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Database: PDB
Entry: 2BRQ
LinkDB: 2BRQ
Original site: 2BRQ 
HEADER    STRUCTURAL PROTEIN                      11-MAY-05   2BRQ              
TITLE     CRYSTAL STRUCTURE OF THE FILAMIN A REPEAT 21 COMPLEXED WITH           
TITLE    2 THE INTEGRIN BETA7 CYTOPLASMIC TAIL PEPTIDE                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FILAMIN A;                                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: ROD DOMAIN, RESIDUES 2236-2329;                            
COMPND   5 SYNONYM: ALPHA-FILAMIN, FILAMIN 1, ENDOTHELIAL ACTIN- BINDING        
COMPND   6  PROTEIN, ACTIN-BINDING PROTEIN 280, ABP-280, NONMUSCLE FILAMIN;     
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: INTEGRIN BETA-7 SUBUNIT;                                   
COMPND  10 CHAIN: C, D;                                                         
COMPND  11 FRAGMENT: RESIDUES 768-798                                           
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PGEX4T-3;                                 
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES;                                                      
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606                                                 
KEYWDS    STRUCTURAL PROTEIN, CYTOSKELETON/COMPLEX, ACTIN-BINDING,              
KEYWDS   2 CYTOSKELETON, IMMUNOGLOBULIN LIKE, INTEGRIN, CELL ADHESION           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.-R.KIEMA,J.YLANNE                                                   
REVDAT   5   29-FEB-12 2BRQ    1       REVDAT REMARK HET    HETNAM              
REVDAT   5 2                           HETSYN FORMUL LINK   SCALE1              
REVDAT   5 3                           SCALE3 HETATM CONECT MASTER              
REVDAT   4   13-JUL-11 2BRQ    1       VERSN                                    
REVDAT   3   24-FEB-09 2BRQ    1       VERSN                                    
REVDAT   2   04-DEC-07 2BRQ    1       DBREF  HET    HETNAM FORMUL              
REVDAT   2 2                   1       LINK   HETATM CONECT                     
REVDAT   1   07-FEB-06 2BRQ    0                                                
JRNL        AUTH   T.KIEMA,Y.LAD,P.JIANG,C.L.OXLEY,M.BALDASSARRE,K.L.WEGENER,   
JRNL        AUTH 2 I.D.CAMPBELL,J.YLANNE,D.A.CALDERWOOD                         
JRNL        TITL   THE MOLECULAR BASIS OF FILAMIN BINDING TO INTEGRINS AND      
JRNL        TITL 2 COMPETITION WITH TALIN.                                      
JRNL        REF    MOL.CELL                      V.  21   337 2006              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   16455489                                                     
JRNL        DOI    10.1016/J.MOLCEL.2006.01.011                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.68                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 12367                          
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) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1381                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 890                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2240                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 112                          
REMARK   3   BIN FREE R VALUE                    : 0.2710                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1564                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 50                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.43                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.78000                                              
REMARK   3    B22 (A**2) : 1.33000                                              
REMARK   3    B33 (A**2) : -1.65000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.65000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.228         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.196         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.136         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.227        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.925                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1652 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2238 ; 1.465 ; 1.998       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   209 ; 6.583 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    64 ;34.081 ;24.375       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   229 ;16.876 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;17.414 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   239 ; 0.108 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1288 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   595 ; 0.196 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1054 ; 0.302 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    79 ; 0.125 ; 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):    29 ; 0.174 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.154 ; 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):  1089 ; 0.769 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1696 ; 1.236 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   636 ; 2.025 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   542 ; 3.223 ; 4.500       
