GenomeNet

Database: PDB
Entry: 5F28
LinkDB: 5F28
Original site: 5F28 
HEADER    TRANSCRIPTION, PROTEIN BINDING          01-DEC-15   5F28              
TITLE     CRYSTAL STRUCTURE OF FAT DOMAIN OF FOCAL ADHESION KINASE (FAK) BOUND  
TITLE    2 TO THE TRANSCRIPTION FACTOR MEF2C                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MEF2C;                                                     
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 1-95;                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: FOCAL ADHESION KINASE 1;                                   
COMPND   8 CHAIN: E, F, G;                                                      
COMPND   9 FRAGMENT: UNP RESIDUES 935-1083;                                     
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: C41 (DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PETSUMO;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  12 ORGANISM_COMMON: MOUSE;                                              
SOURCE  13 ORGANISM_TAXID: 10090;                                               
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: C41 (DE3);                                 
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PET28A-TEV                                
KEYWDS    TRANSCRIPTION FACTOR, KINASE, CARDIOVASCULAR DISEASE, TRANSCRIPTION,  
KEYWDS   2 PROTEIN BINDING                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.C.CARDOSO,A.L.B.AMBROSIO,A.DESSEN,K.G.FRANCHINI                     
REVDAT   4   01-JAN-20 5F28    1       REMARK                                   
REVDAT   3   17-APR-19 5F28    1       REMARK                                   
REVDAT   2   23-JAN-19 5F28    1       JRNL   REMARK                            
REVDAT   1   13-JUL-16 5F28    0                                                
JRNL        AUTH   A.C.CARDOSO,A.H.M.PEREIRA,A.L.B.AMBROSIO,S.R.CONSONNI,       
JRNL        AUTH 2 R.ROCHA DE OLIVEIRA,M.C.BAJGELMAN,S.M.G.DIAS,K.G.FRANCHINI   
JRNL        TITL   FAK FORMS A COMPLEX WITH MEF2 TO COUPLE BIOMECHANICAL        
JRNL        TITL 2 SIGNALING TO TRANSCRIPTION IN CARDIOMYOCYTES.                
JRNL        REF    STRUCTURE                     V.  24  1301 2016              
JRNL        REFN                   ISSN 1878-4186                               
JRNL        PMID   27427476                                                     
JRNL        DOI    10.1016/J.STR.2016.06.003                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (DEV_2196)                                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.22                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 37566                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1880                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 43.2260 -  6.8108    1.00     2747   145  0.1607 0.1471        
REMARK   3     2  6.8108 -  5.4092    1.00     2732   160  0.2096 0.2231        
REMARK   3     3  5.4092 -  4.7264    1.00     2753   141  0.1515 0.1832        
REMARK   3     4  4.7264 -  4.2947    1.00     2768   120  0.1563 0.2047        
REMARK   3     5  4.2947 -  3.9871    1.00     2742   148  0.1652 0.1857        
REMARK   3     6  3.9871 -  3.7522    1.00     2738   141  0.1900 0.2438        
REMARK   3     7  3.7522 -  3.5644    1.00     2721   174  0.2079 0.2641        
REMARK   3     8  3.5644 -  3.4093    1.00     2761   148  0.2388 0.2555        
REMARK   3     9  3.4093 -  3.2781    1.00     2751   143  0.2636 0.2715        
REMARK   3    10  3.2781 -  3.1650    1.00     2758   144  0.2793 0.3241        
REMARK   3    11  3.1650 -  3.0661    1.00     2754   129  0.2973 0.3126        
REMARK   3    12  3.0661 -  2.9784    1.00     2747   144  0.3238 0.3834        
REMARK   3    13  2.9784 -  2.9000    1.00     2714   143  0.3616 0.3762        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.420            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.040           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004           5429                                  
REMARK   3   ANGLE     :  0.593           7318                                  
REMARK   3   CHIRALITY :  0.038            873                                  
REMARK   3   PLANARITY :  0.004            919                                  
REMARK   3   DIHEDRAL  : 16.138           2095                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5F28 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-DEC-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000215886.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-APR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8729                             
REMARK 200  MONOCHROMATOR                  : SILICON 111 CRYSTAL                
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37566                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.220                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 13.70                              
