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Database: PDB
Entry: 2AL4
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Original site: 2AL4 
HEADER    MEMBRANE PROTEIN                        04-AUG-05   2AL4              
TITLE     CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX 
TITLE    2 WITH QUISQUALATE AND CX614.                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMATE RECEPTOR 2;                                      
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 FRAGMENT: LIGAND BINDING CORE (S1S2J);                               
COMPND   5 SYNONYM: GLUR-2, GLUR-B, GLUR-K2, GLUTAMATE RECEPTOR IONOTROPIC, AMPA
COMPND   6 2;                                                                   
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: GRIA2, GLUR2;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PETGQ                                     
KEYWDS    IONOTROPIC GLUTAMATE RECEPTOR, GLUR2, LIGAND BINDING CORE, S1S2,      
KEYWDS   2 QUISQUALATE, CX614, MODULATOR, MEMBRANE PROTEIN                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.JIN,S.CLARK,A.M.WEEKS,J.T.DUDMAN,E.GOUAUX,K.M.PARTIN                
REVDAT   4   02-AUG-17 2AL4    1       SOURCE                                   
REVDAT   3   13-JUL-11 2AL4    1       VERSN                                    
REVDAT   2   24-FEB-09 2AL4    1       VERSN                                    
REVDAT   1   25-OCT-05 2AL4    0                                                
JRNL        AUTH   R.JIN,S.CLARK,A.M.WEEKS,J.T.DUDMAN,E.GOUAUX,K.M.PARTIN       
JRNL        TITL   MECHANISM OF POSITIVE ALLOSTERIC MODULATORS ACTING ON AMPA   
JRNL        TITL 2 RECEPTORS.                                                   
JRNL        REF    J.NEUROSCI.                   V.  25  9027 2005              
JRNL        REFN                   ISSN 0270-6474                               
JRNL        PMID   16192394                                                     
JRNL        DOI    10.1523/JNEUROSCI.2567-05.2005                               
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   R.JIN,M.HORNING,M.MAYER,E.GOUAUX                             
REMARK   1  TITL   MECHANISM OF ACTIVATION AND SELECTIVITY IN A LIGAND-GATED    
REMARK   1  TITL 2 ION CHANNEL: STRUCTURAL AND FUNCTIONAL STUDIES OF GLUR2 AND  
REMARK   1  TITL 3 QUISQUALATE.                                                 
REMARK   1  REF    BIOCHEMISTRY                  V.  41 15635 2002              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   Y.SUN,R.OLSON,M.HORNING,N.ARMSTRONG,M.MAYER,E.GOUAUX         
REMARK   1  TITL   MECHANISM OF GLUTAMATE RECEPTOR DESENSITIZATION.             
REMARK   1  REF    NATURE                        V. 417   245 2002              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.88                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 710412.340                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 80.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 153708                         
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) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 15343                           
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) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.81                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 38.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 11040                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2360                       
REMARK   3   BIN FREE R VALUE                    : 0.2580                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1206                         
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            : 11750                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 142                                     
REMARK   3   SOLVENT ATOMS            : 776                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.76000                                              
REMARK   3    B22 (A**2) : 0.78000                                              
REMARK   3    B33 (A**2) : -2.54000                                             
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) : 0.02                            
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) : 0.09                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.200                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.770                           
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) : 1.200 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.790 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.930 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.810 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.40                                                 
REMARK   3   BSOL        : 48.17                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : CX614_12.PAR                                   
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : CX614_1.TOP                                    
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2AL4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-AUG-05.                  
REMARK 100 THE DEPOSITION ID IS D_1000034022.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-SEP-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 153708                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 80.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 34.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB 1MM7                                             
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-14% PEG8000, 0.1-0.15 M ZINC          
REMARK 280  ACETATE, 0.1 M SODIUM ACETATE, PH 5.5, VAPOR DIFFUSION, HANGING     
