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Database: PDB
Entry: 5C5C
LinkDB: 5C5C
Original site: 5C5C 
HEADER    SIGNALING PROTEIN                       19-JUN-15   5C5C              
TITLE     HUMAN METABOTROPIC GLUTAMATE RECEPTOR 7, EXTRACELLULAR LIGAND BINDING 
TITLE    2 DOMAIN                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: METABOTROPIC GLUTAMATE RECEPTOR 7;                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MGLUR7;                                                     
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GRM7, GPRC1G, MGLUR7;                                          
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFHMSP-LIC-N                              
KEYWDS    GLUTAMATE RECEPTORS, GLUTAMIC ACID BINDING, MGLUR7, SIGNALING         
KEYWDS   2 PROTEIN, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.DONG,E.DOBROVETSKY,A.HUTCHINSON,W.TEMPEL,A.M.EDWARDS,C.BOUNTRA,     
AUTHOR   2 C.H.ARROWSMITH,STRUCTURAL GENOMICS CONSORTIUM (SGC)                  
REVDAT   2   29-JUL-20 5C5C    1       COMPND SOURCE AUTHOR JRNL                
REVDAT   2 2                   1       REMARK HETNAM LINK   SITE                
REVDAT   1   15-JUL-15 5C5C    0                                                
JRNL        AUTH   E.DOBROVETSKY,A.DONG,A.HUTCHINSON,W.TEMPEL,A.M.EDWARDS,      
JRNL        AUTH 2 C.BOUNTRA,C.H.ARROWSMITH,                                    
JRNL        AUTH 3 STRUCTURAL GENOMICS CONSORTIUM (SGC)                         
JRNL        TITL   HUMAN METABOTROPIC GLUTAMATE RECEPTOR 7, EXTRACELLULAR       
JRNL        TITL 2 LIGAND BINDING DOMAIN                                        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.86 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.86                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 43231                          
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) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1420                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3236                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 81                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.79000                                              
REMARK   3    B22 (A**2) : -3.87000                                             
REMARK   3    B33 (A**2) : -0.65000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 2.57000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.133         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.133         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.105         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.605         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 5C5C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000211020.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-APR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97929                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44656                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.860                              
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     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : 0.05400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.89                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.78100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.7                                          
REMARK 200 STARTING MODEL: 3MQ4                                                 
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: 20% PEG 3350, 0.2 M K2PO4, VAPOR         
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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       53.08750            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       50.60150            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       53.08750            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       50.60150            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 840 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 19030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
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 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    33                                                      
REMARK 465     ALA A    34                                                      
REMARK 465     MET A    35                                                      
REMARK 465     ASP A    36                                                      
REMARK 465     MET A    37                                                      
REMARK 465     TYR A    38                                                      
