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Database: PDB
Entry: 5W93
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HEADER    CELL ADHESION                           22-JUN-17   5W93              
TITLE     P130CAS COMPLEX WITH PAXILLIN LD1                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BREAST CANCER ANTI-ESTROGEN RESISTANCE PROTEIN 1;          
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: CCHD DOMAIN (UNP RESIDUES 738-874);                        
COMPND   5 SYNONYM: CRK-ASSOCIATED SUBSTRATE,P130CAS;                           
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PAXILLIN;                                                  
COMPND  10 CHAIN: D, E, F;                                                      
COMPND  11 FRAGMENT: UNP RESIDUES 1-20;                                         
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: BCAR1, CAS, CRKAS;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  11 ORGANISM_COMMON: MOUSE;                                              
SOURCE  12 ORGANISM_TAXID: 10090                                                
KEYWDS    P130CAS, BCAR1, PAXILLIN, FOCAL ADHESION, CELL ADHESION               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.J.MILLER,J.J.ZHENG                                                  
REVDAT   2   06-DEC-17 5W93    1       JRNL                                     
REVDAT   1   06-SEP-17 5W93    0                                                
JRNL        AUTH   C.ZHANG,D.J.MILLER,C.D.GUIBAO,D.M.DONATO,S.K.HANKS,J.J.ZHENG 
JRNL        TITL   STRUCTURAL AND FUNCTIONAL INSIGHTS INTO THE INTERACTION      
JRNL        TITL 2 BETWEEN THE CAS FAMILY SCAFFOLDING PROTEIN P130CAS AND THE   
JRNL        TITL 3 FOCAL ADHESION-ASSOCIATED PROTEIN PAXILLIN.                  
JRNL        REF    J. BIOL. CHEM.                V. 292 18281 2017              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   28860193                                                     
JRNL        DOI    10.1074/JBC.M117.807271                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.95                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 31396                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1589                            
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 29.9498 -  4.4452    1.00     2899   178  0.1994 0.2329        
REMARK   3     2  4.4452 -  3.5301    1.00     2797   150  0.1800 0.2210        
REMARK   3     3  3.5301 -  3.0844    1.00     2817   138  0.1956 0.2200        
REMARK   3     4  3.0844 -  2.8026    1.00     2799   173  0.2094 0.2569        
REMARK   3     5  2.8026 -  2.6019    1.00     2797   135  0.1959 0.2057        
REMARK   3     6  2.6019 -  2.4485    1.00     2797   132  0.1929 0.2482        
REMARK   3     7  2.4485 -  2.3260    1.00     2746   144  0.1911 0.2878        
REMARK   3     8  2.3260 -  2.2247    1.00     2753   148  0.1900 0.2443        
REMARK   3     9  2.2247 -  2.1391    0.99     2775   140  0.2008 0.2578        
REMARK   3    10  2.1391 -  2.0653    0.95     2619   150  0.2152 0.2569        
REMARK   3    11  2.0653 -  2.0008    0.73     2008   101  0.2365 0.3594        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.890           
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      :  0.007           3172                                  
REMARK   3   ANGLE     :  0.900           4319                                  
REMARK   3   CHIRALITY :  0.038            535                                  
REMARK   3   PLANARITY :  0.005            555                                  
REMARK   3   DIHEDRAL  : 13.721           1112                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 741 THROUGH 774 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.1098  -9.5640  52.2860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3358 T22:   0.2323                                     
REMARK   3      T33:   0.2972 T12:   0.0118                                     
REMARK   3      T13:  -0.0069 T23:  -0.0110                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6453 L22:   0.4301                                     
REMARK   3      L33:   0.6919 L12:   0.4199                                     
REMARK   3      L13:  -0.4183 L23:  -0.2688                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0410 S12:  -0.1753 S13:  -0.0010                       
REMARK   3      S21:   0.5209 S22:  -0.0574 S23:   0.2058                       
REMARK   3      S31:   0.2858 S32:  -0.1007 S33:  -0.0003                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 775 THROUGH 839 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   9.0123  -8.2878  41.1230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2130 T22:   0.1532                                     
REMARK   3      T33:   0.2352 T12:   0.0211                                     
REMARK   3      T13:  -0.0050 T23:   0.0080                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3713 L22:   0.3226                                     
REMARK   3      L33:   1.6641 L12:   0.2450                                     
REMARK   3      L13:  -0.1050 L23:   0.5987                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0252 S12:   0.0464 S13:   0.0956                       
REMARK   3      S21:   0.0237 S22:  -0.0519 S23:   0.0175                       
