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Database: PDB
Entry: 3BIN
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HEADER    CELL ADHESION                           30-NOV-07   3BIN              
TITLE     STRUCTURE OF THE DAL-1 AND TSLC1 (372-383) COMPLEX                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BAND 4.1-LIKE PROTEIN 3;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: FERM DOMAIN;                                               
COMPND   5 SYNONYM: 4.1B, DIFFERENTIALLY EXPRESSED IN ADENOCARCINOMA OF THE LUNG
COMPND   6 PROTEIN 1, DAL-1;                                                    
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CELL ADHESION MOLECULE 1;                                  
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: PEPTIDE FROM CYTOPLASMIC DOMAIN, UNP RESIDUES 400-411;     
COMPND  12 SYNONYM: IMMUNOGLOBULIN SUPERFAMILY MEMBER 4, NECTIN-LIKE PROTEIN 2, 
COMPND  13 NECL-2, TUMOR SUPPRESSOR IN LUNG CANCER 1, TSLC-1, SYNAPTIC CELL     
COMPND  14 ADHESION MOLECULE, SPERMATOGENIC IMMUNOGLOBULIN SUPERFAMILY, SGIGSF; 
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: EPB41L3, DAL1, KIAA0987;                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-PRARE2;                          
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC-BSA4;                                
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 OTHER_DETAILS: PEPTIDE SYNTHETIC                                     
KEYWDS    FERM DOMAIN, DAL-1, TSLC1, ACTIN-BINDING, CYTOSKELETON,               
KEYWDS   2 PHOSPHOPROTEIN, STRUCTURAL PROTEIN, ANTI-ONCOGENE, APOPTOSIS, CELL   
KEYWDS   3 ADHESION, CELL CYCLE, DEVELOPMENTAL PROTEIN, DIFFERENTIATION,        
KEYWDS   4 GLYCOPROTEIN, IMMUNE RESPONSE, IMMUNOGLOBULIN DOMAIN, MEMBRANE,      
KEYWDS   5 SPERMATOGENESIS, TRANSMEMBRANE                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.D.BUSAM,C.H.ARROWSMITH,R.COLLINS,L.G.DAHLGREN,A.M.EDWARDS,S.FLODIN, 
AUTHOR   2 A.FLORES,S.GRASLUND,M.HAMMARSTROM,A.JOHANSSON,I.JOHANSSON,A.KALLAS,  
AUTHOR   3 T.KARLBERG,T.KOTENYOVA,L.LEHTIO,M.MOCHE,M.E.NILSSON,P.NORDLUND,      
AUTHOR   4 T.NYMAN,J.SAGEMARK,L.SVENSSON,A.G.THORSELL,L.TRESAUGUES,S.VAN DEN    
AUTHOR   5 BERG,J.WEIGELT,M.WELIN,H.BERGLUND,C.PERSSON,B.M.HALLBERG             
REVDAT   5   13-JUL-11 3BIN    1       VERSN                                    
REVDAT   4   16-FEB-11 3BIN    1       JRNL                                     
REVDAT   3   12-JAN-11 3BIN    1       JRNL                                     
REVDAT   2   24-FEB-09 3BIN    1       VERSN                                    
REVDAT   1   15-JAN-08 3BIN    0                                                
JRNL        AUTH   R.D.BUSAM,A.-G.THORSELL,A.FLORES,M.HAMMARSTROM,C.PERSSON,    
JRNL        AUTH 2 B.OBRINK,B.M.HALLBERG                                        
JRNL        TITL   STRUCTURAL BASIS OF TUMOR SUPPRESSOR IN LUNG CANCER 1        
JRNL        TITL 2 (TSLC1) BINDING TO DIFFERENTIALLY EXPRESSED IN               
JRNL        TITL 3 ADENOCARCINOMA OF THE LUNG (DAL-1/4.1B)                      
JRNL        REF    J.BIOL.CHEM.                  V. 286  4511 2011              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   21131357                                                     
JRNL        DOI    10.1074/JBC.M110.174011                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 23120                          
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) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1131                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1649                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2590                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 75                           
REMARK   3   BIN FREE R VALUE                    : 0.3100                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2364                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 144                                     
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) : 38.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.70000                                             
REMARK   3    B22 (A**2) : -0.70000                                             
REMARK   3    B33 (A**2) : 1.06000                                              
REMARK   3    B12 (A**2) : -0.35000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.199         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.185         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.138         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.911        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.935                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2497 ; 0.022 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1759 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3375 ; 1.814 ; 1.950       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4251 ; 0.998 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   299 ; 7.036 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   128 ;33.799 ;23.125       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   445 ;17.066 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;17.715 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   350 ; 0.108 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2794 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   554 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   487 ; 0.209 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1774 ; 0.207 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1141 ; 