GenomeNet

Database: PDB
Entry: 2XXH
LinkDB: 2XXH
Original site: 2XXH 
HEADER    TRANSPORT PROTEIN                       10-NOV-10   2XXH              
TITLE     CRYSTAL STRUCTURE OF 1-(4-(2-OXO-2-(1-PYRROLIDINYL)ETHYL)PHENYL)-3-   
TITLE    2 (TRIFLUOROMETHYL)-4,5,6,7-TETRAHYDRO-1H-INDAZOLE IN COMPLEX WITH     
TITLE    3 THE LIGAND BINDING DOMAIN OF THE RAT GLUA2 RECEPTOR AND GLUTAMATE    
TITLE    4 AT 1.5A RESOLUTION.                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMATE RECEPTOR 2;                                      
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: LIGAND BINDING DOMAIN, RESIDUES 413-527,653-796;           
COMPND   5 SYNONYM: GLUR-2, AMPA-SELECTIVE GLUTAMATE RECEPTOR 2, GLUR-B,        
COMPND   6  GLUR-K2, GLUTAMATE RECEPTOR IONOTROPIC\,AMPA 2, GLUA2;              
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 OTHER_DETAILS: GLUA2FLOPS1-GLYTHR-S2                                 
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    TRANSPORT PROTEIN, AMPA RECEPTOR LIGAND-BINDING CORE, ION CHANNEL     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.E.WARD,M.HARRIES,L.ALDEGHERI,N.E.AUSTIN,S.BALLANTINE,E.BALLINI,     
AUTHOR   2 D.M.BRADLEY,B.D.BAX,B.P.CLARKE,A.J.HARRIS,S.A.HARRISON,              
AUTHOR   3 R.A.MELARANGE,C.MOOKHERJEE,J.MOSLEY,G.DALNEGRO,B.OLIOSI,K.J.SMITH,   
AUTHOR   4 K.M.THEWLIS,P.M.WOOLLARD,S.P.YUSAF                                   
REVDAT   2   28-SEP-11 2XXH    1       JRNL   REMARK VERSN                      
REVDAT   1   06-APR-11 2XXH    0                                                
JRNL        AUTH   S.E.WARD,M.HARRIES,L.ALDEGHERI,N.E.AUSTIN,S.BALLANTINE,      
JRNL        AUTH 2 E.BALLINI,D.M.BRADLEY,B.D.BAX,B.P.CLARKE,A.J.HARRIS,         
JRNL        AUTH 3 S.A.HARRISON,R.A.MELARANGE,C.MOOKHERJEE,J.MOSLEY,            
JRNL        AUTH 4 G.DAL NEGRO,B.OLIOSI,K.J.SMITH,K.M.THEWLIS,P.M.WOOLLARD,     
JRNL        AUTH 5 S.P.YUSAF                                                    
JRNL        TITL   INTEGRATION OF LEAD OPTIMIZATION WITH CRYSTALLOGRAPHY FOR A  
JRNL        TITL 2 MEMBRANE-BOUND ION CHANNEL TARGET: DISCOVERY OF A NEW CLASS  
JRNL        TITL 3 OF AMPA RECEPTOR POSITIVE ALLOSTERIC MODULATORS.             
JRNL        REF    J.MED.CHEM.                   V.  54    78 2011              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   21128618                                                     
JRNL        DOI    10.1021/JM100679E                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.50                          
REMARK   3   NUMBER OF REFLECTIONS             : 127261                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.19487                         
REMARK   3   R VALUE            (WORKING SET) : 0.19367                         
REMARK   3   FREE R VALUE                     : 0.21757                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 6704                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.500                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.539                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 9198                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.10                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.254                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 431                          
REMARK   3   BIN FREE R VALUE                    : 0.294                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6142                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 121                                     
REMARK   3   SOLVENT ATOMS            : 521                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.02                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.093                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.27                                                 
REMARK   3    B22 (A**2) : 0.23                                                 
REMARK   3    B33 (A**2) : -0.50                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.079         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.078         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.049         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.308         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6391 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8641 ; 1.344 ; 2.005       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   810 ; 5.501 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   243 ;31.730 ;24.403       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1168 ;12.397 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    29 ;16.529 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   946 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4708 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3964 ; 1.114 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6368 ; 2.173 ; 5.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2427 ; 3.253 ; 6.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2273 ; 4.998 ; 8.000       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 2XXH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-NOV-10.                  