REMARK 280  DROP, TEMPERATURE 277K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       81.86100            
REMARK 290   SMTRY3   2  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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3610 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -198.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F                                     
REMARK 350   BIOMT1   1 -1.000000  0.000000  0.000000      114.31323            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000      -81.86100            
REMARK 350   BIOMT3   1  0.000000  0.000000 -1.000000       47.30999            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -198.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1 -1.000000  0.000000  0.000000       -0.02477            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000       81.86100            
REMARK 350   BIOMT3   1  0.000000  0.000000 -1.000000       47.30999            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E                                  
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     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     GLY B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     GLY B   262                                                      
REMARK 465     SER B   263                                                      
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 465     GLY D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     ASN D     3                                                      
REMARK 465     GLY D   262                                                      
REMARK 465     SER D   263                                                      
REMARK 465     GLY E     1                                                      
REMARK 465     ALA E     2                                                      
REMARK 465     GLY E   262                                                      
REMARK 465     SER E   263                                                      
REMARK 465     GLY F     1                                                      
REMARK 465     ALA F     2                                                      
REMARK 465     ASN F     3                                                      
REMARK 465     GLY F   262                                                      
REMARK 465     SER F   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    CB   CG   CD   CE   NZ                              
REMARK 470     LYS A  21    CB   CG   CD   CE   NZ                              
REMARK 470     GLU A  24    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  50    CG   CD   CE   NZ                                   
REMARK 470     ASP A  67    CB   CG   OD1  OD2                                  
REMARK 470     LYS A  69    CG   CD   CE   NZ                                   
REMARK 470     LYS A  82    CG   CD   CE   NZ                                   
REMARK 470     GLU A 122    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 125    CG   CD   OE1  OE2                                  
REMARK 470     THR A 131    CB   OG1  CG2                                       
REMARK 470     GLU A 132    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 149    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 151    CG   CD   CE   NZ                                   
REMARK 470     ILE A 152    CD1                                                 
REMARK 470     ALA A 153    CB                                                  
REMARK 470     ARG A 172    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 183    CG   CD   CE   NZ                                   
REMARK 470     LYS A 185    CG   CD   CE   NZ                                   
REMARK 470     LYS A 258    CB   CG   CD   CE   NZ                              
REMARK 470     ASN B   3    CG   OD1  ND2                                       
REMARK 470     LYS B   4    CG   CD   CE   NZ                                   
REMARK 470     GLU B  27    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS B  50    CG   CD   CE   NZ                                   
REMARK 470     ASP B  67    CB   CG   OD1  OD2                                  
REMARK 470     LYS B 151    CB   CG   CD   CE   NZ                              
REMARK 470     LYS B 183    CG   CD   CE   NZ                                   
REMARK 470     LYS B 258    CB   CG   CD   CE   NZ                              
REMARK 470     LYS C   4    CG   CD   CE   NZ                                   
REMARK 470     LYS C  21    CB   CG   CD   CE   NZ                              
REMARK 470     GLU C  24    CB   CG   CD   OE1  OE2                             
REMARK 470     MET C  25    CG   SD   CE                                        
REMARK 470     GLU C  27    CB   CG   CD   OE1  OE2                             
REMARK 470     GLU C  30    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  45    CG   CD   CE   NZ                                   
REMARK 470     GLU C 122    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 125    CG   CD   OE1  OE2                                  
REMARK 470     THR C 131    CB   OG1  CG2                                       
REMARK 470     GLU C 132    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 149    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 151    CB   CG   CD   CE   NZ                              
REMARK 470     ALA C 153    CB                                                  
REMARK 470     GLU C 166    CB   CG   CD   OE1  OE2                             
REMARK 470     ARG C 172    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 183    CG   CD   CE   NZ                                   
REMARK 470     LYS C 258    CB   CG   CD   CE   NZ                              
REMARK 470     LYS D   4    CB   CG   CD   CE   NZ                              