REMARK 465     ALA A    39                                                      
REMARK 465     GLN A   128                                                      
REMARK 465     LYS A   129                                                      
REMARK 465     ASP A   130                                                      
REMARK 465     THR A   131                                                      
REMARK 465     SER A   132                                                      
REMARK 465     ASP A   133                                                      
REMARK 465     VAL A   134                                                      
REMARK 465     ARG A   135                                                      
REMARK 465     CYS A   136                                                      
REMARK 465     THR A   137                                                      
REMARK 465     ASN A   138                                                      
REMARK 465     GLY A   139                                                      
REMARK 465     GLU A   140                                                      
REMARK 465     PRO A   141                                                      
REMARK 465     PRO A   142                                                      
REMARK 465     VAL A   143                                                      
REMARK 465     PHE A   144                                                      
REMARK 465     VAL A   145                                                      
REMARK 465     GLY A   317                                                      
REMARK 465     SER A   318                                                      
REMARK 465     LYS A   319                                                      
REMARK 465     ILE A   320                                                      
REMARK 465     ASN A   321                                                      
REMARK 465     PRO A   322                                                      
REMARK 465     LEU A   323                                                      
REMARK 465     HIS A   324                                                      
REMARK 465     GLN A   325                                                      
REMARK 465     THR A   377                                                      
REMARK 465     ILE A   378                                                      
REMARK 465     SER A   379                                                      
REMARK 465     GLY A   380                                                      
REMARK 465     SER A   381                                                      
REMARK 465     LYS A   382                                                      
REMARK 465     LYS A   383                                                      
REMARK 465     GLU A   384                                                      
REMARK 465     ASP A   385                                                      
REMARK 465     THR A   386                                                      
REMARK 465     THR A   487                                                      
REMARK 465     SER A   488                                                      
REMARK 465     ASN A   489                                                      
REMARK 465     GLY A   512                                                      
REMARK 465     LYS A   513                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  60    CD   CE   NZ                                        
REMARK 470     SER A  63    OG                                                  
REMARK 470     VAL A  65    CG1  CG2                                            
REMARK 470     GLU A  73    CD   OE1  OE2                                       
REMARK 470     ILE A 127    CG1  CG2  CD1                                       
REMARK 470     LYS A 146    CE   NZ                                             
REMARK 470     LYS A 149    CD   CE   NZ                                        
REMARK 470     ARG A 190    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 227    CG   CD   OE1  OE2                                  
REMARK 470     SER A 229    OG                                                  
REMARK 470     GLU A 232    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 233    CG   CD   CE   NZ                                   
REMARK 470     LYS A 243    CD   CE   NZ                                        
REMARK 470     ARG A 255    NE   CZ   NH1  NH2                                  
REMARK 470     GLN A 258    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 259    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 260    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 261    CG   CD   CE   NZ                                   