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 : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A   2236       A    2328      3                      
REMARK   3           1     B   2236       B    2328      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    372 ;  0.29 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    B    (A):    372 ;  0.29 ;  0.05           
REMARK   3   LOOSE POSITIONAL   1    A    (A):    306 ;  0.72 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    B    (A):    306 ;  0.72 ;  5.00           
REMARK   3   TIGHT THERMAL      1    A (A**2):    372 ;  1.36 ;  0.50           
REMARK   3   TIGHT THERMAL      1    B (A**2):    372 ;  1.36 ;  0.50           
REMARK   3   LOOSE THERMAL      1    A (A**2):    306 ;  1.97 ; 10.00           
REMARK   3   LOOSE THERMAL      1    B (A**2):    306 ;  1.97 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : C D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C    776       C     788      3                      
REMARK   3           1     D    776       D     788      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    C    (A):     52 ;  0.20 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    D    (A):     52 ;  0.20 ;  0.05           
REMARK   3   LOOSE POSITIONAL   2    C    (A):     48 ;  0.40 ;  5.00           
REMARK   3   LOOSE POSITIONAL   2    D    (A):     48 ;  0.40 ;  5.00           
REMARK   3   TIGHT THERMAL      2    C (A**2):     52 ;  1.53 ;  0.50           
REMARK   3   TIGHT THERMAL      2    D (A**2):     52 ;  1.53 ;  0.50           
REMARK   3   LOOSE THERMAL      2    C (A**2):     48 ;  1.92 ; 10.00           
REMARK   3   LOOSE THERMAL      2    D (A**2):     48 ;  1.92 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  2236        A  2329                          
REMARK   3    RESIDUE RANGE :   C   776        C   788                          
REMARK   3    RESIDUE RANGE :   A  3330        A  3330                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.9740  16.2999  26.9218              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1638 T22:  -0.2009                                     
REMARK   3      T33:  -0.1593 T12:   0.0642                                     
REMARK   3      T13:   0.0418 T23:  -0.0049                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2708 L22:   4.3399                                     
REMARK   3      L33:   5.5690 L12:   1.3323                                     
REMARK   3      L13:   1.5035 L23:   1.5463                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1169 S12:   0.0301 S13:  -0.1845                       
REMARK   3      S21:  -0.3916 S22:  -0.0439 S23:   0.0365                       
REMARK   3      S31:  -0.1575 S32:  -0.1203 S33:   0.1608                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  2236        B  2328                          
REMARK   3    RESIDUE RANGE :   D   776        D   788                          
REMARK   3    RESIDUE RANGE :   B  3329        B  3329                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.9277  17.6535  49.1184              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1613 T22:  -0.0083                                     
REMARK   3      T33:  -0.1593 T12:   0.0583                                     
REMARK   3      T13:   0.0349 T23:   0.0323                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1139 L22:   5.9181                                     
REMARK   3      L33:   7.4417 L12:  -2.2535                                     
REMARK   3      L13:   0.8623 L23:  -2.3516                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2123 S12:  -0.6395 S13:  -0.2705                       
REMARK   3      S21:   0.5601 S22:   0.1693 S23:   0.1267                       
REMARK   3      S31:   0.0561 S32:   0.4311 S33:   0.0430                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS. SOME OF THE SIDE CHAIN ATOMS OF RESIDUES A        
REMARK   3  2264 ARG, A 2280 LYS, A 2287 ASP, B 2240 LYS, B 2250 ARG, B         
REMARK   3  2262 TRP, B 2280 LYS, B 2287 ASP, B 2288 ARG, D 785 THR AND D       
REMARK   3  787 ASN HAVE A POORLY DEFINED DENSITY. THE SIDE CHAIN ATOMS OF      
REMARK   3  RESIDUES A 2289 LYS, B 2239 HIS, B 2264 ARG, B 2286 GLU, B          
REMARK   3  2289 LYS AND B 2314 GLU HAVE NO ELECTRON DENSITY BUT THEY WERE      
REMARK   3  MODELED. BREAK IN THE MAIN CHAIN ELECTRON DENSITY BETWEEN           
REMARK   3  RESIDUES B 2286 GLU - B 2287 ASP, B 2288 ARG - B 2289 LYS AND       
REMARK   3  D 786 ILE - D 787 ASN.                                              
REMARK   4                                                                      
REMARK   4 2BRQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-MAY-05.                  