REMARK 470     LYS D  21    CB   CG   CD   CE   NZ                              
REMARK 470     GLU D  24    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  50    CG   CD   CE   NZ                                   
REMARK 470     ASP D  67    CB   CG   OD1  OD2                                  
REMARK 470     LYS D  69    CG   CD   CE   NZ                                   
REMARK 470     LYS D  82    CG   CD   CE   NZ                                   
REMARK 470     GLU D 122    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 125    CG   CD   OE1  OE2                                  
REMARK 470     THR D 131    CB   OG1  CG2                                       
REMARK 470     GLU D 132    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 149    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 151    CG   CD   CE   NZ                                   
REMARK 470     ILE D 152    CD1                                                 
REMARK 470     ALA D 153    CB                                                  
REMARK 470     ARG D 172    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 183    CG   CD   CE   NZ                                   
REMARK 470     LYS D 185    CG   CD   CE   NZ                                   
REMARK 470     LYS D 258    CB   CG   CD   CE   NZ                              
REMARK 470     ASN E   3    CG   OD1  ND2                                       
REMARK 470     LYS E   4    CG   CD   CE   NZ                                   
REMARK 470     GLU E  27    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS E  50    CG   CD   CE   NZ                                   
REMARK 470     ASP E  67    CB   CG   OD1  OD2                                  
REMARK 470     LYS E 151    CB   CG   CD   CE   NZ                              
REMARK 470     LYS E 183    CG   CD   CE   NZ                                   
REMARK 470     LYS E 258    CB   CG   CD   CE   NZ                              
REMARK 470     LYS F   4    CG   CD   CE   NZ                                   
REMARK 470     LYS F  21    CB   CG   CD   CE   NZ                              
REMARK 470     GLU F  24    CB   CG   CD   OE1  OE2                             
REMARK 470     MET F  25    CG   SD   CE                                        
REMARK 470     GLU F  27    CB   CG   CD   OE1  OE2                             
REMARK 470     GLU F  30    CG   CD   OE1  OE2                                  
REMARK 470     LYS F  45    CG   CD   CE   NZ                                   
REMARK 470     GLU F 122    CG   CD   OE1  OE2                                  
REMARK 470     GLU F 125    CG   CD   OE1  OE2                                  
REMARK 470     THR F 131    CB   OG1  CG2                                       
REMARK 470     GLU F 132    CG   CD   OE1  OE2                                  
REMARK 470     ARG F 149    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS F 151    CB   CG   CD   CE   NZ                              
REMARK 470     ALA F 153    CB                                                  
REMARK 470     GLU F 166    CB   CG   CD   OE1  OE2                             
REMARK 470     ARG F 172    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS F 183    CG   CD   CE   NZ                                   
REMARK 470     LYS F 258    CB   CG   CD   CE   NZ                              
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  67      -63.40    124.77                                   
REMARK 500    THR A 131       -7.15   -140.12                                   
REMARK 500    PRO B 205       21.35    -78.42                                   
REMARK 500    ASN C  22       42.33   -101.83                                   
REMARK 500    PRO C 120       53.47    -69.09                                   
REMARK 500    ASP D  67      -63.39    124.91                                   
REMARK 500    THR D 131       -7.32   -140.19                                   
REMARK 500    PRO E 205       21.30    -78.52                                   
REMARK 500    ASN F  22       42.52   -101.83                                   
REMARK 500    PRO F 120       53.29    -68.95                                   
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 821  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  46   NE2                                                    
REMARK 620 2 GLU B 166   OE2 118.0                                              
REMARK 620 3 GLU A  42   OE1  95.5 102.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 822  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  23   NE2                                                    
REMARK 620 2 GLU B  30   OE2 121.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 824  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  46   NE2                                                    
REMARK 620 2 HOH B 825   O   114.5                                              
REMARK 620 3 GLU B  42   OE1  99.1 109.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 825  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C  42   OE1                                                    
REMARK 620 2 HIS C  46   NE2 102.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 826  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D  42   OE1                                                    
REMARK 620 2 HIS D  46   NE2  94.5                                              
REMARK 620 3 GLU E 166   OE2 101.6 117.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 827  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  23   NE2                                                    
REMARK 620 2 GLU E  30   OE2 121.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 829  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  46   NE2                                                    