REMARK 100 THE PDBE ID CODE IS EBI-46146.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.93928                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 134500                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.50                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.8                               
REMARK 200  DATA REDUNDANCY                : 2.8                                
REMARK 200  R MERGE                    (I) : 0.07                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.40                              
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     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.5                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.39                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.60                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       57.18700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       81.79150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       57.18700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       81.79150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: 2770 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -125.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      114.37400            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      163.58300            
REMARK 350   BIOMT3   2  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: 2210 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 775 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ASN 775 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, ASN 775 TO SER                        
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 465     GLY B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     SER B   263                                                      
REMARK 465     GLY C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     ASN C     3                                                      
REMARK 465     SER C   263                                                      
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 A   4    CG   CD   CE   NZ                                   
REMARK 470     LYS A  21    CG   CD   CE   NZ                                   
REMARK 470     GLU A  24    CG   CD   OE1  OE2                                  
REMARK 470     ASP A  67    CG   OD1  OD2                                       
REMARK 470     GLU A 122    CG   CD   OE1  OE2                                  
REMARK 470     THR A 131    OG1  CG2                                            
REMARK 470     ILE A 152    CD1                                                 
REMARK 470     ARG A 172    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 249    CG   CD   CE   NZ                                   
REMARK 470     LYS A 258    CG   CD   CE   NZ                                   
REMARK 470     GLY A 262    CA   C    O                                         
REMARK 470     ASN B   3    CG   OD1  ND2                                       
REMARK 470     LYS B   4    CG   CD   CE   NZ                                   
REMARK 470     GLU B  27    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 183    CG   CD   CE   NZ                                   
REMARK 470     GLY B 262    CA   C    O                                         
REMARK 470     LYS C   4    CG   CD   CE   NZ                                   
REMARK 470     GLU C  27    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 122    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 172    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 258    CB   CG   CD   CE   NZ                              
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 C   198     O    HOH C  2115              2.16            
REMARK 500  ZN     ZN C  1302     O    HOH C  2151              1.08            
REMARK 500   O    HOH A  2029     O    HOH A  2046              2.06            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NE2  HIS A    23     O    HOH C  2151     4557     2.14            
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    LYS A 218     -163.78   -163.58                                   
REMARK 500    ASN C  22       32.12    -97.62                                   
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 B1303  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  46   NE2                                                    
REMARK 620 2 GLU B 166   OE1 122.7                                              
REMARK 620 3 SO4 B1302   O1  109.7 112.2                                        
REMARK 620 4 GLU A  42   OE1  92.8 100.9 117.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C1303  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C  42   OE1                                                    
REMARK 620 2 HIS C  46   NE2  96.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1304  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  23   NE2                                                    
REMARK 620 2 GLU B  30   OE2 116.4                                              
REMARK 620 3 HIS C  23   NE2 110.7 113.4                                        
REMARK 620 4 HOH B2194   O   100.1 111.6 102.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1305  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  42   OE1                                                    
REMARK 620 2 HIS B  46   NE2  97.7                                              
REMARK 620 3 HOH B2195   O   111.0 112.9                                        
REMARK 620 4 GLU A 166   OE2 107.6 111.6 114.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C1302  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  23   NE2                                                    
REMARK 620 2 HOH C2150   O   106.5                                              
REMARK 620 3 ASP C  65   OD2 103.6 112.7                                        
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 GLU A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1NG A 310                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLU B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1NG B 310                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B1303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B1304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B1305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLU C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN C1302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN C1303                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1M5C   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (                  
REMARK 900  S1S2J) INCOMPLEX WITH BR-HIBO AT 1.65 A RESOLUTION                  
REMARK 900 RELATED ID: 1P1O   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE GLUR2 LIGAND-BINDING CORE (                
REMARK 900  S1S2J)MUTANT L650T IN COMPLEX WITH QUISQUALATE                      
REMARK 900 RELATED ID: 1MQH   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (                