REMARK   3      S31:  -0.0125 S32:  -0.0764 S33:  -0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 840 THROUGH 873 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.6970 -13.4509  44.6793              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2783 T22:   0.2599                                     
REMARK   3      T33:   0.3347 T12:   0.0235                                     
REMARK   3      T13:  -0.0290 T23:  -0.0037                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7737 L22:   0.7669                                     
REMARK   3      L33:   0.9587 L12:  -0.0087                                     
REMARK   3      L13:   1.0411 L23:  -0.0888                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1019 S12:  -0.0563 S13:  -0.1420                       
REMARK   3      S21:   0.2569 S22:   0.3025 S23:  -0.3475                       
REMARK   3      S31:   0.4446 S32:   0.6164 S33:   0.0009                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 741 THROUGH 774 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  35.2371  -9.8482  47.2227              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2646 T22:   0.3529                                     
REMARK   3      T33:   0.3258 T12:  -0.0129                                     
REMARK   3      T13:  -0.0214 T23:  -0.1043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2628 L22:   0.7940                                     
REMARK   3      L33:   1.4678 L12:  -0.3314                                     
REMARK   3      L13:   0.3444 L23:   0.6813                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1239 S12:   0.2263 S13:  -0.0519                       
REMARK   3      S21:  -0.5969 S22:  -0.1454 S23:  -0.2329                       
REMARK   3      S31:   0.2934 S32:   0.2103 S33:  -0.0010                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 775 THROUGH 839 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  29.8032  -7.0351  57.5359              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2273 T22:   0.2851                                     
REMARK   3      T33:   0.3076 T12:   0.0258                                     
REMARK   3      T13:   0.0125 T23:  -0.0860                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7312 L22:   0.5102                                     
REMARK   3      L33:   2.5983 L12:  -0.5445                                     
REMARK   3      L13:   0.0428 L23:   0.3304                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0719 S12:  -0.0352 S13:   0.1495                       
REMARK   3      S21:  -0.0339 S22:   0.1037 S23:  -0.0647                       
REMARK   3      S31:  -0.1304 S32:  -0.1935 S33:  -0.0000                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 840 THROUGH 873 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  23.8867 -12.9459  53.7179              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2432 T22:   0.4043                                     
REMARK   3      T33:   0.3189 T12:  -0.0319                                     
REMARK   3      T13:  -0.0254 T23:  -0.0387                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7065 L22:   0.9073                                     
REMARK   3      L33:   0.9748 L12:  -0.1054                                     
REMARK   3      L13:   0.6976 L23:   0.4149                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0111 S12:  -0.0171 S13:  -0.0735                       
REMARK   3      S21:  -0.2290 S22:   0.1246 S23:   0.0676                       
REMARK   3      S31:   0.4096 S32:  -0.5028 S33:  -0.0001                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 744 THROUGH 778 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  14.3173 -21.0610   1.8558              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7507 T22:   1.2435                                     
REMARK   3      T33:   0.5141 T12:  -0.0493                                     
REMARK   3      T13:   0.0393 T23:  -0.1488                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9518 L22:   0.3951                                     
REMARK   3      L33:   1.9025 L12:  -0.3461                                     
REMARK   3      L13:   1.0100 L23:  -0.4597                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1511 S12:   1.1832 S13:   0.0587                       
REMARK   3      S21:  -0.2827 S22:  -0.0102 S23:  -0.3303                       
REMARK   3      S31:   0.5122 S32:   0.9937 S33:   0.0959                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 779 THROUGH 839 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  10.1474 -13.6911   8.2720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4110 T22:   0.8831                                     
REMARK   3      T33:   0.4377 T12:  -0.0721                                     
REMARK   3      T13:   0.0598 T23:   0.0350                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0719 L22:   0.5907                                     
REMARK   3      L33:   1.2555 L12:   0.7696                                     
REMARK   3      L13:  -0.0777 L23:   0.1895                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2089 S12:   1.0125 S13:   0.3846                       
REMARK   3      S21:  -0.1634 S22:   0.3318 S23:   0.0011                       