0.183 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1318 ; 0.093 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   131 ; 0.192 ; 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):    10 ; 0.174 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    48 ; 0.237 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    16 ; 0.224 ; 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):  1904 ; 1.007 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   593 ; 0.213 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2383 ; 1.252 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1212 ; 2.255 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   992 ; 3.070 ; 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 : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 10                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   108        A   156                          
REMARK   3    ORIGIN FOR THE GROUP (A):  62.7700  48.6540  -7.7390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2122 T22:  -0.1705                                     
REMARK   3      T33:  -0.2814 T12:   0.0479                                     
REMARK   3      T13:   0.0199 T23:   0.0034                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1504 L22:   4.3193                                     
REMARK   3      L33:   2.9907 L12:   2.4454                                     
REMARK   3      L13:   3.1640 L23:   1.7069                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1839 S12:   0.1432 S13:   0.2839                       
REMARK   3      S21:  -0.1656 S22:  -0.0154 S23:  -0.1350                       
REMARK   3      S31:  -0.1716 S32:   0.2538 S33:   0.1993                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   157        A   212                          
REMARK   3    ORIGIN FOR THE GROUP (A):  55.3110  50.0310  -2.6420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2067 T22:  -0.1614                                     
REMARK   3      T33:  -0.2266 T12:   0.0805                                     
REMARK   3      T13:   0.0073 T23:  -0.0246                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7714 L22:   2.5692                                     
REMARK   3      L33:   2.1302 L12:   1.2360                                     
REMARK   3      L13:   2.0053 L23:   0.7313                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0689 S12:  -0.5712 S13:   0.3151                       
REMARK   3      S21:   0.0877 S22:  -0.1022 S23:   0.1852                       
REMARK   3      S31:  -0.1573 S32:  -0.2356 S33:   0.1712                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   213        A   236                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.1480  36.9450   2.3950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0645 T22:   0.2437                                     
REMARK   3      T33:   0.0070 T12:  -0.0002                                     
REMARK   3      T13:   0.0993 T23:   0.1291                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2393 L22:   8.5675                                     
REMARK   3      L33:   2.2160 L12:   3.3641                                     
REMARK   3      L13:   2.9981 L23:   4.0056                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2691 S12:  -1.4547 S13:  -0.2520                       
REMARK   3      S21:   0.4688 S22:  -0.2223 S23:   0.6316                       
REMARK   3      S31:   0.1356 S32:  -0.3481 S33:  -0.0468                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   237        A   243                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.3260  20.0760  -6.6020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5708 T22:   0.0609                                     
REMARK   3      T33:   0.6162 T12:  -0.0054                                     
REMARK   3      T13:  -0.0010 T23:   0.1123                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2946 L22:   5.5112                                     
REMARK   3      L33:  18.3171 L12:  -1.1278                                     
REMARK   3      L13:   6.0290 L23:   0.5402                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0080 S12:  -0.4499 S13:  -1.8538                       
REMARK   3      S21:   0.4226 S22:   0.0612 S23:   0.7417                       
REMARK   3      S31:   4.0298 S32:  -0.1130 S33:  -0.0533                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   244        A   262                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.6290  26.6170   5.1950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4660 T22:   0.4451                                     
REMARK   3      T33:   0.3621 T12:  -0.0362                                     
REMARK   3      T13:  -0.1234 T23:   0.3585                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2435 L22:  32.4371                                     
REMARK   3      L33:  18.2863 L12:   0.1356                                     
REMARK   3      L13:  -4.2165 L23:  18.3898                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7723 S12:  -0.7452 S13:  -1.1024                       
REMARK   3      S21:   2.2095 S22:  -0.6511 S23:  -0.5291                       
REMARK   3      S31:   2.3784 S32:  -0.7279 S33:  -0.1212                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   263        A   283                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.0600  29.2630  -3.8900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0963 T22:   0.0764                                     
