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Database: PDB
Entry: 5EUU
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Original site: 5EUU 
HEADER    TRANSPORT PROTEIN                       19-NOV-15   5EUU              
TITLE     RAT PRESTIN STAS DOMAIN IN COMPLEX WITH CHLORIDE                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PRESTIN,PRESTIN;                                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: STAS DOMAIN,STAS DOMAIN,STAS DOMAIN,STAS DOMAIN;           
COMPND   5 SYNONYM: SOLUTE CARRIER FAMILY 26 MEMBER 5,SOLUTE CARRIER FAMILY 26  
COMPND   6 MEMBER 5;                                                            
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 OTHER_DETAILS: RESIDUES 564-636 (VARIABLE LOOP) ARE DELETED, GLYSER  
COMPND  10 ARE INSERTED BETWEEN POSITION 563 AND 637                            
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: SLC26A5, PRES;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET SUMO                                  
KEYWDS    ANION-BINDING SITE, PROTEIN-ANION COMPLEX, TRANSPORT PROTEIN          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.LOLLI,E.PASQUALETTO,E.COSTANZI,G.BONETTO,R.BATTISTUTTA              
REVDAT   3   10-JAN-24 5EUU    1       REMARK                                   
REVDAT   2   17-FEB-16 5EUU    1       JRNL                                     
REVDAT   1   16-DEC-15 5EUU    0                                                
JRNL        AUTH   G.LOLLI,E.PASQUALETTO,E.COSTANZI,G.BONETTO,R.BATTISTUTTA     
JRNL        TITL   THE STAS DOMAIN OF MAMMALIAN SLC26A5 PRESTIN HARBOURS AN     
JRNL        TITL 2 ANION-BINDING SITE.                                          
JRNL        REF    BIOCHEM.J.                    V. 473   365 2016              
JRNL        REFN                   ESSN 1470-8728                               
JRNL        PMID   26635354                                                     
JRNL        DOI    10.1042/BJ20151089                                           
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   E.PASQUALETTO,R.AIELLO,L.GESIOT,G.BONETTO,M.BELLANDA,        
REMARK   1  AUTH 2 R.BATTISTUTTA                                                
REMARK   1  TITL   STRUCTURE OF THE CYTOSOLIC PORTION OF THE MOTOR PROTEIN      
REMARK   1  TITL 2 PRESTIN AND FUNCTIONAL ROLE OF THE STAS DOMAIN IN SLC26/SULP 
REMARK   1  TITL 3 ANION TRANSPORTERS                                           
REMARK   1  REF    J.MOL.BIOL.                   V. 400   448 2010              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   20471983                                                     
REMARK   1  DOI    10.1016/J.JMB.2010.05.013                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.87 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.87                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.07                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 23464                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.159                           
REMARK   3   R VALUE            (WORKING SET) : 0.157                           
REMARK   3   FREE R VALUE                     : 0.196                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.490                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1288                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 31.0708 -  3.8877    1.00     2503   141  0.1555 0.1864        
REMARK   3     2  3.8877 -  3.0867    1.00     2466   183  0.1432 0.1984        
REMARK   3     3  3.0867 -  2.6968    1.00     2499   130  0.1595 0.1831        
REMARK   3     4  2.6968 -  2.4503    1.00     2527   122  0.1552 0.1859        
REMARK   3     5  2.4503 -  2.2747    1.00     2471   153  0.1419 0.1866        
REMARK   3     6  2.2747 -  2.1407    1.00     2469   164  0.1437 0.2046        
REMARK   3     7  2.1407 -  2.0335    1.00     2535   144  0.1677 0.1980        
REMARK   3     8  2.0335 -  1.9450    1.00     2496   112  0.1822 0.1942        
REMARK   3     9  1.9450 -  1.8701    0.88     2210   139  0.2789 0.3373        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.140           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.22                          
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           1065                                  
REMARK   3   ANGLE     :  0.764           1436                                  
REMARK   3   CHIRALITY :  0.031            164                                  
REMARK   3   PLANARITY :  0.003            182                                  
REMARK   3   DIHEDRAL  : 14.107            384                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 505 THROUGH 539 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.8338  14.0232 -12.9306              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2021 T22:   0.2148                                     
REMARK   3      T33:   0.2826 T12:  -0.0002                                     
REMARK   3      T13:  -0.0587 T23:   0.0181                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1369 L22:   0.4025                                     
REMARK   3      L33:   0.2688 L12:   0.0485                                     
REMARK   3      L13:   0.0555 L23:  -0.1524                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0492 S12:  -0.1718 S13:  -0.3016                       
REMARK   3      S21:   0.0884 S22:   0.0897 S23:   0.0419                       
REMARK   3      S31:   0.3412 S32:   0.0706 S33:  -0.0018                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 540 THROUGH 552)                  
REMARK   3    ORIGIN FOR THE GROUP (A): -14.1283  22.7623   0.6108              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2370 T22:   0.3402                                     
REMARK   3      T33:   0.2312 T12:  -0.1391                                     
REMARK   3      T13:   0.0253 T23:   0.0396                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1045 L22:   0.1754                                     
