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Database: PDB
Entry: 3BBR
LinkDB: 3BBR
Original site: 3BBR 
HEADER    MEMBRANE PROTEIN                        11-NOV-07   3BBR              
TITLE     CRYSTAL STRUCTURE OF THE IGLUR2 LIGAND BINDING CORE (S1S2J-N775S) IN  
TITLE    2 COMPLEX WITH A DIMERIC POSITIVE MODULATOR AS WELL AS GLUTAMATE AT    
TITLE    3 2.25 A RESOLUTION                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMATE RECEPTOR 2;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: LIGAND BINDING CORE;                                       
COMPND   5 SYNONYM: GLUR-2, GLUR-B, GLUR-K2, GLUTAMATE RECEPTOR IONOTROPIC, AMPA
COMPND   6 2, AMPA-SELECTIVE GLUTAMATE RECEPTOR 2;                              
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 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: GRIA2, GLUR2;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PETGQ KANR                                
KEYWDS    AMPA RECEPTOR, GLUR2, S1S2, LIGAND BINDING CORE, POINT MUTATION,      
KEYWDS   2 N775S, DIMERIC POSITIVE MODULATOR, AGONIST, CELL JUNCTION,           
KEYWDS   3 GLYCOPROTEIN, ION TRANSPORT, IONIC CHANNEL, LIPOPROTEIN, MEMBRANE,   
KEYWDS   4 PALMITATE, PHOSPHORYLATION, POSTSYNAPTIC CELL MEMBRANE, RNA EDITING, 
KEYWDS   5 SYNAPSE, TRANSMEMBRANE, TRANSPORT, MEMBRANE PROTEIN                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.S.KASTRUP,M.GAJHEDE                                                 
REVDAT   5   16-AUG-17 3BBR    1       SOURCE REMARK                            
REVDAT   4   13-JUL-11 3BBR    1       VERSN                                    
REVDAT   3   24-FEB-09 3BBR    1       VERSN                                    
REVDAT   2   24-JUN-08 3BBR    1       JRNL                                     
REVDAT   1   04-DEC-07 3BBR    0                                                
JRNL        AUTH   B.H.KAAE,K.HARPSOE,J.S.KASTRUP,A.C.SANZ,D.S.PICKERING,       
JRNL        AUTH 2 B.METZLER,R.P.CLAUSEN,M.GAJHEDE,P.SAUERBERG,T.LILJEFORS,     
JRNL        AUTH 3 U.MADSEN                                                     
JRNL        TITL   STRUCTURAL PROOF OF A DIMERIC POSITIVE MODULATOR BRIDGING    
JRNL        TITL 2 TWO IDENTICAL AMPA RECEPTOR-BINDING SITES                    
JRNL        REF    CHEM.BIOL.                    V.  14  1294 2007              
JRNL        REFN                   ISSN 1074-5521                               
JRNL        PMID   18022568                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2007.10.012                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 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 : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.43                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 27839                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1394                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3   K_SOL              : 0.34                                          
REMARK   3   B_SOL              : 50.06                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 11.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 9.00000                                              
REMARK   3    B22 (A**2) : 5.30500                                              
REMARK   3    B33 (A**2) : 5.45900                                              
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  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      :  0.005           NULL                                  
REMARK   3   ANGLE     :  0.698           NULL                                  
REMARK   3   CHIRALITY :  0.049           NULL                                  
REMARK   3   PLANARITY :  0.003           NULL                                  
REMARK   3   DIHEDRAL  : 10.357           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 3BBR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-NOV-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000045326.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-MAR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I911-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.043                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27875                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 122.169                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : 0.09000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.37                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26300                            