REMARK 900  S1S2J)IN COMPLEX WITH BROMO-WILLARDIINE AT 1.8                      
REMARK 900  ANGSTROMSRESOLUTION                                                 
REMARK 900 RELATED ID: 1LB8   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE NON-DESENSITIZING GLUR2                    
REMARK 900  LIGANDBINDING CORE MUTANT (S1S2J-L483Y) IN COMPLEX WITH             
REMARK 900   AMPA AT2.3 RESOLUTION                                              
REMARK 900 RELATED ID: 1P1U   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE GLUR2 LIGAND-BINDING CORE (                
REMARK 900  S1S2J)L650T MUTANT IN COMPLEX WITH AMPA (AMMONIUM                   
REMARK 900  SULFATECRYSTAL FORM)                                                
REMARK 900 RELATED ID: 1MM7   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (                
REMARK 900  S1S2J)IN COMPLEX WITH QUISQUALATE IN A ZINC CRYSTAL                 
REMARK 900  FORM AT 1.65ANGSTROMS RESOLUTION                                    
REMARK 900 RELATED ID: 1NNP   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF THE GLUR2 LIGAND-BINDING CORE (                  
REMARK 900  S1S2J) INCOMPLEX WITH (S)-ATPA AT 1.9 A RESOLUTION                  
REMARK 900  . CRYSTALLIZATIONWITHOUT ZINC IONS.                                 
REMARK 900 RELATED ID: 1M5D   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (                  
REMARK 900  S1S2J-Y702F) IN COMPLEX WITH BR-HIBO AT 1.73 A                      
REMARK 900  RESOLUTION                                                          
REMARK 900 RELATED ID: 1SYI   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF THE Y702F MUTANT OF THE GLUR2                    
REMARK 900  LIGAND-BINDING CORE (S1S2J) IN COMPLEX WITH (S)-CPW399              
REMARK 900   AT 2.1 ARESOLUTION.                                                
REMARK 900 RELATED ID: 1P1Q   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (                
REMARK 900  S1S2J)L650T MUTANT IN COMPLEX WITH AMPA                             
REMARK 900 RELATED ID: 1MQD   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF THE GLUR2 LIGAND-BINDING CORE (                  
REMARK 900  S1S2J) INCOMPLEX WITH (S)-DES-ME-AMPA AT 1.46 A                     
REMARK 900  RESOLUTION.CRYSTALLIZATION IN THE PRESENCE OF LITHIUM               
REMARK 900  SULFATE.                                                            
REMARK 900 RELATED ID: 1P1W   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE GLUR2 LIGAND-BINDING CORE (                
REMARK 900  S1S2J)WITH THE L483Y AND L650T MUTATIONS AND IN                     
REMARK 900  COMPLEX WITH AMPA                                                   
REMARK 900 RELATED ID: 1MXU   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (                
REMARK 900  S1S2J)IN COMPLEX WITH BROMO-WILLARDIINE (CONTROL FOR                
REMARK 900  THE CRYSTALTITRATION EXPERIMENTS)                                   
REMARK 900 RELATED ID: 1MY4   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF GLUTAMATE RECEPTOR LIGAND-BINDING              
REMARK 900  COREIN COMPLEX WITH IODO-WILLARDIINE IN THE ZN CRYSTAL              
REMARK 900   FORM                                                               
REMARK 900 RELATED ID: 2I3V   RELATED DB: PDB                                   
REMARK 900  MEASUREMENT OF CONFORMATIONAL CHANGES                               
REMARK 900  ACCOMPANYINGDESENSITIZATION IN AN IONOTROPIC GLUTAMATE              
REMARK 900  RECEPTOR:STRUCTURE OF G725C MUTANT                                  
REMARK 900 RELATED ID: 2I3W   RELATED DB: PDB                                   
REMARK 900  MEASUREMENT OF CONFORMATIONAL CHANGES                               
REMARK 900  ACCOMPANYINGDESENSITIZATION IN AN IONOTROPIC GLUTAMATE              
REMARK 900  RECEPTOR:STRUCTURE OF S729C MUTANT                                  
REMARK 900 RELATED ID: 1N0T   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF THE GLUR2 LIGAND-BINDING CORE (                  
REMARK 900  S1S2J) INCOMPLEX WITH THE ANTAGONIST (S)-ATPO AT 2.1                
REMARK 900   A RESOLUTION.                                                      
REMARK 900 RELATED ID: 2XXI   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF 1-((4-(3-(TRIFLUOROMETHYL)-6,7-                
REMARK 900  DIHYDROPYRANO(4,3-C(PYRAZOL-1(4H)-YL)PHENYL)METHYL                  
REMARK 900  )-2-PYRROLIDINONE IN COMPLEX WITH THE LIGAND BINDING                
REMARK 900  DOMAIN OF THE RAT GLUA2 RECEPTOR AND GLUTAMATE AT 1                 
REMARK 900  .6A RESOLUTION.                                                     
REMARK 900 RELATED ID: 1MQI   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (                
REMARK 900  S1S2J)IN COMPLEX WITH FLUORO-WILLARDIINE AT 1.35                    
REMARK 900  ANGSTROMSRESOLUTION                                                 
REMARK 900 RELATED ID: 1FTK   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (                
REMARK 900  S1S2I)IN COMPLEX WITH KAINATE AT 1.6 A RESOLUTION                   
REMARK 900 RELATED ID: 1MY3   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF GLUTAMATE RECEPTOR LIGAND-BINDING              
REMARK 900  COREIN COMPLEX WITH BROMO-WILLARDIINE IN THE ZN                     
REMARK 900  CRYSTAL FORM                                                        
REMARK 900 RELATED ID: 2ANJ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (                
REMARK 900  S1S2J-Y450W) MUTANT IN COMPLEX WITH THE PARTIAL                     
REMARK 900  AGONIST KAINICACID AT 2.1 A RESOLUTION                              
REMARK 900 RELATED ID: 1FTO   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (                
REMARK 900  S1S2J)IN THE APO STATE AT 2.0 A RESOLUTION                          
REMARK 900 RELATED ID: 1MXV   RELATED DB: PDB                                   
REMARK 900  CRYSTAL TITRATION EXPERIMENTS (AMPA CO-CRYSTALS SOAKED              
REMARK 900  IN10 MM BRW)                                                        
REMARK 900 RELATED ID: 1P1N   RELATED DB: PDB                                   
REMARK 900  GLUR2 LIGAND BINDING CORE (S1S2J) MUTANT L650T IN                   
REMARK 900  COMPLEXWITH KAINATE                                                 
REMARK 900 RELATED ID: 2XX9   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF 1-((2-FLUORO-4-(3-(                            
REMARK 900  TRIFLUOROMETHYL)-4,5,6,7-TETRAHYDRO-1H-INDAZOL-1-YL                 
REMARK 900  )PHENYL)METHYL)-2-PYRROLIDINONE IN COMPLEX WITH THE                 
REMARK 900  LIGAND BINDING DOMAIN OF THE RAT GLUA2 RECEPTOR AND                 
REMARK 900  GLUTAMATE AT 2.2A RESOLUTION.                                       
REMARK 900 RELATED ID: 1FTJ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (                
REMARK 900  S1S2J)IN COMPLEX WITH GLUTAMATE AT 1.9 RESOLUTION                   
REMARK 900 RELATED ID: 1SYH   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF THE GLUR2 LIGAND-BINDING CORE (                  
REMARK 900  S1S2J) INCOMPLEX WITH (S)-CPW399 AT 1.85 A                          
REMARK 900  RESOLUTION.                                                         
