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Database: PDB
Entry: 3T9X
LinkDB: 3T9X
Original site: 3T9X 
HEADER    TRANSPORT PROTEIN                       03-AUG-11   3T9X              
TITLE     GLUTAMATE BOUND TO A DOUBLE CYSTEINE MUTANT (V484C/E657C) OF THE      
TITLE    2 LIGAND BINDING DOMAIN OF GLUA2                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMATE RECEPTOR 2;                                      
COMPND   3 CHAIN: B, D, F;                                                      
COMPND   4 FRAGMENT: SEE REMARK 999;                                            
COMPND   5 SYNONYM: GLUA2, GLUR2, AMPA-SELECTIVE GLUTAMATE RECEPTOR 2, GLUR-B,  
COMPND   6 GLUR-K2;                                                             
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,GLUA2;                                                   
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    S1S2, NEUROTRANSMITTER RECEPTOR, TRANSPORT PROTEIN                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.H.AHMED,R.E.OSWALD                                                  
REVDAT   4   26-JUL-17 3T9X    1       SOURCE                                   
REVDAT   3   19-OCT-11 3T9X    1       JRNL                                     
REVDAT   2   31-AUG-11 3T9X    1       JRNL                                     
REVDAT   1   17-AUG-11 3T9X    0                                                
JRNL        AUTH   A.H.AHMED,S.WANG,H.H.CHUANG,R.E.OSWALD                       
JRNL        TITL   MECHANISM OF AMPA RECEPTOR ACTIVATION BY PARTIAL AGONISTS:   
JRNL        TITL 2 DISULFIDE TRAPPING OF CLOSED LOBE CONFORMATIONS.             
JRNL        REF    J.BIOL.CHEM.                  V. 286 35257 2011              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   21846932                                                     
JRNL        DOI    10.1074/JBC.M111.269001                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.82 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
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) : 1.82                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.84                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.130                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 74434                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.620                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1953                            
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 46.8583 -  4.3930    0.76     4503   123  0.2157 0.2792        
REMARK   3     2  4.3930 -  3.4872    0.88     5044   135  0.1723 0.2001        
REMARK   3     3  3.4872 -  3.0465    0.96     5368   145  0.1826 0.1938        
REMARK   3     4  3.0465 -  2.7680    0.98     5432   147  0.2029 0.2518        
REMARK   3     5  2.7680 -  2.5696    0.98     5466   147  0.2008 0.2551        
REMARK   3     6  2.5696 -  2.4181    0.98     5457   144  0.2041 0.2457        
REMARK   3     7  2.4181 -  2.2970    0.97     5354   143  0.1985 0.2289        
REMARK   3     8  2.2970 -  2.1970    0.97     5339   145  0.1966 0.2641        
REMARK   3     9  2.1970 -  2.1125    0.96     5314   144  0.1953 0.2299        
REMARK   3    10  2.1125 -  2.0396    0.96     5257   140  0.2025 0.2373        
REMARK   3    11  2.0396 -  1.9758    0.95     5199   143  0.2090 0.2647        
REMARK   3    12  1.9758 -  1.9193    0.92     5116   135  0.2193 0.2538        
REMARK   3    13  1.9193 -  1.8688    0.92     5061   138  0.2148 0.2572        
REMARK   3    14  1.8688 -  1.8232    0.84     4571   124  0.2200 0.2556        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.42                                          
REMARK   3   B_SOL              : 66.92                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.250            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.700           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.51660                                             
REMARK   3    B22 (A**2) : 0.33970                                              
REMARK   3    B33 (A**2) : 4.17690                                              
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      :  0.008           6145                                  
REMARK   3   ANGLE     :  1.096           8256                                  
REMARK   3   CHIRALITY :  0.076            912                                  
REMARK   3   PLANARITY :  0.004           1034                                  
REMARK   3   DIHEDRAL  : 15.495           2270                                  
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 3T9X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-AUG-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000067221.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-MAR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.977                              
REMARK 200  MONOCHROMATOR                  : RH COATED SI                       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 76183                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.820                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.5                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : 0.07300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 33.5800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.30900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.103                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3DP6                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 14-15% PEG8000, 0.1 M SODIUM             
REMARK 280  CACODYLATE, 0.1-0.15 M ZINC ACETATE, 0.25 M AMMONIUM SULFATE, PH    
REMARK 280  6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
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+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-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       57.11150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       81.88200            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.11150            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       81.88200            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 2160 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F                                  
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 2090 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22490 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -100.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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      114.22300            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      163.76400            
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 D 760  LIES ON A SPECIAL POSITION.                          