REMARK 200  R SYM FOR SHELL            (I) : 0.26300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 1LB8                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.3M AMMONIUM SULFATE, 0.1M SODIUM       
REMARK 280  ACETATE, 25% PEG 4000, PH 5.5, VAPOR DIFFUSION, HANGING DROP,       
REMARK 280  TEMPERATURE 280K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       49.54000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       60.89000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       49.54000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       60.89000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3340 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -79.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ASP A   257                                                      
REMARK 465     LYS A   258                                                      
REMARK 465     GLY A   259                                                      
REMARK 465     GLY A   262                                                      
REMARK 465     SER A   263                                                      
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  67      -73.62    -70.81                                   
REMARK 500    ASN A  72     -168.56   -104.35                                   
REMARK 500    THR A 131       -4.85   -142.10                                   
REMARK 500    ASN B  22       19.20     84.64                                   
REMARK 500    ASN B  72     -164.72   -106.47                                   
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 SO4 B 264                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 265                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 264                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 266                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 265                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 266                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLU A 267                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLU B 267                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BHY A 268                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 268                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 269                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1LBC   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF GLUR2 LIGAND BINDING CORE (S1S2J-N775S) IN      
REMARK 900 COMPLEX WITH CYCLOTHIAZIDE (CTZ) AS WELL AS GLUTAMATE AT 1.8 A       
REMARK 900 RESOLUTION                                                           
REMARK 900 RELATED ID: 2AL5   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN        
REMARK 900 COMPLEX WITH FLUORO-WILLARDIINE AND ANIRACETAM                       
REMARK 900 RELATED ID: 2AL4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN        
REMARK 900 COMPLEX WITH QUISQUALATE AND CX614                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE NATIVE GLUR2 IS A MEMBRANE PROTEIN.                              
REMARK 999 TRANSMEMBRANE REGIONS WERE GENETICALLY REMOVED AND REPLACED          
REMARK 999 WITH A GLY-THR LINKER.                                               
DBREF  3BBR A    3   117  UNP    P19491   GRIA2_RAT      413    527             
DBREF  3BBR A  120   263  UNP    P19491   GRIA2_RAT      653    796             
DBREF  3BBR B    3   117  UNP    P19491   GRIA2_RAT      413    527             
DBREF  3BBR B  120   263  UNP    P19491   GRIA2_RAT      653    796             
SEQADV 3BBR GLY A    1  UNP  P19491              EXPRESSION TAG                 
SEQADV 3BBR ALA A    2  UNP  P19491              EXPRESSION TAG                 
SEQADV 3BBR GLY A  118  UNP  P19491              SEE REMARK 999                 
SEQADV 3BBR THR A  119  UNP  P19491              SEE REMARK 999                 
SEQADV 3BBR SER A  242  UNP  P19491    ASN   775 ENGINEERED                     