REMARK 900 RELATED ID: 1M5E   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (                  
REMARK 900  S1S2J) INCOMPLEX WITH ACPA AT 1.46 A RESOLUTION                     
REMARK 900 RELATED ID: 1LBB   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING DOMAIN                
REMARK 900  MUTANT(S1S2J-N754D) IN COMPLEX WITH KAINATE AT 2.1                  
REMARK 900  A RESOLUTION                                                        
REMARK 900 RELATED ID: 1FW0   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (                
REMARK 900  S1S2J)IN COMPLEX WITH KAINATE AT 2.0 A RESOLUTION                   
REMARK 900 RELATED ID: 1MXZ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL TITRATION EXPERIMENTS (AMPA CO-CRYSTALS SOAKED              
REMARK 900  IN 1UM BRW)                                                         
REMARK 900 RELATED ID: 1MXY   RELATED DB: PDB                                   
REMARK 900  CRYSTAL TITRATION EXPERIMENTS (AMPA CO-CRYSTALS SOAKED              
REMARK 900  IN10 UM BRW)                                                        
REMARK 900 RELATED ID: 1MQG   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (                
REMARK 900  S1S2J)IN COMPLEX WITH IODO-WILLARDIINE AT 2.15                      
REMARK 900  ANGSTROMSRESOLUTION                                                 
REMARK 900 RELATED ID: 2XX8   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF N,N-DIMETHYL-4-(3-(                            
REMARK 900  TRIFLUOROMETHYL)-4,5,6,7-TETRAHYDRO-1H-INDAZOL-1-YL                 
REMARK 900  )BENZAMIDE IN COMPLEX WITH THE LIGAND BINDING DOMAIN                
REMARK 900  OF THE RAT GLUA2 RECEPTOR AND GLUTAMATE AT 2.2A                     
REMARK 900  RESOLUTION.                                                         
REMARK 900 RELATED ID: 2AIX   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF THE GLUR2 LIGAND-BINDING CORE (                  
REMARK 900  S1S2J) INCOMPLEX WITH (S)-THIO-ATPA AT 2.2 A                        
REMARK 900  RESOLUTION.                                                         
REMARK 900 RELATED ID: 1M5B   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (                  
REMARK 900  S1S2J) INCOMPLEX WITH 2-ME-TET-AMPA AT 1.85 A                       
REMARK 900  RESOLUTION.                                                         
REMARK 900 RELATED ID: 1MXW   RELATED DB: PDB                                   
REMARK 900  CRYSTAL TITRATION EXPERIMENTS (AMPA CO-CRYSTALS SOAKED              
REMARK 900  IN 1MM BRW)                                                         
REMARK 900 RELATED ID: 1MS7   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF THE GLUR2 LIGAND-BINDING CORE (                  
REMARK 900  S1S2J) INCOMPLEX WITH (S)-DES-ME-AMPA AT 1.97 A                     
REMARK 900  RESOLUTION,CRYSTALLIZATION IN THE PRESENCE OF ZINC                  
REMARK 900  ACETATE                                                             
REMARK 900 RELATED ID: 2XX7   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF 1-(4-(1-PYRROLIDINYLCARBONYL)PHENYL            
REMARK 900  )-3-(TRIFLUOROMETHYL)-4,5,6,7-TETRAHYDRO-1H-INDAZOLE                
REMARK 900   IN COMPLEX WITH THE LIGAND BINDING DOMAIN OF THE                   
REMARK 900  RAT GLUA2 RECEPTOR AND GLUTAMATE AT 2.2A RESOLUTION.                
REMARK 900 RELATED ID: 1MY0   RELATED DB: PDB                                   
REMARK 900  CRYSTAL TITRATION EXPERIMENTS (AMPA CO-CRYSTALS SOAKED              
REMARK 900  IN100 NM BRW)                                                       
REMARK 900 RELATED ID: 1M5F   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (                  
REMARK 900  S1S2J-Y702F) IN COMPLEX WITH ACPA AT 1.95 A                         
REMARK 900  RESOLUTION                                                          
REMARK 900 RELATED ID: 1XHY   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF THE Y702F MUTANT OF THE GLUR2                    
REMARK 900  LIGAND-BINDING CORE (S1S2J) IN COMPLEX WITH KAINATE AT              
REMARK 900   1.85 ARESOLUTION                                                   
REMARK 900 RELATED ID: 1MY1   RELATED DB: PDB                                   
REMARK 900  CRYSTAL TITRATION EXPERIMENTS (AMPA CO-CRYSTALS SOAKED              
REMARK 900  IN10 NM BRW)                                                        
REMARK 900 RELATED ID: 1MM6   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (                
REMARK 900  S1S2J)IN COMPLEX WITH QUISQUALATE IN A NON ZINC                     
REMARK 900  CRYSTAL FORM AT2.15 ANGSTROMS RESOLUTION                            
REMARK 900 RELATED ID: 2CMO   RELATED DB: PDB                                   
REMARK 900   THE STRUCTURE OF A MIXED GLUR2 LIGAND-BINDING CORE                 
REMARK 900  DIMER IN COMPLEX WITH (S)-GLUTAMATE AND THE ANTAGONIST              
REMARK 900   (S)-NS1209                                                         
REMARK 900 RELATED ID: 2AL4   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (                
REMARK 900  S1S2J)IN COMPLEX WITH QUISQUALATE AND CX614.                        
REMARK 900 RELATED ID: 1WVJ   RELATED DB: PDB                                   
REMARK 900  EXPLORING THE GLUR2 LIGAND-BINDING CORE IN COMPLEX                  
REMARK 900  WITH THEBICYCLIC AMPA ANALOGUE (S)-4-AHCP                           
REMARK 900 RELATED ID: 2UXA   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE GLUR2-FLIP LIGAND BINDING                  
REMARK 900  DOMAIN                                                              
REMARK 900 RELATED ID: 1FTL   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (                
REMARK 900  S1S2J)IN COMPLEX WITH THE ANTAGONIST DNQX AT 1.8 A                  
REMARK 900   RESOLUTION                                                         
REMARK 900 RELATED ID: 1MXX   RELATED DB: PDB                                   
REMARK 900  CRYSTAL TITRATION EXPERIMENTS (AMPA CO-CRYSTALS SOAKED              
REMARK 900  IN100 UM BRW)                                                       
REMARK 900 RELATED ID: 1FTM   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (                
REMARK 900  S1S2J)IN COMPLEX WITH AMPA AT 1.7 RESOLUTION                        
REMARK 900 RELATED ID: 1LB9   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE NON-DESENSITIZING GLUR2                    
REMARK 900  LIGANDBINDING CORE MUTANT (S1S2J-L483Y) IN COMPLEX                  
REMARK 900  WITHANTAGONIST DNQX AT 2.3 A RESOLUTION                             
REMARK 900 RELATED ID: 1LBC   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF GLUR2 LIGAND BINDING CORE (S1S2J-              
REMARK 900  N775S)IN COMPLEX WITH CYCLOTHIAZIDE (CTZ) AS WELL AS                
REMARK 900  GLUTAMATEAT 1.8 A RESOLUTION                                        
REMARK 900 RELATED ID: 1NNK   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF THE GLUR2 LIGAND-BINDING CORE (                  
REMARK 900  S1S2J) INCOMPLEX WITH (S)-ATPA AT 1.85 A RESOLUTION                 
REMARK 900  .CRYSTALLIZATION WITH ZINC IONS.                                    