REMARK 200  R MERGE                    (I) : 0.34400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.70                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.55900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
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: PDB ENTRIES 1K40 (FAT) AND 3KOV (MEF2)               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MAGNSEIUM ACETATE, 0.1M MES, PH     
REMARK 280  6.5, 12% PEG 8000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE       
REMARK 280  291K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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  0.000000 -1.000000  0.000000       69.60500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       69.60500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       45.17500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       69.60500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       69.60500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       45.17500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       69.60500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       69.60500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       45.17500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       69.60500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       69.60500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       45.17500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, F                               
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRADECAMERIC             
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 42370 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 65140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -317.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G                   
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     ILE A     6                                                      
REMARK 465     GLN A     7                                                      
REMARK 465     ILE A     8                                                      
REMARK 465     THR A     9                                                      
REMARK 465     ARG A    10                                                      
REMARK 465     ILE A    11                                                      
REMARK 465     MET A    12                                                      
REMARK 465     ASP A    13                                                      
REMARK 465     GLU A    14                                                      
REMARK 465     ARG A    15                                                      
REMARK 465     ASN A    16                                                      
REMARK 465     ARG A    17                                                      
REMARK 465     GLN A    18                                                      
REMARK 465     VAL A    19                                                      
REMARK 465     THR A    20                                                      
REMARK 465     LYS A    91                                                      
REMARK 465     GLU A    92                                                      
REMARK 465     ASN A    93                                                      
REMARK 465     LYS A    94                                                      
REMARK 465     GLY A    95                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     LYS B     4                                                      
REMARK 465     LYS B     5                                                      
REMARK 465     ILE B     6                                                      
REMARK 465     GLN B     7                                                      
REMARK 465     ILE B     8                                                      
REMARK 465     THR B     9                                                      
REMARK 465     ARG B    10                                                      
REMARK 465     ILE B    11                                                      
REMARK 465     MET B    12                                                      
REMARK 465     ASP B    13                                                      
REMARK 465     GLU B    14                                                      
REMARK 465     ARG B    15                                                      
REMARK 465     ASN B    16                                                      
REMARK 465     ARG B    17                                                      
REMARK 465     GLN B    18                                                      
REMARK 465     GLU B    92                                                      
REMARK 465     ASN B    93                                                      
REMARK 465     LYS B    94                                                      