SEQADV 3BBR GLY B    1  UNP  P19491              EXPRESSION TAG                 
SEQADV 3BBR ALA B    2  UNP  P19491              EXPRESSION TAG                 
SEQADV 3BBR GLY B  118  UNP  P19491              SEE REMARK 999                 
SEQADV 3BBR THR B  119  UNP  P19491              SEE REMARK 999                 
SEQADV 3BBR SER B  242  UNP  P19491    ASN   775 ENGINEERED                     
SEQRES   1 A  263  GLY ALA ASN LYS THR VAL VAL VAL THR THR ILE LEU GLU          
SEQRES   2 A  263  SER PRO TYR VAL MET MET LYS LYS ASN HIS GLU MET LEU          
SEQRES   3 A  263  GLU GLY ASN GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU          
SEQRES   4 A  263  ALA ALA GLU ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS          
SEQRES   5 A  263  LEU THR ILE VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP          
SEQRES   6 A  263  ALA ASP THR LYS ILE TRP ASN GLY MET VAL GLY GLU LEU          
SEQRES   7 A  263  VAL TYR GLY LYS ALA ASP ILE ALA ILE ALA PRO LEU THR          
SEQRES   8 A  263  ILE THR LEU VAL ARG GLU GLU VAL ILE ASP PHE SER LYS          
SEQRES   9 A  263  PRO PHE MET SER LEU GLY ILE SER ILE MET ILE LYS LYS          
SEQRES  10 A  263  GLY THR PRO ILE GLU SER ALA GLU ASP LEU SER LYS GLN          
SEQRES  11 A  263  THR GLU ILE ALA TYR GLY THR LEU ASP SER GLY SER THR          
SEQRES  12 A  263  LYS GLU PHE PHE ARG ARG SER LYS ILE ALA VAL PHE ASP          
SEQRES  13 A  263  LYS MET TRP THR TYR MET ARG SER ALA GLU PRO SER VAL          
SEQRES  14 A  263  PHE VAL ARG THR THR ALA GLU GLY VAL ALA ARG VAL ARG          
SEQRES  15 A  263  LYS SER LYS GLY LYS TYR ALA TYR LEU LEU GLU SER THR          
SEQRES  16 A  263  MET ASN GLU TYR ILE GLU GLN ARG LYS PRO CYS ASP THR          
SEQRES  17 A  263  MET LYS VAL GLY GLY ASN LEU ASP SER LYS GLY TYR GLY          
SEQRES  18 A  263  ILE ALA THR PRO LYS GLY SER SER LEU GLY ASN ALA VAL          
SEQRES  19 A  263  ASN LEU ALA VAL LEU LYS LEU SER GLU GLN GLY LEU LEU          
SEQRES  20 A  263  ASP LYS LEU LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU          
SEQRES  21 A  263  CYS GLY SER                                                  
SEQRES   1 B  263  GLY ALA ASN LYS THR VAL VAL VAL THR THR ILE LEU GLU          
SEQRES   2 B  263  SER PRO TYR VAL MET MET LYS LYS ASN HIS GLU MET LEU          
SEQRES   3 B  263  GLU GLY ASN GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU          
SEQRES   4 B  263  ALA ALA GLU ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS          
SEQRES   5 B  263  LEU THR ILE VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP          
SEQRES   6 B  263  ALA ASP THR LYS ILE TRP ASN GLY MET VAL GLY GLU LEU          
SEQRES   7 B  263  VAL TYR GLY LYS ALA ASP ILE ALA ILE ALA PRO LEU THR          
SEQRES   8 B  263  ILE THR LEU VAL ARG GLU GLU VAL ILE ASP PHE SER LYS          
SEQRES   9 B  263  PRO PHE MET SER LEU GLY ILE SER ILE MET ILE LYS LYS          
SEQRES  10 B  263  GLY THR PRO ILE GLU SER ALA GLU ASP LEU SER LYS GLN          
SEQRES  11 B  263  THR GLU ILE ALA TYR GLY THR LEU ASP SER GLY SER THR          
SEQRES  12 B  263  LYS GLU PHE PHE ARG ARG SER LYS ILE ALA VAL PHE ASP          
SEQRES  13 B  263  LYS MET TRP THR TYR MET ARG SER ALA GLU PRO SER VAL          
SEQRES  14 B  263  PHE VAL ARG THR THR ALA GLU GLY VAL ALA ARG VAL ARG          
SEQRES  15 B  263  LYS SER LYS GLY LYS TYR ALA TYR LEU LEU GLU SER THR          
SEQRES  16 B  263  MET ASN GLU TYR ILE GLU GLN ARG LYS PRO CYS ASP THR          
SEQRES  17 B  263  MET LYS VAL GLY GLY ASN LEU ASP SER LYS GLY TYR GLY          
SEQRES  18 B  263  ILE ALA THR PRO LYS GLY SER SER LEU GLY ASN ALA VAL          
SEQRES  19 B  263  ASN LEU ALA VAL LEU LYS LEU SER GLU GLN GLY LEU LEU          
SEQRES  20 B  263  ASP LYS LEU LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU          
SEQRES  21 B  263  CYS GLY SER                                                  
HET    SO4  A 264       5                                                       
HET    SO4  A 265       5                                                       
HET     CL  A 266       1                                                       
HET    GLU  A 267      10                                                       