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS B   4    CB   CG   CD   CE   NZ                              
REMARK 470     ASP B  67    CB   CG   OD1  OD2                                  
REMARK 470     CYS B 261    O                                                   
REMARK 470     LYS D   4    CB   CG   CD   CE   NZ                              
REMARK 470     ASP D  67    CB   CG   OD1  OD2                                  
REMARK 470     GLU D 122    CB   CG   CD   OE1  OE2                             
REMARK 470     ILE D 152    CD1                                                 
REMARK 470     CYS D 261    O                                                   
REMARK 470     LYS F   4    CB   CG   CD   CE   NZ                              
REMARK 470     ASN F 232    CG   OD1  ND2                                       
REMARK 470     CYS F 261    O                                                   
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 B  67      -70.62    -79.55                                   
REMARK 500    THR F 131      -24.43   -143.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              ZN D 262  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU F  24   OE2                                                    
REMARK 620 2 GLU D  30   OE2 131.4                                              
REMARK 620 3 HIS D  23   NE2 121.5 103.2                                        
REMARK 620 4 GLU F  24   OE1  55.2 123.5 114.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D   2  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  46   NE2                                                    
REMARK 620 2 GLU D  42   OE1  91.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B   1  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  42   OE1                                                    
REMARK 620 2 HIS B  46   NE2  88.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 262  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  46   NE2                                                    
REMARK 620 2 GLU F  42   OE1 104.8                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLU B 274                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 3                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLU D 274                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 262                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLU F 274                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 262                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3T93   RELATED DB: PDB                                   
REMARK 900 GLUTAMATE BOUND TO A DOUBLE CYSTEINE MUTANT (A452C/S652C) OF THE     
REMARK 900 LIGAND BINDING DOMAIN OF GLUA2                                       
REMARK 900 RELATED ID: 3T96   RELATED DB: PDB                                   
REMARK 900 IODOWILLARDIINE BOUND TO A DOUBLE CYSTEINE MUTANT (A452C/S652C) OF   
REMARK 900 THE LIGAND BINDING DOMAIN OF GLUA2                                   
REMARK 900 RELATED ID: 3T9H   RELATED DB: PDB                                   
REMARK 900 KAINATE BOUND TO A DOUBLE CYSTEINE MUTANT (A452C/S652C) OF THE       
REMARK 900 LIGAND BINDING DOMAIN OF GLUA2                                       
REMARK 900 RELATED ID: 3T9U   RELATED DB: PDB                                   
REMARK 900 CNQX BOUND TO AN OXIDIZED DOUBLE CYSTEINE MUTANT (A452C/S652C) OF    
REMARK 900 THE LIGAND BINDING DOMAIN OF GLUA2                                   
REMARK 900 RELATED ID: 3T9V   RELATED DB: PDB                                   
REMARK 900 CNQX BOUND TO A REDUCED DOUBLE CYSTEINE MUTANT (A452C/S652C) OF THE  
REMARK 900 LIGAND BINDING DOMAIN OF GLUA2                                       
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 PROTEIN FRAGMENT COMPRISES UNP RESIDUES 414-527 AND UNP RESIDUES     
REMARK 999 653-794 CONNECTED BY AN ENGINEERED GT LINKER.                        
