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Database: PDB
Entry: 4U90
LinkDB: 4U90
Original site: 4U90 
HEADER    TRANSFER PROTEIN / STRUCTURAL PROTEIN   05-AUG-14   4U90              
TITLE     GEPHE IN COMPLEX WITH PEG CROSSLINKED GABA RECEPTOR ALPHA3 SUBUNIT    
TITLE    2 DERIVED DIMERIC PEPTIDE                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GEPHYRIN;                                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: GEPHYRIN E DOMAIN, UNP RESIDUES 344-762;                   
COMPND   5 SYNONYM: PUTATIVE GLYCINE RECEPTOR-TUBULIN LINKER PROTEIN;           
COMPND   6 EC: 2.7.7.75,2.10.1.1;                                               
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT ALPHA-3;          
COMPND  10 CHAIN: D, E;                                                         
COMPND  11 SYNONYM: GABA(A) RECEPTOR SUBUNIT ALPHA-3;                           
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: GPHN, GPH;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  11 ORGANISM_COMMON: RAT;                                                
SOURCE  12 ORGANISM_TAXID: 10116                                                
KEYWDS    INHIBITORY SYNAPSE, SCAFFOLDING PROTEIN, GABA TYPE A RECEPTOR,        
KEYWDS   2 TRANSFERASE, TRANSFER PROTEIN - STRUCTURAL PROTEIN COMPLEX           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.B.KASARAGOD,H.M.MARIC,H.SCHINDELIN                                  
REVDAT   3   20-DEC-23 4U90    1       REMARK ATOM                              
REVDAT   2   11-FEB-15 4U90    1       JRNL                                     
REVDAT   1   10-DEC-14 4U90    0                                                
JRNL        AUTH   H.M.MARIC,V.B.KASARAGOD,L.HAUGAARD-KEDSTROM,T.J.HAUSRAT,     
JRNL        AUTH 2 M.KNEUSSEL,H.SCHINDELIN,K.STRMGAARD                          
JRNL        TITL   DESIGN AND SYNTHESIS OF HIGH-AFFINITY DIMERIC INHIBITORS     
JRNL        TITL 2 TARGETING THE INTERACTIONS BETWEEN GEPHYRIN AND INHIBITORY   
JRNL        TITL 3 NEUROTRANSMITTER RECEPTORS.                                  
JRNL        REF    ANGEW.CHEM.INT.ED.ENGL.       V.  54   490 2015              
JRNL        REFN                   ESSN 1521-3773                               
JRNL        PMID   25413248                                                     
JRNL        DOI    10.1002/ANIE.201409043                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 32616                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.211                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1694                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2392                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.92                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2670                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 107                          
REMARK   3   BIN FREE R VALUE                    : 0.3340                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3293                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 255                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.21                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.13000                                             
REMARK   3    B22 (A**2) : -1.50000                                             
REMARK   3    B33 (A**2) : 1.63000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.151         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.143         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.115         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.411         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.951                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3433 ; 0.019 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3345 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4676 ; 1.907 ; 1.991       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7716 ; 0.933 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   440 ; 6.630 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   143 ;39.854 ;24.406       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   569 ;16.241 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;21.521 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   544 ; 0.111 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3861 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   713 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1739 ; 3.173 ; 3.370       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1738 ; 3.172 ; 3.368       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2171 ; 4.440 ; 5.024       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2172 ; 4.440 ; 5.027       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1693 ; 4.296 ; 3.918       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1693 ; 4.286 ; 3.918       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2501 ; 6.199 ; 5.677       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 13691 ; 8.999 ;32.735       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 13692 ; 8.999 ;32.736       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   319        A   736                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.5557 128.7595 117.6979              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2009 T22:   0.1103                                     
