GenomeNet

Database: PDB
Entry: 3DP6
LinkDB: 3DP6
Original site: 3DP6 
HEADER    SIGNALING PROTEIN                       07-JUL-08   3DP6              
TITLE     CRYSTAL STRUCTURE OF THE BINDING DOMAIN OF THE AMPA SUBUNIT GLUR2     
TITLE    2 BOUND TO GLUTAMATE                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMATE RECEPTOR 2;                                      
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: S1S2 BINDING DOMAIN;                                       
COMPND   5 SYNONYM: GLUR-2, GLUR-B, GLUR-K2, GLUTAMATE RECEPTOR IONOTROPIC, AMPA
COMPND   6 2, AMPA-SELECTIVE GLUTAMATE RECEPTOR 2;                              
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_TAXID: 10116;                                               
SOURCE   4 GENE: GRIA2, GLUR2;                                                  
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: ORIGAMI B (DE3);                           
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET22B(+)                                 
KEYWDS    GLUTAMATE RECEPTOR, GLUR2, AMPA RECEPTOR, NEUROTRANSMITTER RECEPTOR,  
KEYWDS   2 S1S2, ALTERNATIVE SPLICING, CELL JUNCTION, ENDOPLASMIC RETICULUM,    
KEYWDS   3 GLYCOPROTEIN, ION TRANSPORT, IONIC CHANNEL, LIPOPROTEIN, MEMBRANE,   
KEYWDS   4 PALMITATE, PHOSPHOPROTEIN, POSTSYNAPTIC CELL MEMBRANE, RNA EDITING,  
KEYWDS   5 SYNAPSE, TRANSMEMBRANE, TRANSPORT, SIGNALING PROTEIN                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.H.AHMED,Q.WANG,H.SONDERMANN,R.E.OSWALD                              
REVDAT   5   02-AUG-17 3DP6    1       SOURCE                                   
REVDAT   4   07-APR-09 3DP6    1       AUTHOR JRNL                              
REVDAT   3   17-MAR-09 3DP6    1       HELIX                                    
REVDAT   2   24-FEB-09 3DP6    1       VERSN                                    
REVDAT   1   25-NOV-08 3DP6    0                                                
JRNL        AUTH   A.H.AHMED,Q.WANG,H.SONDERMANN,R.E.OSWALD                     
JRNL        TITL   STRUCTURE OF THE S1S2 GLUTAMATE BINDING DOMAIN OF GLUR3.     
JRNL        REF    PROTEINS                      V.  75   628 2008              
JRNL        REFN                   ISSN 0887-3585                               
JRNL        PMID   19003990                                                     
JRNL        DOI    10.1002/PROT.22274                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : MLF                                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 106939.070                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 119263                         
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 SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 11864                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.002                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.65                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 15681                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2720                       
REMARK   3   BIN FREE R VALUE                    : 0.2920                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1695                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.007                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6054                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 673                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.06                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.02500                                              
REMARK   3    B22 (A**2) : 0.46000                                              
REMARK   3    B33 (A**2) : -0.48400                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.20                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.13                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.22                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.13                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.210                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.750                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 33.11                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : CNS_TOPPAR:PROTEIN_REP.PARAM                   
REMARK   3  PARAMETER FILE  2  : CNS_TOPPAR:WATER_REP.PARAM                     
