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Database: PDB
Entry: 5TP9
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HEADER    TRANSPORT PROTEIN                       20-OCT-16   5TP9              
TITLE     STRUCTURE OF THE HUMAN GLUN1/GLUN2A LBD IN COMPLEX WITH COMPOUND 2    
TITLE    2 (GNE9178)                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMATE RECEPTOR IONOTROPIC, NMDA 2A;                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: LIGAND BINDING DOMAIN (UNP RESIDUES 401-539, GT LINKER, UNP
COMPND   5 RESIDUES 661-802);                                                   
COMPND   6 SYNONYM: GLUN2A, GLUTAMATE [NMDA] RECEPTOR SUBUNIT EPSILON-1, N-     
COMPND   7 METHYL D-ASPARTATE RECEPTOR SUBTYPE 2A, HNR2A;                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: GLUTAMATE RECEPTOR IONOTROPIC, NMDA 1;                     
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: UNP RESIDUES 394-544, GT LINKER, UNP RESIDUES 663-800;     
COMPND  13 SYNONYM: GLUN1, GLUTAMATE [NMDA] RECEPTOR SUBUNIT ZETA-1, N-METHYL-D-
COMPND  14 ASPARTATE RECEPTOR SUBUNIT NR1, NMD-R1;                              
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GRIN2A, NMDAR2A;                                               
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: GRIN1, NMDAR1;                                                 
SOURCE  14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  15 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    NMDA RECEPTOR, GLUTAMATE, GLYCINE, CALCIUM CHANNEL, MEMBRANE,         
KEYWDS   2 TRANSPORT PROTEIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.J.A.WALLWEBER,P.J.LUPARDUS                                          
REVDAT   3   08-FEB-17 5TP9    1       JRNL                                     
REVDAT   2   28-DEC-16 5TP9    1       JRNL                                     
REVDAT   1   30-NOV-16 5TP9    0                                                
JRNL        AUTH   E.VILLEMURE,M.VOLGRAF,Y.JIANG,G.WU,C.Q.LY,P.W.YUEN,A.LU,     
JRNL        AUTH 2 X.LUO,M.LIU,S.ZHANG,P.J.LUPARDUS,H.J.WALLWEBER,B.M.LIEDERER, 
JRNL        AUTH 3 G.DESHMUKH,E.PLISE,S.TAY,T.M.WANG,J.E.HANSON,D.H.HACKOS,     
JRNL        AUTH 4 K.SCEARCE-LEVIE,J.B.SCHWARZ,B.D.SELLERS                      
JRNL        TITL   GLUN2A-SELECTIVE PYRIDOPYRIMIDINONE SERIES OF NMDAR POSITIVE 
JRNL        TITL 2 ALLOSTERIC MODULATORS WITH AN IMPROVED IN VIVO PROFILE.      
JRNL        REF    ACS MED CHEM LETT             V.   8    84 2017              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   28105280                                                     
JRNL        DOI    10.1021/ACSMEDCHEMLETT.6B00388                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.6                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.67                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 24871                          
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)  : 0.192                          
REMARK   3   R VALUE            (WORKING SET)  : 0.190                          
REMARK   3   FREE R VALUE                      : 0.237                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.030                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1251                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : 0.000                          
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 12                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.39                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.50                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 97.81                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2914                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2320                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2794                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2280                   
REMARK   3   BIN FREE R VALUE                        : 0.3260                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.12                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 120                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4367                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 47                                      
REMARK   3   SOLVENT ATOMS            : 124                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 55.22                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.11                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.66840                                             
REMARK   3    B22 (A**2) : 4.05420                                              