DBREF  3T9X B    4   117  UNP    P19491   GRIA2_RAT      414    527             
DBREF  3T9X B  120   261  UNP    P19491   GRIA2_RAT      653    794             
DBREF  3T9X D    4   117  UNP    P19491   GRIA2_RAT      414    527             
DBREF  3T9X D  120   261  UNP    P19491   GRIA2_RAT      653    794             
DBREF  3T9X F    4   117  UNP    P19491   GRIA2_RAT      414    527             
DBREF  3T9X F  120   261  UNP    P19491   GRIA2_RAT      653    794             
SEQADV 3T9X CYS B   95  UNP  P19491    VAL   505 ENGINEERED MUTATION            
SEQADV 3T9X GLY B  118  UNP  P19491              LINKER                         
SEQADV 3T9X THR B  119  UNP  P19491              LINKER                         
SEQADV 3T9X CYS B  145  UNP  P19491    GLU   678 ENGINEERED MUTATION            
SEQADV 3T9X CYS D   95  UNP  P19491    VAL   505 ENGINEERED MUTATION            
SEQADV 3T9X GLY D  118  UNP  P19491              LINKER                         
SEQADV 3T9X THR D  119  UNP  P19491              LINKER                         
SEQADV 3T9X CYS D  145  UNP  P19491    GLU   678 ENGINEERED MUTATION            
SEQADV 3T9X CYS F   95  UNP  P19491    VAL   505 ENGINEERED MUTATION            
SEQADV 3T9X GLY F  118  UNP  P19491              LINKER                         
SEQADV 3T9X THR F  119  UNP  P19491              LINKER                         
SEQADV 3T9X CYS F  145  UNP  P19491    GLU   678 ENGINEERED MUTATION            
SEQRES   1 B  258  LYS THR VAL VAL VAL THR THR ILE LEU GLU SER PRO TYR          
SEQRES   2 B  258  VAL MET MET LYS LYS ASN HIS GLU MET LEU GLU GLY ASN          
SEQRES   3 B  258  GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU ALA ALA GLU          
SEQRES   4 B  258  ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS LEU THR ILE          
SEQRES   5 B  258  VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP ALA ASP THR          
SEQRES   6 B  258  LYS ILE TRP ASN GLY MET VAL GLY GLU LEU VAL TYR GLY          
SEQRES   7 B  258  LYS ALA ASP ILE ALA ILE ALA PRO LEU THR ILE THR LEU          
SEQRES   8 B  258  CYS ARG GLU GLU VAL ILE ASP PHE SER LYS PRO PHE MET          
SEQRES   9 B  258  SER LEU GLY ILE SER ILE MET ILE LYS LYS GLY THR PRO          
SEQRES  10 B  258  ILE GLU SER ALA GLU ASP LEU SER LYS GLN THR GLU ILE          
SEQRES  11 B  258  ALA TYR GLY THR LEU ASP SER GLY SER THR LYS CYS PHE          
SEQRES  12 B  258  PHE ARG ARG SER LYS ILE ALA VAL PHE ASP LYS MET TRP          
SEQRES  13 B  258  THR TYR MET ARG SER ALA GLU PRO SER VAL PHE VAL ARG          
SEQRES  14 B  258  THR THR ALA GLU GLY VAL ALA ARG VAL ARG LYS SER LYS          
SEQRES  15 B  258  GLY LYS TYR ALA TYR LEU LEU GLU SER THR MET ASN GLU          
SEQRES  16 B  258  TYR ILE GLU GLN ARG LYS PRO CYS ASP THR MET LYS VAL          
SEQRES  17 B  258  GLY GLY ASN LEU ASP SER LYS GLY TYR GLY ILE ALA THR          
SEQRES  18 B  258  PRO LYS GLY SER SER LEU GLY ASN ALA VAL ASN LEU ALA          
SEQRES  19 B  258  VAL LEU LYS LEU ASN GLU GLN GLY LEU LEU ASP LYS LEU          
SEQRES  20 B  258  LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU CYS                  
SEQRES   1 D  258  LYS THR VAL VAL VAL THR THR ILE LEU GLU SER PRO TYR          
SEQRES   2 D  258  VAL MET MET LYS LYS ASN HIS GLU MET LEU GLU GLY ASN          
SEQRES   3 D  258  GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU ALA ALA GLU          
SEQRES   4 D  258  ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS LEU THR ILE          
