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Database: PDB
Entry: 3H7W
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HEADER    TRANSCRIPTION                           28-APR-09   3H7W              
TITLE     CRYSTAL STRUCTURE OF THE HIGH AFFINITY HETERODIMER OF HIF2            
TITLE    2 ALPHA AND ARNT C-TERMINAL PAS DOMAINS WITH THE ARTIFICIAL            
TITLE    3 LIGAND THS017                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDOTHELIAL PAS DOMAIN-CONTAINING PROTEIN 1;               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: HIF2ALPHA C-TERMINAL PAS DOMAIN (UNP RESIDUES 239          
COMPND   5 TO 350);                                                             
COMPND   6 SYNONYM: EPAS-1, MEMBER OF PAS PROTEIN 2, BASIC-HELIX-LOOP-          
COMPND   7 HELIX-PAS PROTEIN MOP2, HYPOXIA-INDUCIBLE FACTOR 2 ALPHA,            
COMPND   8 HIF-2 ALPHA, HIF2 ALPHA, HIF-1 ALPHA-LIKE FACTOR, HLF;               
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: ARNT C-TERMINAL PAS DOMAIN (UNP RESIDUES 356 TO            
COMPND  15 470);                                                                
COMPND  16 SYNONYM: ARNT PROTEIN, CLASS E BASIC HELIX-LOOP-HELIX                
COMPND  17 PROTEIN 2, BHLHE2, DIOXIN RECEPTOR, NUCLEAR TRANSLOCATOR,            
COMPND  18 HYPOXIA-INDUCIBLE FACTOR 1 BETA, HIF-1 BETA;                         
COMPND  19 ENGINEERED: YES;                                                     
COMPND  20 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(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PHIS-GB1-HIF2APAS-B;                      
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: ARNT, ARYL HYDROCARBON RECEPTOR NUCLEAR TRANSLOCATOR,          
SOURCE  16 BHLHE2;                                                              
SOURCE  17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  19 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  21 EXPRESSION_SYSTEM_PLASMID: PHIS-GB1-ARNT-PAS-B                       
KEYWDS    PAS DOMAIN, HETERODIMER, PROTEIN LIGAND COMPLEX., ACTIVATOR,          
KEYWDS   2 ANGIOGENESIS, CONGENITAL ERYTHROCYTOSIS, DEVELOPMENTAL               
KEYWDS   3 PROTEIN, DIFFERENTIATION, DISEASE MUTATION, DNA-BINDING,             
KEYWDS   4 HYDROXYLATION, NUCLEUS, PHOSPHOPROTEIN, TRANSCRIPTION,               
KEYWDS   5 TRANSCRIPTION REGULATION, UBL CONJUGATION, ALTERNATIVE               
KEYWDS   6 SPLICING, POLYMORPHISM                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.KEY,T.H.SCHEUERMANN,P.C.ANDERSON,V.DAGGETT,K.H.GARDNER            
REVDAT   1   12-JAN-10 3H7W    0                                                
JRNL        AUTH   J.KEY,T.H.SCHEUERMANN,P.C.ANDERSON,V.DAGGETT,                
JRNL        AUTH 2 K.H.GARDNER                                                  
JRNL        TITL   PRINCIPLES OF LIGAND BINDING WITHIN A COMPLETELY             
JRNL        TITL 2 BURIED CAVITY IN HIF2ALPHA PAS-B                             
JRNL        REF    J.AM.CHEM.SOC.                V. 131 17647 2009              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   19950993                                                     
JRNL        DOI    10.1021/JA9073062                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.71                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 28092                          
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) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1409                            
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) : 1.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.68                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1827                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.20                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2980                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 103                          
REMARK   3   BIN FREE R VALUE                    : 0.3720                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1857                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 182                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.49                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.111         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.111         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.073         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.094         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1913 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2594 ; 1.481 ; 1.943       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   234 ; 6.839 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    95 ;38.129 ;24.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   337 ;13.196 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;16.084 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   276 ; 0.102 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1466 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   864 ; 0.214 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1334 ; 0.303 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   143 ; 0.100 ; 0.200       
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):    50 ; 0.206 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    24 ; 0.204 ; 0.200       
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):  1167 ; 1.027 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1840 ; 1.588 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   875 ; 2.452 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   750 ; 3.559 ; 4.500       
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: NULL                                      
REMARK   4                                                                      
REMARK   4 3H7W COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAY-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB052803.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-DEC-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97915                            
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-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28092                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.06300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.68                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51900                            
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: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3F1P                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BISTRIS, 17% PEG3350, PH 6.0,       
REMARK 280  VAPOR DIFFUSION, SITTING 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       36.94500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.36350            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       36.94500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       41.36350            
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 300 REMARK: TO GENERATE THE BIOLOGICALLY RELEVANT COMPLEX, THE           
REMARK 300 SYMMETRY OPERATOR (1/2-X,Y-1/2,1-Z) SHOULD APPLIED TO CHAIN B.       