REMARK   3  PARAMETER FILE  3  : CNS_TOPPAR:ION.PARAM                           
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3DP6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUL-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000048316.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-MAY-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97700                            
REMARK 200  MONOCHROMATOR                  : RH COATED SI                       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 126527                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.10200                            
REMARK 200  R SYM                      (I) : 0.09600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.61                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.41600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3DLN                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 14-17% PEG 8000, 0.1-0.2 M ZN ACETATE,   
REMARK 280  0.1 M NA CACODYLATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP,         
REMARK 280  TEMPERATURE 277K, PH 6.50                                           
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       56.92000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       81.59200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       56.92000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       81.59200            
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, 3                                                 
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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     LEU A   -15                                                      
REMARK 465     VAL A   -14                                                      
REMARK 465     PRO A   -13                                                      
REMARK 465     ARG A   -12                                                      
REMARK 465     GLY A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     ALA A    -9                                                      
REMARK 465     MET A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     SER A    -6                                                      
REMARK 465     GLY A    -5                                                      
REMARK 465     ASN A    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     THR A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     ARG A     0                                                      
REMARK 465     GLY A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ASN A     3                                                      
REMARK 465     GLY A   262                                                      
REMARK 465     SER A   263                                                      
REMARK 465     LEU B   -15                                                      
REMARK 465     VAL B   -14                                                      
REMARK 465     PRO B   -13                                                      
REMARK 465     ARG B   -12                                                      
REMARK 465     GLY B   -11                                                      
REMARK 465     SER B   -10                                                      
REMARK 465     ALA B    -9                                                      
REMARK 465     MET B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     SER B    -6                                                      
REMARK 465     GLY B    -5                                                      
REMARK 465     ASN B    -4                                                      
REMARK 465     ASP B    -3                                                      
REMARK 465     THR B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     ARG B     0                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     ASN B     3                                                      
REMARK 465     GLY B   262                                                      
REMARK 465     SER B   263                                                      
REMARK 465     LEU C   -15                                                      
REMARK 465     VAL C   -14                                                      
REMARK 465     PRO C   -13                                                      