REMARK   3      L33:   1.1889 L12:  -0.1658                                     
REMARK   3      L13:  -0.2238 L23:   0.3130                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4048 S12:  -0.3765 S13:  -0.2211                       
REMARK   3      S21:   0.3733 S22:  -0.0718 S23:   0.0653                       
REMARK   3      S31:  -0.3238 S32:  -0.4335 S33:   0.1091                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 638 THROUGH 657 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -10.0165  27.3197  -6.8376              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1643 T22:   0.2693                                     
REMARK   3      T33:   0.2066 T12:  -0.0258                                     
REMARK   3      T13:  -0.0096 T23:   0.0066                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2169 L22:   0.3142                                     
REMARK   3      L33:  -0.0159 L12:   0.2651                                     
REMARK   3      L13:   0.0236 L23:   0.0499                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1365 S12:  -0.2848 S13:  -0.1736                       
REMARK   3      S21:   0.2531 S22:  -0.1451 S23:   0.0555                       
REMARK   3      S31:   0.0176 S32:  -0.1444 S33:  -0.0006                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 658 THROUGH 671 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.4480  30.6695   2.1346              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2795 T22:   0.3757                                     
REMARK   3      T33:   0.1728 T12:  -0.1101                                     
REMARK   3      T13:  -0.0495 T23:   0.0220                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2001 L22:   0.4258                                     
REMARK   3      L33:  -0.0026 L12:   0.2819                                     
REMARK   3      L13:  -0.0513 L23:  -0.0328                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2752 S12:  -0.6224 S13:  -0.2070                       
REMARK   3      S21:   0.6422 S22:  -0.3412 S23:  -0.1368                       
REMARK   3      S31:  -0.1562 S32:  -0.0330 S33:  -0.0371                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 672 THROUGH 698 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.3405  36.6665  -7.5454              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2165 T22:   0.2331                                     
REMARK   3      T33:   0.2476 T12:  -0.0271                                     
REMARK   3      T13:  -0.0204 T23:  -0.0317                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1651 L22:   0.1201                                     
REMARK   3      L33:   0.0785 L12:   0.0940                                     
REMARK   3      L13:   0.0934 L23:   0.0281                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0843 S12:  -0.1617 S13:   0.2129                       
REMARK   3      S21:   0.1042 S22:  -0.1184 S23:  -0.0048                       
REMARK   3      S31:  -0.1530 S32:   0.0318 S33:   0.0005                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 699 THROUGH 718 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   1.7405  29.7920 -13.6513              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1855 T22:   0.2872                                     
REMARK   3      T33:   0.2233 T12:  -0.0268                                     
REMARK   3      T13:  -0.0211 T23:  -0.0043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0984 L22:   0.1544                                     
REMARK   3      L33:   0.2229 L12:  -0.0200                                     
REMARK   3      L13:  -0.1401 L23:  -0.0059                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0379 S12:   0.1164 S13:   0.0822                       
REMARK   3      S21:  -0.0851 S22:   0.1248 S23:  -0.1090                       
REMARK   3      S31:  -0.1671 S32:   0.2707 S33:   0.0004                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5EUU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-NOV-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000215548.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-OCT-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ELETTRA                            
REMARK 200  BEAMLINE                       : 5.2R                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 2.0                                
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12555                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.870                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.850                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 15.60                              
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : 0.07500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.87                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.91                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.74900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
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: 3LLO                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.73                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5, 1.8 M AMMONIUM         
REMARK 280  SULPHATE, 5% (W/V) PEG400, 0.1% (W/V) OCTYL-BETA-D-                 
REMARK 280  GLUCOPYRANOSIDE. CRYSTALS WERE SOAKED WITH PRECIPITANT SOLUTION     
REMARK 280  SUPPLEMENTED WITH 1 M AMMONIUM CHLORIDE, VAPOR DIFFUSION,           
REMARK 280  SITTING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       22.19567            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       44.39133            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       44.39133            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       22.19567            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7830 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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 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     SER A   553                                                      
