GenomeNet

Database: PDB
Entry: 4O3C
LinkDB: 4O3C
Original site: 4O3C 
HEADER    MEMBRANE PROTEIN/AGONIST                18-DEC-13   4O3C              
TITLE     CRYSTAL STRUCTURE OF THE GLUA2 LIGAND-BINDING DOMAIN IN COMPLEX WITH  
TITLE    2 L-ASPARTATE AT 1.50 A RESOLUTION                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMATE RECEPTOR 2;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: LIGAND BINDING DOMAIN (UNP RESIDUES 413-527 AND UNP        
COMPND   5 RESIDUES 653-796);                                                   
COMPND   6 SYNONYM: GLUR-2,AMPA-SELECTIVE GLUTAMATE RECEPTOR 2,GLUR-B,GLUR-K2,  
COMPND   7 GLUTAMATE RECEPTOR IONOTROPIC,AMPA 2;                                
COMPND   8 ENGINEERED: 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: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ORIGAMI B (DE3);                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-22B(+)                                
KEYWDS    AMPA RECEPTOR LIGAND-BINDING DOMAIN, GLUA2, AGONIST, MEMBRANE         
KEYWDS   2 PROTEIN, MEMBRANE PROTEIN-AGONIST COMPLEX                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.KRINTEL,K.FRYDENVANG,A.M.KAERN,M.GAJHEDE,J.S.KASTRUP                
REVDAT   5   07-MAR-18 4O3C    1       REMARK                                   
REVDAT   4   31-MAY-17 4O3C    1       COMPND REMARK DBREF                      
REVDAT   3   14-DEC-16 4O3C    1       TITLE                                    
REVDAT   2   18-JUN-14 4O3C    1       JRNL                                     
REVDAT   1   16-APR-14 4O3C    0                                                
JRNL        AUTH   C.KRINTEL,K.FRYDENVANG,A.CERAVALLS DE RABASSA,A.M.KAERN,     
JRNL        AUTH 2 M.GAJHEDE,D.S.PICKERING,J.S.KASTRUP                          
JRNL        TITL   L-ASP IS A USEFUL TOOL IN THE PURIFICATION OF THE IONOTROPIC 
JRNL        TITL 2 GLUTAMATE RECEPTOR A2 LIGAND-BINDING DOMAIN.                 
JRNL        REF    FEBS J.                       V. 281  2422 2014              
JRNL        REFN                   ISSN 1742-464X                               
JRNL        PMID   24673938                                                     
JRNL        DOI    10.1111/FEBS.12795                                           
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   N.ARMSTRONG,E.GOUAUX                                         
REMARK   1  TITL   MECHANISMS FOR ACTIVATION AND ANTAGONISM OF AN               
REMARK   1  TITL 2 AMPA-SENSITIVE GLUTAMATE RECEPTOR: CRYSTAL STRUCTURES OF THE 
REMARK   1  TITL 3 GLUR2 LIGAND BINDING CORE.                                   
REMARK   1  REF    NEURON                        V.  28   165 2000              
REMARK   1  REFN                   ISSN 0896-6273                               
REMARK   1  PMID   11086992                                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.64                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 43220                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.129                           
REMARK   3   R VALUE            (WORKING SET) : 0.127                           
REMARK   3   FREE R VALUE                     : 0.158                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2177                            
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 26.6391 -  3.7764    0.99        0   149  0.1641 0.1718        
REMARK   3     2  3.7764 -  2.9988    1.00        0   151  0.1408 0.1481        
REMARK   3     3  2.9988 -  2.6201    1.00        0   143  0.1358 0.1397        
REMARK   3     4  2.6201 -  2.3807    1.00        0   132  0.1261 0.1536        
REMARK   3     5  2.3807 -  2.2102    1.00        0   133  0.1090 0.1441        
REMARK   3     6  2.2102 -  2.0799    1.00        0   134  0.1069 0.1595        
REMARK   3     7  2.0799 -  1.9758    1.00        0   132  0.1032 0.1590        
REMARK   3     8  1.9758 -  1.8898    1.00        0   135  0.0970 0.1390        
REMARK   3     9  1.8898 -  1.8171    1.00        0   141  0.1035 0.1510        
REMARK   3    10  1.8171 -  1.7544    1.00        0   112  0.1022 0.1685        
REMARK   3    11  1.7544 -  1.6995    1.00        0   131  0.0981 0.1687        
REMARK   3    12  1.6995 -  1.6510    1.00        0   139  0.1050 0.1736        
REMARK   3    13  1.6510 -  1.6075    1.00        0   138  0.1108 0.1727        
REMARK   3    14  1.6075 -  1.5683    1.00        0   133  0.1142 0.1728        
REMARK   3    15  1.5683 -  1.5326    1.00        0   137  0.1215 0.1996        
REMARK   3    16  1.5326 -  1.5000    1.00        0   137  0.1351 0.2064        
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              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
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) : 14.17                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.91                          
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      :  0.008           NULL                                  
REMARK   3   ANGLE     :  1.251           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :  0.006           NULL                                  
REMARK   3   DIHEDRAL  : 11.703           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: REFINEMENT DONE WITH RIDING HYDROGEN      
REMARK   3  ATOMS AND ANISOTROPIC B-FACTORS (NOT INCLUDING WATER).              