REMARK   3    B33 (A**2) : -1.38580                                             
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) : 0.290               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.392               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.241               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.377               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.242               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 4546   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 6161   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1579   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 107    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 686    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 4546   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 596    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 5142   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.08                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.11                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.28                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5TP9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-OCT-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000224592.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JAN-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : LIQUID NITROGEN-COOLED DUAL        
REMARK 200                                   CRYSTAL SI(111)                    
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24941                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.900                              
REMARK 200  R MERGE                    (I) : 0.08100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.72200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, PH 7.0, 10-13% PEG8000, 2   
REMARK 280  MM CALCIUM ACETATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE      
REMARK 280  277K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       28.13000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.43000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.89000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.43000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.13000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.89000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2450 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25180 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     SER A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     ASP A     4                                                      
REMARK 465     ASP A     5                                                      
REMARK 465     PRO A    26                                                      
REMARK 465     LEU A    27                                                      
REMARK 465     THR A    28                                                      
REMARK 465     HIS A   284                                                      
REMARK 465     ASN A   285                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     ASN B   100                                                      
REMARK 465     ASN B   101                                                      
REMARK 465     SER B   102                                                      
REMARK 465     GLU B   290                                                      
REMARK 465     CYS B   291                                                      
REMARK 465     ASP B   292                                                      
REMARK 465     SER B   293                                                      
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     ASP A  25    CG   OD1  OD2                                       
REMARK 470     GLU A  29    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  33    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 144    CG   CD   OE1  NE2                                  
REMARK 470     SER A 149    OG                                                  
REMARK 470     GLU A 226    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 229    CG   CD   CE   NZ                                   
REMARK 470     SER A 235    OG                                                  
REMARK 470     ASP B  50    CG   OD1  OD2                                       
REMARK 470     THR B  51    OG1  CG2                                            
REMARK 470     ARG B  77    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  98    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B 103    CG   OD1  ND2                                       
REMARK 470     LYS B 104    CG   CD   CE   NZ                                   
