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Database: PDB
Entry: 3IL1
LinkDB: 3IL1
Original site: 3IL1 
HEADER    MEMBRANE PROTEIN                        06-AUG-09   3IL1              
TITLE     CRYSTAL STRUCTURE OF THE AMPA SUBUNIT GLUR2 BOUND TO THE ALLOSTERIC   
TITLE    2 MODULATOR, IDRA-21                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMATE RECEPTOR 2;                                      
COMPND   3 CHAIN: B, E, H;                                                      
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;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: GLUR2, GRIA2, GRIA2; GLUR2;                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ORIGAMI B (DE3);                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-22B(+)                                
KEYWDS    GLUTAMATE RECEPTOR, GLUR2, AMPA RECEPTOR, NEUROTRANSMITTER RECEPTOR,  
KEYWDS   2 S1S2, ALLOSTERIC MODULATOR, ALTERNATIVE SPLICING, CELL JUNCTION,     
KEYWDS   3 CELL MEMBRANE, ENDOPLASMIC RETICULUM, GLYCOPROTEIN, ION TRANSPORT,   
KEYWDS   4 IONIC CHANNEL, LIPOPROTEIN, MEMBRANE, PALMITATE, PHOSPHOPROTEIN,     
KEYWDS   5 POSTSYNAPTIC CELL MEMBRANE, RECEPTOR, RNA EDITING, SYNAPSE,          
KEYWDS   6 TRANSMEMBRANE, TRANSPORT, MEMBRANE PROTEIN                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.H.AHMED,C.P.PTAK,R.E.OSWALD                                         
REVDAT   4   01-NOV-17 3IL1    1       REMARK                                   
REVDAT   3   26-JUL-17 3IL1    1       SOURCE                                   
REVDAT   2   22-SEP-09 3IL1    1       JRNL                                     
REVDAT   1   15-SEP-09 3IL1    0                                                
JRNL        AUTH   C.P.PTAK,A.H.AHMED,R.E.OSWALD                                
JRNL        TITL   PROBING THE ALLOSTERIC MODULATOR BINDING SITE OF GLUR2 WITH  
JRNL        TITL 2 THIAZIDE DERIVATIVES                                         
JRNL        REF    BIOCHEMISTRY                  V.  48  8594 2009              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   19673491                                                     
JRNL        DOI    10.1021/BI901127S                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.02                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.300                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 56937                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.510                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 15.0240 -  4.7670    0.99     4490   163  0.2000 0.2040        
REMARK   3     2  4.7670 -  3.8040    0.99     4343   158  0.1540 0.1920        
REMARK   3     3  3.8040 -  3.3290    1.00     4275   156  0.1670 0.2230        
REMARK   3     4  3.3290 -  3.0280    0.98     4212   153  0.1810 0.2260        
REMARK   3     5  3.0280 -  2.8120    0.96     4102   150  0.1980 0.2270        
REMARK   3     6  2.8120 -  2.6470    0.96     4040   146  0.1930 0.2660        
REMARK   3     7  2.6470 -  2.5150    0.94     3993   146  0.1960 0.3130        
REMARK   3     8  2.5150 -  2.4060    0.92     3925   142  0.2080 0.2610        
REMARK   3     9  2.4060 -  2.3140    0.91     3840   141  0.2020 0.2840        
REMARK   3    10  2.3140 -  2.2340    0.88     3692   135  0.1840 0.2550        
REMARK   3    11  2.2340 -  2.1650    0.87     3672   133  0.1830 0.2340        
REMARK   3    12  2.1650 -  2.1030    0.88     3711   135  0.1750 0.2710        
REMARK   3    13  2.1030 -  2.0480    0.86     3567   130  0.1980 0.2340        
REMARK   3    14  2.0480 -  1.9980    0.73     3075   112  0.2230 0.2980        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.37                                          
REMARK   3   B_SOL              : 57.14                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.310            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.23                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.02800                                              
REMARK   3    B22 (A**2) : 0.33000                                              
REMARK   3    B33 (A**2) : -1.35700                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           6210                                  
REMARK   3   ANGLE     :  1.049           8352                                  
REMARK   3   CHIRALITY :  0.068            920                                  