REMARK 470     ASP A 262    CG   OD1  OD2                                       
REMARK 470     ARG A 263    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 269    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 272    CG   CD   CE   NZ                                   
REMARK 470     GLN A 273    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 279    CG   OD1  ND2                                       
REMARK 470     LYS A 293    CD   CE   NZ                                        
REMARK 470     ASP A 314    CG   OD1  OD2                                       
REMARK 470     SER A 315    OG                                                  
REMARK 470     TRP A 316    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 316    CZ3  CH2                                            
REMARK 470     LYS A 375    CD   CE   NZ                                        
REMARK 470     ASP A 387    CG   OD1  OD2                                       
REMARK 470     ARG A 388    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 389    CD   CE   NZ                                        
REMARK 470     LYS A 398    CG   CD   CE   NZ                                   
REMARK 470     LYS A 427    CG   CD   CE   NZ                                   
REMARK 470     ASP A 432    CG   OD1  OD2                                       
REMARK 470     ARG A 434    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 439    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 441    CD   OE1  OE2                                       
REMARK 470     GLN A 442    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 446    CG   CD   CE   NZ                                   
REMARK 470     LYS A 447    CD   CE   NZ                                        
REMARK 470     LYS A 450    CD   CE   NZ                                        
REMARK 470     LYS A 469    CG   CD   CE   NZ                                   
REMARK 470     ASN A 486    CG   OD1  ND2                                       
REMARK 470     ARG A 493    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 501    CD   OE1  OE2                                       
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   OD2  ASP A   328     UNK  UNX A   605              1.77            
REMARK 500   NE2  HIS A   326     UNK  UNX A   605              1.94            
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   OD1  ASP A   428     UNK  UNX A   605     1556     1.75            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 107   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
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 A  41      -62.91   -127.81                                   
REMARK 500    HIS A  41      -41.91   -138.06                                   
REMARK 500    SER A  63      -59.58   -161.54                                   
REMARK 500    CYS A 109       29.77     47.80                                   
REMARK 500    SER A 157      -66.63    -94.83                                   
REMARK 500    ALA A 180      -19.16   -150.89                                   
REMARK 500    ASN A 279      -38.26     82.64                                   
REMARK 500    SER A 313     -173.89     66.68                                   
REMARK 500    ASN A 456      102.47   -160.48                                   
REMARK 500    THR A 499     -123.83   -134.10                                   
REMARK 500    THR A 499     -124.44   -134.10                                   
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                              CA A 603  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE A  89   O                                                      
REMARK 620 2 ASP A  92   O    85.5                                              
REMARK 620 3 LEU A  95   O    97.1  77.6                                        
REMARK 620 4 LEU A  96   O   148.4 119.9  73.0                                  
REMARK 620 5 HOH A 737   O    79.2 163.2 110.9  76.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 604  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU A 186   O                                                      
REMARK 620 2 ASP A 189   OD1 134.4                                              
REMARK 620 3 TYR A 192   O   100.6  74.9                                        
REMARK 620 4 PHE A 195   O   117.7 106.0  78.7                                  
REMARK 620 5 ASN A 470   O   113.4  74.7 144.7  92.9                            
REMARK 620 6 HOH A 739   O    71.1 136.9 143.0  74.4  62.4                      
REMARK 620 N                    1     2     3     4     5                       
DBREF  5C5C A   37   513  UNP    Q14831   GRM7_HUMAN      37    513             
