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Database: PDB
Entry: 5NG9
LinkDB: 5NG9
Original site: 5NG9 
HEADER    MEMBRANE PROTEIN                        17-MAR-17   5NG9              
TITLE     CRYSTAL STRUCTURE OF THE GLUA2 LIGAND-BINDING DOMAIN (S1S2J) IN       
TITLE    2 COMPLEX WITH AGONIST CIP-AS AT 1.15 A RESOLUTION.                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMATE RECEPTOR 2;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: GLUR-2,AMPA-SELECTIVE GLUTAMATE RECEPTOR 2,GLUR-B,GLUR-K2,  
COMPND   5 GLUTAMATE RECEPTOR IONOTROPIC,AMPA 2,GLUA2;                          
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: THE PROTEIN CRYSTALLIZED IS THE EXTRACELLULAR LIGAND- 
COMPND   8 BINDING DOMIAN OF GLUA2. TRANSMEMBRANE REGIONS WERE REPLACED WITH A  
COMPND   9 GLY-THR LINKER (118-119). SEQUENCE MATCHES DISCONTINUOUSLY WITH THE  
COMPND  10 REFERENCE DATABASE (413-527, 653-797). RESIDUES 1-2 ARE CLONING      
COMPND  11 REMNANTS.                                                            
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: GRIA2, GLUR2;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562, 469008;                                
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: ORIGAMI B (DE3);                          
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PET22B                                     
KEYWDS    IONOTROPIC GLUTAMATE RECEPTOR, AMPA RECEPTOR, LIGAND-BINDING DOMAIN,  
KEYWDS   2 GLUA2, GLUR2, AGONIST, MEMBRANE PROTEIN                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.LAULUMAA,K.A.FRYDENVANG,S.WINTHER,J.S.KASTRUP                       
REVDAT   2   27-SEP-17 5NG9    1       JRNL                                     
REVDAT   1   26-JUL-17 5NG9    0                                                
JRNL        AUTH   S.MLLERUD,A.PINTO,L.MARCONI,K.FRYDENVANG,T.S.THORSEN,        
JRNL        AUTH 2 S.LAULUMAA,R.VENSKUTONYTE,S.WINTHER,A.M.C.MORAL,L.TAMBORINI, 
JRNL        AUTH 3 P.CONTI,D.S.PICKERING,J.S.KASTRUP                            
JRNL        TITL   STRUCTURE AND AFFINITY OF TWO BICYCLIC GLUTAMATE ANALOGUES   
JRNL        TITL 2 AT AMPA AND KAINATE RECEPTORS.                               
JRNL        REF    ACS CHEM NEUROSCI             V.   8  2056 2017              
JRNL        REFN                   ESSN 1948-7193                               
JRNL        PMID   28691798                                                     
JRNL        DOI    10.1021/ACSCHEMNEURO.7B00201                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.15 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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.98                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.380                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 93190                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.110                           
REMARK   3   R VALUE            (WORKING SET) : 0.109                           
REMARK   3   FREE R VALUE                     : 0.133                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4676                            
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 38.0044 -  3.5724    0.98     3159   170  0.1429 0.1549        
REMARK   3     2  3.5724 -  2.8358    1.00     3079   152  0.1309 0.1488        
REMARK   3     3  2.8358 -  2.4774    1.00     3063   168  0.1270 0.1324        
REMARK   3     4  2.4774 -  2.2509    1.00     3036   135  0.1160 0.1455        
REMARK   3     5  2.2509 -  2.0896    1.00     3027   146  0.1043 0.1268        
REMARK   3     6  2.0896 -  1.9664    1.00     2999   172  0.1021 0.1200        
REMARK   3     7  1.9664 -  1.8679    1.00     3000   172  0.1003 0.1310        
REMARK   3     8  1.8679 -  1.7866    1.00     2972   158  0.0960 0.1165        
REMARK   3     9  1.7866 -  1.7178    1.00     3001   152  0.0942 0.1368        
REMARK   3    10  1.7178 -  1.6586    1.00     3005   149  0.0874 0.1220        
REMARK   3    11  1.6586 -  1.6067    1.00     2952   158  0.0830 0.1075        
REMARK   3    12  1.6067 -  1.5608    1.00     3003   160  0.0805 0.1055        
REMARK   3    13  1.5608 -  1.5197    1.00     2945   144  0.0824 0.1152        
REMARK   3    14  1.5197 -  1.4826    1.00     2987   156  0.0814 0.1261        
REMARK   3    15  1.4826 -  1.4489    1.00     2967   151  0.0842 0.1299        
REMARK   3    16  1.4489 -  1.4181    1.00     2986   142  0.0828 0.1224        