REMARK   3   PLANARITY :  0.004           1033                                  
REMARK   3   DIHEDRAL  : 16.023           2310                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3IL1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-AUG-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000054544.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-DEC-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.977                              
REMARK 200  MONOCHROMATOR                  : RH COATED SI                       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 60130                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : 0.09600                            
REMARK 200  R SYM                      (I) : 0.09600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.67700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.67700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.391                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3DP6                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16-18 PEG8K, 0.1 M NA CACODYLATE, 0.1    
REMARK 280  -0.15 ZINC ACETATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP,          
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   X,-Y,-Z                                                 
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,Z+1/2                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.35550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       82.68300            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.35550            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       82.68300            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1480 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1520 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000     -114.71100            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      165.36600            
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     GLN B 244    CG   CD   OE1  NE2                                  
REMARK 470     ASP E  67    CG   OD1  OD2                                       
REMARK 470     GLN E 244    CG   CD   OE1  NE2                                  
REMARK 470     LEU H  26    CG   CD1  CD2                                       
REMARK 470     GLU H  27    CG   CD   OE1  OE2                                  
REMARK 470     ASP H  67    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HIS E    23     N    MET E    25              2.06            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE1  GLU E    24    ZN     ZN H     2     3545     1.65            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS E  23     -110.64    -10.37                                   
REMARK 500    GLU E  24      -21.27    -11.24                                   
REMARK 500    LEU H  26     -178.04    -64.16                                   
REMARK 500    TRP H 255      -65.02   -102.02                                   
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 B 263  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  42   OE2                                                    
REMARK 620 2 HIS B  46   NE2 105.5                                              
REMARK 620 3 GLU H 166   OE1  92.2 118.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H   2  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H  23   NE2                                                    
REMARK 620 2 GLU H  30   OE2 106.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H   3  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU H  42   OE1                                                    
REMARK 620 2 HIS H  46   NE2 116.1                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLU B 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLU E 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLU H 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 263                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 262                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 3                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B5D B 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B5D B 262                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B5D H 801                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3IJO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3IJX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3IK6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3ILT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3ILU   RELATED DB: PDB                                   