REMARK   3      T33:   0.2257 T12:   0.0111                                     
REMARK   3      T13:  -0.0033 T23:   0.0488                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1424 L22:   0.0643                                     
REMARK   3      L33:   0.4607 L12:   0.0340                                     
REMARK   3      L13:  -0.0508 L23:  -0.0793                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0173 S12:  -0.0125 S13:  -0.0107                       
REMARK   3      S21:  -0.0139 S22:  -0.0664 S23:   0.0350                       
REMARK   3      S31:   0.0330 S32:   0.1318 S33:   0.0838                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   368        D   377                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.0804 109.3488 106.3605              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2704 T22:   0.0783                                     
REMARK   3      T33:   0.2175 T12:   0.0701                                     
REMARK   3      T13:   0.0324 T23:   0.0040                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5021 L22:   4.0018                                     
REMARK   3      L33:   2.5746 L12:   2.4633                                     
REMARK   3      L13:  -0.0625 L23:  -2.0750                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1200 S12:   0.0299 S13:   0.0303                       
REMARK   3      S21:  -0.0582 S22:  -0.2556 S23:  -0.0757                       
REMARK   3      S31:   0.2453 S32:   0.3474 S33:   0.1356                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   368        E   377                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.1954  89.1361 122.4718              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3686 T22:   0.1743                                     
REMARK   3      T33:   0.2823 T12:  -0.1418                                     
REMARK   3      T13:   0.0424 T23:   0.1349                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.5619 L22:  16.8073                                     
REMARK   3      L33:   2.8547 L12: -12.2525                                     
REMARK   3      L13:   1.4026 L23:   0.0592                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1614 S12:  -0.2403 S13:   0.6064                       
REMARK   3      S21:  -0.6986 S22:   0.0589 S23:  -1.4144                       
REMARK   3      S31:  -0.4103 S32:   0.1000 S33:  -0.2202                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4U90 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-AUG-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000203006.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-MAY-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9100                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34354                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.62300                            
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: 2FU3                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE PH 4.5, 20-30 % 2   
REMARK 280  -METHYL-2,4-PENTANEDIOL., VAPOR DIFFUSION, SITTING DROP,            
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  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       44.26900            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       49.62000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       57.20300            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       44.26900            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       49.62000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       57.20300            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       44.26900            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       49.62000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       57.20300            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       44.26900            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       49.62000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       57.20300            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, E                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, E                               