SEQRES   5 D  258  VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP ALA ASP THR          
SEQRES   6 D  258  LYS ILE TRP ASN GLY MET VAL GLY GLU LEU VAL TYR GLY          
SEQRES   7 D  258  LYS ALA ASP ILE ALA ILE ALA PRO LEU THR ILE THR LEU          
SEQRES   8 D  258  CYS ARG GLU GLU VAL ILE ASP PHE SER LYS PRO PHE MET          
SEQRES   9 D  258  SER LEU GLY ILE SER ILE MET ILE LYS LYS GLY THR PRO          
SEQRES  10 D  258  ILE GLU SER ALA GLU ASP LEU SER LYS GLN THR GLU ILE          
SEQRES  11 D  258  ALA TYR GLY THR LEU ASP SER GLY SER THR LYS CYS PHE          
SEQRES  12 D  258  PHE ARG ARG SER LYS ILE ALA VAL PHE ASP LYS MET TRP          
SEQRES  13 D  258  THR TYR MET ARG SER ALA GLU PRO SER VAL PHE VAL ARG          
SEQRES  14 D  258  THR THR ALA GLU GLY VAL ALA ARG VAL ARG LYS SER LYS          
SEQRES  15 D  258  GLY LYS TYR ALA TYR LEU LEU GLU SER THR MET ASN GLU          
SEQRES  16 D  258  TYR ILE GLU GLN ARG LYS PRO CYS ASP THR MET LYS VAL          
SEQRES  17 D  258  GLY GLY ASN LEU ASP SER LYS GLY TYR GLY ILE ALA THR          
SEQRES  18 D  258  PRO LYS GLY SER SER LEU GLY ASN ALA VAL ASN LEU ALA          
SEQRES  19 D  258  VAL LEU LYS LEU ASN GLU GLN GLY LEU LEU ASP LYS LEU          
SEQRES  20 D  258  LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU CYS                  
SEQRES   1 F  258  LYS THR VAL VAL VAL THR THR ILE LEU GLU SER PRO TYR          
SEQRES   2 F  258  VAL MET MET LYS LYS ASN HIS GLU MET LEU GLU GLY ASN          
SEQRES   3 F  258  GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU ALA ALA GLU          
SEQRES   4 F  258  ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS LEU THR ILE          
SEQRES   5 F  258  VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP ALA ASP THR          
SEQRES   6 F  258  LYS ILE TRP ASN GLY MET VAL GLY GLU LEU VAL TYR GLY          
SEQRES   7 F  258  LYS ALA ASP ILE ALA ILE ALA PRO LEU THR ILE THR LEU          
SEQRES   8 F  258  CYS ARG GLU GLU VAL ILE ASP PHE SER LYS PRO PHE MET          
SEQRES   9 F  258  SER LEU GLY ILE SER ILE MET ILE LYS LYS GLY THR PRO          
SEQRES  10 F  258  ILE GLU SER ALA GLU ASP LEU SER LYS GLN THR GLU ILE          
SEQRES  11 F  258  ALA TYR GLY THR LEU ASP SER GLY SER THR LYS CYS PHE          
SEQRES  12 F  258  PHE ARG ARG SER LYS ILE ALA VAL PHE ASP LYS MET TRP          
SEQRES  13 F  258  THR TYR MET ARG SER ALA GLU PRO SER VAL PHE VAL ARG          
SEQRES  14 F  258  THR THR ALA GLU GLY VAL ALA ARG VAL ARG LYS SER LYS          
SEQRES  15 F  258  GLY LYS TYR ALA TYR LEU LEU GLU SER THR MET ASN GLU          
SEQRES  16 F  258  TYR ILE GLU GLN ARG LYS PRO CYS ASP THR MET LYS VAL          
SEQRES  17 F  258  GLY GLY ASN LEU ASP SER LYS GLY TYR GLY ILE ALA THR          
SEQRES  18 F  258  PRO LYS GLY SER SER LEU GLY ASN ALA VAL ASN LEU ALA          
SEQRES  19 F  258  VAL LEU LYS LEU ASN GLU GLN GLY LEU LEU ASP LYS LEU          
SEQRES  20 F  258  LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU CYS                  
HET    GLU  B 274      10                                                       
HET     ZN  B   1       1                                                       
HET     ZN  B   3       1                                                       
HET    GLU  D 274      10                                                       
HET     ZN  D   2       1                                                       