REMARK 620 2 HOH E 832   O   115.3                                              
REMARK 620 3 GLU E  42   OE1  99.0 110.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 830  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  46   NE2                                                    
REMARK 620 2 GLU F  42   OE1 103.0                                              
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 821                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 822                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 823                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 824                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 825                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 826                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 827                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 828                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 829                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 830                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CX6 C 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CX6 E 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CX6 F 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE QUS A 807                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE QUS B 808                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE QUS C 809                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE QUS D 810                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE QUS E 811                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE QUS F 812                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1MM6   RELATED DB: PDB                                   
REMARK 900 GLUR2 LIGAND BINDING CORE IN COMPLEX WITH QUISQUALATE                
REMARK 900 RELATED ID: 1LBC   RELATED DB: PDB                                   
REMARK 900 GLUR2 LIGAND BINDING CORE IN COMPLEX WITH GLUTAMATE AND              
REMARK 900 CYCLOTHIAZIDE                                                        
REMARK 900 RELATED ID: 1MM7   RELATED DB: PDB                                   
REMARK 900 GLUR2 LIGAND BINDING CORE IN COMPLEX WITH QUISQUALATE                
REMARK 900 RELATED ID: 2AL5   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE THE NATIVE GLUR2 IS A MEMBRANE PROTEIN. TRANSMEMBRANE       
REMARK 999 REGIONS WERE GENETICALLY REMOVED AND REPLACED WITH A GLY-THR         
REMARK 999 LINKER.                                                              
DBREF  2AL4 A    3   117  UNP    P19491   GLR2_RAT       413    527             
DBREF  2AL4 B    3   117  UNP    P19491   GLR2_RAT       413    527             
DBREF  2AL4 C    3   117  UNP    P19491   GLR2_RAT       413    527             
DBREF  2AL4 D    3   117  UNP    P19491   GLR2_RAT       413    527             
DBREF  2AL4 E    3   117  UNP    P19491   GLR2_RAT       413    527             
DBREF  2AL4 F    3   117  UNP    P19491   GLR2_RAT       413    527             
DBREF  2AL4 A  120   263  UNP    P19491   GLR2_RAT       653    796             
DBREF  2AL4 B  120   263  UNP    P19491   GLR2_RAT       653    796             
DBREF  2AL4 C  120   263  UNP    P19491   GLR2_RAT       653    796             
DBREF  2AL4 D  120   263  UNP    P19491   GLR2_RAT       653    796             
DBREF  2AL4 E  120   263  UNP    P19491   GLR2_RAT       653    796             
DBREF  2AL4 F  120   263  UNP    P19491   GLR2_RAT       653    796             
SEQADV 2AL4 GLY A    1  UNP  P19491              CLONING ARTIFACT               
SEQADV 2AL4 ALA A    2  UNP  P19491              CLONING ARTIFACT               
SEQADV 2AL4 GLY A  118  UNP  P19491              SEE REMARK 999                 
SEQADV 2AL4 THR A  119  UNP  P19491              SEE REMARK 999                 
SEQADV 2AL4 GLY B    1  UNP  P19491              CLONING ARTIFACT               
SEQADV 2AL4 ALA B    2  UNP  P19491              CLONING ARTIFACT               
SEQADV 2AL4 GLY B  118  UNP  P19491              SEE REMARK 999                 
SEQADV 2AL4 THR B  119  UNP  P19491              SEE REMARK 999                 
SEQADV 2AL4 GLY C    1  UNP  P19491              CLONING ARTIFACT               
SEQADV 2AL4 ALA C    2  UNP  P19491              CLONING ARTIFACT               
SEQADV 2AL4 GLY C  118  UNP  P19491              SEE REMARK 999                 
SEQADV 2AL4 THR C  119  UNP  P19491              SEE REMARK 999                 
SEQADV 2AL4 GLY D    1  UNP  P19491              CLONING ARTIFACT               
SEQADV 2AL4 ALA D    2  UNP  P19491              CLONING ARTIFACT               
SEQADV 2AL4 GLY D  118  UNP  P19491              SEE REMARK 999                 
SEQADV 2AL4 THR D  119  UNP  P19491              SEE REMARK 999                 
SEQADV 2AL4 GLY E    1  UNP  P19491              CLONING ARTIFACT               
SEQADV 2AL4 ALA E    2  UNP  P19491              CLONING ARTIFACT               
SEQADV 2AL4 GLY E  118  UNP  P19491              SEE REMARK 999                 
SEQADV 2AL4 THR E  119  UNP  P19491              SEE REMARK 999                 
SEQADV 2AL4 GLY F    1  UNP  P19491              CLONING ARTIFACT               
SEQADV 2AL4 ALA F    2  UNP  P19491              CLONING ARTIFACT               
SEQADV 2AL4 GLY F  118  UNP  P19491              SEE REMARK 999                 
SEQADV 2AL4 THR F  119  UNP  P19491              SEE REMARK 999                 
SEQRES   1 A  263  GLY ALA ASN LYS THR VAL VAL VAL THR THR ILE LEU GLU          
SEQRES   2 A  263  SER PRO TYR VAL MET MET LYS LYS ASN HIS GLU MET LEU          
SEQRES   3 A  263  GLU GLY ASN GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU          
SEQRES   4 A  263  ALA ALA GLU ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS          