REMARK 100 THE PDBE ID CODE IS EBI-23905.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-FEB-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.931                              
REMARK 200  MONOCHROMATOR                  : DIAMOND (111), GE(220)             
REMARK 200  OPTICS                         : TOROIDAL MIRROR                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (MAR165)                       
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13748                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.00                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.68                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 5.2                                
REMARK 200  R MERGE                    (I) : 0.07                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.60                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.1                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.05                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.00                               
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 ENTRY 1V05                                       
REMARK 200                                                                      
REMARK 200 REMARK: FILAMIN C REPEAT 24                                          
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.6                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.6                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.26 M SODIUM CITRATE, 0.1 M             
REMARK 280  CITRIC ACID PH 5.5                                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       30.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  1                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4680 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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  2233                                                      
REMARK 465     ALA A  2234                                                      
REMARK 465     MET A  2235                                                      
REMARK 465     GLY B  2233                                                      
REMARK 465     ALA B  2234                                                      
REMARK 465     MET B  2235                                                      
REMARK 465     LEU C   768                                                      
REMARK 465     ASN C   769                                                      
REMARK 465     TRP C   770                                                      
REMARK 465     LYS C   771                                                      
REMARK 465     GLN C   772                                                      
REMARK 465     ASP C   773                                                      
REMARK 465     SER C   774                                                      
REMARK 465     ASN C   775                                                      
REMARK 465     PHE C   790                                                      
REMARK 465     GLN C   791                                                      
REMARK 465     GLU C   792                                                      
REMARK 465     ALA C   793                                                      
REMARK 465     ASP C   794                                                      
REMARK 465     SER C   795                                                      
REMARK 465     PRO C   796                                                      
REMARK 465     THR C   797                                                      
REMARK 465     LEU C   798                                                      
REMARK 465     LEU D   768                                                      
REMARK 465     ASN D   769                                                      
REMARK 465     TRP D   770                                                      
REMARK 465     LYS D   771                                                      
REMARK 465     GLN D   772                                                      
REMARK 465     ASP D   773                                                      
REMARK 465     SER D   774                                                      
REMARK 465     ASN D   775                                                      
REMARK 465     PHE D   790                                                      