REMARK 470     GLU B 106    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 170    CG   OD1  OD2                                       
REMARK 470     LYS B 171    CG   CD   CE   NZ                                   
REMARK 470     GLU B 244    CG   CD   OE1  OE2                                  
REMARK 470     TYR B 288    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN B 289    CG   CD   OE1  NE2                                  
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    GLU A  15       96.83   -173.31                                   
REMARK 500    THR A  30     -166.46   -120.20                                   
REMARK 500    ARG A  33     -134.32     55.14                                   
REMARK 500    LYS A  74       72.07     63.21                                   
REMARK 500    LYS A  86     -113.76   -119.46                                   
REMARK 500    ASN A  96     -164.95   -112.28                                   
REMARK 500    SER A 235       49.12    -98.78                                   
REMARK 500    THR A 242     -157.93   -156.33                                   
REMARK 500    SER B   4      123.02    172.96                                   
REMARK 500    ASN B  80       69.95     63.63                                   
REMARK 500    ASN B 108     -167.44   -101.51                                   
REMARK 500    ASN B 217        5.91     56.70                                   
REMARK 500    ASN B 217        6.36     56.40                                   
REMARK 500    PHE B 247       67.99     18.90                                   
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 ACT A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GLU A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7H0 A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GLY B 302                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5TPA   RELATED DB: PDB                                   
DBREF  5TP9 A    3   141  UNP    Q12879   NMDE1_HUMAN    401    539             
DBREF  5TP9 A  144   285  UNP    Q12879   NMDE1_HUMAN    661    802             
DBREF  5TP9 B    3   153  UNP    Q05586   NMDZ1_HUMAN    415    565             
DBREF  5TP9 B  156   293  UNP    Q05586   NMDZ1_HUMAN    684    821             
SEQADV 5TP9 GLY A    1  UNP  Q12879              EXPRESSION TAG                 
SEQADV 5TP9 SER A    2  UNP  Q12879              EXPRESSION TAG                 
SEQADV 5TP9 GLY A  142  UNP  Q12879              LINKER                         
SEQADV 5TP9 THR A  143  UNP  Q12879              LINKER                         
SEQADV 5TP9 GLY B    1  UNP  Q05586              EXPRESSION TAG                 
SEQADV 5TP9 SER B    2  UNP  Q05586              EXPRESSION TAG                 
SEQADV 5TP9 GLY B  154  UNP  Q05586              LINKER                         
SEQADV 5TP9 THR B  155  UNP  Q05586              LINKER                         
SEQRES   1 A  285  GLY SER PRO ASP ASP ASN HIS LEU SER ILE VAL THR LEU          
SEQRES   2 A  285  GLU GLU ALA PRO PHE VAL ILE VAL GLU ASP ILE ASP PRO          
SEQRES   3 A  285  LEU THR GLU THR CYS VAL ARG ASN THR VAL PRO CYS ARG          
SEQRES   4 A  285  LYS PHE VAL LYS ILE ASN ASN SER THR ASN GLU GLY MET          
SEQRES   5 A  285  ASN VAL LYS LYS CYS CYS LYS GLY PHE CYS ILE ASP ILE          
SEQRES   6 A  285  LEU LYS LYS LEU SER ARG THR VAL LYS PHE THR TYR ASP          
SEQRES   7 A  285  LEU TYR LEU VAL THR ASN GLY LYS HIS GLY LYS LYS VAL          
SEQRES   8 A  285  ASN ASN VAL TRP ASN GLY MET ILE GLY GLU VAL VAL TYR          
SEQRES   9 A  285  GLN ARG ALA VAL MET ALA VAL GLY SER LEU THR ILE ASN          
SEQRES  10 A  285  GLU GLU ARG SER GLU VAL VAL ASP PHE SER VAL PRO PHE          
SEQRES  11 A  285  VAL GLU THR GLY ILE SER VAL MET VAL SER ARG GLY THR          
SEQRES  12 A  285  GLN VAL THR GLY LEU SER ASP LYS LYS PHE GLN ARG PRO          
SEQRES  13 A  285  HIS ASP TYR SER PRO PRO PHE ARG PHE GLY THR VAL PRO          
SEQRES  14 A  285  ASN GLY SER THR GLU ARG ASN ILE ARG ASN ASN TYR PRO          
SEQRES  15 A  285  TYR MET HIS GLN TYR MET THR LYS PHE ASN GLN LYS GLY          
SEQRES  16 A  285  VAL GLU ASP ALA LEU VAL SER LEU LYS THR GLY LYS LEU          
SEQRES  17 A  285  ASP ALA PHE ILE TYR ASP ALA ALA VAL LEU ASN TYR LYS          
SEQRES  18 A  285  ALA GLY ARG ASP GLU GLY CYS LYS LEU VAL THR ILE GLY          
SEQRES  19 A  285  SER GLY TYR ILE PHE ALA THR THR GLY TYR GLY ILE ALA          
SEQRES  20 A  285  LEU GLN LYS GLY SER PRO TRP LYS ARG GLN ILE ASP LEU          
SEQRES  21 A  285  ALA LEU LEU GLN PHE VAL GLY ASP GLY GLU MET GLU GLU          
SEQRES  22 A  285  LEU GLU THR LEU TRP LEU THR GLY ILE CYS HIS ASN              
SEQRES   1 B  293  GLY SER MET SER THR ARG LEU LYS ILE VAL THR ILE HIS          