SEQRES   5 A  263  LEU THR ILE VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP          
SEQRES   6 A  263  ALA ASP THR LYS ILE TRP ASN GLY MET VAL GLY GLU LEU          
SEQRES   7 A  263  VAL TYR GLY LYS ALA ASP ILE ALA ILE ALA PRO LEU THR          
SEQRES   8 A  263  ILE THR LEU VAL ARG GLU GLU VAL ILE ASP PHE SER LYS          
SEQRES   9 A  263  PRO PHE MET SER LEU GLY ILE SER ILE MET ILE LYS LYS          
SEQRES  10 A  263  GLY THR PRO ILE GLU SER ALA GLU ASP LEU SER LYS GLN          
SEQRES  11 A  263  THR GLU ILE ALA TYR GLY THR LEU ASP SER GLY SER THR          
SEQRES  12 A  263  LYS GLU PHE PHE ARG ARG SER LYS ILE ALA VAL PHE ASP          
SEQRES  13 A  263  LYS MET TRP THR TYR MET ARG SER ALA GLU PRO SER VAL          
SEQRES  14 A  263  PHE VAL ARG THR THR ALA GLU GLY VAL ALA ARG VAL ARG          
SEQRES  15 A  263  LYS SER LYS GLY LYS TYR ALA TYR LEU LEU GLU SER THR          
SEQRES  16 A  263  MET ASN GLU TYR ILE GLU GLN ARG LYS PRO CYS ASP THR          
SEQRES  17 A  263  MET LYS VAL GLY GLY ASN LEU ASP SER LYS GLY TYR GLY          
SEQRES  18 A  263  ILE ALA THR PRO LYS GLY SER SER LEU GLY ASN ALA VAL          
SEQRES  19 A  263  ASN LEU ALA VAL LEU LYS LEU ASN GLU GLN GLY LEU LEU          
SEQRES  20 A  263  ASP LYS LEU LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU          
SEQRES  21 A  263  CYS GLY SER                                                  
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 ASN 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 ASN 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                                                  
SEQRES   1 D  263  GLY ALA ASN LYS THR VAL VAL VAL THR THR ILE LEU GLU          
SEQRES   2 D  263  SER PRO TYR VAL MET MET LYS LYS ASN HIS GLU MET LEU          
SEQRES   3 D  263  GLU GLY ASN GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU          
SEQRES   4 D  263  ALA ALA GLU ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS          
SEQRES   5 D  263  LEU THR ILE VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP          
SEQRES   6 D  263  ALA ASP THR LYS ILE TRP ASN GLY MET VAL GLY GLU LEU          
SEQRES   7 D  263  VAL TYR GLY LYS ALA ASP ILE ALA ILE ALA PRO LEU THR          
SEQRES   8 D  263  ILE THR LEU VAL ARG GLU GLU VAL ILE ASP PHE SER LYS          
SEQRES   9 D  263  PRO PHE MET SER LEU GLY ILE SER ILE MET ILE LYS LYS          
SEQRES  10 D  263  GLY THR PRO ILE GLU SER ALA GLU ASP LEU SER LYS GLN          
SEQRES  11 D  263  THR GLU ILE ALA TYR GLY THR LEU ASP SER GLY SER THR          
SEQRES  12 D  263  LYS GLU PHE PHE ARG ARG SER LYS ILE ALA VAL PHE ASP          
SEQRES  13 D  263  LYS MET TRP THR TYR MET ARG SER ALA GLU PRO SER VAL          
SEQRES  14 D  263  PHE VAL ARG THR THR ALA GLU GLY VAL ALA ARG VAL ARG          
SEQRES  15 D  263  LYS SER LYS GLY LYS TYR ALA TYR LEU LEU GLU SER THR          
SEQRES  16 D  263  MET ASN GLU TYR ILE GLU GLN ARG LYS PRO CYS ASP THR          
SEQRES  17 D  263  MET LYS VAL GLY GLY ASN LEU ASP SER LYS GLY TYR GLY          
SEQRES  18 D  263  ILE ALA THR PRO LYS GLY SER SER LEU GLY ASN ALA VAL          
SEQRES  19 D  263  ASN LEU ALA VAL LEU LYS LEU ASN GLU GLN GLY LEU LEU          
SEQRES  20 D  263  ASP LYS LEU LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU          
SEQRES  21 D  263  CYS GLY SER                                                  
SEQRES   1 E  263  GLY ALA ASN LYS THR VAL VAL VAL THR THR ILE LEU GLU          
SEQRES   2 E  263  SER PRO TYR VAL MET MET LYS LYS ASN HIS GLU MET LEU          
SEQRES   3 E  263  GLU GLY ASN GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU          
SEQRES   4 E  263  ALA ALA GLU ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS          
SEQRES   5 E  263  LEU THR ILE VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP          
SEQRES   6 E  263  ALA ASP THR LYS ILE TRP ASN GLY MET VAL GLY GLU LEU          
SEQRES   7 E  263  VAL TYR GLY LYS ALA ASP ILE ALA ILE ALA PRO LEU THR          
SEQRES   8 E  263  ILE THR LEU VAL ARG GLU GLU VAL ILE ASP PHE SER LYS          
SEQRES   9 E  263  PRO PHE MET SER LEU GLY ILE SER ILE MET ILE LYS LYS          
SEQRES  10 E  263  GLY THR PRO ILE GLU SER ALA GLU ASP LEU SER LYS GLN          
SEQRES  11 E  263  THR GLU ILE ALA TYR GLY THR LEU ASP SER GLY SER THR          
SEQRES  12 E  263  LYS GLU PHE PHE ARG ARG SER LYS ILE ALA VAL PHE ASP          
SEQRES  13 E  263  LYS MET TRP THR TYR MET ARG SER ALA GLU PRO SER VAL          
SEQRES  14 E  263  PHE VAL ARG THR THR ALA GLU GLY VAL ALA ARG VAL ARG          
SEQRES  15 E  263  LYS SER LYS GLY LYS TYR ALA TYR LEU LEU GLU SER THR          
SEQRES  16 E  263  MET ASN GLU TYR ILE GLU GLN ARG LYS PRO CYS ASP THR          
SEQRES  17 E  263  MET LYS VAL GLY GLY ASN LEU ASP SER LYS GLY TYR GLY          
SEQRES  18 E  263  ILE ALA THR PRO LYS GLY SER SER LEU GLY ASN ALA VAL          
SEQRES  19 E  263  ASN LEU ALA VAL LEU LYS LEU ASN GLU GLN GLY LEU LEU          
SEQRES  20 E  263  ASP LYS LEU LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU          
SEQRES  21 E  263  CYS GLY SER                                                  
SEQRES   1 F  263  GLY ALA ASN LYS THR VAL VAL VAL THR THR ILE LEU GLU          
SEQRES   2 F  263  SER PRO TYR VAL MET MET LYS LYS ASN HIS GLU MET LEU          
SEQRES   3 F  263  GLU GLY ASN GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU          
SEQRES   4 F  263  ALA ALA GLU ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS          
SEQRES   5 F  263  LEU THR ILE VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP          
SEQRES   6 F  263  ALA ASP THR LYS ILE TRP ASN GLY MET VAL GLY GLU LEU          
SEQRES   7 F  263  VAL TYR GLY LYS ALA ASP ILE ALA ILE ALA PRO LEU THR          
SEQRES   8 F  263  ILE THR LEU VAL ARG GLU GLU VAL ILE ASP PHE SER LYS          