HET    BHY  A 268      28                                                       
HET    GOL  A 269       6                                                       
HET    SO4  B 264       5                                                       
HET    SO4  B 265       5                                                       
HET    SO4  B 266       5                                                       
HET    GLU  B 267      10                                                       
HET    GOL  B 268       6                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GLU GLUTAMIC ACID                                                    
HETNAM     BHY N,N'-[BIPHENYL-4,4'-DIYLDI(2R)PROPANE-2,1-                       
HETNAM   2 BHY  DIYL]DIMETHANESULFONAMIDE                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     BHY (R,R)-N,N-(2,2'-(BIPHENYL-4-4'-DIYL)BIS(PROPANE-2,1-             
HETSYN   2 BHY  DIYL))DIMETHANESULFONAMIDE                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  SO4    5(O4 S 2-)                                                   
FORMUL   5   CL    CL 1-                                                        
FORMUL   6  GLU    2(C5 H9 N O4)                                                
FORMUL   7  BHY    C20 H28 N2 O4 S2                                             
FORMUL   8  GOL    2(C3 H8 O3)                                                  
FORMUL  14  HOH   *524(H2 O)                                                    
HELIX    1   1 ASN A   22  LEU A   26  5                                   5    
HELIX    2   2 GLU A   27  GLU A   30  5                                   4    
HELIX    3   3 GLY A   34  GLY A   48  1                                  15    
HELIX    4   4 ASN A   72  TYR A   80  1                                   9    
HELIX    5   5 THR A   93  GLU A   98  1                                   6    
HELIX    6   6 SER A  123  LYS A  129  1                                   7    
HELIX    7   7 GLY A  141  SER A  150  1                                  10    
HELIX    8   8 ILE A  152  ALA A  165  1                                  14    
HELIX    9   9 THR A  173  SER A  184  1                                  12    
HELIX   10  10 SER A  194  GLN A  202  1                                   9    
HELIX   11  11 LEU A  230  GLN A  244  1                                  15    
HELIX   12  12 GLY A  245  TRP A  255  1                                  11    
HELIX   13  13 ASN B   22  LEU B   26  5                                   5    
HELIX   14  14 GLU B   27  GLU B   30  5                                   4    
HELIX   15  15 GLY B   34  GLY B   48  1                                  15    
HELIX   16  16 ASN B   72  TYR B   80  1                                   9    
HELIX   17  17 THR B   93  GLU B   98  1                                   6    
HELIX   18  18 SER B  123  LYS B  129  1                                   7    
HELIX   19  19 GLY B  141  SER B  150  1                                  10    
HELIX   20  20 ILE B  152  ALA B  165  1                                  14    
HELIX   21  21 THR B  173  SER B  184  1                                  12    
HELIX   22  22 SER B  194  GLN B  202  1                                   9    
HELIX   23  23 LEU B  230  GLN B  244  1                                  15    
HELIX   24  24 GLY B  245  TYR B  256  1                                  12    
SHEET    1   A 3 TYR A  51  ILE A  55  0                                        
SHEET    2   A 3 VAL A   6  THR A  10  1  N  VAL A   6   O  LYS A  52           
SHEET    3   A 3 ILE A  85  ALA A  86  1  O  ILE A  85   N  THR A   9           
SHEET    1   B 2 MET A  18  MET A  19  0                                        
SHEET    2   B 2 TYR A  32  GLU A  33 -1  O  GLU A  33   N  MET A  18           
SHEET    1   C 2 ILE A 100  PHE A 102  0                                        
SHEET    2   C 2 ALA A 223  PRO A 225 -1  O  THR A 224   N  ASP A 101           
SHEET    1   D 2 MET A 107  LEU A 109  0                                        
SHEET    2   D 2 LYS A 218  TYR A 220 -1  O  LYS A 218   N  LEU A 109           
SHEET    1   E 4 ALA A 134  THR A 137  0                                        
SHEET    2   E 4 TYR A 188  GLU A 193  1  O  ALA A 189   N  ALA A 134           