REMARK 900 RELATED ID: 1MY2   RELATED DB: PDB                                   
REMARK 900  CRYSTAL TITRATION EXPERIMENT (AMPA COMPLEX CONTROL)                 
REMARK 900 RELATED ID: 1MQJ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (                
REMARK 900  S1S2J)IN COMPLEX WITH WILLARDIINE AT 1.65 ANGSTROMS                 
REMARK 900  RESOLUTION                                                          
REMARK 900 RELATED ID: 2AL5   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (                
REMARK 900  S1S2J)IN COMPLEX WITH FLUORO-WILLARDIINE AND ANIRACETAM             
REMARK 900 RELATED ID: 1GR2   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF A GLUTAMATE RECEPTOR LIGAND BINDING CORE (             
REMARK 900  GLUR2) COMPLEXED WITH KAINATE                                       
DBREF  2XXH A    3   117  UNP    P19491   GRIA2_RAT      413    527             
DBREF  2XXH A  120   263  UNP    P19491   GRIA2_RAT      653    796             
DBREF  2XXH B    3   117  UNP    P19491   GRIA2_RAT      413    527             
DBREF  2XXH B  120   263  UNP    P19491   GRIA2_RAT      653    796             
DBREF  2XXH C    3   117  UNP    P19491   GRIA2_RAT      413    527             
DBREF  2XXH C  120   263  UNP    P19491   GRIA2_RAT      653    796             
SEQADV 2XXH GLY A    1  UNP  P19491              EXPRESSION TAG                 
SEQADV 2XXH ALA A    2  UNP  P19491              EXPRESSION TAG                 
SEQADV 2XXH GLY A  118  UNP  P19491    PRO   528 LINKER                         
SEQADV 2XXH THR A  119  UNP  P19491    SER   652 LINKER                         
SEQADV 2XXH SER A  242  UNP  P19491    ASN   775 ENGINEERED MUTATION            
SEQADV 2XXH GLY B    1  UNP  P19491              EXPRESSION TAG                 
SEQADV 2XXH ALA B    2  UNP  P19491              EXPRESSION TAG                 
SEQADV 2XXH GLY B  118  UNP  P19491    PRO   528 LINKER                         
SEQADV 2XXH THR B  119  UNP  P19491    SER   652 LINKER                         
SEQADV 2XXH SER B  242  UNP  P19491    ASN   775 ENGINEERED MUTATION            
SEQADV 2XXH GLY C    1  UNP  P19491              EXPRESSION TAG                 
SEQADV 2XXH ALA C    2  UNP  P19491              EXPRESSION TAG                 
SEQADV 2XXH GLY C  118  UNP  P19491    PRO   528 LINKER                         
SEQADV 2XXH THR C  119  UNP  P19491    SER   652 LINKER                         
SEQADV 2XXH SER C  242  UNP  P19491    ASN   775 ENGINEERED MUTATION            
SEQRES   1 A  263  GLY ALA ASN LYS THR VAL VAL VAL THR THR ILE LEU GLU          
SEQRES   2 A  263  SER PRO TYR VAL MET MET LYS LYS ASN HIS GLU MET LEU          
SEQRES   3 A  263  GLU GLY ASN GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU          
SEQRES   4 A  263  ALA ALA GLU ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS          
SEQRES   5 A  263  LEU THR ILE VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP          
SEQRES   6 A  263  ALA ASP THR LYS ILE TRP ASN GLY MET VAL GLY GLU LEU          
SEQRES   7 A  263  VAL TYR GLY LYS ALA ASP ILE ALA ILE ALA PRO LEU THR          
SEQRES   8 A  263  ILE THR LEU VAL ARG GLU GLU VAL ILE ASP PHE SER LYS          
SEQRES   9 A  263  PRO PHE MET SER LEU GLY ILE SER ILE MET ILE LYS LYS          
SEQRES  10 A  263  GLY THR PRO ILE GLU SER ALA GLU ASP LEU SER LYS GLN          
SEQRES  11 A  263  THR GLU ILE ALA TYR GLY THR LEU ASP SER GLY SER THR          
SEQRES  12 A  263  LYS GLU PHE PHE ARG ARG SER LYS ILE ALA VAL PHE ASP          
SEQRES  13 A  263  LYS MET TRP THR TYR MET ARG SER ALA GLU PRO SER VAL          
SEQRES  14 A  263  PHE VAL ARG THR THR ALA GLU GLY VAL ALA ARG VAL ARG          
SEQRES  15 A  263  LYS SER LYS GLY LYS TYR ALA TYR LEU LEU GLU SER THR          
SEQRES  16 A  263  MET ASN GLU TYR ILE GLU GLN ARG LYS PRO CYS ASP THR          
SEQRES  17 A  263  MET LYS VAL GLY GLY ASN LEU ASP SER LYS GLY TYR GLY          
SEQRES  18 A  263  ILE ALA THR PRO LYS GLY SER SER LEU GLY ASN ALA VAL          
SEQRES  19 A  263  ASN LEU ALA VAL LEU LYS LEU SER GLU GLN GLY LEU LEU          
SEQRES  20 A  263  ASP LYS LEU LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU          
SEQRES  21 A  263  CYS GLY SER                                                  
SEQRES   1 B  263  GLY ALA ASN LYS THR VAL VAL VAL THR THR ILE LEU GLU          
SEQRES   2 B  263  SER PRO TYR VAL MET MET LYS LYS ASN HIS GLU MET LEU          
SEQRES   3 B  263  GLU GLY ASN GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU          
SEQRES   4 B  263  ALA ALA GLU ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS          
SEQRES   5 B  263  LEU THR ILE VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP          
SEQRES   6 B  263  ALA ASP THR LYS ILE TRP ASN GLY MET VAL GLY GLU LEU          
SEQRES   7 B  263  VAL TYR GLY LYS ALA ASP ILE ALA ILE ALA PRO LEU THR          
SEQRES   8 B  263  ILE THR LEU VAL ARG GLU GLU VAL ILE ASP PHE SER LYS          
SEQRES   9 B  263  PRO PHE MET SER LEU GLY ILE SER ILE MET ILE LYS LYS          
