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Database: PDB
Entry: 2QT5
LinkDB: 2QT5
Original site: 2QT5 
HEADER    PEPTIDE BINDING PROTEIN                 01-AUG-07   2QT5              
TITLE     CRYSTAL STRUCTURE OF GRIP1 PDZ12 IN COMPLEX WITH THE FRAS1 PEPTIDE    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMATE RECEPTOR-INTERACTING PROTEIN 1;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: PDZ12;                                                     
COMPND   5 SYNONYM: GRIP1 PROTEIN, AMPA RECEPTOR-INTERACTING PROTEIN GRIP1;     
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: (ASN)(ASN)(LEU)(GLN)(ASP)(GLY)(THR)(GLU)(VAL);             
COMPND   9 CHAIN: X, Y;                                                         
COMPND  10 SYNONYM: FRAS1;                                                      
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 GENE: GRIP1;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 SYNTHETIC: YES;                                                      
SOURCE   8 OTHER_DETAILS: COMMERCIALLY SYNTHESIZED                              
KEYWDS    PDZ-PEPTIDE COMPLEX, PDZ TANDEM, ALTERNATIVE SPLICING, CELL JUNCTION, 
KEYWDS   2 CYTOPLASM, ENDOPLASMIC RETICULUM, MEMBRANE, POSTSYNAPTIC CELL        
KEYWDS   3 MEMBRANE, SYNAPSE, PROTEIN BINDING, PEPTIDE BINDING PROTEIN          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.LONG,Z.WEI,W.FENG,Y.ZHAO,M.ZHANG                                    
REVDAT   3   13-MAR-24 2QT5    1       REMARK SEQADV                            
REVDAT   2   24-FEB-09 2QT5    1       VERSN                                    
REVDAT   1   03-JUN-08 2QT5    0                                                
JRNL        AUTH   J.LONG,Z.WEI,W.FENG,C.YU,Y.X.ZHAO,M.ZHANG                    
JRNL        TITL   SUPRAMODULAR NATURE OF GRIP1 REVEALED BY THE STRUCTURE OF    
JRNL        TITL 2 ITS PDZ12 TANDEM IN COMPLEX WITH THE CARBOXYL TAIL OF FRAS1. 
JRNL        REF    J.MOL.BIOL.                   V. 375  1457 2008              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   18155042                                                     
JRNL        DOI    10.1016/J.JMB.2007.11.088                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.15                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 25976                          
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) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.247                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1344                            
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1747                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.46                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2350                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 102                          
REMARK   3   BIN FREE R VALUE                    : 0.2480                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2983                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 16                                      
REMARK   3   SOLVENT ATOMS            : 212                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.41000                                             
REMARK   3    B22 (A**2) : -0.47000                                             
REMARK   3    B33 (A**2) : 0.88000                                              
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): 0.246         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.209         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.136         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.423         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.936                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.906                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3059 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4124 ; 1.087 ; 1.987       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   401 ; 5.685 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   126 ;37.234 ;23.810       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   560 ;14.002 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    27 ;14.585 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   484 ; 0.066 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2257 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1186 ; 0.179 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2057 ; 0.292 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   254 ; 0.127 ; 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):    33 ; 0.240 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    23 ; 0.126 ; 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):  2011 ; 1.148 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3162 ; 1.992 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1129 ; 2.607 ; 4.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   957 ; 4.120 ; 6.000       
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 : BABINET MODEL WITH 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 2QT5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-AUG-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000044022.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-FEB-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25986                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 26.157                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 8.200                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : 0.06000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.35500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER, RESOLVE                                       