SEQADV 5C5C GLY A   33  UNP  Q14831              EXPRESSION TAG                 
SEQADV 5C5C ALA A   34  UNP  Q14831              EXPRESSION TAG                 
SEQADV 5C5C MET A   35  UNP  Q14831              EXPRESSION TAG                 
SEQADV 5C5C ASP A   36  UNP  Q14831              EXPRESSION TAG                 
SEQADV 5C5C SER A  249  UNP  Q14831    CYS   249 ENGINEERED MUTATION            
SEQRES   1 A  481  GLY ALA MET ASP MET TYR ALA PRO HIS SER ILE ARG ILE          
SEQRES   2 A  481  GLU GLY ASP VAL THR LEU GLY GLY LEU PHE PRO VAL HIS          
SEQRES   3 A  481  ALA LYS GLY PRO SER GLY VAL PRO CYS GLY ASP ILE LYS          
SEQRES   4 A  481  ARG GLU ASN GLY ILE HIS ARG LEU GLU ALA MET LEU TYR          
SEQRES   5 A  481  ALA LEU ASP GLN ILE ASN SER ASP PRO ASN LEU LEU PRO          
SEQRES   6 A  481  ASN VAL THR LEU GLY ALA ARG ILE LEU ASP THR CYS SER          
SEQRES   7 A  481  ARG ASP THR TYR ALA LEU GLU GLN SER LEU THR PHE VAL          
SEQRES   8 A  481  GLN ALA LEU ILE GLN LYS ASP THR SER ASP VAL ARG CYS          
SEQRES   9 A  481  THR ASN GLY GLU PRO PRO VAL PHE VAL LYS PRO GLU LYS          
SEQRES  10 A  481  VAL VAL GLY VAL ILE GLY ALA SER GLY SER SER VAL SER          
SEQRES  11 A  481  ILE MET VAL ALA ASN ILE LEU ARG LEU PHE GLN ILE PRO          
SEQRES  12 A  481  GLN ILE SER TYR ALA SER THR ALA PRO GLU LEU SER ASP          
SEQRES  13 A  481  ASP ARG ARG TYR ASP PHE PHE SER ARG VAL VAL PRO PRO          
SEQRES  14 A  481  ASP SER PHE GLN ALA GLN ALA MET VAL ASP ILE VAL LYS          
SEQRES  15 A  481  ALA LEU GLY TRP ASN TYR VAL SER THR LEU ALA SER GLU          
SEQRES  16 A  481  GLY SER TYR GLY GLU LYS GLY VAL GLU SER PHE THR GLN          
SEQRES  17 A  481  ILE SER LYS GLU ALA GLY GLY LEU SER ILE ALA GLN SER          
SEQRES  18 A  481  VAL ARG ILE PRO GLN GLU ARG LYS ASP ARG THR ILE ASP          
SEQRES  19 A  481  PHE ASP ARG ILE ILE LYS GLN LEU LEU ASP THR PRO ASN          
SEQRES  20 A  481  SER ARG ALA VAL VAL ILE PHE ALA ASN ASP GLU ASP ILE          
SEQRES  21 A  481  LYS GLN ILE LEU ALA ALA ALA LYS ARG ALA ASP GLN VAL          
SEQRES  22 A  481  GLY HIS PHE LEU TRP VAL GLY SER ASP SER TRP GLY SER          
SEQRES  23 A  481  LYS ILE ASN PRO LEU HIS GLN HIS GLU ASP ILE ALA GLU          
SEQRES  24 A  481  GLY ALA ILE THR ILE GLN PRO LYS ARG ALA THR VAL GLU          
SEQRES  25 A  481  GLY PHE ASP ALA TYR PHE THR SER ARG THR LEU GLU ASN          
SEQRES  26 A  481  ASN ARG ARG ASN VAL TRP PHE ALA GLU TYR TRP GLU GLU          
SEQRES  27 A  481  ASN PHE ASN CYS LYS LEU THR ILE SER GLY SER LYS LYS          
SEQRES  28 A  481  GLU ASP THR ASP ARG LYS CYS THR GLY GLN GLU ARG ILE          
SEQRES  29 A  481  GLY LYS ASP SER ASN TYR GLU GLN GLU GLY LYS VAL GLN          
SEQRES  30 A  481  PHE VAL ILE ASP ALA VAL TYR ALA MET ALA HIS ALA LEU          
SEQRES  31 A  481  HIS HIS MET ASN LYS ASP LEU CYS ALA ASP TYR ARG GLY          
SEQRES  32 A  481  VAL CYS PRO GLU MET GLU GLN ALA GLY GLY LYS LYS LEU          
SEQRES  33 A  481  LEU LYS TYR ILE ARG ASN VAL ASN PHE ASN GLY SER ALA          
SEQRES  34 A  481  GLY THR PRO VAL MET PHE ASN LYS ASN GLY ASP ALA PRO          
SEQRES  35 A  481  GLY ARG TYR ASP ILE PHE GLN TYR GLN THR THR ASN THR          
SEQRES  36 A  481  SER ASN PRO GLY TYR ARG LEU ILE GLY GLN TRP THR ASP          
SEQRES  37 A  481  GLU LEU GLN LEU ASN ILE GLU ASP MET GLN TRP GLY LYS          
HET    NAG  A 601      14                                                       
HET    GOL  A 602       6                                                       
HET     CA  A 603       1                                                       
HET     CA  A 604       1                                                       
HET    UNX  A 605       1                                                       
HET    UNX  A 606       1                                                       
HET    UNX  A 607       1                                                       
HET    UNX  A 608       1                                                       
HET    UNX  A 609       1                                                       
HET    UNX  A 610       1                                                       
HET    UNX  A 611       1                                                       
HET    UNX  A 612       1                                                       
HET    UNX  A 613       1                                                       
HET    UNX  A 614       1                                                       
HET    UNX  A 615       1                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     GOL GLYCEROL                                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM     UNX UNKNOWN ATOM OR ION                                              