SEQRES  10 B  263  GLY THR PRO ILE GLU SER ALA GLU ASP LEU SER LYS GLN          
SEQRES  11 B  263  THR GLU ILE ALA TYR GLY THR LEU ASP SER GLY SER THR          
SEQRES  12 B  263  LYS GLU PHE PHE ARG ARG SER LYS ILE ALA VAL PHE ASP          
SEQRES  13 B  263  LYS MET TRP THR TYR MET ARG SER ALA GLU PRO SER VAL          
SEQRES  14 B  263  PHE VAL ARG THR THR ALA GLU GLY VAL ALA ARG VAL ARG          
SEQRES  15 B  263  LYS SER LYS GLY LYS TYR ALA TYR LEU LEU GLU SER THR          
SEQRES  16 B  263  MET ASN GLU TYR ILE GLU GLN ARG LYS PRO CYS ASP THR          
SEQRES  17 B  263  MET LYS VAL GLY GLY ASN LEU ASP SER LYS GLY TYR GLY          
SEQRES  18 B  263  ILE ALA THR PRO LYS GLY SER SER LEU GLY ASN ALA VAL          
SEQRES  19 B  263  ASN LEU ALA VAL LEU LYS LEU SER GLU GLN GLY LEU LEU          
SEQRES  20 B  263  ASP LYS LEU LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU          
SEQRES  21 B  263  CYS GLY SER                                                  
SEQRES   1 C  263  GLY ALA ASN LYS THR VAL VAL VAL THR THR ILE LEU GLU          
SEQRES   2 C  263  SER PRO TYR VAL MET MET LYS LYS ASN HIS GLU MET LEU          
SEQRES   3 C  263  GLU GLY ASN GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU          
SEQRES   4 C  263  ALA ALA GLU ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS          
SEQRES   5 C  263  LEU THR ILE VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP          
SEQRES   6 C  263  ALA ASP THR LYS ILE TRP ASN GLY MET VAL GLY GLU LEU          
SEQRES   7 C  263  VAL TYR GLY LYS ALA ASP ILE ALA ILE ALA PRO LEU THR          
SEQRES   8 C  263  ILE THR LEU VAL ARG GLU GLU VAL ILE ASP PHE SER LYS          
SEQRES   9 C  263  PRO PHE MET SER LEU GLY ILE SER ILE MET ILE LYS LYS          
SEQRES  10 C  263  GLY THR PRO ILE GLU SER ALA GLU ASP LEU SER LYS GLN          
SEQRES  11 C  263  THR GLU ILE ALA TYR GLY THR LEU ASP SER GLY SER THR          
SEQRES  12 C  263  LYS GLU PHE PHE ARG ARG SER LYS ILE ALA VAL PHE ASP          
SEQRES  13 C  263  LYS MET TRP THR TYR MET ARG SER ALA GLU PRO SER VAL          
SEQRES  14 C  263  PHE VAL ARG THR THR ALA GLU GLY VAL ALA ARG VAL ARG          
SEQRES  15 C  263  LYS SER LYS GLY LYS TYR ALA TYR LEU LEU GLU SER THR          
SEQRES  16 C  263  MET ASN GLU TYR ILE GLU GLN ARG LYS PRO CYS ASP THR          
SEQRES  17 C  263  MET LYS VAL GLY GLY ASN LEU ASP SER LYS GLY TYR GLY          
SEQRES  18 C  263  ILE ALA THR PRO LYS GLY SER SER LEU GLY ASN ALA VAL          
SEQRES  19 C  263  ASN LEU ALA VAL LEU LYS LEU SER GLU GLN GLY LEU LEU          
SEQRES  20 C  263  ASP LYS LEU LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU          
SEQRES  21 C  263  CYS GLY SER                                                  
HET    GLU  A 301      10                                                       
HET    1NG  A 310      54                                                       
HET    GLU  B 301      10                                                       
HET    1NG  B 310      27                                                       
HET    SO4  B1302       5                                                       
HET     ZN  B1303       1                                                       
HET     ZN  B1304       1                                                       
HET     ZN  B1305       1                                                       
HET    GLU  C 301      10                                                       
HET     ZN  C1302       1                                                       
HET     ZN  C1303       1                                                       
HETNAM     GLU GLUTAMIC ACID                                                    
HETNAM     1NG 1-{4-[2-OXO-2-(1-PYRROLIDINYL)ETHYL]PHENYL}-                     
HETNAM   2 1NG  3-( TRIFLUOROMETHYL)-4,5,6,7-TETRAHYDRO-1H-                     
HETNAM   3 1NG  INDAZOLE                                                        
HETNAM     SO4 SULFATE ION                                                      
HETNAM      ZN ZINC ION                                                         
FORMUL   4  GLU    3(C5 H9 N O4)                                                
FORMUL   5  1NG    2(C20 H22 F3 N3 O)                                           
FORMUL   6  SO4    O4 S 2-                                                      
FORMUL   7   ZN    5(ZN 2+)                                                     
FORMUL   8  HOH   *521(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  GLN A  130  1                                   8    
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  TYR A  256  1                                  12    
HELIX   13  13 GLU B   27  GLU B   30  5                                   4    
HELIX   14  14 GLY B   34  GLY B   48  1                                  15    
HELIX   15  15 ASN B   72  TYR B   80  1                                   9    
HELIX   16  16 THR B   93  GLU B   98  1                                   6    
HELIX   17  17 SER B  123  LYS B  129  1                                   7    
