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Database: PDB
Entry: 3O28
LinkDB: 3O28
Original site: 3O28 
HEADER    TRANSPORT PROTEIN                       22-JUL-10   3O28              
TITLE     LIGAND-BINDING DOMAIN OF GLUA2 (FLIP) IONOTROPIC GLUTAMATE RECEPTOR IN
TITLE    2 COMPLEX WITH AN ALLOSTERIC MODULATOR                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMATE RECEPTOR 2;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: LIGAND BINDING DOMAIN, UNP RESIDUES 413 TO 527 AND 653 TO  
COMPND   5 796;                                                                 
COMPND   6 SYNONYM: GLUR-2, GLUR-B, GLUR-K2, GLUTAMATE RECEPTOR IONOTROPIC, AMPA
COMPND   7 2, GLUA2, AMPA-SELECTIVE GLUTAMATE RECEPTOR 2;                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 OTHER_DETAILS: S1-S2 FUSION IN WHICH GLY118 AND THR119 REPLACE A     
COMPND  10 MEMBRANE-SPANNING REGION                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: 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: ORIGAMI B (DE3);                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-32A                                   
KEYWDS    TRANSPORT PROTEIN, MEMBRANE PROTEIN, FUSION PROTEIN, CHIMERA PROTEIN  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.K.F.MACLEAN,S.BASTEN,R.A.CAMPBELL,I.A.CUMMING,K.J.GILLEN,           
AUTHOR   2 J.GILLESPIE,C.JAMIESON,B.KAZEMIER,M.KICZUN,Y.LAMONT,A.J.LYONS,       
AUTHOR   3 E.M.MOIR,J.A.MORROW,M.PAPAKOSTA,Z.RANKOVIC,L.SMITH                   
REVDAT   4   09-AUG-17 3O28    1       SOURCE REMARK                            
REVDAT   3   01-DEC-10 3O28    1       COMPND REMARK SOURCE                     
REVDAT   2   29-SEP-10 3O28    1       JRNL   REMARK                            
REVDAT   1   15-SEP-10 3O28    0                                                
JRNL        AUTH   C.JAMIESON,S.BASTEN,R.A.CAMPBELL,I.A.CUMMING,K.J.GILLEN,     
JRNL        AUTH 2 J.GILLESPIE,B.KAZEMIER,M.KICZUN,Y.LAMONT,A.J.LYONS,          
JRNL        AUTH 3 J.K.MACLEAN,E.M.MOIR,J.A.MORROW,M.PAPAKOSTA,Z.RANKOVIC,      
JRNL        AUTH 4 L.SMITH                                                      
JRNL        TITL   A NOVEL SERIES OF POSITIVE MODULATORS OF THE AMPA RECEPTOR:  
JRNL        TITL 2 DISCOVERY AND STRUCTURE BASED HIT-TO-LEAD STUDIES.           
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  20  5753 2010              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   20805031                                                     
JRNL        DOI    10.1016/J.BMCL.2010.07.138                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 52.49                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 18291                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.184                           
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 988                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1320                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2130                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 75                           
REMARK   3   BIN FREE R VALUE                    : 0.2630                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2025                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 94                                      
REMARK   3   SOLVENT ATOMS            : 147                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.48                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.40000                                             
REMARK   3    B22 (A**2) : 1.97000                                              
REMARK   3    B33 (A**2) : -0.57000                                             
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.170         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.114         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.965         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.911                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2210 ; 0.019 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2960 ; 1.836 ; 2.016       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   259 ; 6.201 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    86 ;29.906 ;24.419       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   435 ;15.298 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;21.339 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   316 ; 0.113 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1557 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   966 ; 0.231 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1478 ; 0.319 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   117 ; 0.177 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    85 ; 0.253 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    11 ; 0.229 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1360 ; 1.606 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2100 ; 1.634 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1021 ; 3.028 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   860 ; 4.004 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3O28 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000060572.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95375                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18586                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 52.490                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.800                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.13200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.2000                            
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) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.700                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 8000, 100MM SODIUM CACODYLATE    
REMARK 280  PH 4.5, 50MM LITHIUM SULPHATE, VAPOR DIFFUSION, HANGING DROP,       
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       32.56550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.35950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.56550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.35950            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        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     SER A   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     ASN A   3    CG   OD1  ND2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU A    77     O    HOH A   318              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  69       16.54     59.92                                   