REMARK 465     GLY B    95                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLY C     2                                                      
REMARK 465     ARG C     3                                                      
REMARK 465     LYS C     4                                                      
REMARK 465     LYS C     5                                                      
REMARK 465     ILE C     6                                                      
REMARK 465     GLN C     7                                                      
REMARK 465     ILE C     8                                                      
REMARK 465     THR C     9                                                      
REMARK 465     ARG C    10                                                      
REMARK 465     ILE C    11                                                      
REMARK 465     MET C    12                                                      
REMARK 465     ASP C    13                                                      
REMARK 465     GLU C    14                                                      
REMARK 465     ARG C    15                                                      
REMARK 465     ASN C    16                                                      
REMARK 465     ARG C    17                                                      
REMARK 465     GLN C    18                                                      
REMARK 465     VAL C    19                                                      
REMARK 465     GLU C    92                                                      
REMARK 465     ASN C    93                                                      
REMARK 465     LYS C    94                                                      
REMARK 465     GLY C    95                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLY D     2                                                      
REMARK 465     ARG D     3                                                      
REMARK 465     LYS D     4                                                      
REMARK 465     LYS D     5                                                      
REMARK 465     ILE D     6                                                      
REMARK 465     GLN D     7                                                      
REMARK 465     ILE D     8                                                      
REMARK 465     THR D     9                                                      
REMARK 465     ARG D    10                                                      
REMARK 465     ILE D    11                                                      
REMARK 465     MET D    12                                                      
REMARK 465     ASP D    13                                                      
REMARK 465     GLU D    14                                                      
REMARK 465     ARG D    15                                                      
REMARK 465     ASN D    16                                                      
REMARK 465     ARG D    17                                                      
REMARK 465     GLN D    18                                                      
REMARK 465     VAL D    19                                                      
REMARK 465     GLU D    92                                                      
REMARK 465     ASN D    93                                                      
REMARK 465     LYS D    94                                                      
REMARK 465     GLY D    95                                                      
REMARK 465     LEU E   904                                                      
REMARK 465     GLN E   905                                                      
REMARK 465     PRO E   906                                                      
REMARK 465     GLN E   907                                                      
REMARK 465     GLU E   908                                                      
REMARK 465     ILE E   909                                                      
REMARK 465     SER E   910                                                      
REMARK 465     PRO E   911                                                      
REMARK 465     PRO E   912                                                      
REMARK 465     PRO E   913                                                      
REMARK 465     THR E   914                                                      
REMARK 465     ALA E   915                                                      
REMARK 465     ASN E   916                                                      
REMARK 465     MET E  1045                                                      
REMARK 465     LEU E  1046                                                      
REMARK 465     GLY E  1047                                                      
REMARK 465     GLN E  1048                                                      
REMARK 465     THR E  1049                                                      