REMARK 465     ARG C   -12                                                      
REMARK 465     GLY C   -11                                                      
REMARK 465     SER C   -10                                                      
REMARK 465     ALA C    -9                                                      
REMARK 465     MET C    -8                                                      
REMARK 465     GLY C    -7                                                      
REMARK 465     SER C    -6                                                      
REMARK 465     GLY C    -5                                                      
REMARK 465     ASN C    -4                                                      
REMARK 465     ASP C    -3                                                      
REMARK 465     THR C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     ARG C     0                                                      
REMARK 465     GLY C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     ASN C     3                                                      
REMARK 465     GLY C   262                                                      
REMARK 465     SER C   263                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TRP C 255      -64.12   -108.65                                   
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 A 302  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  42   OE1                                                    
REMARK 620 2 LYS A  45   NZ  107.4                                              
REMARK 620 3 HIS A  46   NE2  92.1 109.3                                        
REMARK 620 4 GLU C 166   OE2  99.6 120.0 122.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 302  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C  42   OE1                                                    
REMARK 620 2 HIS C  46   NE2  97.4                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLU A 374                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLU B 374                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLU C 374                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3DLN   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE BINDING DOMAIN OF THE AMPA SUBUNIT GLUR3    
REMARK 900 BOUND TO GLUTAMATE                                                   
REMARK 900 RELATED ID: 3DP4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE BINDING DOMAIN OF THE AMPA SUBUNIT GLUR3    
REMARK 900 BOUND TO AMPA                                                        
DBREF  3DP6 A    3   117  UNP    P19491   GRIA2_RAT      413    527             
DBREF  3DP6 A  120   263  UNP    P19491   GRIA2_RAT      653    796             
DBREF  3DP6 B    3   117  UNP    P19491   GRIA2_RAT      413    527             
DBREF  3DP6 B  120   263  UNP    P19491   GRIA2_RAT      653    796             
DBREF  3DP6 C    3   117  UNP    P19491   GRIA2_RAT      413    527             
DBREF  3DP6 C  120   263  UNP    P19491   GRIA2_RAT      653    796             
SEQADV 3DP6 LEU A  -15  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 VAL A  -14  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 PRO A  -13  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 ARG A  -12  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 GLY A  -11  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 SER A  -10  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 ALA A   -9  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 MET A   -8  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 GLY A   -7  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 SER A   -6  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 GLY A   -5  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 ASN A   -4  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 ASP A   -3  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 THR A   -2  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 SER A   -1  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 ARG A    0  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 GLY A    1  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 ALA A    2  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 GLY A  118  UNP  P19491              LINKER                         
SEQADV 3DP6 THR A  119  UNP  P19491              LINKER                         