HET     ZN  D 262       1                                                       
HET    GLU  F 274      10                                                       
HET     ZN  F 262       1                                                       
HETNAM     GLU GLUTAMIC ACID                                                    
HETNAM      ZN ZINC ION                                                         
FORMUL   4  GLU    3(C5 H9 N O4)                                                
FORMUL   5   ZN    5(ZN 2+)                                                     
FORMUL  12  HOH   *834(H2 O)                                                    
HELIX    1   1 ASN B   22  LEU B   26  5                                   5    
HELIX    2   2 GLU B   27  GLU B   30  5                                   4    
HELIX    3   3 GLY B   34  GLY B   48  1                                  15    
HELIX    4   4 ASN B   72  TYR B   80  1                                   9    
HELIX    5   5 THR B   93  GLU B   98  1                                   6    
HELIX    6   6 SER B  123  LYS B  129  1                                   7    
HELIX    7   7 GLY B  141  SER B  150  1                                  10    
HELIX    8   8 ILE B  152  ALA B  165  1                                  14    
HELIX    9   9 THR B  173  SER B  184  1                                  12    
HELIX   10  10 SER B  194  GLN B  202  1                                   9    
HELIX   11  11 LEU B  230  GLN B  244  1                                  15    
HELIX   12  12 GLY B  245  TYR B  256  1                                  12    
HELIX   13  13 GLU D   27  GLU D   30  5                                   4    
HELIX   14  14 GLY D   34  GLY D   48  1                                  15    
HELIX   15  15 ASN D   72  TYR D   80  1                                   9    
HELIX   16  16 THR D   93  GLU D   98  1                                   6    
HELIX   17  17 SER D  123  LYS D  129  1                                   7    
HELIX   18  18 GLY D  141  SER D  150  1                                  10    
HELIX   19  19 ILE D  152  ALA D  165  1                                  14    
HELIX   20  20 THR D  173  SER D  184  1                                  12    
HELIX   21  21 SER D  194  GLN D  202  1                                   9    
HELIX   22  22 LEU D  230  GLN D  244  1                                  15    
HELIX   23  23 GLY D  245  TRP D  255  1                                  11    
HELIX   24  24 ASN F   22  LEU F   26  5                                   5    
HELIX   25  25 GLU F   27  GLU F   30  5                                   4    
HELIX   26  26 GLY F   34  GLY F   48  1                                  15    
HELIX   27  27 ASN F   72  TYR F   80  1                                   9    
HELIX   28  28 THR F   93  GLU F   98  1                                   6    
HELIX   29  29 SER F  123  LYS F  129  1                                   7    
HELIX   30  30 GLY F  141  ARG F  149  1                                   9    
HELIX   31  31 ILE F  152  ARG F  163  1                                  12    
HELIX   32  32 THR F  173  LYS F  183  1                                  11    
HELIX   33  33 SER F  194  GLN F  202  1                                   9    
HELIX   34  34 LEU F  230  GLN F  244  1                                  15    
HELIX   35  35 GLY F  245  TYR F  256  1                                  12    