REMARK   3      T33:   0.2596 T12:  -0.0481                                     
REMARK   3      T13:   0.0609 T23:   0.1233                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9716 L22:   9.4596                                     
REMARK   3      L33:   9.3403 L12:  -0.7626                                     
REMARK   3      L13:   0.0805 L23:  -1.8433                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1423 S12:  -0.6913 S13:  -0.9962                       
REMARK   3      S21:   0.5204 S22:  -0.1871 S23:   1.0357                       
REMARK   3      S31:   0.8467 S32:  -0.2005 S33:   0.0448                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   284        A   321                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.2610  54.5150   7.0460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1217 T22:   0.4490                                     
REMARK   3      T33:   0.0681 T12:   0.0798                                     
REMARK   3      T13:   0.1591 T23:  -0.1882                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8995 L22:  10.9747                                     
REMARK   3      L33:   1.8348 L12:   2.0821                                     
REMARK   3      L13:   1.0194 L23:   4.4049                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4043 S12:  -0.5825 S13:  -0.0454                       
REMARK   3      S21:   0.6755 S22:  -0.1176 S23:   0.7939                       
REMARK   3      S31:   0.2590 S32:  -0.8979 S33:   0.5220                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   322        A   344                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.5810  65.1970   8.0730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0661 T22:   0.0916                                     
REMARK   3      T33:   0.0148 T12:   0.1552                                     
REMARK   3      T13:   0.0954 T23:  -0.1848                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.6363 L22:  12.5414                                     
REMARK   3      L33:   6.1828 L12:  -1.2438                                     
REMARK   3      L13:   0.6817 L23:  -0.4860                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4920 S12:  -0.4300 S13:   0.0714                       
REMARK   3      S21:   0.1474 S22:   0.6560 S23:   0.5768                       
REMARK   3      S31:   0.4542 S32:  -0.4339 S33:  -0.1640                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   345        A   369                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.7210  72.4620   9.6520              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0439 T22:  -0.0070                                     
REMARK   3      T33:   0.0540 T12:   0.0468                                     
REMARK   3      T13:   0.0652 T23:  -0.1196                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.6996 L22:   5.0205                                     
REMARK   3      L33:   0.8562 L12:  -7.1970                                     
REMARK   3      L13:   0.7802 L23:  -0.7005                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1992 S12:  -0.3001 S13:   1.1050                       
REMARK   3      S21:   0.2661 S22:   0.4614 S23:  -0.4606                       
REMARK   3      S31:  -0.1491 S32:   0.3051 S33:  -0.2622                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   370        A   390                          
REMARK   3    ORIGIN FOR THE GROUP (A):  50.2850  63.2090   0.0170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0627 T22:  -0.1054                                     
REMARK   3      T33:  -0.0373 T12:   0.1474                                     
REMARK   3      T13:   0.0567 T23:  -0.0482                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.5454 L22:  10.2385                                     
REMARK   3      L33:  27.0294 L12:   1.8891                                     
REMARK   3      L13:  12.7995 L23:   7.7048                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1318 S12:   0.4572 S13:   0.5908                       
REMARK   3      S21:  -0.7427 S22:  -0.0925 S23:  -0.0018                       
REMARK   3      S31:  -0.5720 S32:   0.7320 S33:   0.2244                       
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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3BIN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-DEC-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB045567.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-NOV-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.03992                            
REMARK 200  MONOCHROMATOR                  : SI-111                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23489                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
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     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 3.650                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.8900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.36                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.75                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.41700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.950                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% ETOH, 0.1M TRIS PH 8.5, VAPOR        