REMARK   3    17  1.4181 -  1.3897    1.00     2981   157  0.0847 0.1074        
REMARK   3    18  1.3897 -  1.3635    1.00     2966   137  0.0874 0.1115        
REMARK   3    19  1.3635 -  1.3391    1.00     2923   189  0.0879 0.1311        
REMARK   3    20  1.3391 -  1.3164    1.00     2960   174  0.0920 0.1274        
REMARK   3    21  1.3164 -  1.2952    1.00     2949   140  0.0906 0.1245        
REMARK   3    22  1.2952 -  1.2753    1.00     2970   179  0.0939 0.1274        
REMARK   3    23  1.2753 -  1.2565    1.00     2901   177  0.1001 0.1322        
REMARK   3    24  1.2565 -  1.2388    1.00     2952   174  0.1023 0.1350        
REMARK   3    25  1.2388 -  1.2221    1.00     2959   142  0.1061 0.1418        
REMARK   3    26  1.2221 -  1.2062    1.00     2911   167  0.1090 0.1374        
REMARK   3    27  1.2062 -  1.1911    0.96     2830   149  0.1086 0.1445        
REMARK   3    28  1.1911 -  1.1768    0.94     2822   138  0.1102 0.1331        
REMARK   3    29  1.1768 -  1.1631    0.92     2712   138  0.1319 0.1585        
REMARK   3    30  1.1631 -  1.1500    0.85     2497   130  0.1475 0.1598        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.060            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 9.370            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 8.08                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.18                          
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      :  0.009           2354                                  
REMARK   3   ANGLE     :  1.177           3211                                  
REMARK   3   CHIRALITY :  0.089            351                                  
REMARK   3   PLANARITY :  0.008            407                                  
REMARK   3   DIHEDRAL  : 13.328            940                                  
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 5NG9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-MAR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200004067.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-APR-15                          
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          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.20                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 93257                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.960                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.22900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.22900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1M5B                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15.2% PEG4000, 0.1 M LITHIUM SULFATE,    
REMARK 280  0.1 M PHOSPHATE-CITRATE BUFFER, 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       31.10900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.07000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.10900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.07000            
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: 4540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 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      124.43600            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      176.28000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
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 A 593  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 734  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 827  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   264                                                      
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   OA2  FLC A   302     O    HOH A   401              1.97            
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 830        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH A 831        DISTANCE =  5.85 ANGSTROMS                       
REMARK 525    HOH A 832        DISTANCE =  6.23 ANGSTROMS                       
REMARK 525    HOH A 833        DISTANCE =  6.30 ANGSTROMS                       
REMARK 525    HOH A 834        DISTANCE =  6.40 ANGSTROMS                       
REMARK 525    HOH A 835        DISTANCE =  6.68 ANGSTROMS                       
REMARK 525    HOH A 836        DISTANCE =  6.75 ANGSTROMS                       
REMARK 525    HOH A 837        DISTANCE =  6.79 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 303  LI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  97   O                                                      