SHEET    1   A 3 TYR B  51  ILE B  55  0                                        
SHEET    2   A 3 VAL B   6  THR B  10  1  N  VAL B   6   O  LYS B  52           
SHEET    3   A 3 ILE B  85  ALA B  86  1  O  ILE B  85   N  THR B   9           
SHEET    1   B 2 MET B  18  MET B  19  0                                        
SHEET    2   B 2 TYR B  32  GLU B  33 -1  O  GLU B  33   N  MET B  18           
SHEET    1   C 2 ILE B 100  PHE B 102  0                                        
SHEET    2   C 2 ALA B 223  PRO B 225 -1  O  THR B 224   N  ASP B 101           
SHEET    1   D 2 MET B 107  LEU B 109  0                                        
SHEET    2   D 2 LYS B 218  TYR B 220 -1  O  LYS B 218   N  LEU B 109           
SHEET    1   E 4 ALA B 134  THR B 137  0                                        
SHEET    2   E 4 TYR B 188  GLU B 193  1  O  ALA B 189   N  ALA B 134           
SHEET    3   E 4 ILE B 111  LYS B 116 -1  N  SER B 112   O  LEU B 192           
SHEET    4   E 4 THR B 208  VAL B 211 -1  O  MET B 209   N  ILE B 115           
SHEET    1   F 3 TYR D  51  ILE D  55  0                                        
SHEET    2   F 3 VAL D   6  THR D  10  1  N  VAL D   8   O  LYS D  52           
SHEET    3   F 3 ILE D  85  ALA D  86  1  O  ILE D  85   N  THR D   9           
SHEET    1   G 2 MET D  18  MET D  19  0                                        
SHEET    2   G 2 TYR D  32  GLU D  33 -1  O  GLU D  33   N  MET D  18           
SHEET    1   H 2 ILE D 100  PHE D 102  0                                        
SHEET    2   H 2 ALA D 223  PRO D 225 -1  O  THR D 224   N  ASP D 101           
SHEET    1   I 2 MET D 107  LEU D 109  0                                        
SHEET    2   I 2 LYS D 218  TYR D 220 -1  O  LYS D 218   N  LEU D 109           
SHEET    1   J 4 ALA D 134  THR D 137  0                                        
SHEET    2   J 4 TYR D 188  GLU D 193  1  O  LEU D 191   N  GLY D 136           
SHEET    3   J 4 ILE D 111  LYS D 116 -1  N  MET D 114   O  TYR D 190           
SHEET    4   J 4 THR D 208  VAL D 211 -1  O  MET D 209   N  ILE D 115           
SHEET    1   K 3 TYR F  51  ILE F  55  0                                        
SHEET    2   K 3 VAL F   6  THR F  10  1  N  VAL F   8   O  LYS F  52           
SHEET    3   K 3 ILE F  85  ALA F  86  1  O  ILE F  85   N  THR F   9           
SHEET    1   L 2 MET F  18  MET F  19  0                                        
SHEET    2   L 2 TYR F  32  GLU F  33 -1  O  GLU F  33   N  MET F  18           
SHEET    1   M 2 ILE F 100  PHE F 102  0                                        
SHEET    2   M 2 ALA F 223  PRO F 225 -1  O  THR F 224   N  ASP F 101           
SHEET    1   N 2 MET F 107  LEU F 109  0                                        
SHEET    2   N 2 LYS F 218  TYR F 220 -1  O  LYS F 218   N  LEU F 109           
SHEET    1   O 4 ALA F 134  GLY F 136  0                                        
SHEET    2   O 4 TYR F 188  GLU F 193  1  O  LEU F 191   N  GLY F 136           
SHEET    3   O 4 ILE F 111  LYS F 116 -1  N  SER F 112   O  LEU F 192           
SHEET    4   O 4 THR F 208  VAL F 211 -1  O  MET F 209   N  ILE F 115           
SSBOND   1 CYS B  206    CYS B  261                          1555   1555  2.32  
SSBOND   2 CYS D  206    CYS D  261                          1555   1555  2.22  
SSBOND   3 CYS F  206    CYS F  261                          1555   1555  2.39  