SEQADV 3DP6 GLY A  262  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 SER A  263  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 LEU B  -15  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 VAL B  -14  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 PRO B  -13  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 ARG B  -12  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 GLY B  -11  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 SER B  -10  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 ALA B   -9  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 MET B   -8  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 GLY B   -7  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 SER B   -6  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 GLY B   -5  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 ASN B   -4  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 ASP B   -3  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 THR B   -2  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 SER B   -1  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 ARG B    0  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 GLY B    1  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 ALA B    2  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 GLY B  118  UNP  P19491              LINKER                         
SEQADV 3DP6 THR B  119  UNP  P19491              LINKER                         
SEQADV 3DP6 GLY B  262  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 SER B  263  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 LEU C  -15  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 VAL C  -14  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 PRO C  -13  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 ARG C  -12  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 GLY C  -11  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 SER C  -10  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 ALA C   -9  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 MET C   -8  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 GLY C   -7  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 SER C   -6  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 GLY C   -5  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 ASN C   -4  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 ASP C   -3  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 THR C   -2  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 SER C   -1  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 ARG C    0  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 GLY C    1  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 ALA C    2  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 GLY C  118  UNP  P19491              LINKER                         
SEQADV 3DP6 THR C  119  UNP  P19491              LINKER                         
SEQADV 3DP6 GLY C  262  UNP  P19491              EXPRESSION TAG                 
SEQADV 3DP6 SER C  263  UNP  P19491              EXPRESSION TAG                 
SEQRES   1 A  279  LEU VAL PRO ARG GLY SER ALA MET GLY SER GLY ASN ASP          
SEQRES   2 A  279  THR SER ARG GLY ALA ASN LYS THR VAL VAL VAL THR THR          
SEQRES   3 A  279  ILE LEU GLU SER PRO TYR VAL MET MET LYS LYS ASN HIS          
SEQRES   4 A  279  GLU MET LEU GLU GLY ASN GLU ARG TYR GLU GLY TYR CYS          
SEQRES   5 A  279  VAL ASP LEU ALA ALA GLU ILE ALA LYS HIS CYS GLY PHE          
SEQRES   6 A  279  LYS TYR LYS LEU THR ILE VAL GLY ASP GLY LYS TYR GLY          
SEQRES   7 A  279  ALA ARG ASP ALA ASP THR LYS ILE TRP ASN GLY MET VAL          
SEQRES   8 A  279  GLY GLU LEU VAL TYR GLY LYS ALA ASP ILE ALA ILE ALA          
SEQRES   9 A  279  PRO LEU THR ILE THR LEU VAL ARG GLU GLU VAL ILE ASP          
SEQRES  10 A  279  PHE SER LYS PRO PHE MET SER LEU GLY ILE SER ILE MET          
SEQRES  11 A  279  ILE LYS LYS GLY THR PRO ILE GLU SER ALA GLU ASP LEU          
SEQRES  12 A  279  SER LYS GLN THR GLU ILE ALA TYR GLY THR LEU ASP SER          
SEQRES  13 A  279  GLY SER THR LYS GLU PHE PHE ARG ARG SER LYS ILE ALA          
SEQRES  14 A  279  VAL PHE ASP LYS MET TRP THR TYR MET ARG SER ALA GLU          
SEQRES  15 A  279  PRO SER VAL PHE VAL ARG THR THR ALA GLU GLY VAL ALA          
SEQRES  16 A  279  ARG VAL ARG LYS SER LYS GLY LYS TYR ALA TYR LEU LEU          
SEQRES  17 A  279  GLU SER THR MET ASN GLU TYR ILE GLU GLN ARG LYS PRO          
SEQRES  18 A  279  CYS ASP THR MET LYS VAL GLY GLY ASN LEU ASP SER LYS          