REMARK 465     GLN D   791                                                      
REMARK 465     GLU D   792                                                      
REMARK 465     ALA D   793                                                      
REMARK 465     ASP D   794                                                      
REMARK 465     SER D   795                                                      
REMARK 465     PRO D   796                                                      
REMARK 465     THR D   797                                                      
REMARK 465     LEU D   798                                                      
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     SER B2329    CA   C    O    CB   OG                              
REMARK 470     ARG C 789    CA   C    O    CB   CG   CD   NE   CZ   NH1  NH2    
REMARK 470     ARG D 789    CA   C    O    CB   CG   CD   NE   CZ   NH1  NH2    
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    ASP A2318       -3.13     75.70                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 GLUTATHIONE (GTT): GLUTATHIONES X1 AND X2 ARE COVALENTLY             
REMARK 600  ATTACHED TO A 2293 CYS AND B 2293 CYS, RESPECTIVELY,                
REMARK 600  FORMING A DISULFIDE BOND.                                           
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH A3330                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH B3329                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A3331                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A3332                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2BP3   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF FILAMIN A DOMAIN 17                            
REMARK 900  AND GPIB ALPHA CYTOPLASMIC DOMAIN COMPLEX                           
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE FIRST THREE RESIDUES GAM ORIGINATES FROM THE                     
REMARK 999 EXPRESSION PLASMID.                                                  
DBREF  2BRQ A 2236  2329  UNP    P21333   FLNA_HUMAN    2236   2329             
DBREF  2BRQ B 2236  2329  UNP    P21333   FLNA_HUMAN    2236   2329             
DBREF  2BRQ C  768   798  UNP    P26010   ITB7_HUMAN     768    798             
DBREF  2BRQ D  768   798  UNP    P26010   ITB7_HUMAN     768    798             
SEQADV 2BRQ GLY A 2233  UNP  P21333              EXPRESSION TAG                 
SEQADV 2BRQ ALA A 2234  UNP  P21333              EXPRESSION TAG                 
SEQADV 2BRQ MET A 2235  UNP  P21333              EXPRESSION TAG                 
SEQADV 2BRQ GLY B 2233  UNP  P21333              EXPRESSION TAG                 
SEQADV 2BRQ ALA B 2234  UNP  P21333              EXPRESSION TAG                 
SEQADV 2BRQ MET B 2235  UNP  P21333              EXPRESSION TAG                 
SEQRES   1 A   97  GLY ALA MET GLY GLY ALA HIS LYS VAL ARG ALA GLY GLY          
SEQRES   2 A   97  PRO GLY LEU GLU ARG ALA GLU ALA GLY VAL PRO ALA GLU          
SEQRES   3 A   97  PHE SER ILE TRP THR ARG GLU ALA GLY ALA GLY GLY LEU          
SEQRES   4 A   97  ALA ILE ALA VAL GLU GLY PRO SER LYS ALA GLU ILE SER          
SEQRES   5 A   97  PHE GLU ASP ARG LYS ASP GLY SER CYS GLY VAL ALA TYR          
SEQRES   6 A   97  VAL VAL GLN GLU PRO GLY ASP TYR GLU VAL SER VAL LYS          
SEQRES   7 A   97  PHE ASN GLU GLU HIS ILE PRO ASP SER PRO PHE VAL VAL          
SEQRES   8 A   97  PRO VAL ALA SER PRO SER                                      
SEQRES   1 B   97  GLY ALA MET GLY GLY ALA HIS LYS VAL ARG ALA GLY GLY          
SEQRES   2 B   97  PRO GLY LEU GLU ARG ALA GLU ALA GLY VAL PRO ALA GLU          
SEQRES   3 B   97  PHE SER ILE TRP THR ARG GLU ALA GLY ALA GLY GLY LEU          
SEQRES   4 B   97  ALA ILE ALA VAL GLU GLY PRO SER LYS ALA GLU ILE SER          
SEQRES   5 B   97  PHE GLU ASP ARG LYS ASP GLY SER CYS GLY VAL ALA TYR          
SEQRES   6 B   97  VAL VAL GLN GLU PRO GLY ASP TYR GLU VAL SER VAL LYS          
SEQRES   7 B   97  PHE ASN GLU GLU HIS ILE PRO ASP SER PRO PHE VAL VAL          
SEQRES   8 B   97  PRO VAL ALA SER PRO SER                                      
SEQRES   1 C   31  LEU ASN TRP LYS GLN ASP SER ASN PRO LEU TYR LYS SER          
SEQRES   2 C   31  ALA ILE THR THR THR ILE ASN PRO ARG PHE GLN GLU ALA          
SEQRES   3 C   31  ASP SER PRO THR LEU                                          
SEQRES   1 D   31  LEU ASN TRP LYS GLN ASP SER ASN PRO LEU TYR LYS SER          
SEQRES   2 D   31  ALA ILE THR THR THR ILE ASN PRO ARG PHE GLN GLU ALA          