REMARK 620 2 GLU A  97   OE2 112.1                                              
REMARK 620 3 ILE A 100   O   101.3 117.4                                        
REMARK 620 4 HOH A 459   O   110.4 108.7 106.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LI A 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8VN A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8WQ 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 GOL A 309                 
DBREF  5NG9 A    3   117  UNP    P19491   GRIA2_RAT      413    527             
DBREF  5NG9 A  120   264  UNP    P19491   GRIA2_RAT      653    797             
SEQADV 5NG9 GLY A    1  UNP  P19491              CLONING ARTIFACT               
SEQADV 5NG9 ALA A    2  UNP  P19491              CLONING ARTIFACT               
SEQADV 5NG9 GLY A  118  UNP  P19491              LINKER                         
SEQADV 5NG9 THR A  119  UNP  P19491              LINKER                         
SEQRES   1 A  264  GLY ALA ASN LYS THR VAL VAL VAL THR THR ILE LEU GLU          
SEQRES   2 A  264  SER PRO TYR VAL MET MET LYS LYS ASN HIS GLU MET LEU          
SEQRES   3 A  264  GLU GLY ASN GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU          
SEQRES   4 A  264  ALA ALA GLU ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS          
SEQRES   5 A  264  LEU THR ILE VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP          
SEQRES   6 A  264  ALA ASP THR LYS ILE TRP ASN GLY MET VAL GLY GLU LEU          
SEQRES   7 A  264  VAL TYR GLY LYS ALA ASP ILE ALA ILE ALA PRO LEU THR          
SEQRES   8 A  264  ILE THR LEU VAL ARG GLU GLU VAL ILE ASP PHE SER LYS          
SEQRES   9 A  264  PRO PHE MET SER LEU GLY ILE SER ILE MET ILE LYS LYS          
SEQRES  10 A  264  GLY THR PRO ILE GLU SER ALA GLU ASP LEU SER LYS GLN          
SEQRES  11 A  264  THR GLU ILE ALA TYR GLY THR LEU ASP SER GLY SER THR          
SEQRES  12 A  264  LYS GLU PHE PHE ARG ARG SER LYS ILE ALA VAL PHE ASP          
SEQRES  13 A  264  LYS MET TRP THR TYR MET ARG SER ALA GLU PRO SER VAL          
SEQRES  14 A  264  PHE VAL ARG THR THR ALA GLU GLY VAL ALA ARG VAL ARG          
SEQRES  15 A  264  LYS SER LYS GLY LYS TYR ALA TYR LEU LEU GLU SER THR          
SEQRES  16 A  264  MET ASN GLU TYR ILE GLU GLN ARG LYS PRO CYS ASP THR          
SEQRES  17 A  264  MET LYS VAL GLY GLY ASN LEU ASP SER LYS GLY TYR GLY          
SEQRES  18 A  264  ILE ALA THR PRO LYS GLY SER SER LEU GLY ASN ALA VAL          
SEQRES  19 A  264  ASN LEU ALA VAL LEU LYS LEU ASN GLU GLN GLY LEU LEU          
SEQRES  20 A  264  ASP LYS LEU LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU          
SEQRES  21 A  264  CYS GLY SER GLY                                              
HET    FLC  A 301      13                                                       
HET    FLC  A 302      13                                                       
HET     LI  A 303       1                                                       
HET    8VN  A 304      14                                                       
HET    8WQ  A 305      14                                                       
HET    SO4  A 306       5                                                       
HET    SO4  A 307       5                                                       
HET    SO4  A 308       5                                                       
HET    GOL  A 309       6                                                       
HETNAM     FLC CITRATE ANION                                                    
HETNAM      LI LITHIUM ION                                                      
HETNAM     8VN (3~{A}~{S},4~{S},6~{A}~{R})-4,5,6,6~{A}-TETRAHYDRO-              
HETNAM   2 8VN  3~{A}~{H}-PYRROLO[3,4-D][1,2]OXAZOLE-3,4-DICARBOXYLIC           
HETNAM   3 8VN  ACID                                                            
HETNAM     8WQ (2~{S},3~{R},4~{R})-3-(CARBOXYCARBONYL)-4-OXIDANYL-              
HETNAM   2 8WQ  PYRROLIDINE-2-CARBOXYLIC ACID                                   
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  FLC    2(C6 H5 O7 3-)                                               
FORMUL   4   LI    LI 1+                                                        
FORMUL   5  8VN    C7 H8 N2 O5                                                  
FORMUL   6  8WQ    C7 H9 N O6                                                   
FORMUL   7  SO4    3(O4 S 2-)                                                   
FORMUL  10  GOL    C3 H8 O3                                                     