SHEET    3   E 4 ILE A 111  LYS A 116 -1  N  MET A 114   O  TYR A 190           
SHEET    4   E 4 THR A 208  VAL A 211 -1  O  MET A 209   N  ILE A 115           
SHEET    1   F 3 TYR B  51  ILE B  55  0                                        
SHEET    2   F 3 VAL B   6  THR B  10  1  N  VAL B   8   O  THR B  54           
SHEET    3   F 3 ILE B  85  ALA B  86  1  O  ILE B  85   N  THR B   9           
SHEET    1   G 2 MET B  18  MET B  19  0                                        
SHEET    2   G 2 TYR B  32  GLU B  33 -1  O  GLU B  33   N  MET B  18           
SHEET    1   H 2 ILE B 100  PHE B 102  0                                        
SHEET    2   H 2 ALA B 223  PRO B 225 -1  O  THR B 224   N  ASP B 101           
SHEET    1   I 2 MET B 107  LEU B 109  0                                        
SHEET    2   I 2 LYS B 218  TYR B 220 -1  O  LYS B 218   N  LEU B 109           
SHEET    1   J 4 ALA B 134  GLY B 136  0                                        
SHEET    2   J 4 TYR B 188  GLU B 193  1  O  LEU B 191   N  GLY B 136           
SHEET    3   J 4 ILE B 111  LYS B 116 -1  N  MET B 114   O  TYR B 190           
SHEET    4   J 4 THR B 208  VAL B 211 -1  O  MET B 209   N  ILE B 115           
SSBOND   1 CYS A  206    CYS A  261                          1555   1555  2.03  
SSBOND   2 CYS B  206    CYS B  261                          1555   1555  2.03  
CISPEP   1 SER A   14    PRO A   15          0        -0.93                     
CISPEP   2 GLU A  166    PRO A  167          0        -0.05                     
CISPEP   3 LYS A  204    PRO A  205          0         6.91                     
CISPEP   4 SER B   14    PRO B   15          0        -2.32                     
CISPEP   5 GLU B  166    PRO B  167          0        -2.81                     
CISPEP   6 LYS B  204    PRO B  205          0         4.73                     
SITE     1 AC1  3 ARG B 148  TRP B 159  ARG B 163                               
SITE     1 AC2  8 ASP B 139  SER B 140  LYS B 144  ARG B 148                    
SITE     2 AC2  8 HOH B 297  HOH B 379  HOH B 399  HOH B 442                    
SITE     1 AC3  6 SER A 140  LYS A 144  ARG A 148  HOH A 295                    
SITE     2 AC3  6 HOH A 312  HOH A 366                                          
SITE     1 AC4  5 HIS B  23  ARG B  31  HOH B 285  HOH B 523                    
SITE     2 AC4  5 HOH B 534                                                     
SITE     1 AC5  6 ARG A  31  HOH A 294  HOH A 318  HOH A 328                    
SITE     2 AC5  6 HOH A 461  LYS B 183                                          
SITE     1 AC6  1 ASN A  22                                                     
SITE     1 AC7 14 TYR A  61  PRO A  89  LEU A  90  THR A  91                    
SITE     2 AC7 14 ARG A  96  LEU A 138  GLY A 141  SER A 142                    
SITE     3 AC7 14 THR A 143  GLU A 193  TYR A 220  HOH A 281                    
SITE     4 AC7 14 HOH A 282  HOH A 304                                          
SITE     1 AC8 13 TYR B  61  PRO B  89  LEU B  90  THR B  91                    
SITE     2 AC8 13 ARG B  96  GLY B 141  SER B 142  THR B 143                    
SITE     3 AC8 13 GLU B 193  TYR B 220  HOH B 276  HOH B 287                    
SITE     4 AC8 13 HOH B 298                                                     
SITE     1 AC9 19 LYS A 104  PRO A 105  MET A 107  SER A 108                    
SITE     2 AC9 19 SER A 217  LYS A 218  GLY A 219  LEU A 239                    
SITE     3 AC9 19 HOH A 416  HOH A 437  LYS B 104  PRO B 105                    
SITE     4 AC9 19 MET B 107  SER B 108  SER B 217  LYS B 218                    
SITE     5 AC9 19 GLY B 219  LEU B 239  SER B 242                               
SITE     1 BC1  6 TYR B 161  SER B 164  ALA B 165  GLU B 166                    
SITE     2 BC1  6 HOH B 425  HOH B 457                                          
SITE     1 BC2  3 ARG A 148  TRP A 159  ARG A 163                               
CRYST1   99.080  121.780   47.427  90.00  90.00  90.00 P 21 21 2     8          
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      0.010093  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008212  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021085        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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