SEQRES  19 A  279  GLY TYR GLY ILE ALA THR PRO LYS GLY SER SER LEU GLY          
SEQRES  20 A  279  ASN ALA VAL ASN LEU ALA VAL LEU LYS LEU ASN GLU GLN          
SEQRES  21 A  279  GLY LEU LEU ASP LYS LEU LYS ASN LYS TRP TRP TYR ASP          
SEQRES  22 A  279  LYS GLY GLU CYS GLY SER                                      
SEQRES   1 B  279  LEU VAL PRO ARG GLY SER ALA MET GLY SER GLY ASN ASP          
SEQRES   2 B  279  THR SER ARG GLY ALA ASN LYS THR VAL VAL VAL THR THR          
SEQRES   3 B  279  ILE LEU GLU SER PRO TYR VAL MET MET LYS LYS ASN HIS          
SEQRES   4 B  279  GLU MET LEU GLU GLY ASN GLU ARG TYR GLU GLY TYR CYS          
SEQRES   5 B  279  VAL ASP LEU ALA ALA GLU ILE ALA LYS HIS CYS GLY PHE          
SEQRES   6 B  279  LYS TYR LYS LEU THR ILE VAL GLY ASP GLY LYS TYR GLY          
SEQRES   7 B  279  ALA ARG ASP ALA ASP THR LYS ILE TRP ASN GLY MET VAL          
SEQRES   8 B  279  GLY GLU LEU VAL TYR GLY LYS ALA ASP ILE ALA ILE ALA          
SEQRES   9 B  279  PRO LEU THR ILE THR LEU VAL ARG GLU GLU VAL ILE ASP          
SEQRES  10 B  279  PHE SER LYS PRO PHE MET SER LEU GLY ILE SER ILE MET          
SEQRES  11 B  279  ILE LYS LYS GLY THR PRO ILE GLU SER ALA GLU ASP LEU          
SEQRES  12 B  279  SER LYS GLN THR GLU ILE ALA TYR GLY THR LEU ASP SER          
SEQRES  13 B  279  GLY SER THR LYS GLU PHE PHE ARG ARG SER LYS ILE ALA          
SEQRES  14 B  279  VAL PHE ASP LYS MET TRP THR TYR MET ARG SER ALA GLU          
SEQRES  15 B  279  PRO SER VAL PHE VAL ARG THR THR ALA GLU GLY VAL ALA          
SEQRES  16 B  279  ARG VAL ARG LYS SER LYS GLY LYS TYR ALA TYR LEU LEU          
SEQRES  17 B  279  GLU SER THR MET ASN GLU TYR ILE GLU GLN ARG LYS PRO          
SEQRES  18 B  279  CYS ASP THR MET LYS VAL GLY GLY ASN LEU ASP SER LYS          
SEQRES  19 B  279  GLY TYR GLY ILE ALA THR PRO LYS GLY SER SER LEU GLY          
SEQRES  20 B  279  ASN ALA VAL ASN LEU ALA VAL LEU LYS LEU ASN GLU GLN          
SEQRES  21 B  279  GLY LEU LEU ASP LYS LEU LYS ASN LYS TRP TRP TYR ASP          
SEQRES  22 B  279  LYS GLY GLU CYS GLY SER                                      
SEQRES   1 C  279  LEU VAL PRO ARG GLY SER ALA MET GLY SER GLY ASN ASP          
SEQRES   2 C  279  THR SER ARG GLY ALA ASN LYS THR VAL VAL VAL THR THR          
SEQRES   3 C  279  ILE LEU GLU SER PRO TYR VAL MET MET LYS LYS ASN HIS          
SEQRES   4 C  279  GLU MET LEU GLU GLY ASN GLU ARG TYR GLU GLY TYR CYS          
SEQRES   5 C  279  VAL ASP LEU ALA ALA GLU ILE ALA LYS HIS CYS GLY PHE          
SEQRES   6 C  279  LYS TYR LYS LEU THR ILE VAL GLY ASP GLY LYS TYR GLY          
SEQRES   7 C  279  ALA ARG ASP ALA ASP THR LYS ILE TRP ASN GLY MET VAL          
SEQRES   8 C  279  GLY GLU LEU VAL TYR GLY LYS ALA ASP ILE ALA ILE ALA          
SEQRES   9 C  279  PRO LEU THR ILE THR LEU VAL ARG GLU GLU VAL ILE ASP          
SEQRES  10 C  279  PHE SER LYS PRO PHE MET SER LEU GLY ILE SER ILE MET          
SEQRES  11 C  279  ILE LYS LYS GLY THR PRO ILE GLU SER ALA GLU ASP LEU          
SEQRES  12 C  279  SER LYS GLN THR GLU ILE ALA TYR GLY THR LEU ASP SER          
SEQRES  13 C  279  GLY SER THR LYS GLU PHE PHE ARG ARG SER LYS ILE ALA          
SEQRES  14 C  279  VAL PHE ASP LYS MET TRP THR TYR MET ARG SER ALA GLU          
SEQRES  15 C  279  PRO SER VAL PHE VAL ARG THR THR ALA GLU GLY VAL ALA          
SEQRES  16 C  279  ARG VAL ARG LYS SER LYS GLY LYS TYR ALA TYR LEU LEU          
SEQRES  17 C  279  GLU SER THR MET ASN GLU TYR ILE GLU GLN ARG LYS PRO          
SEQRES  18 C  279  CYS ASP THR MET LYS VAL GLY GLY ASN LEU ASP SER LYS          
SEQRES  19 C  279  GLY TYR GLY ILE ALA THR PRO LYS GLY SER SER LEU GLY          
SEQRES  20 C  279  ASN ALA VAL ASN LEU ALA VAL LEU LYS LEU ASN GLU GLN          
SEQRES  21 C  279  GLY LEU LEU ASP LYS LEU LYS ASN LYS TRP TRP TYR ASP          
SEQRES  22 C  279  LYS GLY GLU CYS GLY SER                                      
HET     ZN  A 301       1                                                       
HET     ZN  A 302       1                                                       
HET    GLU  A 374      10                                                       
HET     ZN  B 301       1                                                       
HET     ZN  B 302       1                                                       
HET    GLU  B 374      10                                                       
HET     ZN  C 301       1                                                       