DBREF  3IL1 B    4   117  UNP    P19491   GRIA2_RAT      414    527             
DBREF  3IL1 B  120   261  UNP    P19491   GRIA2_RAT      653    794             
DBREF  3IL1 E    4   117  UNP    P19491   GRIA2_RAT      414    527             
DBREF  3IL1 E  120   261  UNP    P19491   GRIA2_RAT      653    794             
DBREF  3IL1 H    4   117  UNP    P19491   GRIA2_RAT      414    527             
DBREF  3IL1 H  120   261  UNP    P19491   GRIA2_RAT      653    794             
SEQADV 3IL1 GLY B  118  UNP  P19491              LINKER                         
SEQADV 3IL1 THR B  119  UNP  P19491              LINKER                         
SEQADV 3IL1 SER B  242  UNP  P19491    ASN   775 ENGINEERED                     
SEQADV 3IL1 GLY E  118  UNP  P19491              LINKER                         
SEQADV 3IL1 THR E  119  UNP  P19491              LINKER                         
SEQADV 3IL1 SER E  242  UNP  P19491    ASN   775 ENGINEERED                     
SEQADV 3IL1 GLY H  118  UNP  P19491              LINKER                         
SEQADV 3IL1 THR H  119  UNP  P19491              LINKER                         
SEQADV 3IL1 SER H  242  UNP  P19491    ASN   775 ENGINEERED                     
SEQRES   1 B  258  LYS THR VAL VAL VAL THR THR ILE LEU GLU SER PRO TYR          
SEQRES   2 B  258  VAL MET MET LYS LYS ASN HIS GLU MET LEU GLU GLY ASN          
SEQRES   3 B  258  GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU ALA ALA GLU          
SEQRES   4 B  258  ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS LEU THR ILE          
SEQRES   5 B  258  VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP ALA ASP THR          
SEQRES   6 B  258  LYS ILE TRP ASN GLY MET VAL GLY GLU LEU VAL TYR GLY          
SEQRES   7 B  258  LYS ALA ASP ILE ALA ILE ALA PRO LEU THR ILE THR LEU          
SEQRES   8 B  258  VAL ARG GLU GLU VAL ILE ASP PHE SER LYS PRO PHE MET          
SEQRES   9 B  258  SER LEU GLY ILE SER ILE MET ILE LYS LYS GLY THR PRO          
SEQRES  10 B  258  ILE GLU SER ALA GLU ASP LEU SER LYS GLN THR GLU ILE          
SEQRES  11 B  258  ALA TYR GLY THR LEU ASP SER GLY SER THR LYS GLU PHE          
SEQRES  12 B  258  PHE ARG ARG SER LYS ILE ALA VAL PHE ASP LYS MET TRP          
SEQRES  13 B  258  THR TYR MET ARG SER ALA GLU PRO SER VAL PHE VAL ARG          
SEQRES  14 B  258  THR THR ALA GLU GLY VAL ALA ARG VAL ARG LYS SER LYS          
SEQRES  15 B  258  GLY LYS TYR ALA TYR LEU LEU GLU SER THR MET ASN GLU          
SEQRES  16 B  258  TYR ILE GLU GLN ARG LYS PRO CYS ASP THR MET LYS VAL          
SEQRES  17 B  258  GLY GLY ASN LEU ASP SER LYS GLY TYR GLY ILE ALA THR          
SEQRES  18 B  258  PRO LYS GLY SER SER LEU GLY ASN ALA VAL ASN LEU ALA          
SEQRES  19 B  258  VAL LEU LYS LEU SER GLU GLN GLY LEU LEU ASP LYS LEU          
SEQRES  20 B  258  LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU CYS                  
SEQRES   1 E  258  LYS THR VAL VAL VAL THR THR ILE LEU GLU SER PRO TYR          
SEQRES   2 E  258  VAL MET MET LYS LYS ASN HIS GLU MET LEU GLU GLY ASN          
SEQRES   3 E  258  GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU ALA ALA GLU          
SEQRES   4 E  258  ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS LEU THR ILE          
SEQRES   5 E  258  VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP ALA ASP THR          
SEQRES   6 E  258  LYS ILE TRP ASN GLY MET VAL GLY GLU LEU VAL TYR GLY          
SEQRES   7 E  258  LYS ALA ASP ILE ALA ILE ALA PRO LEU THR ILE THR LEU          
SEQRES   8 E  258  VAL ARG GLU GLU VAL ILE ASP PHE SER LYS PRO PHE MET          
SEQRES   9 E  258  SER LEU GLY ILE SER ILE MET ILE LYS LYS GLY THR PRO          
SEQRES  10 E  258  ILE GLU SER ALA GLU ASP LEU SER LYS GLN THR GLU ILE          
SEQRES  11 E  258  ALA TYR GLY THR LEU ASP SER GLY SER THR LYS GLU PHE          
SEQRES  12 E  258  PHE ARG ARG SER LYS ILE ALA VAL PHE ASP LYS MET TRP          
SEQRES  13 E  258  THR TYR MET ARG SER ALA GLU PRO SER VAL PHE VAL ARG          
SEQRES  14 E  258  THR THR ALA GLU GLY VAL ALA ARG VAL ARG LYS SER LYS          
SEQRES  15 E  258  GLY LYS TYR ALA TYR LEU LEU GLU SER THR MET ASN GLU          
SEQRES  16 E  258  TYR ILE GLU GLN ARG LYS PRO CYS ASP THR MET LYS VAL          
SEQRES  17 E  258  GLY GLY ASN LEU ASP SER LYS GLY TYR GLY ILE ALA THR          
