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Database: PDB
Entry: 3D57
LinkDB: 3D57
Original site: 3D57 
HEADER    HORMONE, TRANSCRIPTION RECEPTOR         15-MAY-08   3D57              
TITLE     TR VARIANT D355R                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THYROID HORMONE RECEPTOR BETA;                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: C-TERMINAL DOMAIN;                                         
COMPND   5 SYNONYM: NUCLEAR RECEPTOR SUBFAMILY 1 GROUP A MEMBER 2;              
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 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: 7068, ERBA2, NR1A2, THR1, THRB;                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PETDUET-1                                 
KEYWDS    THYROID HORMONE RECEPTOR, LIGAND BINDING DOMAIN, D355R MUTANT,        
KEYWDS   2 HOMODIMER, ALTERNATIVE SPLICING, DEAFNESS, DISEASE MUTATION, DNA-    
KEYWDS   3 BINDING, METAL-BINDING, NUCLEUS, POLYMORPHISM, RECEPTOR,             
KEYWDS   4 TRANSCRIPTION, TRANSCRIPTION REGULATION, ZINC, ZINC-FINGER, HORMONE, 
KEYWDS   5 TRANSCRIPTION RECEPTOR                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.JOURAVEL                                                            
REVDAT   4   30-AUG-23 3D57    1       REMARK                                   
REVDAT   3   20-OCT-21 3D57    1       REMARK SEQADV                            
REVDAT   2   10-FEB-09 3D57    1       JRNL   VERSN                             
REVDAT   1   14-OCT-08 3D57    0                                                
JRNL        AUTH   N.JOURAVEL,E.SABLIN,M.TOGASHI,J.D.BAXTER,P.WEBB,             
JRNL        AUTH 2 R.J.FLETTERICK                                               
JRNL        TITL   MOLECULAR BASIS FOR DIMER FORMATION OF TRBETA VARIANT D355R. 
JRNL        REF    PROTEINS                      V.  75   111 2008              
JRNL        REFN                   ISSN 0887-3585                               
JRNL        PMID   18798561                                                     
JRNL        DOI    10.1002/PROT.22225                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 25784                          
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 SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 28545                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.37                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3917                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 47                                      
REMARK   3   SOLVENT ATOMS            : 105                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 29.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 5.30                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.77300                                              
REMARK   3    B22 (A**2) : 8.55500                                              
REMARK   3    B33 (A**2) : -9.32900                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.89900                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.197                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3D57 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAY-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000047606.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-SEP-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.115891                           
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28545                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY                : 2.700                              
REMARK 200  R MERGE                    (I) : 0.07800                            
REMARK 200  R SYM                      (I) : 0.06900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.37                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.22000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1NAX                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% ETHYLENE GLYCOL, PH 7.0, VAPOR       
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       46.48150            
REMARK 290   SMTRY3   2  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: 3220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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     MET A   195                                                      
REMARK 465     GLY A   196                                                      
REMARK 465     SER A   197                                                      
