLY B   351                                                      
REMARK 465     GLU B   352                                                      
REMARK 465     PHE B   353                                                      
REMARK 465     LEU B   354                                                      
REMARK 465     GLY B   355                                                      
REMARK 465     ASN B   356                                                      
REMARK 465     VAL 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   OH   TYR A   278     OG1  THR A   290              1.96            
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   OD1  ASP B   410     OD1  ASP B   410     2554     1.69            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS B 367   CG    HIS B 367   CD2     0.061                       
REMARK 500    HIS B 401   CG    HIS B 401   CD2     0.058                       
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    ARG A 275   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    LEU A 319   CA  -  CB  -  CG  ANGL. DEV. =  15.6 DEGREES          
REMARK 500    ARG B 409   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 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    MET A 252       -1.96     71.35                                   
REMARK 500    ARG A 260      -19.40    -49.71                                   
REMARK 500    ASN A 328     -132.86   -105.47                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 86D A 401                 
DBREF  5UFP A  239   348  UNP    Q99814   EPAS1_HUMAN    239    348             
DBREF  5UFP B  356   467  UNP    P27540   ARNT_HUMAN     342    453             
SEQADV 5UFP GLY A  234  UNP  Q99814              EXPRESSION TAG                 
SEQADV 5UFP GLU A  235  UNP  Q99814              EXPRESSION TAG                 
SEQADV 5UFP PHE A  236  UNP  Q99814              EXPRESSION TAG                 
SEQADV 5UFP LEU A  237  UNP  Q99814              EXPRESSION TAG                 
SEQADV 5UFP GLY A  238  UNP  Q99814              EXPRESSION TAG                 
SEQADV 5UFP GLU A  247  UNP  Q99814    ARG   247 ENGINEERED MUTATION            
SEQADV 5UFP GLY B  351  UNP  P27540              EXPRESSION TAG                 
SEQADV 5UFP GLU B  352  UNP  P27540              EXPRESSION TAG                 
SEQADV 5UFP PHE B  353  UNP  P27540              EXPRESSION TAG                 
SEQADV 5UFP LEU B  354  UNP  P27540              EXPRESSION TAG                 
SEQADV 5UFP GLY B  355  UNP  P27540              EXPRESSION TAG                 
SEQADV 5UFP ARG B  362  UNP  P27540    GLU   348 ENGINEERED MUTATION            
SEQRES   1 A  115  GLY GLU PHE LEU GLY LEU ASP SER LYS THR PHE LEU SER          
SEQRES   2 A  115  GLU HIS SER MET ASP MET LYS PHE THR TYR CYS ASP ASP          
SEQRES   3 A  115  ARG ILE THR GLU LEU ILE GLY TYR HIS PRO GLU GLU LEU          
SEQRES   4 A  115  LEU GLY ARG SER ALA TYR GLU PHE TYR HIS ALA LEU ASP          
SEQRES   5 A  115  SER GLU ASN MET THR LYS SER HIS GLN ASN LEU CYS THR          
SEQRES   6 A  115  LYS GLY GLN VAL VAL SER GLY GLN TYR ARG MET LEU ALA          
SEQRES   7 A  115  LYS HIS GLY GLY TYR VAL TRP LEU GLU THR GLN GLY THR          
SEQRES   8 A  115  VAL ILE TYR ASN PRO ARG ASN LEU GLN PRO GLN CYS ILE          
SEQRES   9 A  115  MET CYS VAL ASN TYR VAL LEU SER GLU ILE GLU                  
SEQRES   1 B  117  GLY GLU PHE LEU GLY ASN VAL CYS GLN PRO THR ARG PHE          
SEQRES   2 B  117  ILE SER ARG HIS ASN ILE GLU GLY ILE PHE THR PHE VAL          
SEQRES   3 B  117  ASP HIS ARG CYS VAL ALA THR VAL GLY TYR GLN PRO GLN          
SEQRES   4 B  117  GLU LEU LEU GLY LYS ASN ILE VAL GLU PHE CYS HIS PRO          