SEQRES   9 F  263  PRO PHE MET SER LEU GLY ILE SER ILE MET ILE LYS LYS          
SEQRES  10 F  263  GLY THR PRO ILE GLU SER ALA GLU ASP LEU SER LYS GLN          
SEQRES  11 F  263  THR GLU ILE ALA TYR GLY THR LEU ASP SER GLY SER THR          
SEQRES  12 F  263  LYS GLU PHE PHE ARG ARG SER LYS ILE ALA VAL PHE ASP          
SEQRES  13 F  263  LYS MET TRP THR TYR MET ARG SER ALA GLU PRO SER VAL          
SEQRES  14 F  263  PHE VAL ARG THR THR ALA GLU GLY VAL ALA ARG VAL ARG          
SEQRES  15 F  263  LYS SER LYS GLY LYS TYR ALA TYR LEU LEU GLU SER THR          
SEQRES  16 F  263  MET ASN GLU TYR ILE GLU GLN ARG LYS PRO CYS ASP THR          
SEQRES  17 F  263  MET LYS VAL GLY GLY ASN LEU ASP SER LYS GLY TYR GLY          
SEQRES  18 F  263  ILE ALA THR PRO LYS GLY SER SER LEU GLY ASN ALA VAL          
SEQRES  19 F  263  ASN LEU ALA VAL LEU LYS LEU ASN GLU GLN GLY LEU LEU          
SEQRES  20 F  263  ASP LYS LEU LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU          
SEQRES  21 F  263  CYS GLY SER                                                  
HET     ZN  A 821       1                                                       
HET    QUS  A 807      13                                                       
HET     ZN  B 822       1                                                       
HET     ZN  B 824       1                                                       
HET    QUS  B 808      13                                                       
HET     ZN  C 823       1                                                       
HET     ZN  C 825       1                                                       
HET    CX6  C 801      36                                                       
HET    QUS  C 809      13                                                       
HET     ZN  D 826       1                                                       
HET    QUS  D 810      13                                                       
HET     ZN  E 827       1                                                       
HET     ZN  E 829       1                                                       
HET    CX6  E 802      36                                                       
HET    QUS  E 811      13                                                       
HET     ZN  F 828       1                                                       
HET     ZN  F 830       1                                                       
HET    CX6  F 803      36                                                       
HET    QUS  F 812      13                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     QUS (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-             
HETNAM   2 QUS  PROPIONIC ACID                                                  
HETNAM     CX6 2,3,6A,7,8,9-HEXAHYDRO-11H-[1,4]DIOXINO[2,3-                     
HETNAM   2 CX6  G]PYRROLO[2,1-B][1,3]BENZOXAZIN-11-ONE                          
HETSYN     QUS QUISQUALATE                                                      
FORMUL   7   ZN    10(ZN 2+)                                                    
FORMUL   8  QUS    6(C5 H7 N3 O5)                                               
FORMUL  14  CX6    3(C13 H13 N O4)                                              
FORMUL  26  HOH   *776(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 GLY B   28  GLU B   30  5                                   3    
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  GLU B  201  1                                   8    
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    
HELIX   36  36 ASN D   22  LEU D   26  5                                   5    
HELIX   37  37 GLU D   27  GLU D   30  5                                   4    
HELIX   38  38 GLY D   34  GLY D   48  1                                  15    
HELIX   39  39 ASN D   72  TYR D   80  1                                   9    
HELIX   40  40 THR D   93  GLU D   98  1                                   6    
HELIX   41  41 SER D  123  LYS D  129  1                                   7    
HELIX   42  42 GLY D  141  SER D  150  1                                  10    
HELIX   43  43 ILE D  152  ALA D  165  1                                  14    
HELIX   44  44 THR D  173  SER D  184  1                                  12    
HELIX   45  45 SER D  194  GLN D  202  1                                   9    
HELIX   46  46 LEU D  230  GLN D  244  1                                  15    
HELIX   47  47 GLY D  245  TYR D  256  1                                  12    
HELIX   48  48 GLY E   28  GLU E   30  5                                   3    
HELIX   49  49 GLY E   34  GLY E   48  1                                  15    
HELIX   50  50 ASN E   72  TYR E   80  1                                   9    
HELIX   51  51 THR E   93  GLU E   98  1                                   6    
HELIX   52  52 SER E  123  LYS E  129  1                                   7    
HELIX   53  53 GLY E  141  SER E  150  1                                  10    
HELIX   54  54 ILE E  152  ALA E  165  1                                  14    
HELIX   55  55 THR E  173  SER E  184  1                                  12    
HELIX   56  56 SER E  194  GLU E  201  1                                   8    
HELIX   57  57 LEU E  230  GLN E  244  1                                  15    
HELIX   58  58 GLY E  245  TYR E  256  1                                  12    
HELIX   59  59 ASN F   22  LEU F   26  5                                   5    
HELIX   60  60 GLU F   27  GLU F   30  5                                   4    
HELIX   61  61 GLY F   34  GLY F   48  1                                  15    
HELIX   62  62 ASN F   72  TYR F   80  1                                   9    
HELIX   63  63 THR F   93  GLU F   98  1                                   6    
HELIX   64  64 SER F  123  LYS F  129  1                                   7    