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MAGNESIUM ACETATE, 0.1M SODIUM      
REMARK 280  CACODYLATE PH 6.5, 20% PEG 8K, VAPOR DIFFUSION, HANGING DROP,       
REMARK 280  TEMPERATURE 289K                                                    
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       29.55000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       63.19000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.96250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       63.19000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.55000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.96250            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 980 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 10740 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, X                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 970 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 10530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, Y                                  
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    44                                                      
REMARK 465     PRO A    45                                                      
REMARK 465     GLY A    46                                                      
REMARK 465     MET A   241                                                      
REMARK 465     ASP A   242                                                      
REMARK 465     SER A   243                                                      
REMARK 465     GLY B    44                                                      
REMARK 465     PRO B    45                                                      
REMARK 465     GLY B    46                                                      
REMARK 465     VAL B   240                                                      
REMARK 465     MET B   241                                                      
REMARK 465     ASP B   242                                                      
REMARK 465     SER B   243                                                      
REMARK 465     ASN X  1001                                                      
REMARK 465     ASN X  1002                                                      
REMARK 465     LEU X  1003                                                      
REMARK 465     GLN X  1004                                                      
REMARK 465     ASP X  1005                                                      
REMARK 465     ASN Y  2001                                                      
REMARK 465     ASN Y  2002                                                      
REMARK 465     LEU Y  2003                                                      
REMARK 465     GLN Y  2004                                                      
REMARK 465     ASP Y  2005                                                      
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  60      -58.74    -27.96                                   
REMARK 500    GLU B 126      -29.55   -143.93                                   
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 EDO A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 244                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 2                   
DBREF  2QT5 A   48   243  UNP    P97879   GRIP1_RAT       48    243             
DBREF  2QT5 B   48   243  UNP    P97879   GRIP1_RAT       48    243             
DBREF  2QT5 X 1001  1009  PDB    2QT5     2QT5          1001   1009             
DBREF  2QT5 Y 2001  2009  PDB    2QT5     2QT5          2001   2009             
SEQADV 2QT5 GLY A   44  UNP  P97879              EXPRESSION TAG                 
SEQADV 2QT5 PRO A   45  UNP  P97879              EXPRESSION TAG                 
SEQADV 2QT5 GLY A   46  UNP  P97879              EXPRESSION TAG                 
SEQADV 2QT5 SER A   47  UNP  P97879              EXPRESSION TAG                 
SEQADV 2QT5 GLY B   44  UNP  P97879              EXPRESSION TAG                 
SEQADV 2QT5 PRO B   45  UNP  P97879              EXPRESSION TAG                 
SEQADV 2QT5 GLY B   46  UNP  P97879              EXPRESSION TAG                 
SEQADV 2QT5 SER B   47  UNP  P97879              EXPRESSION TAG                 
SEQRES   1 A  200  GLY PRO GLY SER PHE LYS GLY SER THR VAL VAL GLU LEU          
SEQRES   2 A  200  MET LYS LYS GLU GLY THR THR LEU GLY LEU THR VAL SER          
SEQRES   3 A  200  GLY GLY ILE ASP LYS ASP GLY LYS PRO ARG VAL SER ASN          
SEQRES   4 A  200  LEU ARG GLN GLY GLY ILE ALA ALA ARG SER ASP GLN LEU          
SEQRES   5 A  200  ASP VAL GLY ASP TYR ILE LYS ALA VAL ASN GLY ILE ASN          
SEQRES   6 A  200  LEU ALA LYS PHE ARG HIS ASP GLU ILE ILE SER LEU LEU          
SEQRES   7 A  200  LYS ASN VAL GLY GLU ARG VAL VAL LEU GLU VAL GLU TYR          
SEQRES   8 A  200  GLU LEU PRO PRO VAL SER ILE GLN GLY SER SER VAL MET          
SEQRES   9 A  200  PHE ARG THR VAL GLU VAL THR LEU HIS LYS GLU GLY ASN          
SEQRES  10 A  200  THR PHE GLY PHE VAL ILE ARG GLY GLY ALA HIS ASP ASP          
SEQRES  11 A  200  ARG ASN LYS SER ARG PRO VAL VAL ILE THR CYS VAL ARG          
SEQRES  12 A  200  PRO GLY GLY PRO ALA ASP ARG GLU GLY THR ILE LYS PRO          
SEQRES  13 A  200  GLY ASP ARG LEU LEU SER VAL ASP GLY ILE ARG LEU LEU          
SEQRES  14 A  200  GLY THR THR HIS ALA GLU ALA MET SER ILE LEU LYS GLN          
SEQRES  15 A  200  CYS GLY GLN GLU ALA THR LEU LEU ILE GLU TYR ASP VAL          
SEQRES  16 A  200  SER VAL MET ASP SER                                          
SEQRES   1 B  200  GLY PRO GLY SER PHE LYS GLY SER THR VAL VAL GLU LEU          