REMARK   3      S31:  -0.2236 S32:  -0.0914 S33:   0.0116                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 840 THROUGH 867 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   4.0177 -22.0446   8.3687              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5043 T22:   1.0530                                     
REMARK   3      T33:   0.3740 T12:  -0.2301                                     
REMARK   3      T13:  -0.0428 T23:  -0.1198                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2238 L22:   0.4917                                     
REMARK   3      L33:   1.4000 L12:  -0.1184                                     
REMARK   3      L13:  -0.4607 L23:  -0.1611                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0541 S12:   1.1790 S13:   0.0503                       
REMARK   3      S21:  -0.4468 S22:   0.1908 S23:   0.1250                       
REMARK   3      S31:   0.8266 S32:  -0.4175 S33:   0.1993                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 616 THROUGH 627 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   3.6671  -7.9344  32.6861              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3835 T22:   0.3163                                     
REMARK   3      T33:   0.4178 T12:   0.0602                                     
REMARK   3      T13:  -0.0764 T23:   0.0083                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0620 L22:   0.1405                                     
REMARK   3      L33:   0.1352 L12:  -0.0273                                     
REMARK   3      L13:   0.0575 L23:  -0.1296                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0640 S12:   0.0657 S13:   0.3675                       
REMARK   3      S21:  -0.5239 S22:  -0.1542 S23:   0.4687                       
REMARK   3      S31:  -0.5676 S32:  -0.0465 S33:  -0.0000                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 616 THROUGH 628 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  33.5327  -5.3761  67.1657              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5707 T22:   0.5295                                     
REMARK   3      T33:   0.4397 T12:   0.0068                                     
REMARK   3      T13:  -0.0254 T23:  -0.1076                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1994 L22:   0.1524                                     
REMARK   3      L33:   0.0577 L12:   0.1499                                     
REMARK   3      L13:  -0.0219 L23:   0.0320                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1388 S12:  -0.1062 S13:   0.0158                       
REMARK   3      S21:   0.5962 S22:  -0.0976 S23:  -0.3453                       
REMARK   3      S31:  -0.5031 S32:   0.1162 S33:   0.0000                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 618 THROUGH 627 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  14.6081 -11.0064  16.4945              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6750 T22:   0.6778                                     
REMARK   3      T33:   0.5273 T12:  -0.0901                                     
REMARK   3      T13:   0.0081 T23:  -0.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0076 L22:   0.0052                                     
REMARK   3      L33:   0.0201 L12:   0.0062                                     
REMARK   3      L13:  -0.0117 L23:  -0.0109                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1615 S12:   0.0892 S13:   0.5530                       
REMARK   3      S21:  -0.3028 S22:  -0.0301 S23:   0.3247                       
REMARK   3      S31:  -0.5437 S32:   0.0382 S33:   0.0000                       
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 5W93 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000228570.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-OCT-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL - LIQUID NITROGEN   
REMARK 200                                   COOLED                             
REMARK 200  OPTICS                         : SI 111                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31426                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 30.3000                            
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) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 77.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.37600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
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: 3T6G CHAIN B                                         
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: THE FINAL 5 UL CRYSTALLIZATION DROP      
REMARK 280  CONTAINED 0.5 MM PROTEIN AND 2 MM PEPTIDE. THE DROP AND 500 UL      
REMARK 280  RESERVOIR SOLUTION BOTH CONTAINED 20 MM HEPES, PH 7.5, AND 50 MM    
REMARK 280  KCL, BATCH MODE, TEMPERATURE 291K                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       42.14500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       18.87050            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       42.14500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       18.87050            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7450 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7660 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 820 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 7000 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH C 909  LIES ON A SPECIAL POSITION.                          