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  NAG    C8 H15 N O6                                                  
FORMUL   3  GOL    C3 H8 O3                                                     
FORMUL   4   CA    2(CA 2+)                                                     
FORMUL   6  UNX    11(X)                                                        
FORMUL  17  HOH   *81(H2 O)                                                     
HELIX    1 AA1 GLY A   75  SER A   91  1                                  17    
HELIX    2 AA2 ARG A  111  LEU A  120  1                                  10    
HELIX    3 AA3 THR A  121  GLN A  124  5                                   4    
HELIX    4 AA4 GLY A  158  PHE A  172  1                                  15    
HELIX    5 AA5 ALA A  183  ASP A  188  5                                   6    
HELIX    6 AA6 PRO A  201  LEU A  216  1                                  16    
HELIX    7 AA7 GLY A  228  GLY A  246  1                                  19    
HELIX    8 AA8 ASP A  266  ASP A  276  1                                  11    
HELIX    9 AA9 ASN A  288  ALA A  302  1                                  15    
HELIX   10 AB1 VAL A  343  SER A  352  1                                  10    
HELIX   11 AB2 TRP A  363  PHE A  372  1                                  10    
HELIX   12 AB3 LYS A  407  CYS A  430  1                                  24    
HELIX   13 AB4 CYS A  437  ASN A  454  1                                  18    
HELIX   14 AB5 ILE A  506  MET A  509  5                                   4    
SHEET    1 AA1 6 SER A  42  ILE A  45  0                                        
SHEET    2 AA1 6 LEU A 101  ASP A 107 -1  O  ALA A 103   N  ILE A  45           
SHEET    3 AA1 6 VAL A  49  PHE A  55  1  N  VAL A  49   O  GLY A 102           
SHEET    4 AA1 6 VAL A 150  ILE A 154  1  O  GLY A 152   N  GLY A  52           
SHEET    5 AA1 6 GLN A 176  SER A 178  1  O  ILE A 177   N  VAL A 153           
SHEET    6 AA1 6 PHE A 195  ARG A 197  1  O  SER A 196   N  GLN A 176           
SHEET    1 AA2 2 HIS A  58  LYS A  60  0                                        
SHEET    2 AA2 2 CYS A  67  ILE A  70 -1  O  GLY A  68   N  ALA A  59           
SHEET    1 AA3 8 SER A 249  ILE A 256  0                                        
SHEET    2 AA3 8 TYR A 220  SER A 226  1  N  VAL A 221   O  ALA A 251           
SHEET    3 AA3 8 ALA A 282  ALA A 287  1  O  VAL A 284   N  SER A 222           
SHEET    4 AA3 8 PHE A 308  GLY A 312  1  O  LEU A 309   N  ILE A 285           
SHEET    5 AA3 8 ILE A 334  PRO A 338  1  O  ILE A 334   N  PHE A 308           
SHEET    6 AA3 8 TYR A 477  GLN A 483 -1  O  PHE A 480   N  THR A 335           
SHEET    7 AA3 8 GLY A 491  TRP A 498 -1  O  ARG A 493   N  GLN A 481           
SHEET    8 AA3 8 LEU A 502  LEU A 504 -1  O  GLN A 503   N  GLN A 497           
SHEET    1 AA4 2 PHE A 457  ASN A 458  0                                        
SHEET    2 AA4 2 PRO A 464  VAL A 465 -1  O  VAL A 465   N  PHE A 457           
SSBOND   1 CYS A   67    CYS A  109                          1555   1555  2.04  
SSBOND   2 CYS A  374    CYS A  390                          1555   1555  2.02  
SSBOND   3 CYS A  430    CYS A  437                          1555   1555  2.03  
LINK         ND2 ASN A  98                 C1  NAG A 601     1555   1555  1.46  
LINK         O   ILE A  89                CA    CA A 603     1555   1555  2.65  
LINK         O   ASP A  92                CA    CA A 603     1555   1555  2.58  
LINK         O   LEU A  95                CA    CA A 603     1555   1555  2.42  
LINK         O   LEU A  96                CA    CA A 603     1555   1555  2.86  
LINK         O   LEU A 186                CA    CA A 604     1555   1555  2.70  
LINK         OD1 ASP A 189                CA    CA A 604     1555   1555  2.76  
LINK         O   TYR A 192                CA    CA A 604     1555   1555  2.79  
LINK         O   PHE A 195                CA    CA A 604     1555   1555  2.76  
LINK         O   ASN A 470                CA    CA A 604     1555   1555  2.65  
LINK        CA    CA A 603                 O   HOH A 737     1555   1555  2.59  
LINK        CA    CA A 604                 O   HOH A 739     1555   1555  3.08  
CISPEP   1 GLY A  155    ALA A  156          0        -6.84                     
CRYST1  106.175  101.203   55.318  90.00 110.46  90.00 C 1 2 1       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      0.009418  0.000000  0.003514        0.00000                         
SCALE2      0.000000  0.009881  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019294        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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