REMARK 465     SER A   554                                                      
REMARK 465     ALA A   555                                                      
REMARK 465     LEU A   556                                                      
REMARK 465     LYS A   557                                                      
REMARK 465     ARG A   558                                                      
REMARK 465     LYS A   559                                                      
REMARK 465     THR A   560                                                      
REMARK 465     GLY A   561                                                      
REMARK 465     VAL A   562                                                      
REMARK 465     ASN A   563                                                      
REMARK 465     GLY A   635                                                      
REMARK 465     SER A   636                                                      
REMARK 465     GLU A   637                                                      
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 801                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 805                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 806                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 807                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3LLO   RELATED DB: PDB                                   
REMARK 900 3LLO CONTAINS THE SAME PROTEIN IN THE APO FORM                       
REMARK 900 RELATED ID: 5EUS   RELATED DB: PDB                                   
REMARK 900 5EUS CONTAINS THE SAME PROTEIN IN COMPLEX WITH BROMIDE               
DBREF  5EUU A  505   563  UNP    Q9EPH0   S26A5_RAT      505    563             
DBREF  5EUU A  637   718  UNP    Q9EPH0   S26A5_RAT      637    718             
SEQADV 5EUU GLY A  635  UNP  Q9EPH0              LINKER                         
SEQADV 5EUU SER A  636  UNP  Q9EPH0              LINKER                         
SEQRES   1 A  143  SER PRO SER TYR THR VAL LEU GLY GLN LEU PRO ASP THR          
SEQRES   2 A  143  ASP VAL TYR ILE ASP ILE ASP ALA TYR GLU GLU VAL LYS          
SEQRES   3 A  143  GLU ILE PRO GLY ILE LYS ILE PHE GLN ILE ASN ALA PRO          
SEQRES   4 A  143  ILE TYR TYR ALA ASN SER ASP LEU TYR SER SER ALA LEU          
SEQRES   5 A  143  LYS ARG LYS THR GLY VAL ASN GLY SER GLU ASN ILE HIS          
SEQRES   6 A  143  THR VAL ILE LEU ASP PHE THR GLN VAL ASN PHE MET ASP          
SEQRES   7 A  143  SER VAL GLY VAL LYS THR LEU ALA GLY ILE VAL LYS GLU          
SEQRES   8 A  143  TYR GLY ASP VAL GLY ILE TYR VAL TYR LEU ALA GLY CYS          
SEQRES   9 A  143  SER ALA GLN VAL VAL ASN ASP LEU THR SER ASN ARG PHE          
SEQRES  10 A  143  PHE GLU ASN PRO ALA LEU LYS GLU LEU LEU PHE HIS SER          
SEQRES  11 A  143  ILE HIS ASP ALA VAL LEU GLY SER GLN VAL ARG GLU ALA          
HET     CL  A 801       1                                                       
HET     CL  A 802       1                                                       
HET    EDO  A 803      10                                                       
HET    EDO  A 804      10                                                       
HET    EDO  A 805      10                                                       
HET    PG4  A 806      31                                                       
HET    PGE  A 807      24                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2   CL    2(CL 1-)                                                     
FORMUL   4  EDO    3(C2 H6 O2)                                                  
FORMUL   7  PG4    C8 H18 O5                                                    
FORMUL   8  PGE    C6 H14 O4                                                    
FORMUL   9  HOH   *87(H2 O)                                                     
HELIX    1 AA1 PRO A  543  TYR A  552  1                                  10    
HELIX    2 AA2 ASP A  653  ASP A  669  1                                  17    
HELIX    3 AA3 SER A  680  ASN A  690  1                                  11    
HELIX    4 AA4 ASN A  695  GLU A  700  5                                   6    
HELIX    5 AA5 SER A  705  SER A  713  1                                   9    
SHEET    1 AA1 6 TYR A 520  ASP A 522  0                                        
SHEET    2 AA1 6 TYR A 508  GLN A 513 -1  N  GLY A 512   O  ILE A 521           
SHEET    3 AA1 6 ILE A 535  ILE A 540 -1  O  GLN A 539   N  THR A 509           
SHEET    4 AA1 6 THR A 641  ASP A 645  1  O  ASP A 645   N  PHE A 538           
SHEET    5 AA1 6 TYR A 673  ALA A 677  1  O  TYR A 675   N  LEU A 644           
SHEET    6 AA1 6 LEU A 702  PHE A 703  1  O  PHE A 703   N  LEU A 676           
SITE     1 AC1  6 MET A 652  ASP A 653  GLY A 656  GLN A 714                    
SITE     2 AC1  6 HOH A 929  HOH A 949                                          
SITE     1 AC2  1 ILE A 706                                                     
SITE     1 AC3  1 GLN A 513                                                     
SITE     1 AC4  4 VAL A 684  THR A 688  LYS A 699  HOH A 919                    
SITE     1 AC5  1 GLU A 666                                                     
SITE     1 AC6  8 GLY A 668  TYR A 673  ALA A 697  GLU A 700                    
SITE     2 AC6  8 LEU A 701  HIS A 704  ALA A 718  HOH A 901                    
SITE     1 AC7  3 PRO A 506  ALA A 542  ASN A 695                               
CRYST1   62.133   62.133   66.587  90.00  90.00 120.00 P 31 2 1      6          
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      0.016095  0.009292  0.000000        0.00000                         
SCALE2      0.000000  0.018584  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015018        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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