SEQRES   5 B  117  GLU ASP GLN GLN LEU LEU ARG ASP SER PHE GLN GLN VAL          
SEQRES   6 B  117  VAL LYS LEU LYS GLY GLN VAL LEU SER VAL MET PHE ARG          
SEQRES   7 B  117  PHE ARG SER LYS ASN GLN GLU TRP LEU TRP MET ARG THR          
SEQRES   8 B  117  SER SER PHE THR PHE GLN ASN PRO TYR SER ASP GLU ILE          
SEQRES   9 B  117  GLU TYR ILE ILE CYS THR ASN THR ASN VAL LYS ASN SER          
HET    86D  A 401      28                                                       
HETNAM     86D 3-({(1S)-7-[(DIFLUOROMETHYL)SULFONYL]-2,2-DIFLUORO-1-            
HETNAM   2 86D  HYDROXY-2,3-DIHYDRO-1H-INDEN-4-YL}OXY)-5-                       
HETNAM   3 86D  FLUOROBENZONITRILE                                              
FORMUL   3  86D    C17 H10 F5 N O4 S                                            
FORMUL   4  HOH   *60(H2 O)                                                     
HELIX    1 AA1 LEU A  239  SER A  241  5                                   3    
HELIX    2 AA2 ARG A  260  GLY A  266  1                                   7    
HELIX    3 AA3 HIS A  268  LEU A  273  1                                   6    
HELIX    4 AA4 SER A  276  TYR A  281  5                                   6    
HELIX    5 AA5 HIS A  282  LEU A  284  5                                   3    
HELIX    6 AA6 ASP A  285  GLY A  300  1                                  16    
HELIX    7 AA7 ARG B  379  GLY B  385  1                                   7    
HELIX    8 AA8 GLN B  387  LEU B  392  1                                   6    
HELIX    9 AA9 ASN B  395  CYS B  400  5                                   6    
HELIX   10 AB1 HIS B  401  GLU B  403  5                                   3    
HELIX   11 AB2 ASP B  404  VAL B  416  1                                  13    
SHEET    1 AA1 5 PHE A 254  CYS A 257  0                                        
SHEET    2 AA1 5 THR A 243  HIS A 248 -1  N  GLU A 247   O  THR A 255           
SHEET    3 AA1 5 CYS A 336  VAL A 343 -1  O  ILE A 337   N  HIS A 248           
SHEET    4 AA1 5 TYR A 316  ILE A 326 -1  N  ILE A 326   O  CYS A 336           
SHEET    5 AA1 5 GLN A 301  VAL A 303 -1  N  VAL A 302   O  GLY A 323           
SHEET    1 AA2 5 PHE A 254  CYS A 257  0                                        
SHEET    2 AA2 5 THR A 243  HIS A 248 -1  N  GLU A 247   O  THR A 255           
SHEET    3 AA2 5 CYS A 336  VAL A 343 -1  O  ILE A 337   N  HIS A 248           
SHEET    4 AA2 5 TYR A 316  ILE A 326 -1  N  ILE A 326   O  CYS A 336           
SHEET    5 AA2 5 TYR A 307  LEU A 310 -1  N  TYR A 307   O  LEU A 319           
SHEET    1 AA3 5 PHE B 373  VAL B 376  0                                        
SHEET    2 AA3 5 ARG B 362  HIS B 367 -1  N  ARG B 366   O  THR B 374           
SHEET    3 AA3 5 TYR B 456  ASN B 463 -1  O  CYS B 459   N  SER B 365           
SHEET    4 AA3 5 TRP B 436  PHE B 446 -1  N  ARG B 440   O  THR B 462           
SHEET    5 AA3 5 LEU B 423  ARG B 430 -1  N  LEU B 423   O  SER B 443           
SITE     1 AC1 18 PHE A 244  HIS A 248  MET A 252  ALA A 277                    
SITE     2 AC1 18 PHE A 280  TYR A 281  MET A 289  SER A 292                    
SITE     3 AC1 18 HIS A 293  LEU A 296  SER A 304  TYR A 307                    
SITE     4 AC1 18 MET A 309  THR A 321  ILE A 337  CYS A 339                    
SITE     5 AC1 18 ASN A 341  HOH A 504                                          
CRYST1   73.379   84.057   41.472  90.00 106.48  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      0.013628  0.000000  0.004031        0.00000                         
SCALE2      0.000000  0.011897  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.025145        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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