REMARK   4                                                                      
REMARK   4 4O3C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JAN-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000083989.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-MAY-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I911-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
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 : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.9                        
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43268                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.38000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.1.4                                          
REMARK 200 STARTING MODEL: STARTING MODEL 1M5C                                  
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 0.1 M LITHIUM SULFATE      
REMARK 280  AND 0.1 M PHOSPHATE-CITRATE., PH 4.5, VAPOR DIFFUSION, HANGING      
REMARK 280  DROP, TEMPERATURE 279K                                              
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       31.99850            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.93850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.99850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.93850            
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: 4630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -150.0 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 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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   263                                                      
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   OE1  GLU A    77     O    HOH A   461              2.15            
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    ASN A  22       32.00    -97.69                                   
REMARK 500    TRP A 255      -68.47   -105.83                                   
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 A 606        DISTANCE =  5.87 ANGSTROMS                       
REMARK 525    HOH A 646        DISTANCE =  7.16 ANGSTROMS                       
REMARK 525    HOH A 647        DISTANCE =  7.31 ANGSTROMS                       
REMARK 525    HOH A 669        DISTANCE =  9.42 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              LI A 305  LI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 509   O                                                      
REMARK 620 2 ASN A 242   OD1  85.6                                              
REMARK 620 3 HOH A 412   O    98.4  84.7                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ASP A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LI A 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 309                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FTO   RELATED DB: PDB                                   
REMARK 900 GLUA2 LIGAND BINDING CORE (S1S2J) IN THE APO STATE                   
REMARK 900 RELATED ID: 1FTJ   RELATED DB: PDB                                   
REMARK 900 GLUA2 S1S2J IN COMPLEX WITH THE FULL AGONIST GLUTAMATE               
REMARK 900 RELATED ID: 4O3A   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4O3B   RELATED DB: PDB                                   
DBREF  4O3C A    3   117  UNP    P19491   GRIA2_RAT      413    527             
DBREF  4O3C A  120   263  UNP    P19491   GRIA2_RAT      653    796             
SEQADV 4O3C GLY A    1  UNP  P19491              EXPRESSION TAG                 
SEQADV 4O3C ALA A    2  UNP  P19491              EXPRESSION TAG                 
SEQADV 4O3C GLY A  118  UNP  P19491              LINKER                         
SEQADV 4O3C THR A  119  UNP  P19491              LINKER                         
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 ASN 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                                                  
HET    ASP  A 301       9                                                       
HET     CL  A 302       1                                                       
HET    GOL  A 303       6                                                       
HET    ACT  A 304       4                                                       
HET     LI  A 305       1                                                       
HET    SO4  A 306       5                                                       
HET    SO4  A 307       5                                                       
HET    SO4  A 308       5                                                       
HET    SO4  A 309       5                                                       
HETNAM     ASP ASPARTIC ACID                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETNAM     ACT ACETATE ION                                                      
HETNAM      LI LITHIUM ION                                                      
HETNAM     SO4 SULFATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  ASP    C4 H7 N O4                                                   
FORMUL   3   CL    CL 1-                                                        
FORMUL   4  GOL    C3 H8 O3                                                     
FORMUL   5  ACT    C2 H3 O2 1-                                                  
FORMUL   6   LI    LI 1+                                                        
FORMUL   7  SO4    4(O4 S 2-)                                                   
FORMUL  11  HOH   *269(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    
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   8   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  LEU A 191   N  GLY A 136           
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           
SSBOND   1 CYS A  206    CYS A  261                          1555   1555  2.04  
LINK        LI    LI A 305                 O   HOH A 509     1555   1555  2.12  
LINK         OD1 ASN A 242                LI    LI A 305     1555   1555  2.18  
LINK        LI    LI A 305                 O   HOH A 412     1555   1555  2.24  
CISPEP   1 SER A   14    PRO A   15          0         0.02                     
CISPEP   2 GLU A  166    PRO A  167          0        -3.60                     
CISPEP   3 GLU A  166    PRO A  167          0        -4.75                     
CISPEP   4 LYS A  204    PRO A  205          0         6.34                     
SITE     1 AC1 11 TYR A  61  PRO A  89  LEU A  90  THR A  91                    
SITE     2 AC1 11 ARG A  96  GLY A 141  SER A 142  THR A 143                    
SITE     3 AC1 11 GLU A 193  HOH A 420  HOH A 465                               
SITE     1 AC2  2 SER A 108  ACT A 304                                          
SITE     1 AC3  7 ARG A  31  HIS A  46  LYS A 240  GLN A 244                    
SITE     2 AC3  7 SO4 A 306  HOH A 607  HOH A 609                               
SITE     1 AC4  7 MET A 107  SER A 108  SER A 217  ASN A 242                    
SITE     2 AC4  7  CL A 302   LI A 305  HOH A 498                               
SITE     1 AC5  5 SER A 217  ASN A 242  ACT A 304  HOH A 412                    
SITE     2 AC5  5 HOH A 509                                                     
SITE     1 AC6  7 HIS A  23  GLU A  24  ARG A  31  HIS A  46                    
SITE     2 AC6  7 LYS A 240  GOL A 303  HOH A 591                               
SITE     1 AC7  7 SER A 140  LYS A 144  ARG A 148  HOH A 440                    
SITE     2 AC7  7 HOH A 462  HOH A 497  HOH A 615                               
SITE     1 AC8  7 GLU A  27  GLY A  28  ASN A  29  GLU A  30                    
SITE     2 AC8  7 ARG A 149  LYS A 151  HOH A 559                               
SITE     1 AC9  4 ARG A 148  TRP A 159  ARG A 163  HOH A 551                    
CRYST1   63.997   87.877   47.042  90.00  90.00  90.00 P 21 21 2     4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015626  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011380  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021258        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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