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   738                                                      
REMARK 465     GLY A   739                                                      
REMARK 465     LEU A   740                                                      
REMARK 465     ALA A   874                                                      
REMARK 465     GLY B   738                                                      
REMARK 465     GLY B   739                                                      
REMARK 465     LEU B   740                                                      
REMARK 465     ALA B   874                                                      
REMARK 465     GLY C   738                                                      
REMARK 465     GLY C   739                                                      
REMARK 465     LEU C   740                                                      
REMARK 465     GLY C   741                                                      
REMARK 465     PRO C   742                                                      
REMARK 465     SER C   743                                                      
REMARK 465     SER C   804                                                      
REMARK 465     ARG C   805                                                      
REMARK 465     GLN C   806                                                      
REMARK 465     ALA C   807                                                      
REMARK 465     LYS C   808                                                      
REMARK 465     ALA C   809                                                      
REMARK 465     ALA C   810                                                      
REMARK 465     ASP C   811                                                      
REMARK 465     LEU C   868                                                      
REMARK 465     GLY C   869                                                      
REMARK 465     GLN C   870                                                      
REMARK 465     LEU C   871                                                      
REMARK 465     ALA C   872                                                      
REMARK 465     ALA C   873                                                      
REMARK 465     ALA C   874                                                      
REMARK 465     SER D   628                                                      
REMARK 465     THR D   629                                                      
REMARK 465     THR D   630                                                      
REMARK 465     SER D   631                                                      
REMARK 465     HIS D   632                                                      
REMARK 465     ILE D   633                                                      
REMARK 465     SER D   634                                                      
REMARK 465     LYS D   635                                                      
REMARK 465     THR E   629                                                      
REMARK 465     THR E   630                                                      
REMARK 465     SER E   631                                                      
REMARK 465     HIS E   632                                                      
REMARK 465     ILE E   633                                                      
REMARK 465     SER E   634                                                      
REMARK 465     LYS E   635                                                      
REMARK 465     MET F   616                                                      
REMARK 465     ASP F   617                                                      
REMARK 465     SER F   628                                                      
REMARK 465     THR F   629                                                      
REMARK 465     THR F   630                                                      
REMARK 465     SER F   631                                                      
REMARK 465     HIS F   632                                                      
REMARK 465     ILE F   633                                                      