SEQRES  18 E  258  PRO LYS GLY SER SER LEU GLY ASN ALA VAL ASN LEU ALA          
SEQRES  19 E  258  VAL LEU LYS LEU SER GLU GLN GLY LEU LEU ASP LYS LEU          
SEQRES  20 E  258  LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU CYS                  
SEQRES   1 H  258  LYS THR VAL VAL VAL THR THR ILE LEU GLU SER PRO TYR          
SEQRES   2 H  258  VAL MET MET LYS LYS ASN HIS GLU MET LEU GLU GLY ASN          
SEQRES   3 H  258  GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU ALA ALA GLU          
SEQRES   4 H  258  ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS LEU THR ILE          
SEQRES   5 H  258  VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP ALA ASP THR          
SEQRES   6 H  258  LYS ILE TRP ASN GLY MET VAL GLY GLU LEU VAL TYR GLY          
SEQRES   7 H  258  LYS ALA ASP ILE ALA ILE ALA PRO LEU THR ILE THR LEU          
SEQRES   8 H  258  VAL ARG GLU GLU VAL ILE ASP PHE SER LYS PRO PHE MET          
SEQRES   9 H  258  SER LEU GLY ILE SER ILE MET ILE LYS LYS GLY THR PRO          
SEQRES  10 H  258  ILE GLU SER ALA GLU ASP LEU SER LYS GLN THR GLU ILE          
SEQRES  11 H  258  ALA TYR GLY THR LEU ASP SER GLY SER THR LYS GLU PHE          
SEQRES  12 H  258  PHE ARG ARG SER LYS ILE ALA VAL PHE ASP LYS MET TRP          
SEQRES  13 H  258  THR TYR MET ARG SER ALA GLU PRO SER VAL PHE VAL ARG          
SEQRES  14 H  258  THR THR ALA GLU GLY VAL ALA ARG VAL ARG LYS SER LYS          
SEQRES  15 H  258  GLY LYS TYR ALA TYR LEU LEU GLU SER THR MET ASN GLU          
SEQRES  16 H  258  TYR ILE GLU GLN ARG LYS PRO CYS ASP THR MET LYS VAL          
SEQRES  17 H  258  GLY GLY ASN LEU ASP SER LYS GLY TYR GLY ILE ALA THR          
SEQRES  18 H  258  PRO LYS GLY SER SER LEU GLY ASN ALA VAL ASN LEU ALA          
SEQRES  19 H  258  VAL LEU LYS LEU SER GLU GLN GLY LEU LEU ASP LYS LEU          
SEQRES  20 H  258  LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU CYS                  
HET    GLU  B 400      10                                                       
HET     ZN  B 263       1                                                       
HET    B5D  B 801      14                                                       
HET    B5D  B 262      14                                                       
HET    GLU  E 400      10                                                       
HET     ZN  E   1       1                                                       
HET     ZN  E 262       1                                                       
HET    GLU  H 400      10                                                       
HET     ZN  H   2       1                                                       
HET     ZN  H   3       1                                                       
HET    B5D  H 801      14                                                       
HETNAM     GLU GLUTAMIC ACID                                                    
HETNAM      ZN ZINC ION                                                         
HETNAM     B5D (3S)-7-CHLORO-3-METHYL-3,4-DIHYDRO-2H-1,2,4-                     
HETNAM   2 B5D  BENZOTHIADIAZINE 1,1-DIOXIDE                                    
FORMUL   4  GLU    3(C5 H9 N O4)                                                
FORMUL   5   ZN    5(ZN 2+)                                                     
FORMUL   6  B5D    3(C8 H9 CL N2 O2 S)                                          
FORMUL  15  HOH   *828(H2 O)                                                    
HELIX    1   1 ASN B   22  LEU B   26  5                                   5    
HELIX    2   2 GLU B   27  GLU B   30  5                                   4    
HELIX    3   3 GLY B   34  GLY B   48  1                                  15    
HELIX    4   4 ASN B   72  TYR B   80  1                                   9    
HELIX    5   5 THR B   93  GLU B   98  1                                   6    
HELIX    6   6 SER B  123  LYS B  129  1                                   7    
HELIX    7   7 GLY B  141  SER B  150  1                                  10    
HELIX    8   8 ILE B  152  ALA B  165  1                                  14    
HELIX    9   9 THR B  173  SER B  184  1                                  12    
HELIX   10  10 SER B  194  GLN B  202  1                                   9    
HELIX   11  11 LEU B  230  GLN B  244  1                                  15    
HELIX   12  12 GLY B  245  TYR B  256  1                                  12    
HELIX   13  13 ASN E   22  LEU E   26  5                                   5    
