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Database: PDB
Entry: 6D0C
LinkDB: 6D0C
Original site: 6D0C 
HEADER    TRANSCRIPTION                           10-APR-18   6D0C              
TITLE     CRYSTAL STRUCTURE OF 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: RESIDUES 239-350;                                          
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 MUTATION: YES;                                                       
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: ARYL HYDROCARBON RECEPTOR NUCLEAR TRANSLOCATOR;            
COMPND  13 CHAIN: B;                                                            
COMPND  14 FRAGMENT: RESIDUES 356-470;                                          
COMPND  15 SYNONYM: ARNT PROTEIN,CLASS E BASIC HELIX-LOOP-HELIX PROTEIN 2,      
COMPND  16 BHLHE2,DIOXIN RECEPTOR,NUCLEAR TRANSLOCATOR,HYPOXIA-INDUCIBLE FACTOR 
COMPND  17 1-BETA,HIF1-BETA;                                                    
COMPND  18 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;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
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;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HIF2A, PAS B DOMAIN, ARNT, HYPOXIA INDUCIBLE FACTOR, EPAS1,           
KEYWDS   2 TRANSCRIPTION                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.DU                                                                  
REVDAT   1   31-OCT-18 6D0C    0                                                
JRNL        AUTH   X.DU                                                         
JRNL        TITL   CRYSTAL STRUCTURE OF PT1940 BOUND TO HIF2A-B*:ARNT-B*        
JRNL        TITL 2 COMPLEX                                                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.88                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 35386                          
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) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1876                            
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) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2268                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.19                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3550                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 116                          
REMARK   3   BIN FREE R VALUE                    : 0.4480                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1797                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 128                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.66                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.63000                                              
REMARK   3    B22 (A**2) : -0.51000                                             
REMARK   3    B33 (A**2) : 0.14000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.45000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.084         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.086         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.065         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.783         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.946                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1849 ; 0.024 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2495 ; 2.390 ; 1.931       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   217 ; 6.869 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    97 ;37.094 ;24.227       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   324 ;15.023 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;12.740 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   266 ; 0.169 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1407 ; 0.016 ; 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 6D0C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000233823.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-DEC-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
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) : 0.97901                            
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-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37270                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 29.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.55                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.100                              
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: 4XT2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: BIS-TRIS, PH5.4 AND 16% PEG3350,         
REMARK 280  SEEDING WITH CRUSHED CRYSTALS RIGHT AFTER SETUP, 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       36.80200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.41450            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       36.80200            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       41.41450            
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: 1800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       48.63457            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000      -41.41450            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -39.59060            
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 B 502  LIES ON A SPECIAL POSITION.                          
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    -2                                                      
REMARK 465     GLU A    -1                                                      
REMARK 465     ARG A   330                                                      
REMARK 465     ASN A   331                                                      
REMARK 465     LEU A   332                                                      
REMARK 465     GLN A   333                                                      
REMARK 465     LYS A   349                                                      
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     VAL B   357                                                      
REMARK 465     SER B   468                                                      
REMARK 465     GLN B   469                                                      
REMARK 465     GLU B   470                                                      
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   OE1  GLU B   398     O    HOH B   501              1.84            
REMARK 500   O    HOH B   572     O    HOH B   574              2.15            
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    GLY A   2   C     LEU A 239   N       0.258                       
REMARK 500    TRP B 436   CE2   TRP B 436   CD2     0.083                       
REMARK 500    TRP B 438   CE2   TRP B 438   CD2     0.089                       
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    GLY A   2   O   -  C   -  N   ANGL. DEV. = -16.3 DEGREES          
REMARK 500    ASP A 258   N   -  CA  -  CB  ANGL. DEV. = -16.7 DEGREES          
REMARK 500    ASP A 258   CB  -  CG  -  OD2 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500    LEU A 319   CA  -  CB  -  CG  ANGL. DEV. =  16.1 DEGREES          
REMARK 500    MET A 338   CG  -  SD  -  CE  ANGL. DEV. = -11.2 DEGREES          
REMARK 500    ARG B 409   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES          
REMARK 500    ARG B 409   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ARG B 428   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    MET B 439   CG  -  SD  -  CE  ANGL. DEV. = -10.5 DEGREES          
REMARK 500    PHE B 446   CB  -  CG  -  CD1 ANGL. DEV. =  -4.8 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       44.51   -103.81                                   
REMARK 500    ASN A 328     -136.68   -101.74                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    GLY A   2         21.36                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6CZW   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN CRYSTAL                                                 
DBREF  6D0C A  239   350  UNP    Q99814   EPAS1_HUMAN    239    350             
DBREF  6D0C B  356   470  UNP    P27540   ARNT_HUMAN     356    470             
SEQADV 6D0C GLY A   -2  UNP  Q99814              EXPRESSION TAG                 
SEQADV 6D0C GLU A   -1  UNP  Q99814              EXPRESSION TAG                 
SEQADV 6D0C PHE A    0  UNP  Q99814              EXPRESSION TAG                 
SEQADV 6D0C LYS A    1  UNP  Q99814              EXPRESSION TAG                 
SEQADV 6D0C GLY A    2  UNP  Q99814              EXPRESSION TAG                 
SEQADV 6D0C GLU A  247  UNP  Q99814    ARG   247 ENGINEERED MUTATION            
SEQADV 6D0C GLY B  350  UNP  P27540              EXPRESSION TAG                 
SEQADV 6D0C GLU B  351  UNP  P27540              EXPRESSION TAG                 
SEQADV 6D0C PHE B  352  UNP  P27540              EXPRESSION TAG                 
SEQADV 6D0C LYS B  353  UNP  P27540              EXPRESSION TAG                 
SEQADV 6D0C GLY B  354  UNP  P27540              EXPRESSION TAG                 
SEQADV 6D0C LEU B  355  UNP  P27540              EXPRESSION TAG                 
SEQADV 6D0C ARG B  362  UNP  P27540    GLU   362 ENGINEERED MUTATION            
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                                              
FORMUL   3  HOH   *128(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  391  5                                   5    
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  CYS A 339   N  SER A 246           
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  CYS A 339   N  SER A 246           
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  PHE B 444   O  ILE B 458           
SHEET    5 AA3 5 LEU B 423  ARG B 430 -1  N  PHE B 427   O  MET B 439           
CRYST1   73.604   82.829   41.321  90.00 106.64  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      0.013586  0.000000  0.004059        0.00000                         
SCALE2      0.000000  0.012073  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.025258        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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