REMARK 500    PRO A  89       62.29    -64.54                                   
REMARK 500    LYS A 104      152.30    -49.50                                   
REMARK 500    SER A 140       30.89     74.34                                   
REMARK 500    LYS A 218     -168.68   -162.25                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE O28 A 264                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLU A 265                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 266                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 267                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 268                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 269                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 270                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 271                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 272                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 273                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 274                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 275                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3O29   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3O2A   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3O6G   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3O6H   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3O6I   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3PMV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3PMW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3PMX   RELATED DB: PDB                                   
DBREF  3O28 A    3   117  UNP    P19491   GRIA2_RAT      413    527             
DBREF  3O28 A  120   262  UNP    P19491   GRIA2_RAT      653    795             
SEQADV 3O28 GLY A  118  UNP  P19491              LINKER                         
SEQADV 3O28 THR A  119  UNP  P19491              LINKER                         
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 THR PRO VAL          
SEQRES  19 A  263  ASN LEU ALA VAL LEU LYS LEU SER GLU GLN GLY VAL 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                                                  
HET    O28  A 264      29                                                       
HET    GLU  A 265      10                                                       
HET    SO4  A 266       5                                                       
HET    SO4  A 267       5                                                       
HET    SO4  A 268       5                                                       
HET    DMS  A 269       4                                                       
HET    GOL  A 270       6                                                       
HET    GOL  A 271       6                                                       
HET    GOL  A 272       6                                                       
HET    GOL  A 273       6                                                       
HET    GOL  A 274       6                                                       
HET    GOL  A 275       6                                                       
HETNAM     O28 2-({[3-(TRIFLUOROMETHYL)-4,5,6,7-TETRAHYDRO-1H-INDAZOL-          
HETNAM   2 O28  1-YL]ACETYL}AMINO)-4,5,6,7-TETRAHYDRO-1-                        
HETNAM   3 O28  BENZOTHIOPHENE-3-CARBOXAMIDE                                    
HETNAM     GLU GLUTAMIC ACID                                                    
HETNAM     SO4 SULFATE ION                                                      
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  O28    C19 H21 F3 N4 O2 S                                           
FORMUL   3  GLU    C5 H9 N O4                                                   
FORMUL   4  SO4    3(O4 S 2-)                                                   
FORMUL   7  DMS    C2 H6 O S                                                    
FORMUL   8  GOL    6(C3 H8 O3)                                                  
FORMUL  14  HOH   *147(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    
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           
SSBOND   1 CYS A  206    CYS A  261                          1555   1555  2.06  
CISPEP   1 SER A   14    PRO A   15          0        -2.64                     
CISPEP   2 GLU A  166    PRO A  167          0        -1.69                     
CISPEP   3 LYS A  204    PRO A  205          0         6.14                     
SITE     1 AC1  9 ILE A  92  LYS A 104  PRO A 105  SER A 108                    
SITE     2 AC1  9 SER A 217  LYS A 218  GLY A 219  LEU A 239                    
SITE     3 AC1  9 SER A 242                                                     
SITE     1 AC2 13 TYR A  61  PRO A  89  LEU A  90  THR A  91                    
SITE     2 AC2 13 ARG A  96  LEU A 138  GLY A 141  SER A 142                    
SITE     3 AC2 13 THR A 143  GLU A 193  HOH A 278  HOH A 284                    
SITE     4 AC2 13 HOH A 300                                                     
SITE     1 AC3  7 GLU A  24  ARG A  31  HIS A  46  LYS A 240                    
SITE     2 AC3  7 GLN A 244  SO4 A 268  HOH A 319                               
SITE     1 AC4  5 SER A 140  LYS A 144  ARG A 148  HOH A 341                    
SITE     2 AC4  5 HOH A 373                                                     
SITE     1 AC5  5 HIS A  23  GLU A  24  ARG A  31  LYS A 240                    
SITE     2 AC5  5 SO4 A 266                                                     
SITE     1 AC6  6 GLU A  27  ASN A  29  GLU A  30  ARG A 149                    
SITE     2 AC6  6 LYS A 151  HOH A 412                                          
SITE     1 AC7 10 GLY A  62  ALA A  63  TRP A  71  THR A  93                    
SITE     2 AC7 10 VAL A  95  ARG A  96  GLU A 145  HOH A 312                    
SITE     3 AC7 10 HOH A 330  HOH A 373                                          
SITE     1 AC8  4 GLU A  97  ASP A 101  PHE A 102  LYS A 104                    
SITE     1 AC9  2 TRP A 159  ARG A 163                                          
SITE     1 BC1  8 GLU A  27  ARG A 149  LYS A 151  GLU A 243                    
SITE     2 BC1  8 GLN A 244  HOH A 310  HOH A 367  HOH A 417                    
SITE     1 BC2  4 SER A 194  GLU A 198  ASN A 214  HOH A 344                    
SITE     1 BC3  4 ASN A 214  ASP A 216  SER A 217  ASP A 248                    
CRYST1   65.131   88.719   47.620  90.00  90.00  90.00 P 21 21 2     4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015354  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011271  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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