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: 1830 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10750 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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     ASN A   328                                                      
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     VAL B   357                                                      
REMARK 465     SER B   468                                                      
REMARK 465     GLN B   469                                                      
REMARK 465     GLU B   470                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A  263   CD    OE1   OE2                                     
REMARK 480     GLN A  301   CD    OE1   NE2                                     
REMARK 480     LYS A  349   CE    NZ                                            
REMARK 480     GLN B  359   CG    CD    OE1   NE2                               
REMARK 480     GLU B  455   CD    OE1   OE2                                     
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    LYS A 349   CD    LYS A 349   CE     -1.009                       
REMARK 500    GLU B 455   CG    GLU B 455   CD     -0.093                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LYS A 349   CG  -  CD  -  CE  ANGL. DEV. =  21.5 DEGREES          
REMARK 500    LYS A 349   CD  -  CE  -  NZ  ANGL. DEV. =  16.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 168        DISTANCE =  6.32 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 018 A 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3F1O   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HIGH AFFINITY HETERODIMER OF HIF2           
REMARK 900 C-TERMINAL PAS DOMAINS IN COMPLEX WITH THE ARTIFICIAL                
REMARK 900 LIGAND THS-044.                                                      
REMARK 900 RELATED ID: 3F1P   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE APO-HIGH AFFINITY HIF2 PAS-B                
REMARK 900 HETERODIMER.                                                         
REMARK 900 RELATED ID: 3F1N   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HIGH AFFINITY HETERODIMER OF HIF2           
REMARK 900 C-TERMINAL PAS DOMAINS WITH INTERNALLY BOUND ETHYLENE                
REMARK 900 GLYCOL.                                                              
REMARK 900 RELATED ID: 1P97   RELATED DB: PDB                                   
REMARK 900 SOLUTION NMR STRUCTURE OF THE HIF2ALPHA C-TERMINAL PAS               
REMARK 900 DOMAIN.                                                              
REMARK 900 RELATED ID: 1X0O   RELATED DB: PDB                                   
REMARK 900 SOLUTION NMR 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 WILD-TYPE HIF2ALPHA           
REMARK 900 AND ARNT 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: 3H82   RELATED DB: PDB                                   
REMARK 900 HETERODIMER OF HIF2 ALPHA AND ARNT C-TERMINAL PAS DOMAINS            
REMARK 900 WITH THE ARTIFICIAL LIGAND THS020                                    
DBREF  3H7W A  239   350  UNP    Q99814   EPAS1_HUMAN    239    350             
DBREF  3H7W B  356   470  UNP    P27540   ARNT_HUMAN     356    470             
SEQADV 3H7W GLY A  234  UNP  Q99814              EXPRESSION TAG                 
SEQADV 3H7W GLU A  235  UNP  Q99814              EXPRESSION TAG                 
SEQADV 3H7W PHE A  236  UNP  Q99814              EXPRESSION TAG                 
SEQADV 3H7W LYS A  237  UNP  Q99814              EXPRESSION TAG                 
SEQADV 3H7W GLY A  238  UNP  Q99814              EXPRESSION TAG                 
SEQADV 3H7W GLU A  247  UNP  Q99814    ARG   247 ENGINEERED                     
SEQADV 3H7W GLY B  350  UNP  P27540              EXPRESSION TAG                 
SEQADV 3H7W GLU B  351  UNP  P27540              EXPRESSION TAG                 
SEQADV 3H7W PHE B  352  UNP  P27540              EXPRESSION TAG                 
SEQADV 3H7W LYS B  353  UNP  P27540              EXPRESSION TAG                 
SEQADV 3H7W GLY B  354  UNP  P27540              EXPRESSION TAG                 
SEQADV 3H7W LEU B  355  UNP  P27540              EXPRESSION TAG                 
SEQADV 3H7W 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    018  A   1      20                                                       
HETNAM     018 2-NITRO-N-(THIOPHEN-3-YLMETHYL)-4-(TRIFLUOROMETHYL)              
HETNAM   2 018  ANILINE                                                         
FORMUL   3  018    C12 H9 F3 N2 O2 S                                            
FORMUL   4  HOH   *182(H2 O)                                                    
HELIX    1   1 LEU A  239  SER A  241  5                                   3    
HELIX    2   2 ARG A  260  GLY A  266  1                                   7    
HELIX    3   3 HIS A  268  LEU A  273  1                                   6    
HELIX    4   4 SER A  276  TYR A  281  5                                   6    
HELIX    5   5 HIS A  282  LEU A  284  5                                   3    
HELIX    6   6 ASP A  285  GLY A  300  1                                  16    
HELIX    7   7 ARG B  379  GLY B  385  1                                   7    
HELIX    8   8 GLN B  387  LEU B  391  5                                   5    
HELIX    9   9 ASN B  395  CYS B  400  5                                   6    
HELIX   10  10 ASP B  404  VAL B  416  1                                  13    
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  ILE A 326   O  CYS A 336           
SHEET    5   A 5 GLN A 301  VAL A 303 -1  N  VAL A 302   O  GLY A 323           
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  ILE A 326   O  CYS A 336           
SHEET    5   B 5 TYR A 307  LEU A 310 -1  N  MET A 309   O  VAL A 317           
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 429   O  LEU B 437           
SITE     1 AC1 14 HIS A 248  MET A 252  ALA A 277  TYR A 281                    
SITE     2 AC1 14 MET A 289  SER A 292  HIS A 293  VAL A 302                    
SITE     3 AC1 14 SER A 304  TYR A 307  MET A 309  THR A 321                    
SITE     4 AC1 14 CYS A 339  ASN A 341                                          
CRYST1   73.890   82.727   41.158  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      0.013534  0.000000  0.004003        0.00000                         
SCALE2      0.000000  0.012088  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.025337        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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