HELIX   18  18 GLY B  141  SER B  150  1                                  10    
HELIX   19  19 ILE B  152  ALA B  165  1                                  14    
HELIX   20  20 THR B  173  SER B  184  1                                  12    
HELIX   21  21 SER B  194  GLN B  202  1                                   9    
HELIX   22  22 LEU B  230  GLN B  244  1                                  15    
HELIX   23  23 GLY B  245  TYR B  256  1                                  12    
HELIX   24  24 ASN C   22  LEU C   26  5                                   5    
HELIX   25  25 GLU C   27  GLU C   30  5                                   4    
HELIX   26  26 GLY C   34  GLY C   48  1                                  15    
HELIX   27  27 ASN C   72  TYR C   80  1                                   9    
HELIX   28  28 THR C   93  GLU C   98  1                                   6    
HELIX   29  29 SER C  123  LYS C  129  1                                   7    
HELIX   30  30 GLY C  141  SER C  150  1                                  10    
HELIX   31  31 ILE C  152  ALA C  165  1                                  14    
HELIX   32  32 THR C  173  SER C  184  1                                  12    
HELIX   33  33 SER C  194  GLN C  202  1                                   9    
HELIX   34  34 LEU C  230  GLN C  244  1                                  15    
HELIX   35  35 GLY C  245  TYR C  256  1                                  12    
SHEET    1  AA 3 TYR A  51  ILE A  55  0                                        
SHEET    2  AA 3 VAL A   6  THR A  10  1  O  VAL A   6   N  LYS A  52           
SHEET    3  AA 3 ILE A  85  ALA A  86  1  O  ILE A  85   N  THR A   9           
SHEET    1  AB 2 MET A  18  MET A  19  0                                        
SHEET    2  AB 2 TYR A  32  GLU A  33 -1  O  GLU A  33   N  MET A  18           
SHEET    1  AC 2 ILE A 100  PHE A 102  0                                        
SHEET    2  AC 2 ALA A 223  PRO A 225 -1  O  THR A 224   N  ASP A 101           
SHEET    1  AD 2 MET A 107  LEU A 109  0                                        
SHEET    2  AD 2 LYS A 218  TYR A 220 -1  O  LYS A 218   N  LEU A 109           
SHEET    1  AE 4 ALA A 134  GLY A 136  0                                        
SHEET    2  AE 4 TYR A 188  GLU A 193  1  O  ALA A 189   N  GLY A 136           
SHEET    3  AE 4 ILE A 111  LYS A 116 -1  O  SER A 112   N  LEU A 192           
SHEET    4  AE 4 THR A 208  VAL A 211 -1  O  MET A 209   N  ILE A 115           
SHEET    1  BA 3 TYR B  51  ILE B  55  0                                        
SHEET    2  BA 3 VAL B   6  THR B  10  1  O  VAL B   6   N  LYS B  52           
SHEET    3  BA 3 ILE B  85  ALA B  86  1  O  ILE B  85   N  THR B   9           
SHEET    1  BB 2 MET B  18  MET B  19  0                                        
SHEET    2  BB 2 TYR B  32  GLU B  33 -1  O  GLU B  33   N  MET B  18           
SHEET    1  BC 2 ILE B 100  PHE B 102  0                                        
SHEET    2  BC 2 ALA B 223  PRO B 225 -1  O  THR B 224   N  ASP B 101           
SHEET    1  BD 2 MET B 107  LEU B 109  0                                        
SHEET    2  BD 2 LYS B 218  TYR B 220 -1  O  LYS B 218   N  LEU B 109           
SHEET    1  BE 4 ALA B 134  GLY B 136  0                                        
SHEET    2  BE 4 TYR B 188  GLU B 193  1  O  ALA B 189   N  GLY B 136           
SHEET    3  BE 4 ILE B 111  LYS B 116 -1  O  SER B 112   N  LEU B 192           
SHEET    4  BE 4 THR B 208  VAL B 211 -1  O  MET B 209   N  ILE B 115           
SHEET    1  CA 3 TYR C  51  ILE C  55  0                                        
SHEET    2  CA 3 VAL C   6  THR C  10  1  O  VAL C   6   N  LYS C  52           
SHEET    3  CA 3 ILE C  85  ALA C  86  1  O  ILE C  85   N  THR C   9           
SHEET    1  CB 2 MET C  18  MET C  19  0                                        
SHEET    2  CB 2 TYR C  32  GLU C  33 -1  O  GLU C  33   N  MET C  18           
SHEET    1  CC 2 ILE C 100  PHE C 102  0                                        
SHEET    2  CC 2 ALA C 223  PRO C 225 -1  O  THR C 224   N  ASP C 101           
SHEET    1  CD 2 MET C 107  LEU C 109  0                                        
SHEET    2  CD 2 LYS C 218  TYR C 220 -1  O  LYS C 218   N  LEU C 109           
SHEET    1  CE 4 ALA C 134  GLY C 136  0                                        
SHEET    2  CE 4 TYR C 188  GLU C 193  1  O  ALA C 189   N  GLY C 136           
SHEET    3  CE 4 ILE C 111  LYS C 116 -1  O  SER C 112   N  LEU C 192           
SHEET    4  CE 4 THR C 208  VAL C 211 -1  O  MET C 209   N  ILE C 115           
SSBOND   1 CYS A  206    CYS A  261                          1555   1555  2.04  
SSBOND   2 CYS B  206    CYS B  261                          1555   1555  2.04  
SSBOND   3 CYS C  206    CYS C  261                          1555   1555  2.04  
LINK         O1  SO4 B1302                ZN    ZN B1303     1555   1555  2.12  
LINK        ZN    ZN B1303                 NE2 HIS A  46     1555   1555  2.03  