REMARK 465     SER F   634                                                      
REMARK 465     LYS F   635                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS B 808    CG   CD   CE   NZ                                   
REMARK 470     ARG C 745    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C 746    CG   CD   OE1  NE2                                  
REMARK 470     LEU C 747    CG   CD1  CD2                                       
REMARK 470     LEU C 748    CG   CD1  CD2                                       
REMARK 470     LEU C 749    CG   CD1  CD2                                       
REMARK 470     PHE C 750    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU C 753    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 754    CG   CD   OE1  NE2                                  
REMARK 470     GLU C 756    CG   CD   OE1  OE2                                  
REMARK 470     THR C 760    OG1  CG2                                            
REMARK 470     ASP C 767    CG   OD1  OD2                                       
REMARK 470     PHE C 788    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS C 795    CG   CD   CE   NZ                                   
REMARK 470     THR C 802    OG1  CG2                                            
REMARK 470     ARG C 813    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C 815    CG   CD   OE1  NE2                                  
REMARK 470     HIS C 818    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU C 826    CG   CD1  CD2                                       
REMARK 470     GLN C 862    CG   CD   OE1  NE2                                  
REMARK 470     ARG C 865    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 627    CG   CD   OE1  OE2                                  
REMARK 470     ASP E 620    CG   OD1  OD2                                       
REMARK 470     ASP F 618    CG   OD1  OD2                                       
REMARK 470     ASP F 620    CG   OD1  OD2                                       
REMARK 470     LEU F 623    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD2  ASP A   801     O    HOH A   901              2.06            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5W93 A  738   874  UNP    Q61140   BCAR1_MOUSE    738    874             
DBREF  5W93 B  738   874  UNP    Q61140   BCAR1_MOUSE    738    874             
DBREF  5W93 C  738   874  UNP    Q61140   BCAR1_MOUSE    738    874             
DBREF  5W93 D  616   635  UNP    Q8VI36   PAXI_MOUSE       1     20             
DBREF  5W93 E  616   635  UNP    Q8VI36   PAXI_MOUSE       1     20             
DBREF  5W93 F  616   635  UNP    Q8VI36   PAXI_MOUSE       1     20             
SEQADV 5W93 ALA A  755  UNP  Q61140    CYS   755 ENGINEERED MUTATION            
SEQADV 5W93 SER A  824  UNP  Q61140    CYS   824 ENGINEERED MUTATION            
SEQADV 5W93 ALA B  755  UNP  Q61140    CYS   755 ENGINEERED MUTATION            
SEQADV 5W93 SER B  824  UNP  Q61140    CYS   824 ENGINEERED MUTATION            
SEQADV 5W93 ALA C  755  UNP  Q61140    CYS   755 ENGINEERED MUTATION            
SEQADV 5W93 SER C  824  UNP  Q61140    CYS   824 ENGINEERED MUTATION            
SEQRES   1 A  137  GLY GLY LEU GLY PRO SER ASP ARG GLN LEU LEU LEU PHE          
SEQRES   2 A  137  TYR LEU GLU GLN ALA GLU ALA ASN LEU THR THR LEU THR          
SEQRES   3 A  137  ASP ALA VAL ASP ALA PHE PHE THR ALA VAL ALA THR ASN          
SEQRES   4 A  137  GLN PRO PRO LYS ILE PHE VAL ALA HIS SER LYS PHE VAL          
SEQRES   5 A  137  ILE LEU SER ALA HIS LYS LEU VAL PHE ILE GLY ASP THR          
SEQRES   6 A  137  LEU SER ARG GLN ALA LYS ALA ALA ASP VAL ARG SER GLN          
SEQRES   7 A  137  VAL THR HIS TYR SER ASN LEU LEU SER ASP LEU LEU ARG          
SEQRES   8 A  137  GLY ILE VAL ALA THR THR LYS ALA ALA ALA LEU GLN TYR          
SEQRES   9 A  137  PRO SER PRO SER ALA ALA GLN ASP MET VAL ASP ARG VAL          
SEQRES  10 A  137  LYS GLU LEU GLY HIS SER THR GLN GLN PHE ARG ARG VAL          
SEQRES  11 A  137  LEU GLY GLN LEU ALA ALA ALA                                  
SEQRES   1 B  137  GLY GLY LEU GLY PRO SER ASP ARG GLN LEU LEU LEU PHE          
SEQRES   2 B  137  TYR LEU GLU GLN ALA GLU ALA ASN LEU THR THR LEU THR          