REMARK 465     SER A   198                                                      
REMARK 465     HIS A   199                                                      
REMARK 465     HIS A   200                                                      
REMARK 465     HIS A   201                                                      
REMARK 465     HIS A   202                                                      
REMARK 465     HIS A   203                                                      
REMARK 465     HIS A   204                                                      
REMARK 465     SER A   205                                                      
REMARK 465     GLN A   206                                                      
REMARK 465     ASP A   207                                                      
REMARK 465     PRO A   208                                                      
REMARK 465     GLY A   209                                                      
REMARK 465     ILE A   255                                                      
REMARK 465     VAL A   256                                                      
REMARK 465     ASN A   257                                                      
REMARK 465     ALA A   258                                                      
REMARK 465     PRO A   259                                                      
REMARK 465     GLU A   260                                                      
REMARK 465     MET B   195                                                      
REMARK 465     GLY B   196                                                      
REMARK 465     SER B   197                                                      
REMARK 465     SER B   198                                                      
REMARK 465     HIS B   199                                                      
REMARK 465     HIS B   200                                                      
REMARK 465     HIS B   201                                                      
REMARK 465     HIS B   202                                                      
REMARK 465     HIS B   203                                                      
REMARK 465     HIS B   204                                                      
REMARK 465     SER B   205                                                      
REMARK 465     GLN B   206                                                      
REMARK 465     ASP B   207                                                      
REMARK 465     PRO B   208                                                      
REMARK 465     GLY B   209                                                      
REMARK 465     HIS B   210                                                      
REMARK 465     VAL B   256                                                      
REMARK 465     ASN B   257                                                      
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    PRO A 247   CB  -  CA  -  C   ANGL. DEV. = -13.8 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    LYS A 411       41.98     76.57                                   
REMARK 500    ALA B 253      126.56    -35.62                                   
REMARK 500    GLU B 260       -7.18     73.61                                   
REMARK 500    GLU B 333      -26.61   -141.46                                   
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 4HY A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4HY B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 501                 
DBREF  3D57 A  209   460  UNP    P10828   THB_HUMAN      209    460             
DBREF  3D57 B  209   460  UNP    P10828   THB_HUMAN      209    460             
SEQADV 3D57 MET A  195  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 GLY A  196  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 SER A  197  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 SER A  198  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 HIS A  199  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 HIS A  200  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 HIS A  201  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 HIS A  202  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 HIS A  203  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 HIS A  204  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 SER A  205  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 GLN A  206  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 ASP A  207  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 PRO A  208  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 ARG A  355  UNP  P10828    ASP   355 ENGINEERED MUTATION            