REMARK 465     ARG E  1050                                                      
REMARK 465     PRO E  1051                                                      
REMARK 465     HIS E  1052                                                      
REMARK 465     LEU F   904                                                      
REMARK 465     GLN F   905                                                      
REMARK 465     PRO F   906                                                      
REMARK 465     GLN F   907                                                      
REMARK 465     GLU F   908                                                      
REMARK 465     ILE F   909                                                      
REMARK 465     SER F   910                                                      
REMARK 465     PRO F   911                                                      
REMARK 465     PRO F   912                                                      
REMARK 465     PRO F   913                                                      
REMARK 465     THR F   914                                                      
REMARK 465     ALA F   915                                                      
REMARK 465     ASN F   916                                                      
REMARK 465     MET F  1045                                                      
REMARK 465     LEU F  1046                                                      
REMARK 465     GLY F  1047                                                      
REMARK 465     GLN F  1048                                                      
REMARK 465     THR F  1049                                                      
REMARK 465     ARG F  1050                                                      
REMARK 465     PRO F  1051                                                      
REMARK 465     HIS F  1052                                                      
REMARK 465     LEU G   904                                                      
REMARK 465     GLN G   905                                                      
REMARK 465     PRO G   906                                                      
REMARK 465     GLN G   907                                                      
REMARK 465     GLU G   908                                                      
REMARK 465     ILE G   909                                                      
REMARK 465     SER G   910                                                      
REMARK 465     PRO G   911                                                      
REMARK 465     PRO G   912                                                      
REMARK 465     PRO G   913                                                      
REMARK 465     THR G   914                                                      
REMARK 465     ALA G   915                                                      
REMARK 465     THR G  1049                                                      
REMARK 465     ARG G  1050                                                      
REMARK 465     PRO G  1051                                                      
REMARK 465     HIS G  1052                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A   74   CD                                                  
REMARK 480     GLN F 1040   CD                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH G  1106     O    HOH G  1108              0.42            
REMARK 500   O    HOH C   105     O    HOH C   107              0.54            
REMARK 500   O    TYR B    72     NH2  ARG F   962              1.99            
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   OG   SER E  1011     OE1  GLU E  1015     2655     2.14            
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    THR A  60      -69.67   -109.53                                   
REMARK 500    THR B  60     -102.97   -120.49                                   
REMARK 500    GLU B  74      145.11   -176.58                                   
REMARK 500    HIS B  76     -178.23   -176.70                                   
REMARK 500    ASN B  89       32.49    -97.04                                   
REMARK 500    LYS B  90       75.88   -156.77                                   
REMARK 500    THR C  60      -67.46   -137.92                                   
REMARK 500    THR D  60      -99.76   -129.73                                   
REMARK 500    ASP E 918      -70.65    -81.91                                   
REMARK 500    ARG E 919       -8.29     83.69                                   
REMARK 500    TYR E1007       62.46   -102.75                                   
REMARK 500    ALA F 945       65.96   -176.83                                   
REMARK 500    GLU F 948      -38.86     85.31                                   
REMARK 500    TYR F1007       53.68   -116.47                                   
REMARK 500    PRO G 944       52.94   -115.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5F28 A    1    95  UNP    Q8CFN5   MEF2C_MOUSE      1     95             