SEQRES   3 B  137  ASP ALA VAL ASP ALA PHE PHE THR ALA VAL ALA THR ASN          
SEQRES   4 B  137  GLN PRO PRO LYS ILE PHE VAL ALA HIS SER LYS PHE VAL          
SEQRES   5 B  137  ILE LEU SER ALA HIS LYS LEU VAL PHE ILE GLY ASP THR          
SEQRES   6 B  137  LEU SER ARG GLN ALA LYS ALA ALA ASP VAL ARG SER GLN          
SEQRES   7 B  137  VAL THR HIS TYR SER ASN LEU LEU SER ASP LEU LEU ARG          
SEQRES   8 B  137  GLY ILE VAL ALA THR THR LYS ALA ALA ALA LEU GLN TYR          
SEQRES   9 B  137  PRO SER PRO SER ALA ALA GLN ASP MET VAL ASP ARG VAL          
SEQRES  10 B  137  LYS GLU LEU GLY HIS SER THR GLN GLN PHE ARG ARG VAL          
SEQRES  11 B  137  LEU GLY GLN LEU ALA ALA ALA                                  
SEQRES   1 C  137  GLY GLY LEU GLY PRO SER ASP ARG GLN LEU LEU LEU PHE          
SEQRES   2 C  137  TYR LEU GLU GLN ALA GLU ALA ASN LEU THR THR LEU THR          
SEQRES   3 C  137  ASP ALA VAL ASP ALA PHE PHE THR ALA VAL ALA THR ASN          
SEQRES   4 C  137  GLN PRO PRO LYS ILE PHE VAL ALA HIS SER LYS PHE VAL          
SEQRES   5 C  137  ILE LEU SER ALA HIS LYS LEU VAL PHE ILE GLY ASP THR          
SEQRES   6 C  137  LEU SER ARG GLN ALA LYS ALA ALA ASP VAL ARG SER GLN          
SEQRES   7 C  137  VAL THR HIS TYR SER ASN LEU LEU SER ASP LEU LEU ARG          
SEQRES   8 C  137  GLY ILE VAL ALA THR THR LYS ALA ALA ALA LEU GLN TYR          
SEQRES   9 C  137  PRO SER PRO SER ALA ALA GLN ASP MET VAL ASP ARG VAL          
SEQRES  10 C  137  LYS GLU LEU GLY HIS SER THR GLN GLN PHE ARG ARG VAL          
SEQRES  11 C  137  LEU GLY GLN LEU ALA ALA ALA                                  
SEQRES   1 D   20  MET ASP ASP LEU ASP ALA LEU LEU ALA ASP LEU GLU SER          
SEQRES   2 D   20  THR THR SER HIS ILE SER LYS                                  
SEQRES   1 E   20  MET ASP ASP LEU ASP ALA LEU LEU ALA ASP LEU GLU SER          
SEQRES   2 E   20  THR THR SER HIS ILE SER LYS                                  
SEQRES   1 F   20  MET ASP ASP LEU ASP ALA LEU LEU ALA ASP LEU GLU SER          
SEQRES   2 F   20  THR THR SER HIS ILE SER LYS                                  
FORMUL   7  HOH   *181(H2 O)                                                    
HELIX    1 AA1 GLY A  741  THR A  775  1                                  35    
HELIX    2 AA2 PRO A  778  ALA A  807  1                                  30    
HELIX    3 AA3 ALA A  809  GLN A  840  1                                  32    
HELIX    4 AA4 SER A  843  ALA A  873  1                                  31    
HELIX    5 AA5 PRO B  742  THR B  775  1                                  34    
HELIX    6 AA6 PRO B  778  ALA B  807  1                                  30    
HELIX    7 AA7 ALA B  809  GLN B  840  1                                  32    
HELIX    8 AA8 SER B  843  ALA B  873  1                                  31    
HELIX    9 AA9 ARG C  745  GLU C  756  1                                  12    
HELIX   10 AB1 ASN C  758  THR C  775  1                                  18    
HELIX   11 AB2 PRO C  778  LEU C  803  1                                  26    
HELIX   12 AB3 ARG C  813  GLN C  840  1                                  28    
HELIX   13 AB4 SER C  843  VAL C  867  1                                  25    
HELIX   14 AB5 ASP D  618  ASP D  625  1                                   8    
HELIX   15 AB6 ASP E  618  ALA E  624  1                                   7    
HELIX   16 AB7 ASP E  625  GLU E  627  5                                   3    
HELIX   17 AB8 LEU F  619  ALA F  624  1                                   6    
HELIX   18 AB9 ASP F  625  GLU F  627  5                                   3    
CISPEP   1 TYR A  841    PRO A  842          0        -4.83                     
CISPEP   2 TYR B  841    PRO B  842          0        -2.67                     
CISPEP   3 TYR C  841    PRO C  842          0        -2.63                     
CRYST1   84.290   37.741  152.502  90.00 100.94  90.00 C 1 2 1      12          
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      0.011864  0.000000  0.002292        0.00000                         
SCALE2      0.000000  0.026496  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006679        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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