SEQRES   2 B  200  MET LYS LYS GLU GLY THR THR LEU GLY LEU THR VAL SER          
SEQRES   3 B  200  GLY GLY ILE ASP LYS ASP GLY LYS PRO ARG VAL SER ASN          
SEQRES   4 B  200  LEU ARG GLN GLY GLY ILE ALA ALA ARG SER ASP GLN LEU          
SEQRES   5 B  200  ASP VAL GLY ASP TYR ILE LYS ALA VAL ASN GLY ILE ASN          
SEQRES   6 B  200  LEU ALA LYS PHE ARG HIS ASP GLU ILE ILE SER LEU LEU          
SEQRES   7 B  200  LYS ASN VAL GLY GLU ARG VAL VAL LEU GLU VAL GLU TYR          
SEQRES   8 B  200  GLU LEU PRO PRO VAL SER ILE GLN GLY SER SER VAL MET          
SEQRES   9 B  200  PHE ARG THR VAL GLU VAL THR LEU HIS LYS GLU GLY ASN          
SEQRES  10 B  200  THR PHE GLY PHE VAL ILE ARG GLY GLY ALA HIS ASP ASP          
SEQRES  11 B  200  ARG ASN LYS SER ARG PRO VAL VAL ILE THR CYS VAL ARG          
SEQRES  12 B  200  PRO GLY GLY PRO ALA ASP ARG GLU GLY THR ILE LYS PRO          
SEQRES  13 B  200  GLY ASP ARG LEU LEU SER VAL ASP GLY ILE ARG LEU LEU          
SEQRES  14 B  200  GLY THR THR HIS ALA GLU ALA MET SER ILE LEU LYS GLN          
SEQRES  15 B  200  CYS GLY GLN GLU ALA THR LEU LEU ILE GLU TYR ASP VAL          
SEQRES  16 B  200  SER VAL MET ASP SER                                          
SEQRES   1 X    9  ASN ASN LEU GLN ASP GLY THR GLU VAL                          
SEQRES   1 Y    9  ASN ASN LEU GLN ASP GLY THR GLU VAL                          
HET    EDO  A   1       4                                                       
HET    ACY  A 244       4                                                       
HET    ACY  A   2       4                                                       
HET    EDO  B   2       4                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     ACY ACETIC ACID                                                      
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   5  EDO    2(C2 H6 O2)                                                  
FORMUL   6  ACY    2(C2 H4 O2)                                                  
FORMUL   9  HOH   *212(H2 O)                                                    
HELIX    1   1 GLY A   87  SER A   92  1                                   6    
HELIX    2   2 ARG A  113  ASN A  123  1                                  11    
HELIX    3   3 GLY A  189  GLY A  195  1                                   7    
HELIX    4   4 THR A  215  GLN A  225  1                                  11    
HELIX    5   5 GLY B   87  SER B   92  1                                   6    
HELIX    6   6 ARG B  113  VAL B  124  1                                  12    
HELIX    7   7 GLY B  189  GLY B  195  1                                   7    
HELIX    8   8 THR B  215  CYS B  226  1                                  12    
SHEET    1   A 4 LYS A  49  MET A  57  0                                        
SHEET    2   A 4 ARG A 127  GLU A 135 -1  O  VAL A 132   N  THR A  52           
SHEET    3   A 4 TYR A 100  VAL A 104 -1  N  TYR A 100   O  GLU A 133           
SHEET    4   A 4 ILE A 107  ASN A 108 -1  O  ILE A 107   N  VAL A 104           
SHEET    1   B 3 ARG A  79  LEU A  83  0                                        
SHEET    2   B 3 LEU A  66  SER A  69 -1  N  THR A  67   O  SER A  81           
SHEET    3   B 3 THR X1007  VAL X1009 -1  O  VAL X1009   N  LEU A  66           
SHEET    1   C 4 VAL A 146  HIS A 156  0                                        
SHEET    2   C 4 GLU A 229  SER A 239 -1  O  LEU A 232   N  VAL A 153           
SHEET    3   C 4 ARG A 202  VAL A 206 -1  N  ARG A 202   O  GLU A 235           
SHEET    4   C 4 ILE A 209  ARG A 210 -1  O  ILE A 209   N  VAL A 206           
SHEET    1   D 2 PHE A 164  GLY A 169  0                                        
SHEET    2   D 2 ARG A 178  VAL A 185 -1  O  VAL A 181   N  ARG A 167           
SHEET    1   E 4 LYS B  49  MET B  57  0                                        
SHEET    2   E 4 ARG B 127  GLU B 135 -1  O  LEU B 130   N  VAL B  54           
SHEET    3   E 4 TYR B 100  VAL B 104 -1  N  TYR B 100   O  GLU B 133           
SHEET    4   E 4 ILE B 107  ASN B 108 -1  O  ILE B 107   N  VAL B 104           
SHEET    1   F 3 ARG B  79  LEU B  83  0                                        
SHEET    2   F 3 LEU B  66  SER B  69 -1  N  THR B  67   O  ASN B  82           
SHEET    3   F 3 THR Y2007  VAL Y2009 -1  O  VAL Y2009   N  LEU B  66           
SHEET    1   G 4 MET B 147  HIS B 156  0                                        
SHEET    2   G 4 GLU B 229  VAL B 238 -1  O  LEU B 232   N  VAL B 153           
SHEET    3   G 4 ARG B 202  VAL B 206 -1  N  LEU B 204   O  LEU B 233           
SHEET    4   G 4 ILE B 209  ARG B 210 -1  O  ILE B 209   N  VAL B 206           
SHEET    1   H 2 PHE B 164  GLY B 168  0                                        
SHEET    2   H 2 VAL B 180  VAL B 185 -1  O  VAL B 181   N  ARG B 167           
SITE     1 AC1  6 ASP A  93  PHE A 162  PHE A 164  MET A 220                    
SITE     2 AC1  6 HOH A 257  HOH A 312                                          
SITE     1 AC2  6 ASP B  93  THR B 161  PHE B 162  PHE B 164                    
SITE     2 AC2  6 HOH B 283  HOH B 285                                          
SITE     1 AC3  2 LYS A  49  ARG A  84                                          
SITE     1 AC4  5 ARG A 174  ARG A 178  GLU B 152  GLU B 194                    
SITE     2 AC4  5 THR B 196                                                     
CRYST1   59.100   75.925  126.380  90.00  90.00  90.00 P 21 21 21    8          
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      0.016920  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013171  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007913        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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