DBREF  5F28 B    1    95  UNP    Q8CFN5   MEF2C_MOUSE      1     95             
DBREF  5F28 C    1    95  UNP    Q8CFN5   MEF2C_MOUSE      1     95             
DBREF  5F28 D    1    95  UNP    Q8CFN5   MEF2C_MOUSE      1     95             
DBREF  5F28 E  904  1052  UNP    P34152   FAK1_MOUSE     935   1083             
DBREF  5F28 F  904  1052  UNP    P34152   FAK1_MOUSE     935   1083             
DBREF  5F28 G  904  1052  UNP    P34152   FAK1_MOUSE     935   1083             
SEQRES   1 A   95  MET GLY ARG LYS LYS ILE GLN ILE THR ARG ILE MET ASP          
SEQRES   2 A   95  GLU ARG ASN ARG GLN VAL THR PHE THR LYS ARG LYS PHE          
SEQRES   3 A   95  GLY LEU MET LYS LYS ALA TYR GLU LEU SER VAL LEU CYS          
SEQRES   4 A   95  ASP CYS GLU ILE ALA LEU ILE ILE PHE ASN SER THR ASN          
SEQRES   5 A   95  LYS LEU PHE GLN TYR ALA SER THR ASP MET ASP LYS VAL          
SEQRES   6 A   95  LEU LEU LYS TYR THR GLU TYR ASN GLU PRO HIS GLU SER          
SEQRES   7 A   95  ARG THR ASN SER ASP ILE VAL GLU ALA LEU ASN LYS LYS          
SEQRES   8 A   95  GLU ASN LYS GLY                                              
SEQRES   1 B   95  MET GLY ARG LYS LYS ILE GLN ILE THR ARG ILE MET ASP          
SEQRES   2 B   95  GLU ARG ASN ARG GLN VAL THR PHE THR LYS ARG LYS PHE          
SEQRES   3 B   95  GLY LEU MET LYS LYS ALA TYR GLU LEU SER VAL LEU CYS          
SEQRES   4 B   95  ASP CYS GLU ILE ALA LEU ILE ILE PHE ASN SER THR ASN          
SEQRES   5 B   95  LYS LEU PHE GLN TYR ALA SER THR ASP MET ASP LYS VAL          
SEQRES   6 B   95  LEU LEU LYS TYR THR GLU TYR ASN GLU PRO HIS GLU SER          
SEQRES   7 B   95  ARG THR ASN SER ASP ILE VAL GLU ALA LEU ASN LYS LYS          
SEQRES   8 B   95  GLU ASN LYS GLY                                              
SEQRES   1 C   95  MET GLY ARG LYS LYS ILE GLN ILE THR ARG ILE MET ASP          
SEQRES   2 C   95  GLU ARG ASN ARG GLN VAL THR PHE THR LYS ARG LYS PHE          
SEQRES   3 C   95  GLY LEU MET LYS LYS ALA TYR GLU LEU SER VAL LEU CYS          
SEQRES   4 C   95  ASP CYS GLU ILE ALA LEU ILE ILE PHE ASN SER THR ASN          
SEQRES   5 C   95  LYS LEU PHE GLN TYR ALA SER THR ASP MET ASP LYS VAL          
SEQRES   6 C   95  LEU LEU LYS TYR THR GLU TYR ASN GLU PRO HIS GLU SER          
SEQRES   7 C   95  ARG THR ASN SER ASP ILE VAL GLU ALA LEU ASN LYS LYS          
SEQRES   8 C   95  GLU ASN LYS GLY                                              
SEQRES   1 D   95  MET GLY ARG LYS LYS ILE GLN ILE THR ARG ILE MET ASP          
SEQRES   2 D   95  GLU ARG ASN ARG GLN VAL THR PHE THR LYS ARG LYS PHE          
SEQRES   3 D   95  GLY LEU MET LYS LYS ALA TYR GLU LEU SER VAL LEU CYS          
SEQRES   4 D   95  ASP CYS GLU ILE ALA LEU ILE ILE PHE ASN SER THR ASN          
SEQRES   5 D   95  LYS LEU PHE GLN TYR ALA SER THR ASP MET ASP LYS VAL          
SEQRES   6 D   95  LEU LEU LYS TYR THR GLU TYR ASN GLU PRO HIS GLU SER          
SEQRES   7 D   95  ARG THR ASN SER ASP ILE VAL GLU ALA LEU ASN LYS LYS          
SEQRES   8 D   95  GLU ASN LYS GLY                                              
SEQRES   1 E  149  LEU GLN PRO GLN GLU ILE SER PRO PRO PRO THR ALA ASN          
SEQRES   2 E  149  LEU ASP ARG SER ASN ASP LYS VAL TYR GLU ASN VAL THR          
SEQRES   3 E  149  GLY LEU VAL LYS ALA VAL ILE GLU MET SER SER LYS ILE          
SEQRES   4 E  149  GLN PRO ALA PRO PRO GLU GLU TYR VAL PRO MET VAL LYS          
SEQRES   5 E  149  GLU VAL GLY LEU ALA LEU ARG THR LEU LEU ALA THR VAL          
SEQRES   6 E  149  ASP GLU THR ILE PRO ALA LEU PRO ALA SER THR HIS ARG          
SEQRES   7 E  149  GLU ILE GLU MET ALA GLN LYS LEU LEU ASN SER ASP LEU          
SEQRES   8 E  149  GLY GLU LEU ILE SER LYS MET LYS LEU ALA GLN GLN TYR          
SEQRES   9 E  149  VAL MET THR SER LEU GLN GLN GLU TYR LYS LYS GLN MET          
SEQRES  10 E  149  LEU THR ALA ALA HIS ALA LEU ALA VAL ASP ALA LYS ASN          
SEQRES  11 E  149  LEU LEU ASP VAL ILE ASP GLN ALA ARG LEU LYS MET LEU          
SEQRES  12 E  149  GLY GLN THR ARG PRO HIS                                      
SEQRES   1 F  149  LEU GLN PRO GLN GLU ILE SER PRO PRO PRO THR ALA ASN          
SEQRES   2 F  149  LEU ASP ARG SER ASN ASP LYS VAL TYR GLU ASN VAL THR          
SEQRES   3 F  149  GLY LEU VAL LYS ALA VAL ILE GLU MET SER SER LYS ILE          
SEQRES   4 F  149  GLN PRO ALA PRO PRO GLU GLU TYR VAL PRO MET VAL LYS          
SEQRES   5 F  149  GLU VAL GLY LEU ALA LEU ARG THR LEU LEU ALA THR VAL          
SEQRES   6 F  149  ASP GLU THR ILE PRO ALA LEU PRO ALA SER THR HIS ARG          
SEQRES   7 F  149  GLU ILE GLU MET ALA GLN LYS LEU LEU ASN SER ASP LEU          
SEQRES   8 F  149  GLY GLU LEU ILE SER LYS MET LYS LEU ALA GLN GLN TYR          
SEQRES   9 F  149  VAL MET THR SER LEU GLN GLN GLU TYR LYS LYS GLN MET          
SEQRES  10 F  149  LEU THR ALA ALA HIS ALA LEU ALA VAL ASP ALA LYS ASN          
SEQRES  11 F  149  LEU LEU ASP VAL ILE ASP GLN ALA ARG LEU LYS MET LEU          