HELIX   14  14 GLU E   27  GLU E   30  5                                   4    
HELIX   15  15 GLY E   34  GLY E   48  1                                  15    
HELIX   16  16 ASN E   72  TYR E   80  1                                   9    
HELIX   17  17 THR E   93  GLU E   98  1                                   6    
HELIX   18  18 SER E  123  LYS E  129  1                                   7    
HELIX   19  19 GLY E  141  SER E  150  1                                  10    
HELIX   20  20 ILE E  152  ALA E  165  1                                  14    
HELIX   21  21 THR E  173  SER E  184  1                                  12    
HELIX   22  22 SER E  194  GLN E  202  1                                   9    
HELIX   23  23 LEU E  230  GLN E  244  1                                  15    
HELIX   24  24 GLY E  245  TYR E  256  1                                  12    
HELIX   25  25 GLU H   27  GLU H   30  5                                   4    
HELIX   26  26 GLY H   34  GLY H   48  1                                  15    
HELIX   27  27 ASN H   72  TYR H   80  1                                   9    
HELIX   28  28 THR H   93  GLU H   98  1                                   6    
HELIX   29  29 SER H  123  LYS H  129  1                                   7    
HELIX   30  30 GLY H  141  SER H  150  1                                  10    
HELIX   31  31 ILE H  152  ALA H  165  1                                  14    
HELIX   32  32 THR H  173  SER H  184  1                                  12    
HELIX   33  33 SER H  194  GLN H  202  1                                   9    
HELIX   34  34 LEU H  230  GLN H  244  1                                  15    
HELIX   35  35 GLY H  245  TRP H  255  1                                  11    
SHEET    1   A 3 TYR B  51  ILE B  55  0                                        
SHEET    2   A 3 VAL B   6  THR B  10  1  N  VAL B   8   O  LYS B  52           
SHEET    3   A 3 ILE B  85  ALA B  86  1  O  ILE B  85   N  THR B   9           
SHEET    1   B 2 MET B  18  MET B  19  0                                        
SHEET    2   B 2 TYR B  32  GLU B  33 -1  O  GLU B  33   N  MET B  18           
SHEET    1   C 2 ILE B 100  PHE B 102  0                                        
SHEET    2   C 2 ALA B 223  PRO B 225 -1  O  THR B 224   N  ASP B 101           
SHEET    1   D 2 MET B 107  LEU B 109  0                                        
SHEET    2   D 2 LYS B 218  TYR B 220 -1  O  LYS B 218   N  LEU B 109           
SHEET    1   E 4 ALA B 134  GLY B 136  0                                        
SHEET    2   E 4 TYR B 188  GLU B 193  1  O  LEU B 191   N  GLY B 136           
SHEET    3   E 4 ILE B 111  LYS B 116 -1  N  MET B 114   O  TYR B 190           
SHEET    4   E 4 THR B 208  VAL B 211 -1  O  MET B 209   N  ILE B 115           
SHEET    1   F 3 TYR E  51  ILE E  55  0                                        
SHEET    2   F 3 VAL E   6  THR E  10  1  N  VAL E   8   O  THR E  54           
SHEET    3   F 3 ILE E  85  ALA E  86  1  O  ILE E  85   N  THR E   9           
SHEET    1   G 2 MET E  18  MET E  19  0                                        
SHEET    2   G 2 TYR E  32  GLU E  33 -1  O  GLU E  33   N  MET E  18           
SHEET    1   H 2 ILE E 100  PHE E 102  0                                        
SHEET    2   H 2 ALA E 223  PRO E 225 -1  O  THR E 224   N  ASP E 101           
SHEET    1   I 2 MET E 107  LEU E 109  0                                        
SHEET    2   I 2 LYS E 218  TYR E 220 -1  O  LYS E 218   N  LEU E 109           
SHEET    1   J 4 ALA E 134  GLY E 136  0                                        
SHEET    2   J 4 TYR E 188  GLU E 193  1  O  LEU E 191   N  GLY E 136           
SHEET    3   J 4 ILE E 111  LYS E 116 -1  N  SER E 112   O  LEU E 192           
SHEET    4   J 4 THR E 208  VAL E 211 -1  O  MET E 209   N  ILE E 115           
SHEET    1   K 3 TYR H  51  ILE H  55  0                                        
SHEET    2   K 3 VAL H   6  THR H  10  1  N  VAL H   8   O  LYS H  52           
SHEET    3   K 3 ILE H  85  ALA H  86  1  O  ILE H  85   N  THR H   9           
SHEET    1   L 2 MET H  18  MET H  19  0                                        
SHEET    2   L 2 TYR H  32  GLU H  33 -1  O  GLU H  33   N  MET H  18           
SHEET    1   M 2 ILE H 100  PHE H 102  0                                        
SHEET    2   M 2 ALA H 223  PRO H 225 -1  O  THR H 224   N  ASP H 101           
SHEET    1   N 2 MET H 107  LEU H 109  0                                        
