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Database: PDB
Entry: 5EUX
LinkDB: 5EUX
Original site: 5EUX 
HEADER    TRANSPORT PROTEIN                       19-NOV-15   5EUX              
TITLE     RAT PRESTIN STAS DOMAIN IN COMPLEX WITH THIOCYANATE                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PRESTIN,PRESTIN;                                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: 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: NORWAY 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   4   10-JAN-24 5EUX    1       REMARK                                   
REVDAT   3   20-DEC-17 5EUX    1       JRNL                                     
REVDAT   2   17-FEB-16 5EUX    1       JRNL                                     
REVDAT   1   16-DEC-15 5EUX    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                   ESSN 1089-8638                               
REMARK   1  PMID   20471983                                                     
REMARK   1  DOI    10.1016/J.JMB.2010.05.013                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.04 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) : 2.04                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.99                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 9652                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.165                           
REMARK   3   R VALUE            (WORKING SET) : 0.163                           
REMARK   3   FREE R VALUE                     : 0.198                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.280                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 951                             
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 41.9969 -  3.8970    1.00     2521   137  0.1388 0.1531        
REMARK   3     2  3.8970 -  3.0934    1.00     2526   126  0.1548 0.2030        
REMARK   3     3  3.0934 -  2.7025    0.99     2459   170  0.1760 0.2228        
REMARK   3     4  2.7025 -  2.4554    0.98     2479   145  0.1931 0.2297        
REMARK   3     5  2.4554 -  2.2795    0.96     2412   130  0.1957 0.2130        
REMARK   3     6  2.2795 -  2.1451    0.95     2432    89  0.2012 0.2870        
REMARK   3     7  2.1451 -  2.0376    0.89     2240   154  0.2293 0.2896        
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) : 20.370           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.88                          
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      :  0.016           1064                                  
REMARK   3   ANGLE     :  1.259           1433                                  
REMARK   3   CHIRALITY :  0.055            164                                  
REMARK   3   PLANARITY :  0.006            181                                  
REMARK   3   DIHEDRAL  : 14.997            383                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 506 THROUGH 530 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.7450  12.8425 -14.8143              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3910 T22:   0.4148                                     
REMARK   3      T33:   0.4988 T12:   0.0055                                     
REMARK   3      T13:  -0.0340 T23:   0.0465                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6177 L22:   0.9215                                     
REMARK   3      L33:   0.7913 L12:   0.5044                                     
REMARK   3      L13:   0.7147 L23:   0.1937                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0037 S12:  -0.0465 S13:  -0.5209                       
REMARK   3      S21:   0.0588 S22:   0.1761 S23:  -0.1818                       
REMARK   3      S31:   0.4695 S32:   0.1469 S33:   0.0005                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 531 THROUGH 550 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.3535  20.8578  -4.4246              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3242 T22:   0.5160                                     
REMARK   3      T33:   0.4149 T12:  -0.1009                                     
REMARK   3      T13:  -0.0152 T23:   0.0231                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2340 L22:   0.8179                                     
REMARK   3      L33:   0.1190 L12:  -0.1313                                     
REMARK   3      L13:   0.2700 L23:  -0.3893                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2829 S12:  -0.3838 S13:  -0.0597                       
REMARK   3      S21:   0.4268 S22:  -0.2229 S23:   0.0255                       
REMARK   3      S31:   0.2959 S32:  -0.2244 S33:  -0.0005                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 551 THROUGH 553 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.5631  19.5158   6.6089              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5930 T22:   1.2339                                     
REMARK   3      T33:   1.2173 T12:   0.0350                                     
REMARK   3      T13:   0.0253 T23:   0.1510                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0119 L22:   0.0127                                     
REMARK   3      L33:   0.1296 L12:  -0.0265                                     
REMARK   3      L13:   0.0130 L23:   0.0146                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5736 S12:   0.1243 S13:   0.6961                       
REMARK   3      S21:   1.0688 S22:   0.2211 S23:  -0.7123                       
REMARK   3      S31:  -0.0797 S32:  -0.0960 S33:  -0.0015                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 638 THROUGH 666 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.2037  28.7308  -4.2067              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2665 T22:   0.4862                                     
REMARK   3      T33:   0.2817 T12:  -0.0714                                     
REMARK   3      T13:  -0.0158 T23:  -0.0031                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7271 L22:   1.0839                                     
REMARK   3      L33:   0.3551 L12:  -0.1576                                     
REMARK   3      L13:  -0.2159 L23:   0.1870                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3218 S12:  -0.4323 S13:  -0.0747                       
REMARK   3      S21:   0.3373 S22:  -0.2669 S23:  -0.0365                       
REMARK   3      S31:   0.0932 S32:  -0.1060 S33:  -0.0001                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 667 THROUGH 692 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.6429  34.1444  -6.2538              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2825 T22:   0.4667                                     
REMARK   3      T33:   0.3207 T12:  -0.0251                                     
REMARK   3      T13:  -0.0202 T23:  -0.0286                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6843 L22:   1.4253                                     
REMARK   3      L33:  -0.0716 L12:   0.5283                                     
REMARK   3      L13:   0.2490 L23:   0.3109                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1959 S12:  -0.2659 S13:   0.1661                       