HET     ZN  C 302       1                                                       
HET    GLU  C 374      10                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     GLU GLUTAMIC ACID                                                    
FORMUL   4   ZN    6(ZN 2+)                                                     
FORMUL   6  GLU    3(C5 H9 N O4)                                                
FORMUL  13  HOH   *673(H2 O)                                                    
HELIX    1   1 ASN A   22  LEU A   26  5                                   5    
HELIX    2   2 GLU A   27  GLU A   30  5                                   4    
HELIX    3   3 GLY A   34  GLY A   48  1                                  15    
HELIX    4   4 ASN A   72  TYR A   80  1                                   9    
HELIX    5   5 THR A   93  GLU A   98  1                                   6    
HELIX    6   6 SER A  123  LYS A  129  1                                   7    
HELIX    7   7 GLY A  141  SER A  150  1                                  10    
HELIX    8   8 ILE A  152  ALA A  165  1                                  14    
HELIX    9   9 THR A  173  SER A  184  1                                  12    
HELIX   10  10 SER A  194  GLN A  202  1                                   9    
HELIX   11  11 LEU A  230  GLN A  244  1                                  15    
HELIX   12  12 GLY A  245  TYR A  256  1                                  12    
HELIX   13  13 ASN B   22  LEU B   26  5                                   5    
HELIX   14  14 GLU B   27  GLU B   30  5                                   4    
HELIX   15  15 GLY B   34  GLY B   48  1                                  15    
HELIX   16  16 ASN B   72  TYR B   80  1                                   9    
HELIX   17  17 THR B   93  GLU B   98  1                                   6    
HELIX   18  18 SER B  123  LYS B  129  1                                   7    
HELIX   19  19 GLY B  141  SER B  150  1                                  10    
HELIX   20  20 ILE B  152  ARG B  163  1                                  12    
HELIX   21  21 THR B  173  SER B  184  1                                  12    
HELIX   22  22 SER B  194  GLN B  202  1                                   9    
HELIX   23  23 LEU B  230  GLN B  244  1                                  15    
HELIX   24  24 GLY B  245  TYR B  256  1                                  12    
HELIX   25  25 GLY C   28  GLU C   30  5                                   3    
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  TRP C  255  1                                  11    
SHEET    1   A 3 TYR A  51  ILE A  55  0                                        
SHEET    2   A 3 VAL A   6  THR A  10  1  N  VAL A   8   O  LYS A  52           
SHEET    3   A 3 ILE A  85  ALA A  86  1  O  ILE A  85   N  THR A   9           
SHEET    1   B 2 MET A  18  MET A  19  0                                        
SHEET    2   B 2 TYR A  32  GLU A  33 -1  O  GLU A  33   N  MET A  18           
SHEET    1   C 2 ILE A 100  PHE A 102  0                                        
SHEET    2   C 2 ALA A 223  PRO A 225 -1  O  THR A 224   N  ASP A 101           
SHEET    1   D 2 MET A 107  LEU A 109  0                                        
SHEET    2   D 2 LYS A 218  TYR A 220 -1  O  LYS A 218   N  LEU A 109           
SHEET    1   E 4 ALA A 134  GLY A 136  0                                        
SHEET    2   E 4 TYR A 188  GLU A 193  1  O  LEU A 191   N  GLY A 136           
SHEET    3   E 4 ILE A 111  LYS A 116 -1  N  MET A 114   O  TYR A 190           
SHEET    4   E 4 THR A 208  VAL A 211 -1  O  MET A 209   N  ILE A 115           
SHEET    1   F 3 TYR B  51  ILE B  55  0                                        
SHEET    2   F 3 VAL B   6  THR B  10  1  N  VAL B   8   O  LYS B  52           
SHEET    3   F 3 ILE B  85  ALA B  86  1  O  ILE B  85   N  THR B   9           
SHEET    1   G 2 MET B  18  MET B  19  0                                        
SHEET    2   G 2 TYR B  32  GLU B  33 -1  O  GLU B  33   N  MET B  18           
SHEET    1   H 2 ILE B 100  PHE B 102  0                                        
SHEET    2   H 2 ALA B 223  PRO B 225 -1  O  THR B 224   N  ASP B 101           
SHEET    1   I 2 MET B 107  LEU B 109  0                                        
SHEET    2   I 2 LYS B 218  TYR B 220 -1  O  LYS B 218   N  LEU B 109           
SHEET    1   J 4 ALA B 134  GLY B 136  0                                        