SEQRES   3 D   31  ASP SER PRO THR LEU                                          
HET    GSH  A3330      20                                                       
HET    GSH  B3329      20                                                       
HET    GOL  A3331       6                                                       
HET    GOL  A3332       6                                                       
HETNAM     GSH GLUTATHIONE                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  GOL    2(C3 H8 O3)                                                  
FORMUL   6  GSH    2(C10 H17 N3 O6 S)                                           
FORMUL   7  HOH   *50(H2 O)                                                     
HELIX    1   1 GLY A 2237  VAL A 2241  5                                   5    
HELIX    2   2 GLY A 2245  GLU A 2249  5                                   5    
HELIX    3   3 GLY B 2237  VAL B 2241  5                                   5    
HELIX    4   4 GLY B 2245  GLU B 2249  5                                   5    
SHEET    1  AA 4 ARG A2242  GLY A2244  0                                        
SHEET    2  AA 4 ALA A2257  TRP A2262 -1  O  SER A2260   N  GLY A2244           
SHEET    3  AA 4 CYS A2293  VAL A2299 -1  O  CYS A2293   N  ILE A2261           
SHEET    4  AA 4 ALA A2281  GLU A2286 -1  O  GLU A2282   N  VAL A2298           
SHEET    1  AB 8 ALA A2251  GLU A2252  0                                        
SHEET    2  AB 8 PHE A2321  ALA A2326  1  O  PRO A2324   N  ALA A2251           
SHEET    3  AB 8 GLY A2303  PHE A2311 -1  O  GLY A2303   N  VAL A2325           
SHEET    4  AB 8 GLY A2269  GLY A2277 -1  O  ALA A2272   N  LYS A2310           
SHEET    5  AB 8 LEU C 777  ILE C 786 -1  O  TYR C 778   N  GLY A2277           
SHEET    6  AB 8 LEU D 777  ILE D 786 -1  O  LEU D 777   N  THR C 783           
SHEET    7  AB 8 GLY B2269  GLY B2277 -1  O  GLY B2269   N  ILE D 786           
SHEET    8  AB 8 GLY B2303  PHE B2311 -1  O  GLU B2306   N  GLU B2276           
SHEET    1  AC 4 ALA A2251  GLU A2252  0                                        
SHEET    2  AC 4 PHE A2321  ALA A2326  1  O  PRO A2324   N  ALA A2251           
SHEET    3  AC 4 GLY A2303  PHE A2311 -1  O  GLY A2303   N  VAL A2325           
SHEET    4  AC 4 GLU A2314  HIS A2315 -1  O  GLU A2314   N  PHE A2311           
SHEET    1  BA 4 ARG B2242  GLY B2244  0                                        
SHEET    2  BA 4 ALA B2257  TRP B2262 -1  O  SER B2260   N  GLY B2244           
SHEET    3  BA 4 CYS B2293  VAL B2299 -1  O  CYS B2293   N  ILE B2261           
SHEET    4  BA 4 ALA B2281  ASP B2287 -1  O  GLU B2282   N  VAL B2298           
LINK         SG2 GSH A3330                 SG  CYS A2293     1555   1555  2.03  
LINK         SG2 GSH B3329                 SG  CYS B2293     1555   1555  2.03  
CISPEP   1 SER A 2319    PRO A 2320          0         0.26                     
CISPEP   2 SER B 2319    PRO B 2320          0         1.72                     
SITE     1 AC1  8 THR A2263  PHE A2285  GLU A2286  GLY A2291                    
SITE     2 AC1  8 CYS A2293  THR C 784  ILE C 786  ASN C 787                    
SITE     1 AC2 10 THR B2263  PHE B2285  GLU B2286  ASP B2287                    
SITE     2 AC2 10 GLY B2291  CYS B2293  THR D 784  THR D 785                    
SITE     3 AC2 10 ILE D 786  ASN D 787                                          
SITE     1 AC3  4 GLY A2244  GLY A2245  GLU A2249  PHE A2321                    
SITE     1 AC4  6 HOH A2026  GLY A2303  ASP A2304  PRO A2324                    
SITE     2 AC4  6 VAL A2325  ASP B2304                                          
CRYST1   41.970   60.000   51.570  90.00 110.17  90.00 P 1 21 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      0.023827  0.000000  0.008752        0.00000                         
SCALE2      0.000000  0.016667  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020658        0.00000                         
MTRIX1   1 -0.876260  0.481300  0.022670       37.53052    1                    
MTRIX2   1  0.480190  0.868420  0.123560      -14.52401    1                    
MTRIX3   1  0.039780  0.119160 -0.992080       72.62393    1                    
MTRIX1   2 -0.893080  0.449220  0.024650       38.72989    1                    
MTRIX2   2  0.447720  0.882050  0.146740      -14.63607    1                    
MTRIX3   2  0.044180  0.142090 -0.988870       72.13455    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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