SEQRES   2 B  293  GLN GLU PRO PHE VAL TYR VAL LYS PRO THR LEU SER ASP          
SEQRES   3 B  293  GLY THR CYS LYS GLU GLU PHE THR VAL ASN GLY ASP PRO          
SEQRES   4 B  293  VAL LYS LYS VAL ILE CYS THR GLY PRO ASN ASP THR SER          
SEQRES   5 B  293  PRO GLY SER PRO ARG HIS THR VAL PRO GLN CYS CYS TYR          
SEQRES   6 B  293  GLY PHE CYS ILE ASP LEU LEU ILE LYS LEU ALA ARG THR          
SEQRES   7 B  293  MET ASN PHE THR TYR GLU VAL HIS LEU VAL ALA ASP GLY          
SEQRES   8 B  293  LYS PHE GLY THR GLN GLU ARG VAL ASN ASN SER ASN LYS          
SEQRES   9 B  293  LYS GLU TRP ASN GLY MET MET GLY GLU LEU LEU SER GLY          
SEQRES  10 B  293  GLN ALA ASP MET ILE VAL ALA PRO LEU THR ILE ASN ASN          
SEQRES  11 B  293  GLU ARG ALA GLN TYR ILE GLU PHE SER LYS PRO PHE LYS          
SEQRES  12 B  293  TYR GLN GLY LEU THR ILE LEU VAL LYS LYS GLY THR ARG          
SEQRES  13 B  293  ILE THR GLY ILE ASN ASP PRO ARG LEU ARG ASN PRO SER          
SEQRES  14 B  293  ASP LYS PHE ILE TYR ALA THR VAL LYS GLN SER SER VAL          
SEQRES  15 B  293  ASP ILE TYR PHE ARG ARG GLN VAL GLU LEU SER THR MET          
SEQRES  16 B  293  TYR ARG HIS MET GLU LYS HIS ASN TYR GLU SER ALA ALA          
SEQRES  17 B  293  GLU ALA ILE GLN ALA VAL ARG ASP ASN LYS LEU HIS ALA          
SEQRES  18 B  293  PHE ILE TRP ASP SER ALA VAL LEU GLU PHE GLU ALA SER          
SEQRES  19 B  293  GLN LYS CYS ASP LEU VAL THR THR GLY GLU LEU PHE PHE          
SEQRES  20 B  293  ARG SER GLY PHE GLY ILE GLY MET ARG LYS ASP SER PRO          
SEQRES  21 B  293  TRP LYS GLN ASN VAL SER LEU SER ILE LEU LYS SER HIS          
SEQRES  22 B  293  GLU ASN GLY PHE MET GLU ASP LEU ASP LYS THR TRP VAL          
SEQRES  23 B  293  ARG TYR GLN GLU CYS ASP SER                                  
HET    ACT  A 301       4                                                       
HET    GLU  A 302      10                                                       
HET    7H0  A 303      27                                                       
HET     CA  B 301       1                                                       
HET    GLY  B 302       5                                                       
HETNAM     ACT ACETATE ION                                                      
HETNAM     GLU GLUTAMIC ACID                                                    
HETNAM     7H0 7-{[5-CHLORO-3-(TRIFLUOROMETHYL)-1H-PYRAZOL-1-                   
HETNAM   2 7H0  YL]METHYL}-N-ETHYL-2-METHYL-5-OXO-5H-[1,3]THIAZOLO[3,           
HETNAM   3 7H0  2-A]PYRIMIDINE-3-CARBOXAMIDE                                    
HETNAM      CA CALCIUM ION                                                      
HETNAM     GLY GLYCINE                                                          
FORMUL   3  ACT    C2 H3 O2 1-                                                  
FORMUL   4  GLU    C5 H9 N O4                                                   
FORMUL   5  7H0    C15 H13 CL F3 N5 O2 S                                        
FORMUL   6   CA    CA 2+                                                        
FORMUL   7  GLY    C2 H5 N O2                                                   
FORMUL   8  HOH   *124(H2 O)                                                    
HELIX    1 AA1 GLY A   60  VAL A   73  1                                  14    
HELIX    2 AA2 ASN A   96  TYR A  104  1                                   9    
HELIX    3 AA3 ASN A  117  GLU A  122  1                                   6    
HELIX    4 AA4 ASP A  150  ARG A  155  1                                   6    
HELIX    5 AA5 PRO A  156  TYR A  159  5                                   4    
HELIX    6 AA6 GLY A  171  TYR A  181  1                                  11    
HELIX    7 AA7 TYR A  181  THR A  189  1                                   9    
HELIX    8 AA8 LYS A  190  ASN A  192  5                                   3    
HELIX    9 AA9 GLY A  195  THR A  205  1                                  11    
HELIX   10 AB1 ALA A  215  ASP A  225  1                                  11    
HELIX   11 AB2 ILE A  233  TYR A  237  1                                   5    
HELIX   12 AB3 TRP A  254  ASP A  268  1                                  15    
HELIX   13 AB4 GLY A  269  LEU A  279  1                                  11    
HELIX   14 AB5 GLY B   66  ASN B   80  1                                  15    
HELIX   15 AB6 ASN B  108  SER B  116  1                                   9    
HELIX   16 AB7 ASN B  129  GLN B  134  1                                   6    
HELIX   17 AB8 ASP B  162  ASN B  167  1                                   6    
HELIX   18 AB9 SER B  180  GLN B  189  1                                  10    
HELIX   19 AC1 LEU B  192  GLU B  200  1                                   9    