SEQADV 3D57 MET B  195  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 GLY B  196  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 SER B  197  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 SER B  198  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 HIS B  199  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 HIS B  200  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 HIS B  201  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 HIS B  202  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 HIS B  203  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 HIS B  204  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 SER B  205  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 GLN B  206  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 ASP B  207  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 PRO B  208  UNP  P10828              EXPRESSION TAG                 
SEQADV 3D57 ARG B  355  UNP  P10828    ASP   355 ENGINEERED MUTATION            
SEQRES   1 A  266  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP          
SEQRES   2 A  266  PRO GLY HIS LYS PRO GLU PRO THR ASP GLU GLU TRP GLU          
SEQRES   3 A  266  LEU ILE LYS THR VAL THR GLU ALA HIS VAL ALA THR ASN          
SEQRES   4 A  266  ALA GLN GLY SER HIS TRP LYS GLN LYS ARG LYS PHE LEU          
SEQRES   5 A  266  PRO GLU ASP ILE GLY GLN ALA PRO ILE VAL ASN ALA PRO          
SEQRES   6 A  266  GLU GLY GLY LYS VAL ASP LEU GLU ALA PHE SER HIS PHE          
SEQRES   7 A  266  THR LYS ILE ILE THR PRO ALA ILE THR ARG VAL VAL ASP          
SEQRES   8 A  266  PHE ALA LYS LYS LEU PRO MET PHE CYS GLU LEU PRO CYS          
SEQRES   9 A  266  GLU ASP GLN ILE ILE LEU LEU LYS GLY CYS CYS MET GLU          
SEQRES  10 A  266  ILE MET SER LEU ARG ALA ALA VAL ARG TYR ASP PRO GLU          
SEQRES  11 A  266  SER GLU THR LEU THR LEU ASN GLY GLU MET ALA VAL THR          
SEQRES  12 A  266  ARG GLY GLN LEU LYS ASN GLY GLY LEU GLY VAL VAL SER          
SEQRES  13 A  266  ASP ALA ILE PHE ARG LEU GLY MET SER LEU SER SER PHE          
SEQRES  14 A  266  ASN LEU ASP ASP THR GLU VAL ALA LEU LEU GLN ALA VAL          
SEQRES  15 A  266  LEU LEU MET SER SER ASP ARG PRO GLY LEU ALA CYS VAL          
SEQRES  16 A  266  GLU ARG ILE GLU LYS TYR GLN ASP SER PHE LEU LEU ALA          
SEQRES  17 A  266  PHE GLU HIS TYR ILE ASN TYR ARG LYS HIS HIS VAL THR          
SEQRES  18 A  266  HIS PHE TRP PRO LYS LEU LEU MET LYS VAL THR ASP LEU          
SEQRES  19 A  266  ARG MET ILE GLY ALA CYS HIS ALA SER ARG PHE LEU HIS          
SEQRES  20 A  266  MET LYS VAL GLU CYS PRO THR GLU LEU PHE PRO PRO LEU          
SEQRES  21 A  266  PHE LEU GLU VAL PHE GLU                                      
SEQRES   1 B  266  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP          
SEQRES   2 B  266  PRO GLY HIS LYS PRO GLU PRO THR ASP GLU GLU TRP GLU          
SEQRES   3 B  266  LEU ILE LYS THR VAL THR GLU ALA HIS VAL ALA THR ASN          
SEQRES   4 B  266  ALA GLN GLY SER HIS TRP LYS GLN LYS ARG LYS PHE LEU          
SEQRES   5 B  266  PRO GLU ASP ILE GLY GLN ALA PRO ILE VAL ASN ALA PRO          
SEQRES   6 B  266  GLU GLY GLY LYS VAL ASP LEU GLU ALA PHE SER HIS PHE          
SEQRES   7 B  266  THR LYS ILE ILE THR PRO ALA ILE THR ARG VAL VAL ASP          
SEQRES   8 B  266  PHE ALA LYS LYS LEU PRO MET PHE CYS GLU LEU PRO CYS          
SEQRES   9 B  266  GLU ASP GLN ILE ILE LEU LEU LYS GLY CYS CYS MET GLU          
SEQRES  10 B  266  ILE MET SER LEU ARG ALA ALA VAL ARG TYR ASP PRO GLU          
SEQRES  11 B  266  SER GLU THR LEU THR LEU ASN GLY GLU MET ALA VAL THR          
SEQRES  12 B  266  ARG GLY GLN LEU LYS ASN GLY GLY LEU GLY VAL VAL SER          
SEQRES  13 B  266  ASP ALA ILE PHE ARG LEU GLY MET SER LEU SER SER PHE          
SEQRES  14 B  266  ASN LEU ASP ASP THR GLU VAL ALA LEU LEU GLN ALA VAL          
SEQRES  15 B  266  LEU LEU MET SER SER ASP ARG PRO GLY LEU ALA CYS VAL          
SEQRES  16 B  266  GLU ARG ILE GLU LYS TYR GLN ASP SER PHE LEU LEU ALA          
SEQRES  17 B  266  PHE GLU HIS TYR ILE ASN TYR ARG LYS HIS HIS VAL THR          
SEQRES  18 B  266  HIS PHE TRP PRO LYS LEU LEU MET LYS VAL THR ASP LEU          
SEQRES  19 B  266  ARG MET ILE GLY ALA CYS HIS ALA SER ARG PHE LEU HIS          
SEQRES  20 B  266  MET LYS VAL GLU CYS PRO THR GLU LEU PHE PRO PRO LEU          
SEQRES  21 B  266  PHE LEU GLU VAL PHE GLU                                      