REMARK   3      S21:   0.2404 S22:  -0.1798 S23:   0.0438                       
REMARK   3      S31:  -0.0793 S32:  -0.0750 S33:   0.0000                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 693 THROUGH 701 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.0351  40.4049  -6.8132              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3922 T22:   0.4924                                     
REMARK   3      T33:   0.3897 T12:  -0.0488                                     
REMARK   3      T13:  -0.0641 T23:  -0.1390                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2535 L22:   1.0416                                     
REMARK   3      L33:   0.7561 L12:   0.1465                                     
REMARK   3      L13:  -0.2066 L23:  -0.6988                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1989 S12:  -1.0442 S13:   0.5165                       
REMARK   3      S21:  -0.6027 S22:   0.1556 S23:  -0.4997                       
REMARK   3      S31:  -0.3773 S32:   0.4678 S33:  -0.0745                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 702 THROUGH 718 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   2.1685  28.6093 -14.3546              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2301 T22:   0.4287                                     
REMARK   3      T33:   0.2962 T12:  -0.0293                                     
REMARK   3      T13:  -0.0148 T23:  -0.0284                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3196 L22:   0.4806                                     
REMARK   3      L33:   0.1160 L12:   0.2018                                     
REMARK   3      L13:  -0.4867 L23:  -0.2210                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0039 S12:  -0.0054 S13:  -0.0671                       
REMARK   3      S21:  -0.0367 S22:   0.2806 S23:   0.0688                       
REMARK   3      S31:  -0.0998 S32:   0.1785 S33:   0.0012                       
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 5EUX 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_1000215554.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-MAY-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   : 9671                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.038                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.990                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY                : 17.40                              
REMARK 200  R MERGE                    (I) : 0.08100                            
REMARK 200  R SYM                      (I) : 0.08500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.09                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.20                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.13800                            
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: 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   (%): 48.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5, 1.8 M AMMONIUM         
REMARK 280  SULPHATE, 250 MM NASCN, 5% (W/V) PEG400, 0.1% (W/V) OCTYL-BETA-D-   
REMARK 280  GLUCOPYRANOSIDE, VAPOR DIFFUSION, 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       22.25167            
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       44.50333            
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       44.50333            
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       22.25167            
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: 1320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7760 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 8.0 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   505                                                      
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   HG1  THR A   641    HH22  ARG A   716              1.21            
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    ASP A 522      122.97    -33.79                                   
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 SCN A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 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 EDO A 806                 
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               
REMARK 900 RELATED ID: 5EUU   RELATED DB: PDB                                   
REMARK 900 5EUU CONTAINS THE SAME PROTEIN IN COMPLEX WITH CHLORIDE              
REMARK 900 RELATED ID: 5EUW   RELATED DB: PDB                                   
REMARK 900 5EUW CONTAINS THE SAME PROTEIN IN COMPLEX WITH NITRATE               
DBREF  5EUX A  505   563  UNP    Q9EPH0   S26A5_RAT      505    563             
DBREF  5EUX A  637   718  UNP    Q9EPH0   S26A5_RAT      637    718             
SEQADV 5EUX GLY A  635  UNP  Q9EPH0              LINKER                         
SEQADV 5EUX 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    SCN  A 801       3                                                       
HET    PEG  A 802      17                                                       
HET    PG4  A 803      31                                                       
HET    EDO  A 804      10                                                       
HET    EDO  A 805      10                                                       
HET    EDO  A 806      10                                                       
HETNAM     SCN THIOCYANATE ION                                                  
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  SCN    C N S 1-                                                     
FORMUL   3  PEG    C4 H10 O3                                                    
FORMUL   4  PG4    C8 H18 O5                                                    
FORMUL   5  EDO    3(C2 H6 O2)                                                  
FORMUL   8  HOH   *42(H2 O)                                                     
HELIX    1 AA1 PRO A  543  SER A  553  1                                  11    
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  ILE A 643   N  LYS A 536           
SHEET    5 AA1 6 TYR A 673  ALA A 677  1  O  TYR A 673   N  VAL A 642           
SHEET    6 AA1 6 LEU A 702  PHE A 703  1  O  PHE A 703   N  LEU A 676           
SITE     1 AC1  5 ILE A 544  MET A 652  ASP A 653  GLY A 656                    
SITE     2 AC1  5 GLN A 714                                                     
SITE     1 AC2  2 TYR A 552  LYS A 699                                          
SITE     1 AC3  6 GLY A 668  TYR A 673  ALA A 697  HIS A 704                    
SITE     2 AC3  6 ALA A 718  HOH A 919                                          
SITE     1 AC4  2 GLN A 513  VAL A 710                                          
SITE     1 AC5  2 TYR A 508  LYS A 536                                          
SITE     1 AC6  4 THR A 517  ASP A 518  ALA A 525  HOH A 920                    
CRYST1   62.365   62.365   66.755  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      0.016035  0.009258  0.000000        0.00000                         
SCALE2      0.000000  0.018515  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014980        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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