SHEET    2   J 4 TYR B 188  GLU B 193  1  O  LEU B 191   N  GLY B 136           
SHEET    3   J 4 ILE B 111  LYS B 116 -1  N  MET B 114   O  TYR B 190           
SHEET    4   J 4 THR B 208  VAL B 211 -1  O  MET B 209   N  ILE B 115           
SHEET    1   K 3 TYR C  51  ILE C  55  0                                        
SHEET    2   K 3 VAL C   6  THR C  10  1  N  VAL C   8   O  LYS C  52           
SHEET    3   K 3 ILE C  85  ALA C  86  1  O  ILE C  85   N  THR C   9           
SHEET    1   L 2 MET C  18  MET C  19  0                                        
SHEET    2   L 2 TYR C  32  GLU C  33 -1  O  GLU C  33   N  MET C  18           
SHEET    1   M 2 ILE C 100  PHE C 102  0                                        
SHEET    2   M 2 ALA C 223  PRO C 225 -1  O  THR C 224   N  ASP C 101           
SHEET    1   N 2 MET C 107  LEU C 109  0                                        
SHEET    2   N 2 LYS C 218  TYR C 220 -1  O  LYS C 218   N  LEU C 109           
SHEET    1   O 4 ALA C 134  GLY C 136  0                                        
SHEET    2   O 4 TYR C 188  GLU C 193  1  O  LEU C 191   N  GLY C 136           
SHEET    3   O 4 ILE C 111  LYS C 116 -1  N  MET C 114   O  TYR C 190           
SHEET    4   O 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  2.03  
SSBOND   2 CYS B  206    CYS B  261                          1555   1555  2.03  
SSBOND   3 CYS C  206    CYS C  261                          1555   1555  2.02  
LINK         NE2 HIS A  23                ZN    ZN A 301     1555   1555  2.23  
LINK         OE1 GLU A  42                ZN    ZN A 302     1555   1555  2.10  
LINK         NZ  LYS A  45                ZN    ZN A 302     1555   1555  2.23  
LINK         NE2 HIS A  46                ZN    ZN A 302     1555   1555  2.15  
LINK         NE2 HIS C  23                ZN    ZN C 301     1555   1555  2.34  
LINK         OE1 GLU C  42                ZN    ZN C 302     1555   1555  1.94  
LINK         NE2 HIS C  46                ZN    ZN C 302     1555   1555  2.04  
LINK         OE2 GLU C 166                ZN    ZN A 302     1555   1555  2.08  
CISPEP   1 SER A   14    PRO A   15          0         0.02                     
CISPEP   2 GLU A  166    PRO A  167          0         0.04                     
CISPEP   3 LYS A  204    PRO A  205          0         0.43                     
CISPEP   4 SER B   14    PRO B   15          0        -0.02                     
CISPEP   5 GLU B  166    PRO B  167          0        -0.02                     
CISPEP   6 LYS B  204    PRO B  205          0         0.33                     
CISPEP   7 SER C   14    PRO C   15          0        -0.10                     
CISPEP   8 GLU C  166    PRO C  167          0        -0.18                     
CISPEP   9 LYS C  204    PRO C  205          0         0.28                     
SITE     1 AC1  3 HIS A  23  HOH A 465  ASP B  65                               
SITE     1 AC2  4 GLU A  42  LYS A  45  HIS A  46  GLU C 166                    
SITE     1 AC3  4 HIS B  23  GLU B  24  HIS C  23   ZN C 301                    
SITE     1 AC4  3 GLU B  42  LYS B  45  HIS B  46                               
SITE     1 AC5  4 HIS B  23  GLU B  24   ZN B 301  HIS C  23                    
SITE     1 AC6  5 GLU A 166  GLU C  42  HIS C  46  LEU C 241                    
SITE     2 AC6  5 HOH C 375                                                     
SITE     1 AC7 14 TYR A  61  PRO A  89  LEU A  90  THR A  91                    
SITE     2 AC7 14 ARG A  96  LEU A 138  GLY A 141  SER A 142                    
SITE     3 AC7 14 THR A 143  GLU A 193  TYR A 220  HOH A 376                    
SITE     4 AC7 14 HOH A 401  HOH A 403                                          
SITE     1 AC8 14 TYR B  61  PRO B  89  LEU B  90  THR B  91                    
SITE     2 AC8 14 ARG B  96  LEU B 138  GLY B 141  SER B 142                    
SITE     3 AC8 14 THR B 143  GLU B 193  TYR B 220  HOH B 376                    
SITE     4 AC8 14 HOH B 392  HOH B 401                                          
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 C 377                    
SITE     4 AC9 14 HOH C 381  HOH C 392                                          
CRYST1  113.840  163.184   47.324  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      0.008784  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006128  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021131        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system