HET    4HY  A 500      21                                                       
HET    4HY  B 500      21                                                       
HET    SO4  B 501       5                                                       
HETNAM     4HY [4-(4-HYDROXY-3-IODO-PHENOXY)-3,5-DIIODO-PHENYL]-ACETIC          
HETNAM   2 4HY  ACID                                                            
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  4HY    2(C14 H9 I3 O4)                                              
FORMUL   5  SO4    O4 S 2-                                                      
FORMUL   6  HOH   *105(H2 O)                                                    
HELIX    1   1 THR A  215  THR A  232  1                                  18    
HELIX    2   2 ASP A  265  LYS A  274  1                                  10    
HELIX    3   3 ILE A  275  LYS A  289  1                                  15    
HELIX    4   4 LEU A  290  GLU A  295  1                                   6    
HELIX    5   5 PRO A  297  VAL A  319  1                                  23    
HELIX    6   6 ARG A  338  GLY A  344  1                                   7    
HELIX    7   7 VAL A  348  SER A  361  1                                  14    
HELIX    8   8 SER A  362  ASN A  364  5                                   3    
HELIX    9   9 ASP A  366  MET A  379  1                                  14    
HELIX   10  10 CYS A  388  LYS A  411  1                                  24    
HELIX   11  11 HIS A  416  CYS A  446  1                                  31    
HELIX   12  12 PRO A  447  PHE A  451  5                                   5    
HELIX   13  13 PRO A  452  PHE A  459  1                                   8    
HELIX   14  14 THR B  215  THR B  232  1                                  18    
HELIX   15  15 HIS B  238  ARG B  243  1                                   6    
HELIX   16  16 ASP B  265  LYS B  274  1                                  10    
HELIX   17  17 ILE B  275  LYS B  289  1                                  15    
HELIX   18  18 LEU B  290  GLU B  295  1                                   6    
HELIX   19  19 PRO B  297  VAL B  319  1                                  23    
HELIX   20  20 THR B  337  GLY B  344  1                                   8    
HELIX   21  21 GLY B  347  SER B  361  1                                  15    
HELIX   22  22 SER B  362  ASN B  364  5                                   3    
HELIX   23  23 ASP B  366  MET B  379  1                                  14    
HELIX   24  24 CYS B  388  LYS B  411  1                                  24    
HELIX   25  25 HIS B  416  CYS B  446  1                                  31    
HELIX   26  26 PRO B  447  PHE B  451  5                                   5    
HELIX   27  27 PRO B  452  GLU B  460  1                                   9    
SHEET    1   A 4 LYS A 244  PHE A 245  0                                        
SHEET    2   A 4 MET A 334  THR A 337  1  O  ALA A 335   N  LYS A 244           
SHEET    3   A 4 THR A 327  LEU A 330 -1  N  LEU A 330   O  MET A 334           
SHEET    4   A 4 TYR A 321  ASP A 322 -1  N  ASP A 322   O  THR A 327           
SHEET    1   B 4 LYS B 244  PHE B 245  0                                        
SHEET    2   B 4 MET B 334  VAL B 336  1  O  ALA B 335   N  LYS B 244           
SHEET    3   B 4 THR B 327  LEU B 330 -1  N  LEU B 330   O  MET B 334           
SHEET    4   B 4 TYR B 321  ASP B 322 -1  N  ASP B 322   O  THR B 327           
SITE     1 AC1 11 PHE A 272  MET A 313  ALA A 317  ARG A 320                    
SITE     2 AC1 11 LEU A 330  ASN A 331  LEU A 346  ILE A 353                    
SITE     3 AC1 11 HIS A 435  MET A 442  PHE A 455                               
SITE     1 AC2 14 PHE B 272  ILE B 276  MET B 313  ALA B 317                    
SITE     2 AC2 14 ARG B 320  LEU B 330  ASN B 331  GLY B 344                    
SITE     3 AC2 14 LEU B 346  ILE B 353  HIS B 435  MET B 442                    
SITE     4 AC2 14 PHE B 455  HOH B 541                                          
SITE     1 AC3  7 ASN A 364  HIS A 412  HIS A 413  ASN B 364                    
SITE     2 AC3  7 HIS B 412  HIS B 413  HOH B 546                               
CRYST1   55.557   92.963   58.808  90.00 110.02  90.00 P 1 21 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      0.018000  0.000000  0.006558        0.00000                         
SCALE2      0.000000  0.010757  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018098        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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