FORMUL  11  HOH   *437(H2 O)                                                    
HELIX    1 AA1 ASN A   22  LEU A   26  5                                   5    
HELIX    2 AA2 GLU A   27  GLU A   30  5                                   4    
HELIX    3 AA3 GLY A   34  GLY A   48  1                                  15    
HELIX    4 AA4 ASN A   72  TYR A   80  1                                   9    
HELIX    5 AA5 THR A   93  GLU A   98  1                                   6    
HELIX    6 AA6 SER A  123  LYS A  129  1                                   7    
HELIX    7 AA7 GLY A  141  SER A  150  1                                  10    
HELIX    8 AA8 ILE A  152  ALA A  165  1                                  14    
HELIX    9 AA9 THR A  173  SER A  184  1                                  12    
HELIX   10 AB1 SER A  194  GLN A  202  1                                   9    
HELIX   11 AB2 LEU A  230  GLN A  244  1                                  15    
HELIX   12 AB3 GLY A  245  TYR A  256  1                                  12    
SHEET    1 AA1 3 TYR A  51  ILE A  55  0                                        
SHEET    2 AA1 3 VAL A   6  THR A  10  1  N  VAL A   8   O  LYS A  52           
SHEET    3 AA1 3 ILE A  85  ALA A  86  1  O  ILE A  85   N  THR A   9           
SHEET    1 AA2 2 MET A  18  MET A  19  0                                        
SHEET    2 AA2 2 TYR A  32  GLU A  33 -1  O  GLU A  33   N  MET A  18           
SHEET    1 AA3 2 ILE A 100  PHE A 102  0                                        
SHEET    2 AA3 2 ALA A 223  PRO A 225 -1  O  THR A 224   N  ASP A 101           
SHEET    1 AA4 2 MET A 107  LEU A 109  0                                        
SHEET    2 AA4 2 LYS A 218  TYR A 220 -1  O  LYS A 218   N  LEU A 109           
SHEET    1 AA5 4 ALA A 134  THR A 137  0                                        
SHEET    2 AA5 4 TYR A 188  GLU A 193  1  O  LEU A 191   N  GLY A 136           
SHEET    3 AA5 4 ILE A 111  LYS A 116 -1  N  MET A 114   O  TYR A 190           
SHEET    4 AA5 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         O   GLU A  97                LI    LI A 303     1555   1555  1.93  
LINK         OE2 GLU A  97                LI    LI A 303     1555   1555  1.90  
LINK         O   ILE A 100                LI    LI A 303     1555   1555  1.90  
LINK        LI    LI A 303                 O   HOH A 459     1555   1555  1.92  
CISPEP   1 SER A   14    PRO A   15          0        -1.71                     
CISPEP   2 GLU A  166    PRO A  167          0        -5.28                     
CISPEP   3 LYS A  204    PRO A  205          0         6.08                     
SITE     1 AC1  7 MET A  19  HIS A  23  ARG A  31  FLC A 302                    
SITE     2 AC1  7 HOH A 436  HOH A 601  HOH A 659                               
SITE     1 AC2  5 ARG A  31  FLC A 301  HOH A 401  HOH A 411                    
SITE     2 AC2  5 HOH A 482                                                     
SITE     1 AC3  4 GLU A  97  ILE A 100  ASP A 101  HOH A 459                    
SITE     1 AC4 16 TYR A  61  PRO A  89  THR A  91  ARG A  96                    
SITE     2 AC4 16 LEU A 138  GLY A 141  SER A 142  THR A 143                    
SITE     3 AC4 16 GLU A 193  MET A 196  8WQ A 305  HOH A 414                    
SITE     4 AC4 16 HOH A 462  HOH A 579  HOH A 597  HOH A 609                    
SITE     1 AC5 14 TYR A  61  PRO A  89  THR A  91  ARG A  96                    
SITE     2 AC5 14 LEU A 138  GLY A 141  SER A 142  THR A 143                    
SITE     3 AC5 14 GLU A 193  8VN A 304  HOH A 462  HOH A 579                    
SITE     4 AC5 14 HOH A 597  HOH A 609                                          
SITE     1 AC6  5 LYS A  82  LYS A 116  HOH A 403  HOH A 610                    
SITE     2 AC6  5 HOH A 635                                                     
SITE     1 AC7  3 ARG A  64  LYS A  69  HOH A 580                               
SITE     1 AC8  4 ARG A 148  ARG A 149  HOH A 453  HOH A 720                    
SITE     1 AC9  8 LYS A  60  SER A 140  HOH A 406  HOH A 444                    
SITE     2 AC9  8 HOH A 455  HOH A 477  HOH A 614  HOH A 650                    
CRYST1   62.218   88.140   47.958  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      0.016073  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011346  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020852        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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