HELIX   65  65 GLY F  141  SER F  150  1                                  10    
HELIX   66  66 ILE F  152  ALA F  165  1                                  14    
HELIX   67  67 THR F  173  SER F  184  1                                  12    
HELIX   68  68 SER F  194  GLN F  202  1                                   9    
HELIX   69  69 LEU F  230  GLN F  244  1                                  15    
HELIX   70  70 GLY F  245  TYR F  256  1                                  12    
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  SER B 112   O  LEU B 192           
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           
SHEET    1   P 3 TYR D  51  ILE D  55  0                                        
SHEET    2   P 3 VAL D   6  THR D  10  1  N  VAL D   8   O  LYS D  52           
SHEET    3   P 3 ILE D  85  ALA D  86  1  O  ILE D  85   N  THR D   9           
SHEET    1   Q 2 MET D  18  MET D  19  0                                        
SHEET    2   Q 2 TYR D  32  GLU D  33 -1  O  GLU D  33   N  MET D  18           
SHEET    1   R 2 ILE D 100  PHE D 102  0                                        
SHEET    2   R 2 ALA D 223  PRO D 225 -1  O  THR D 224   N  ASP D 101           
SHEET    1   S 2 MET D 107  LEU D 109  0                                        
SHEET    2   S 2 LYS D 218  TYR D 220 -1  O  LYS D 218   N  LEU D 109           
SHEET    1   T 4 ALA D 134  GLY D 136  0                                        
SHEET    2   T 4 TYR D 188  GLU D 193  1  O  LEU D 191   N  GLY D 136           
SHEET    3   T 4 ILE D 111  LYS D 116 -1  N  MET D 114   O  TYR D 190           
SHEET    4   T 4 THR D 208  VAL D 211 -1  O  MET D 209   N  ILE D 115           
SHEET    1   U 3 TYR E  51  ILE E  55  0                                        
SHEET    2   U 3 VAL E   6  THR E  10  1  N  VAL E   8   O  LYS E  52           
SHEET    3   U 3 ILE E  85  ALA E  86  1  O  ILE E  85   N  THR E   9           
SHEET    1   V 2 MET E  18  MET E  19  0                                        
SHEET    2   V 2 TYR E  32  GLU E  33 -1  O  GLU E  33   N  MET E  18           
SHEET    1   W 2 ILE E 100  PHE E 102  0                                        
SHEET    2   W 2 ALA E 223  PRO E 225 -1  O  THR E 224   N  ASP E 101           
SHEET    1   X 2 MET E 107  LEU E 109  0                                        
SHEET    2   X 2 LYS E 218  TYR E 220 -1  O  LYS E 218   N  LEU E 109           
SHEET    1   Y 4 ALA E 134  GLY E 136  0                                        
SHEET    2   Y 4 TYR E 188  GLU E 193  1  O  LEU E 191   N  GLY E 136           
SHEET    3   Y 4 ILE E 111  LYS E 116 -1  N  SER E 112   O  LEU E 192           
SHEET    4   Y 4 THR E 208  VAL E 211 -1  O  MET E 209   N  ILE E 115           
SHEET    1   Z 3 TYR F  51  ILE F  55  0                                        
SHEET    2   Z 3 VAL F   6  THR F  10  1  N  VAL F   8   O  LYS F  52           
SHEET    3   Z 3 ILE F  85  ALA F  86  1  O  ILE F  85   N  THR F   9           
SHEET    1  AA 2 MET F  18  MET F  19  0                                        
SHEET    2  AA 2 TYR F  32  GLU F  33 -1  O  GLU F  33   N  MET F  18           
SHEET    1  AB 2 ILE F 100  PHE F 102  0                                        
SHEET    2  AB 2 ALA F 223  PRO F 225 -1  O  THR F 224   N  ASP F 101           
SHEET    1  AC 2 MET F 107  LEU F 109  0                                        
SHEET    2  AC 2 LYS F 218  TYR F 220 -1  O  LYS F 218   N  LEU F 109           
SHEET    1  AD 4 ALA F 134  GLY F 136  0                                        
SHEET    2  AD 4 TYR F 188  GLU F 193  1  O  ALA F 189   N  ALA F 134           
SHEET    3  AD 4 ILE F 111  LYS F 116 -1  N  MET F 114   O  TYR F 190           
SHEET    4  AD 4 THR F 208  VAL F 211 -1  O  MET F 209   N  ILE F 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  2.03  
SSBOND   4 CYS D  206    CYS D  261                          1555   1555  2.03  
SSBOND   5 CYS E  206    CYS E  261                          1555   1555  2.03  
SSBOND   6 CYS F  206    CYS F  261                          1555   1555  2.03  
LINK        ZN    ZN A 821                 NE2 HIS A  46     1555   1555  2.15  
LINK        ZN    ZN A 821                 OE2 GLU B 166     1555   1555  2.06  
LINK        ZN    ZN A 821                 OE1 GLU A  42     1555   1555  2.07  
LINK        ZN    ZN B 822                 NE2 HIS B  23     1555   1555  2.09  
LINK        ZN    ZN B 822                 OE2 GLU B  30     1555   1555  2.28  
LINK        ZN    ZN B 824                 NE2 HIS B  46     1555   1555  2.05  
LINK        ZN    ZN B 824                 O   HOH B 825     1555   1555  2.29  
LINK        ZN    ZN B 824                 OE1 GLU B  42     1555   1555  2.07  
LINK        ZN    ZN C 823                 OD2 ASP C  65     1555   1555  2.14  
LINK        ZN    ZN C 825                 OE1 GLU C  42     1555   1555  2.29  
LINK        ZN    ZN C 825                 NE2 HIS C  46     1555   1555  2.28  
LINK        ZN    ZN D 826                 OE1 GLU D  42     1555   1555  2.08  
LINK        ZN    ZN D 826                 NE2 HIS D  46     1555   1555  2.18  
LINK        ZN    ZN D 826                 OE2 GLU E 166     1555   1555  2.07  
LINK        ZN    ZN E 827                 NE2 HIS E  23     1555   1555  2.13  
LINK        ZN    ZN E 827                 OE2 GLU E  30     1555   1555  2.24  
LINK        ZN    ZN E 829                 NE2 HIS E  46     1555   1555  2.04  
LINK        ZN    ZN E 829                 O   HOH E 832     1555   1555  2.26  
LINK        ZN    ZN E 829                 OE1 GLU E  42     1555   1555  2.08  
LINK        ZN    ZN F 828                 OD2 ASP F  65     1555   1555  2.15  
LINK        ZN    ZN F 830                 NE2 HIS F  46     1555   1555  2.26  
LINK        ZN    ZN F 830                 OE1 GLU F  42     1555   1555  2.29  
CISPEP   1 SER A   14    PRO A   15          0         0.07                     