LINK        ZN    ZN B1303                 OE1 GLU B 166     1555   1555  1.87  
LINK        ZN    ZN B1303                 OE1 GLU A  42     1555   1555  1.98  
LINK        ZN    ZN B1304                 NE2 HIS B  23     1555   1555  1.99  
LINK        ZN    ZN B1304                 OE2 GLU B  30     1555   1555  1.98  
LINK        ZN    ZN B1304                 NE2 HIS C  23     1555   4557  1.99  
LINK        ZN    ZN B1304                 O   HOH B2194     1555   1555  2.18  
LINK        ZN    ZN B1305                 OE1 GLU B  42     1555   1555  1.98  
LINK        ZN    ZN B1305                 NE2 HIS B  46     1555   1555  1.98  
LINK        ZN    ZN B1305                 OE2 GLU A 166     1555   3657  2.01  
LINK        ZN    ZN B1305                 O   HOH B2195     1555   1555  2.30  
LINK        ZN    ZN C1302                 O   HOH C2150     1555   1555  1.87  
LINK        ZN    ZN C1302                 NE2 HIS A  23     1555   4457  2.08  
LINK        ZN    ZN C1302                 OD2 ASP C  65     1555   1555  2.05  
LINK        ZN    ZN C1303                 NE2 HIS C  46     1555   1555  2.19  
LINK        ZN    ZN C1303                 OE1 GLU C  42     1555   1555  2.21  
CISPEP   1 SER A   14    PRO A   15          0        -0.30                     
CISPEP   2 GLU A  166    PRO A  167          0        -7.05                     
CISPEP   3 LYS A  204    PRO A  205          0         6.01                     
CISPEP   4 SER B   14    PRO B   15          0        -1.54                     
CISPEP   5 GLU B  166    PRO B  167          0        -5.23                     
CISPEP   6 LYS B  204    PRO B  205          0         9.38                     
CISPEP   7 SER C   14    PRO C   15          0        -0.19                     
CISPEP   8 GLU C  166    PRO C  167          0         2.96                     
CISPEP   9 LYS C  204    PRO C  205          0         6.19                     
SITE     1 AC1 14 TYR A  61  PRO A  89  LEU A  90  THR A  91                    
SITE     2 AC1 14 ARG A  96  LEU A 138  GLY A 141  SER A 142                    
SITE     3 AC1 14 THR A 143  GLU A 193  TYR A 220  HOH A2088                    
SITE     4 AC1 14 HOH A2121  HOH A2172                                          
SITE     1 AC2 34 ILE A  92  LYS A 104  PRO A 105  PHE A 106                    
SITE     2 AC2 34 SER A 108  SER A 217  LYS A 218  GLY A 219                    
SITE     3 AC2 34 LEU A 239  SER A 242  LEU A 247  HOH A2071                    
SITE     4 AC2 34 HOH A2072  HOH A2137  HOH A2140  HOH A2152                    
SITE     5 AC2 34 HOH A2165  HOH A2173  HOH A2174  ILE C  92                    
SITE     6 AC2 34 LYS C 104  PRO C 105  PHE C 106  SER C 108                    
SITE     7 AC2 34 SER C 217  LYS C 218  GLY C 219  LEU C 247                    
SITE     8 AC2 34 HOH C2059  HOH C2067  HOH C2068  HOH C2145                    
SITE     9 AC2 34 HOH C2148  HOH C2149                                          
SITE     1 AC3 13 TYR B  61  PRO B  89  LEU B  90  THR B  91                    
SITE     2 AC3 13 ARG B  96  GLY B 141  SER B 142  THR B 143                    
SITE     3 AC3 13 GLU B 193  TYR B 220  HOH B2104  HOH B2151                    
SITE     4 AC3 13 HOH B2190                                                     
SITE     1 AC4 18 ILE B  92  LYS B 104  PRO B 105  PHE B 106                    
SITE     2 AC4 18 SER B 108  SER B 217  LYS B 218  GLY B 219                    
SITE     3 AC4 18 LEU B 239  SER B 242  LEU B 247  HOH B2076                    
SITE     4 AC4 18 HOH B2082  HOH B2084  HOH B2178  HOH B2187                    
SITE     5 AC4 18 HOH B2191  HOH B2192                                          
SITE     1 AC5  8 GLU A  42  HIS A  46  ARG B 163  ALA B 165                    
SITE     2 AC5  8 GLU B 166  SER B 168   ZN B1303  HOH B2193                    
SITE     1 AC6  4 GLU A  42  HIS A  46  GLU B 166  SO4 B1302                    
SITE     1 AC7  4 HIS B  23  GLU B  30  HOH B2194  HIS C  23                    
SITE     1 AC8  5 GLU A 166  GLU B  42  HIS B  46  LEU B 241                    
SITE     2 AC8  5 HOH B2195                                                     
SITE     1 AC9 14 TYR C  61  PRO C  89  LEU C  90  THR C  91                    
SITE     2 AC9 14 ARG C  96  LEU C 138  GLY C 141  SER C 142                    
SITE     3 AC9 14 THR C 143  GLU C 193  TYR C 220  HOH C2082                    
SITE     4 AC9 14 HOH C2113  HOH C2147                                          
SITE     1 BC1  4 HIS A  23  ASP C  65  HOH C2150  HOH C2151                    
SITE     1 BC2  5 GLU C  42  LYS C  45  HIS C  46  GLN C 244                    
SITE     2 BC2  5 HOH C2152                                                     
CRYST1  114.374  163.583   47.481  90.00  90.00  90.00 P 21 21 2    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      0.008743  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006113  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021061        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system