SHEET    2   N 2 LYS H 218  TYR H 220 -1  O  LYS H 218   N  LEU H 109           
SHEET    1   O 4 ALA H 134  GLY H 136  0                                        
SHEET    2   O 4 TYR H 188  GLU H 193  1  O  LEU H 191   N  GLY H 136           
SHEET    3   O 4 ILE H 111  LYS H 116 -1  N  MET H 114   O  TYR H 190           
SHEET    4   O 4 THR H 208  VAL H 211 -1  O  MET H 209   N  ILE H 115           
SSBOND   1 CYS B  206    CYS B  261                          1555   1555  2.04  
SSBOND   2 CYS E  206    CYS E  261                          1555   1555  2.04  
SSBOND   3 CYS H  206    CYS H  261                          1555   1555  2.04  
LINK         OE2 GLU B  42                ZN    ZN B 263     1555   1555  1.80  
LINK         NE2 HIS B  46                ZN    ZN B 263     1555   1555  2.14  
LINK         OE1 GLU E  42                ZN    ZN E   1     1555   1555  1.89  
LINK         OD2 ASP E  65                ZN    ZN E 262     1555   1555  2.16  
LINK         NE2 HIS H  23                ZN    ZN H   2     1555   1555  2.03  
LINK         OE2 GLU H  30                ZN    ZN H   2     1555   1555  2.07  
LINK         OE1 GLU H  42                ZN    ZN H   3     1555   1555  1.99  
LINK         NE2 HIS H  46                ZN    ZN H   3     1555   1555  2.12  
LINK         OE1 GLU H 166                ZN    ZN B 263     1555   1555  2.02  
CISPEP   1 SER B   14    PRO B   15          0        -0.55                     
CISPEP   2 GLU B  166    PRO B  167          0        -0.65                     
CISPEP   3 LYS B  204    PRO B  205          0         8.28                     
CISPEP   4 SER E   14    PRO E   15          0         0.01                     
CISPEP   5 GLU E  166    PRO E  167          0        -1.72                     
CISPEP   6 LYS E  204    PRO E  205          0         7.05                     
CISPEP   7 SER H   14    PRO H   15          0        -3.91                     
CISPEP   8 GLU H  166    PRO H  167          0        -4.05                     
CISPEP   9 LYS H  204    PRO H  205          0         7.20                     
SITE     1 AC1 13 TYR B  61  PRO B  89  LEU B  90  THR B  91                    
SITE     2 AC1 13 ARG B  96  GLY B 141  SER B 142  THR B 143                    
SITE     3 AC1 13 GLU B 193  TYR B 220  HOH B 269  HOH B 287                    
SITE     4 AC1 13 HOH B 289                                                     
SITE     1 AC2 14 TYR E  61  PRO E  89  LEU E  90  THR E  91                    
SITE     2 AC2 14 ARG E  96  LEU E 138  GLY E 141  SER E 142                    
SITE     3 AC2 14 THR E 143  GLU E 193  TYR E 220  HOH E 264                    
SITE     4 AC2 14 HOH E 267  HOH E 339                                          
SITE     1 AC3 12 TYR H  61  PRO H  89  LEU H  90  THR H  91                    
SITE     2 AC3 12 ARG H  96  GLY H 141  SER H 142  THR H 143                    
SITE     3 AC3 12 GLU H 193  HOH H 270  HOH H 287  HOH H 296                    
SITE     1 AC4  3 GLU B  42  HIS B  46  GLU H 166                               
SITE     1 AC5  2 GLU E  42  HIS E  46                                          
SITE     1 AC6  3 HIS B  23  ASP E  65  HOH E 743                               
SITE     1 AC7  4 HIS E  23  GLU E  24  HIS H  23  GLU H  30                    
SITE     1 AC8  5 GLU B 166  GLU H  42  HIS H  46  LEU H 241                    
SITE     2 AC8  5 GLN H 244                                                     
SITE     1 AC9 10 LYS B 104  PRO B 105  VAL B 238  SER B 242                    
SITE     2 AC9 10 B5D B 262  ILE E  92  PRO E 105  SER E 108                    
SITE     3 AC9 10 LYS E 218  GLY E 219                                          
SITE     1 BC1 11 ILE B  92  SER B 108  SER B 217  LYS B 218                    
SITE     2 BC1 11 GLY B 219  B5D B 801  LYS E 104  PRO E 105                    
SITE     3 BC1 11 VAL E 238  SER E 242  HOH E 610                               
SITE     1 BC2  8 ILE H  92  PRO H 105  SER H 108  LYS H 218                    
SITE     2 BC2  8 GLY H 219  VAL H 238  LEU H 239  SER H 242                    
CRYST1   47.327  114.711  165.366  90.00  90.00  90.00 P 2 21 21    12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.021130  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008718  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006047        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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