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       33.68000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       16.84000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       25.26000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        8.42000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       42.10000            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 890 ANGSTROM**2                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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     ASP A   325                                                      
REMARK 465     ARG A   326                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     ARG B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     LYS B     4                                                      
REMARK 465     ALA B    12                                                      
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    PRO A 242      -14.00    -49.67                                   
REMARK 500    ASP A 248        3.32   -151.90                                   
REMARK 500    ILE A 329      -87.32   -108.23                                   
REMARK 500    ARG A 344     -126.59     57.20                                   
REMARK 500    LEU A 389       61.56   -116.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2HE7   RELATED DB: PDB                                   
REMARK 900 FERM DOMAIN OF EPB41L3 (DAL-1)                                       
DBREF  3BIN A  109   390  UNP    Q9Y2J2   E41L3_HUMAN    109    390             
DBREF  3BIN B    1    12  UNP    Q9BY67   CADM1_HUMAN    400    411             
SEQADV 3BIN ALA A  108  UNP  Q9Y2J2              EXPRESSION TAG                 
SEQRES   1 A  283  ALA SER MET GLN CYS LYS VAL ILE LEU LEU ASP GLY SER          
SEQRES   2 A  283  GLU TYR THR CYS ASP VAL GLU LYS ARG SER ARG GLY GLN          
SEQRES   3 A  283  VAL LEU PHE ASP LYS VAL CYS GLU HIS LEU ASN LEU LEU          
SEQRES   4 A  283  GLU LYS ASP TYR PHE GLY LEU THR TYR ARG ASP ALA GLU          
SEQRES   5 A  283  ASN GLN LYS ASN TRP LEU ASP PRO ALA LYS GLU ILE LYS          
SEQRES   6 A  283  LYS GLN VAL ARG SER GLY ALA TRP HIS PHE SER PHE ASN          
SEQRES   7 A  283  VAL LYS PHE TYR PRO PRO ASP PRO ALA GLN LEU SER GLU          
SEQRES   8 A  283  ASP ILE THR ARG TYR TYR LEU CYS LEU GLN LEU ARG ASP          
SEQRES   9 A  283  ASP ILE VAL SER GLY ARG LEU PRO CYS SER PHE VAL THR          
SEQRES  10 A  283  LEU ALA LEU LEU GLY SER TYR THR VAL GLN SER GLU LEU          
SEQRES  11 A  283  GLY ASP TYR ASP PRO ASP GLU CYS GLY SER ASP TYR ILE          
SEQRES  12 A  283  SER GLU PHE ARG PHE ALA PRO ASN HIS THR LYS GLU LEU          
SEQRES  13 A  283  GLU ASP LYS VAL ILE GLU LEU HIS LYS SER HIS ARG GLY          
SEQRES  14 A  283  MET THR PRO ALA GLU ALA GLU MET HIS PHE LEU GLU ASN          
SEQRES  15 A  283  ALA LYS LYS LEU SER MET TYR GLY VAL ASP LEU HIS HIS          
SEQRES  16 A  283  ALA LYS ASP SER GLU GLY VAL GLU ILE MET LEU GLY VAL          
SEQRES  17 A  283  CYS ALA SER GLY LEU LEU ILE TYR ARG ASP ARG LEU ARG          
SEQRES  18 A  283  ILE ASN ARG PHE ALA TRP PRO LYS VAL LEU LYS ILE SER          
SEQRES  19 A  283  TYR LYS ARG ASN ASN PHE TYR ILE LYS ILE ARG PRO GLY          
SEQRES  20 A  283  GLU PHE GLU GLN PHE GLU SER THR ILE GLY PHE LYS LEU          
SEQRES  21 A  283  PRO ASN HIS ARG ALA ALA LYS ARG LEU TRP LYS VAL CYS          
SEQRES  22 A  283  VAL GLU HIS HIS THR PHE PHE ARG LEU LEU                      
SEQRES   1 B   12  ALA ARG HIS LYS GLY THR TYR PHE THR HIS GLU ALA              
FORMUL   3  HOH   *144(H2 O)                                                    
HELIX    1   1 ARG A  131  LEU A  143  1                                  13    
HELIX    2   2 GLU A  147  ASP A  149  5                                   3    
HELIX    3   3 GLU A  170  VAL A  175  1                                   6    
HELIX    4   4 ASP A  192  LEU A  196  5                                   5    
HELIX    5   5 GLU A  198  SER A  215  1                                  18    
HELIX    6   6 SER A  221  GLY A  238  1                                  18    
HELIX    7   7 THR A  260  HIS A  274  1                                  15    
HELIX    8   8 THR A  278  LYS A  292  1                                  15    
HELIX    9   9 ASN A  369  LEU A  389  1                                  21    
SHEET    1   A 5 GLU A 121  GLU A 127  0                                        
SHEET    2   A 5 SER A 109  ILE A 115 -1  N  MET A 110   O  VAL A 126           
SHEET    3   A 5 TRP A 180  VAL A 186  1  O  PHE A 182   N  LYS A 113           
SHEET    4   A 5 PHE A 151  ARG A 156 -1  N  THR A 154   O  SER A 183           
SHEET    5   A 5 LYS A 162  TRP A 164 -1  O  ASN A 163   N  TYR A 155           
SHEET    1   B 4 ASP A 299  LYS A 304  0                                        
SHEET    2   B 4 GLU A 310  VAL A 315 -1  O  LEU A 313   N  HIS A 301           
SHEET    3   B 4 GLY A 319  TYR A 323 -1  O  LEU A 321   N  GLY A 314           
SHEET    4   B 4 ASN A 330  ALA A 333 -1  O  PHE A 332   N  LEU A 320           
SHEET    1   C 4 SER A 361  LYS A 366  0                                        
SHEET    2   C 4 ASN A 346  ILE A 351 -1  N  ILE A 349   O  ILE A 363           
SHEET    3   C 4 VAL A 337  LYS A 343 -1  N  SER A 341   O  TYR A 348           
SHEET    4   C 4 THR B   6  PHE B   8 -1  O  TYR B   7   N  ILE A 340           
CRYST1  135.000  135.000   50.520  90.00  90.00 120.00 P 65          6          
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      0.007407  0.004277  0.000000        0.00000                         
SCALE2      0.000000  0.008553  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019794        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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