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      198.48000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      228.81200            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A1100  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1103  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1104  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   318                                                      
REMARK 465     SER A   575                                                      
REMARK 465     MET A   576                                                      
REMARK 465     GLY A   577                                                      
REMARK 465     GLU A   578                                                      
REMARK 465     LYS A   579                                                      
REMARK 465     MET A   696                                                      
REMARK 465     SER A   697                                                      
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   NH2  ARG A   735     O    HOH A   901              2.03            
REMARK 500   O    HOH A  1046     O    HOH A  1078              2.10            
REMARK 500   OG   SER A   563     O    HOH A   902              2.15            
REMARK 500   N    ALA A   451     O6   BU1 A   801              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A 591       41.12     71.61                                   
REMARK 500    ASP A 615       13.86     82.47                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1146        DISTANCE =  7.27 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4U91   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4PD0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4PD1   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4TK1   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4TK2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4TK3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4TK4   RELATED DB: PDB                                   
DBREF  4U90 A  318   736  UNP    Q03555   GEPH_RAT       344    762             
DBREF  4U90 D  368   376  UNP    P20236   GBRA3_RAT      396    404             
DBREF  4U90 E  368   376  UNP    P20236   GBRA3_RAT      396    404             
SEQADV 4U90 CYS D  377  UNP  P20236              EXPRESSION TAG                 
SEQADV 4U90 CYS E  377  UNP  P20236              EXPRESSION TAG                 
SEQRES   1 A  419  MET SER PRO PHE PRO LEU THR SER MET ASP LYS ALA PHE          
SEQRES   2 A  419  ILE THR VAL LEU GLU MET THR PRO VAL LEU GLY THR GLU          
SEQRES   3 A  419  ILE ILE ASN TYR ARG ASP GLY MET GLY ARG VAL LEU ALA          
SEQRES   4 A  419  GLN ASP VAL TYR ALA LYS ASP ASN LEU PRO PRO PHE PRO          
SEQRES   5 A  419  ALA SER VAL LYS ASP GLY TYR ALA VAL ARG ALA ALA ASP          
SEQRES   6 A  419  GLY PRO GLY ASP ARG PHE ILE ILE GLY GLU SER GLN ALA          
SEQRES   7 A  419  GLY GLU GLN PRO THR GLN THR VAL MET PRO GLY GLN VAL          
SEQRES   8 A  419  MET ARG VAL THR THR GLY ALA PRO ILE PRO CYS GLY ALA          
SEQRES   9 A  419  ASP ALA VAL VAL GLN VAL GLU ASP THR GLU LEU ILE ARG          
SEQRES  10 A  419  GLU SER ASP ASP GLY THR GLU GLU LEU GLU VAL ARG ILE          
SEQRES  11 A  419  LEU VAL GLN ALA ARG PRO GLY GLN ASP ILE ARG PRO ILE          
SEQRES  12 A  419  GLY HIS ASP ILE LYS ARG GLY GLU CYS VAL LEU ALA LYS          
SEQRES  13 A  419  GLY THR HIS MET GLY PRO SER GLU ILE GLY LEU LEU ALA          
SEQRES  14 A  419  THR VAL GLY VAL THR GLU VAL GLU VAL ASN LYS PHE PRO          
SEQRES  15 A  419  VAL VAL ALA VAL MET SER THR GLY ASN GLU LEU LEU ASN          
SEQRES  16 A  419  PRO GLU ASP ASP LEU LEU PRO GLY LYS ILE ARG ASP SER          
SEQRES  17 A  419  ASN ARG SER THR LEU LEU ALA THR ILE GLN GLU HIS GLY          
SEQRES  18 A  419  TYR PRO THR ILE ASN LEU GLY ILE VAL GLY ASP ASN PRO          
SEQRES  19 A  419  ASP ASP LEU LEU ASN ALA LEU ASN GLU GLY ILE SER ARG          
SEQRES  20 A  419  ALA ASP VAL ILE ILE THR SER GLY GLY VAL SER MET GLY          
SEQRES  21 A  419  GLU LYS ASP TYR LEU LYS GLN VAL LEU ASP ILE ASP LEU          
SEQRES  22 A  419  HIS ALA GLN ILE HIS PHE GLY ARG VAL PHE MET LYS PRO          
SEQRES  23 A  419  GLY LEU PRO THR THR PHE ALA THR LEU ASP ILE ASP GLY          
SEQRES  24 A  419  VAL ARG LYS ILE ILE PHE ALA LEU PRO GLY ASN PRO VAL          
SEQRES  25 A  419  SER ALA VAL VAL THR CYS ASN LEU PHE VAL VAL PRO ALA          
SEQRES  26 A  419  LEU ARG LYS MET GLN GLY ILE LEU ASP PRO ARG PRO THR          
SEQRES  27 A  419  ILE ILE LYS ALA ARG LEU SER CYS ASP VAL LYS LEU ASP          
SEQRES  28 A  419  PRO ARG PRO GLU TYR HIS ARG CYS ILE LEU THR TRP HIS          
SEQRES  29 A  419  HIS GLN GLU PRO LEU PRO TRP ALA GLN SER THR GLY ASN          