HELIX   20 AC2 SER B  206  ASP B  216  1                                  11    
HELIX   21 AC3 SER B  226  LYS B  236  1                                  11    
HELIX   22 AC4 TRP B  261  ASN B  275  1                                  15    
HELIX   23 AC5 GLY B  276  VAL B  286  1                                  11    
SHEET    1 AA1 5 THR A  76  LEU A  81  0                                        
SHEET    2 AA1 5 HIS A   7  THR A  12  1  N  LEU A   8   O  THR A  76           
SHEET    3 AA1 5 MET A 109  ALA A 110  1  O  MET A 109   N  VAL A  11           
SHEET    4 AA1 5 ALA A 247  LEU A 248 -1  O  ALA A 247   N  ALA A 110           
SHEET    5 AA1 5 ASP A 125  PHE A 126 -1  N  ASP A 125   O  LEU A 248           
SHEET    1 AA2 3 ILE A  20  ASP A  23  0                                        
SHEET    2 AA2 3 GLY A  51  LYS A  59 -1  O  LYS A  59   N  ILE A  20           
SHEET    3 AA2 3 VAL A  36  LYS A  43 -1  N  VAL A  42   O  MET A  52           
SHEET    1 AA3 2 LYS A  90  VAL A  91  0                                        
SHEET    2 AA3 2 VAL A  94  TRP A  95 -1  O  VAL A  94   N  VAL A  91           
SHEET    1 AA4 4 PHE A 165  GLY A 166  0                                        
SHEET    2 AA4 4 ALA A 210  ASP A 214  1  O  ILE A 212   N  GLY A 166           
SHEET    3 AA4 4 VAL A 131  SER A 140 -1  N  MET A 138   O  PHE A 211           
SHEET    4 AA4 4 LEU A 230  THR A 232 -1  O  VAL A 231   N  VAL A 139           
SHEET    1 AA5 4 PHE A 165  GLY A 166  0                                        
SHEET    2 AA5 4 ALA A 210  ASP A 214  1  O  ILE A 212   N  GLY A 166           
SHEET    3 AA5 4 VAL A 131  SER A 140 -1  N  MET A 138   O  PHE A 211           
SHEET    4 AA5 4 PHE A 239  TYR A 244 -1  O  THR A 242   N  THR A 133           
SHEET    1 AA6 6 TYR B  19  PRO B  22  0                                        
SHEET    2 AA6 6 THR B  59  TYR B  65 -1  O  CYS B  63   N  LYS B  21           
SHEET    3 AA6 6 VAL B  43  PRO B  48 -1  N  VAL B  43   O  CYS B  64           
SHEET    4 AA6 6 TYR B  83  LEU B  87  1  O  LEU B  87   N  THR B  46           
SHEET    5 AA6 6 LEU B   7  THR B  11  1  N  ILE B   9   O  GLU B  84           
SHEET    6 AA6 6 MET B 121  ILE B 122  1  O  MET B 121   N  VAL B  10           
SHEET    1 AA7 2 GLN B  96  ARG B  98  0                                        
SHEET    2 AA7 2 LYS B 105  TRP B 107 -1  O  GLU B 106   N  GLU B  97           
SHEET    1 AA8 2 ILE B 136  PHE B 138  0                                        
SHEET    2 AA8 2 GLY B 254  ARG B 256 -1  O  MET B 255   N  GLU B 137           
SHEET    1 AA9 4 TYR B 174  ALA B 175  0                                        
SHEET    2 AA9 4 ALA B 221  ASP B 225  1  O  ILE B 223   N  ALA B 175           
SHEET    3 AA9 4 LYS B 143  LYS B 152 -1  N  LEU B 150   O  PHE B 222           
SHEET    4 AA9 4 LEU B 239  PHE B 251 -1  O  VAL B 240   N  VAL B 151           
SSBOND   1 CYS A   31    CYS A   57                          1555   1555  2.05  
SSBOND   2 CYS A   38    CYS A   58                          1555   1555  2.08  
SSBOND   3 CYS A  228    CYS A  283                          1555   1555  2.05  
SSBOND   4 CYS B   29    CYS B   63                          1555   1555  2.05  
SSBOND   5 CYS B   45    CYS B   64                          1555   1555  2.04  
CISPEP   1 ALA A   16    PRO A   17          0        -2.94                     
CISPEP   2 SER A  160    PRO A  161          0        -4.11                     
CISPEP   3 GLU B   15    PRO B   16          0         3.28                     
SITE     1 AC1  2 ARG A  39  ARG A 106                                          
SITE     1 AC2 12 HIS A  87  SER A 113  THR A 115  ARG A 120                    
SITE     2 AC2 12 GLY A 171  SER A 172  THR A 173  TYR A 213                    
SITE     3 AC2 12 ASP A 214  HOH A 407  HOH A 411  HOH A 459                    
SITE     1 AC3 15 ILE A 116  VAL A 128  PRO A 129  PHE A 130                    
SITE     2 AC3 15 VAL A 131  GLU A 132  THR A 242  GLY A 243                    
SITE     3 AC3 15 LEU A 262  HOH A 404  LYS B 140  PRO B 141                    
SITE     4 AC3 15 TYR B 144  LEU B 270  HIS B 273                               
SITE     1 AC4  9 PHE B  93  PRO B 125  LEU B 126  THR B 127                    
SITE     2 AC4  9 ARG B 132  SER B 180  SER B 181  ASP B 225                    
SITE     3 AC4  9 PHE B 251                                                     
CRYST1   56.260   89.780  120.860  90.00  90.00  90.00 P 21 21 21    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      0.017775  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011138  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008274        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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