LINK         OE2 GLU F  24                ZN    ZN D 262     1555   1555  2.21  
LINK         NE2 HIS D  46                ZN    ZN D   2     1555   1555  2.21  
LINK         OE1 GLU B  42                ZN    ZN B   1     1555   1555  2.22  
LINK         OE2 GLU D  30                ZN    ZN D 262     1555   1555  2.24  
LINK         NE2 HIS F  46                ZN    ZN F 262     1555   1555  2.25  
LINK         OE1 GLU D  42                ZN    ZN D   2     1555   1555  2.27  
LINK         NE2 HIS B  46                ZN    ZN B   1     1555   1555  2.28  
LINK         NE2 HIS B  23                ZN    ZN B   3     1555   1555  2.30  
LINK         NE2 HIS D  23                ZN    ZN D 262     1555   1555  2.39  
LINK         OE1 GLU F  42                ZN    ZN F 262     1555   1555  2.49  
LINK         OE1 GLU F  24                ZN    ZN D 262     1555   1555  2.49  
CISPEP   1 SER B   14    PRO B   15          0        -1.24                     
CISPEP   2 GLU B  166    PRO B  167          0        -2.57                     
CISPEP   3 LYS B  204    PRO B  205          0         7.30                     
CISPEP   4 SER D   14    PRO D   15          0        -4.81                     
CISPEP   5 GLU D  166    PRO D  167          0        -3.40                     
CISPEP   6 LYS D  204    PRO D  205          0         4.93                     
CISPEP   7 SER F   14    PRO F   15          0        -1.18                     
CISPEP   8 GLU F  166    PRO F  167          0        -3.58                     
CISPEP   9 LYS F  204    PRO F  205          0         8.65                     
SITE     1 AC1 13 TYR B  61  PRO B  89  LEU B  90  THR B  91                    
SITE     2 AC1 13 ARG B  96  GLY B 141  SER B 142  THR B 143                    
SITE     3 AC1 13 GLU B 193  TYR B 220  HOH B 263  HOH B 266                    
SITE     4 AC1 13 HOH B 298                                                     
SITE     1 AC2  3 GLU B  42  HIS B  46  GLU D 166                               
SITE     1 AC3  2 HIS B  23  ASP F  65                                          
SITE     1 AC4 12 TYR D  61  PRO D  89  LEU D  90  THR D  91                    
SITE     2 AC4 12 ARG D  96  GLY D 141  SER D 142  THR D 143                    
SITE     3 AC4 12 GLU D 193  HOH D 312  HOH D 315  HOH D 327                    
SITE     1 AC5  5 GLU B 166  GLU D  42  HIS D  46  LEU D 241                    
SITE     2 AC5  5 GLN D 244                                                     
SITE     1 AC6  5 LYS D  20  HIS D  23  GLU D  30  HIS F  23                    
SITE     2 AC6  5 GLU F  24                                                     
SITE     1 AC7 13 TYR F  61  PRO F  89  LEU F  90  THR F  91                    
SITE     2 AC7 13 ARG F  96  LEU F 138  GLY F 141  SER F 142                    
SITE     3 AC7 13 THR F 143  GLU F 193  HOH F 265  HOH F 278                    
SITE     4 AC7 13 HOH F 321                                                     
SITE     1 AC8  2 GLU F  42  HIS F  46                                          
CRYST1   47.239  114.223  163.764  90.00  90.00  90.00 P 2 21 21    12          
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      0.021169  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008755  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006106        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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