SEQRES  30 A  419  GLN MET SER SER ARG LEU MET SER MET ARG SER ALA ASN          
SEQRES  31 A  419  GLY LEU LEU MET LEU PRO PRO LYS THR GLU GLN TYR VAL          
SEQRES  32 A  419  GLU LEU HIS LYS GLY GLU VAL VAL ASP VAL MET VAL ILE          
SEQRES  33 A  419  GLY ARG LEU                                                  
SEQRES   1 D   10  PHE ASN ILE VAL GLY THR THR TYR PRO CYS                      
SEQRES   1 E   10  PHE ASN ILE VAL GLY THR THR TYR PRO CYS                      
HET    BU1  A 801       6                                                       
HET    3F8  E 401      22                                                       
HETNAM     BU1 1,4-BUTANEDIOL                                                   
HETNAM     3F8 1,1'-[ETHANE-1,2-DIYLBIS(OXYETHANE-2,1-DIYL)]BIS(1H-             
HETNAM   2 3F8  PYRROLE-2,5-DIONE)                                              
FORMUL   4  BU1    C4 H10 O2                                                    
FORMUL   5  3F8    C14 H16 N2 O6                                                
FORMUL   6  HOH   *255(H2 O)                                                    
HELIX    1 AA1 MET A  326  THR A  337  1                                  12    
HELIX    2 AA2 ARG A  348  GLY A  350  5                                   3    
HELIX    3 AA3 ARG A  379  GLY A  383  5                                   5    
HELIX    4 AA4 GLY A  478  GLY A  489  1                                  12    
HELIX    5 AA5 SER A  525  HIS A  537  1                                  13    
HELIX    6 AA6 ASN A  550  ALA A  565  1                                  16    
HELIX    7 AA7 TYR A  581  ILE A  588  1                                   8    
HELIX    8 AA8 ASN A  627  GLN A  647  1                                  21    
HELIX    9 AA9 ARG A  699  MET A  703  1                                   5    
SHEET    1 AA1 2 LEU A 323  SER A 325  0                                        
SHEET    2 AA1 2 ARG A 598  PHE A 600  1  O  PHE A 600   N  THR A 324           
SHEET    1 AA2 2 THR A 342  ASN A 346  0                                        
SHEET    2 AA2 2 GLU A 492  ASN A 496 -1  O  VAL A 493   N  ILE A 345           
SHEET    1 AA3 2 VAL A 359  TYR A 360  0                                        
SHEET    2 AA3 2 CYS A 469  LEU A 471 -1  O  LEU A 471   N  VAL A 359           
SHEET    1 AA4 2 ALA A 370  SER A 371  0                                        
SHEET    2 AA4 2 ILE A 457  ARG A 458 -1  O  ARG A 458   N  ALA A 370           
SHEET    1 AA5 6 ALA A 423  GLN A 426  0                                        
SHEET    2 AA5 6 GLY A 375  VAL A 378 -1  N  VAL A 378   O  ALA A 423           
SHEET    3 AA5 6 GLN A 407  VAL A 411 -1  O  MET A 409   N  ALA A 377           
SHEET    4 AA5 6 GLY A 385  SER A 393  1  N  SER A 393   O  ARG A 410           
SHEET    5 AA5 6 GLU A 442  ILE A 447 -1  O  ILE A 447   N  GLY A 385           
SHEET    6 AA5 6 THR A 430  GLU A 435 -1  N  GLU A 431   O  ARG A 446           
SHEET    1 AA6 6 THR A 541  VAL A 547  0                                        
SHEET    2 AA6 6 VAL A 501  THR A 506  1  N  SER A 505   O  VAL A 547           
SHEET    3 AA6 6 VAL A 567  SER A 571  1  O  ILE A 569   N  ALA A 502           
SHEET    4 AA6 6 VAL A 617  LEU A 624  1  O  LEU A 624   N  THR A 570           
SHEET    5 AA6 6 THR A 608  ILE A 614 -1  N  LEU A 612   O  LYS A 619           
SHEET    6 AA6 6 GLN A 593  PHE A 596 -1  N  GLN A 593   O  THR A 611           
SHEET    1 AA7 2 LEU A 510  LEU A 511  0                                        
SHEET    2 AA7 2 ILE A 522  ARG A 523  1  O  ILE A 522   N  LEU A 511           
SHEET    1 AA8 6 ILE A 656  LEU A 661  0                                        
SHEET    2 AA8 6 TRP A 688  SER A 691  1  O  ALA A 689   N  ARG A 660           
SHEET    3 AA8 6 GLU A 672  THR A 679 -1  N  THR A 679   O  TRP A 688           
SHEET    4 AA8 6 GLY A 708  LEU A 712 -1  O  LEU A 712   N  GLU A 672           
SHEET    5 AA8 6 VAL A 727  VAL A 732 -1  O  MET A 731   N  LEU A 709           
SHEET    6 AA8 6 ILE A 656  LEU A 661 -1  N  ALA A 659   O  VAL A 728           
SHEET    1 AA9 2 VAL A 665  LYS A 666  0                                        
SHEET    2 AA9 2 GLU A 721  LEU A 722 -1  O  LEU A 722   N  VAL A 665           
CISPEP   1 SER A  319    PRO A  320          0         0.23                     
CISPEP   2 LEU A  365    PRO A  366          0        -9.49                     
CISPEP   3 LYS A  602    PRO A  603          0       -12.99                     
CRYST1   88.538   99.240  114.406  90.00  90.00  90.00 I 2 2 2      16          
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      0.011295  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010077  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008741        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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