SEQRES  12 F  149  GLY GLN THR ARG PRO HIS                                      
SEQRES   1 G  149  LEU GLN PRO GLN GLU ILE SER PRO PRO PRO THR ALA ASN          
SEQRES   2 G  149  LEU ASP ARG SER ASN ASP LYS VAL TYR GLU ASN VAL THR          
SEQRES   3 G  149  GLY LEU VAL LYS ALA VAL ILE GLU MET SER SER LYS ILE          
SEQRES   4 G  149  GLN PRO ALA PRO PRO GLU GLU TYR VAL PRO MET VAL LYS          
SEQRES   5 G  149  GLU VAL GLY LEU ALA LEU ARG THR LEU LEU ALA THR VAL          
SEQRES   6 G  149  ASP GLU THR ILE PRO ALA LEU PRO ALA SER THR HIS ARG          
SEQRES   7 G  149  GLU ILE GLU MET ALA GLN LYS LEU LEU ASN SER ASP LEU          
SEQRES   8 G  149  GLY GLU LEU ILE SER LYS MET LYS LEU ALA GLN GLN TYR          
SEQRES   9 G  149  VAL MET THR SER LEU GLN GLN GLU TYR LYS LYS GLN MET          
SEQRES  10 G  149  LEU THR ALA ALA HIS ALA LEU ALA VAL ASP ALA LYS ASN          
SEQRES  11 G  149  LEU LEU ASP VAL ILE ASP GLN ALA ARG LEU LYS MET LEU          
SEQRES  12 G  149  GLY GLN THR ARG PRO HIS                                      
FORMUL   8  HOH   *58(H2 O)                                                     
HELIX    1 AA1 PHE A   21  CYS A   39  1                                  19    
HELIX    2 AA2 ASP A   61  GLU A   71  1                                  11    
HELIX    3 AA3 THR A   80  ASN A   89  1                                  10    
HELIX    4 AA4 THR B   20  CYS B   39  1                                  20    
HELIX    5 AA5 ASP B   61  GLU B   71  1                                  11    
HELIX    6 AA6 ASN B   81  LEU B   88  1                                   8    
HELIX    7 AA7 PHE C   21  ASP C   40  1                                  20    
HELIX    8 AA8 ASP C   61  GLU C   71  1                                  11    
HELIX    9 AA9 THR C   80  ASN C   89  1                                  10    
HELIX   10 AB1 PHE D   21  CYS D   39  1                                  19    
HELIX   11 AB2 ASP D   61  GLU D   71  1                                  11    
HELIX   12 AB3 THR D   80  ASN D   89  1                                  10    
HELIX   13 AB4 ASP E  922  GLN E  943  1                                  22    
HELIX   14 AB5 PRO E  946  GLU E  948  5                                   3    
HELIX   15 AB6 GLU E  949  ILE E  972  1                                  24    
HELIX   16 AB7 PRO E  973  LEU E  975  5                                   3    
HELIX   17 AB8 PRO E  976  SER E  978  5                                   3    
HELIX   18 AB9 THR E  979  GLN E 1005  1                                  27    
HELIX   19 AC1 LEU E 1012  LEU E 1043  1                                  32    
HELIX   20 AC2 ASP F  922  GLN F  943  1                                  22    
HELIX   21 AC3 GLU F  949  ILE F  972  1                                  24    
HELIX   22 AC4 PRO F  973  LEU F  975  5                                   3    
HELIX   23 AC5 PRO F  976  SER F  978  5                                   3    
HELIX   24 AC6 THR F  979  TYR F 1007  1                                  29    
HELIX   25 AC7 LEU F 1012  LEU F 1043  1                                  32    
HELIX   26 AC8 ASP G  922  GLN G  943  1                                  22    
HELIX   27 AC9 PRO G  946  ILE G  972  1                                  27    
HELIX   28 AD1 PRO G  973  LEU G  975  5                                   3    
HELIX   29 AD2 PRO G  976  SER G  978  5                                   3    
HELIX   30 AD3 THR G  979  TYR G 1007  1                                  29    
HELIX   31 AD4 LEU G 1012  LEU G 1046  1                                  35    
SHEET    1 AA1 6 GLU A  77  ARG A  79  0                                        
SHEET    2 AA1 6 LEU B  54  ALA B  58  1  O  GLN B  56   N  GLU A  77           
SHEET    3 AA1 6 GLU B  42  PHE B  48 -1  N  LEU B  45   O  TYR B  57           
SHEET    4 AA1 6 GLU A  42  PHE A  48 -1  N  GLU A  42   O  PHE B  48           
SHEET    5 AA1 6 LEU A  54  ALA A  58 -1  O  PHE A  55   N  ILE A  47           
SHEET    6 AA1 6 GLU B  77  THR B  80  1  O  ARG B  79   N  GLN A  56           
SHEET    1 AA2 6 GLU C  77  ARG C  79  0                                        
SHEET    2 AA2 6 LEU D  54  ALA D  58  1  O  GLN D  56   N  ARG C  79           
SHEET    3 AA2 6 GLU D  42  PHE D  48 -1  N  ILE D  47   O  PHE D  55           
SHEET    4 AA2 6 GLU C  42  PHE C  48 -1  N  GLU C  42   O  PHE D  48           
SHEET    5 AA2 6 LEU C  54  ALA C  58 -1  O  TYR C  57   N  LEU C  45           
SHEET    6 AA2 6 GLU D  77  ARG D  79  1  O  ARG D  79   N  ALA C  58           
CISPEP   1 PRO F  944    ALA F  945          0       -18.61                     
CRYST1  139.210  139.210   90.350  90.00  90.00  90.00 P 42 21 2    32          
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      0.007183  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007183  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011068        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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