CISPEP   2 GLU A  166    PRO A  167          0        -0.10                     
CISPEP   3 LYS A  204    PRO A  205          0         0.32                     
CISPEP   4 SER B   14    PRO B   15          0         0.02                     
CISPEP   5 GLU B  166    PRO B  167          0        -0.14                     
CISPEP   6 LYS B  204    PRO B  205          0         0.22                     
CISPEP   7 SER C   14    PRO C   15          0         0.12                     
CISPEP   8 GLU C  166    PRO C  167          0         0.06                     
CISPEP   9 LYS C  204    PRO C  205          0         0.22                     
CISPEP  10 SER D   14    PRO D   15          0         0.09                     
CISPEP  11 GLU D  166    PRO D  167          0        -0.16                     
CISPEP  12 LYS D  204    PRO D  205          0         0.31                     
CISPEP  13 SER E   14    PRO E   15          0        -0.11                     
CISPEP  14 GLU E  166    PRO E  167          0        -0.30                     
CISPEP  15 LYS E  204    PRO E  205          0         0.31                     
CISPEP  16 SER F   14    PRO F   15          0         0.13                     
CISPEP  17 GLU F  166    PRO F  167          0         0.04                     
CISPEP  18 LYS F  204    PRO F  205          0         0.19                     
SITE     1 AC1  3 GLU A  42  HIS A  46  GLU B 166                               
SITE     1 AC2  2 HIS B  23  GLU B  30                                          
SITE     1 AC3  1 ASP C  65                                                     
SITE     1 AC4  5 GLU B  42  HIS B  46  LEU B 241  GLN B 244                    
SITE     2 AC4  5 HOH B 825                                                     
SITE     1 AC5  2 GLU C  42  HIS C  46                                          
SITE     1 AC6  3 GLU D  42  HIS D  46  GLU E 166                               
SITE     1 AC7  2 HIS E  23  GLU E  30                                          
SITE     1 AC8  1 ASP F  65                                                     
SITE     1 AC9  5 GLU E  42  HIS E  46  LEU E 241  GLN E 244                    
SITE     2 AC9  5 HOH E 832                                                     
SITE     1 BC1  2 GLU F  42  HIS F  46                                          
SITE     1 BC2 20 PRO A 105  PHE A 106  MET A 107  SER A 108                    
SITE     2 BC2 20 SER A 217  LYS A 218  GLY A 219  ASN A 242                    
SITE     3 BC2 20 HOH A 952  PRO C 105  PHE C 106  MET C 107                    
SITE     4 BC2 20 SER C 108  SER C 217  LYS C 218  GLY C 219                    
SITE     5 BC2 20 ASN C 242  HOH C 851  HOH C 911  HOH C 934                    
SITE     1 BC3 20 PRO B 105  PHE B 106  MET B 107  SER B 108                    
SITE     2 BC3 20 SER B 217  LYS B 218  GLY B 219  ASN B 242                    
SITE     3 BC3 20 HOH B 967  PRO E 105  PHE E 106  MET E 107                    
SITE     4 BC3 20 SER E 108  SER E 217  LYS E 218  GLY E 219                    
SITE     5 BC3 20 ASN E 242  HOH E 830  HOH E 860  HOH E 975                    
SITE     1 BC4 20 PRO D 105  PHE D 106  MET D 107  SER D 108                    
SITE     2 BC4 20 SER D 217  LYS D 218  GLY D 219  ASN D 242                    
SITE     3 BC4 20 HOH D 778  PRO F 105  PHE F 106  MET F 107                    
SITE     4 BC4 20 SER F 108  SER F 217  LYS F 218  GLY F 219                    
SITE     5 BC4 20 ASN F 242  HOH F 515  HOH F 706  HOH F 775                    
SITE     1 BC5 15 TYR A  61  PRO A  89  LEU A  90  THR A  91                    
SITE     2 BC5 15 ARG A  96  LEU A 138  GLY A 141  SER A 142                    
SITE     3 BC5 15 THR A 143  LEU A 192  GLU A 193  MET A 196                    
SITE     4 BC5 15 HOH A 822  HOH A 835  HOH A 841                               
SITE     1 BC6 15 TYR B  61  PRO B  89  LEU B  90  THR B  91                    
SITE     2 BC6 15 ARG B  96  LEU B 138  GLY B 141  SER B 142                    
SITE     3 BC6 15 THR B 143  LEU B 192  GLU B 193  MET B 196                    
SITE     4 BC6 15 HOH B 829  HOH B 839  HOH B 850                               
SITE     1 BC7 15 TYR C  61  PRO C  89  LEU C  90  THR C  91                    
SITE     2 BC7 15 ARG C  96  LEU C 138  GLY C 141  SER C 142                    
SITE     3 BC7 15 THR C 143  LEU C 192  GLU C 193  MET C 196                    
SITE     4 BC7 15 HOH C 829  HOH C 837  HOH C 865                               
SITE     1 BC8 15 TYR D  61  PRO D  89  LEU D  90  THR D  91                    
SITE     2 BC8 15 ARG D  96  LEU D 138  GLY D 141  SER D 142                    
SITE     3 BC8 15 THR D 143  LEU D 192  GLU D 193  MET D 196                    
SITE     4 BC8 15 HOH D 392  HOH D 428  HOH D 455                               
SITE     1 BC9 15 TYR E  61  PRO E  89  LEU E  90  THR E  91                    
SITE     2 BC9 15 ARG E  96  LEU E 138  GLY E 141  SER E 142                    
SITE     3 BC9 15 THR E 143  LEU E 192  GLU E 193  MET E 196                    
SITE     4 BC9 15 HOH E 836  HOH E 846  HOH E 857                               
SITE     1 CC1 15 TYR F  61  PRO F  89  LEU F  90  THR F  91                    
SITE     2 CC1 15 ARG F  96  LEU F 138  GLY F 141  SER F 142                    
SITE     3 CC1 15 THR F 143  LEU F 192  GLU F 193  MET F 196                    
SITE     4 CC1 15 HOH F 417  HOH F 448  HOH F 557                               
CRYST1  114.338  163.722   47.310  90.00  90.03  90.00 P 1 21 1     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      0.008746  0.000000  0.000004        0.00000                         
SCALE2      0.000000  0.006108  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021137        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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