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Database: PDB
Entry: 3T6G
LinkDB: 3T6G
Original site: 3T6G 
HEADER    SIGNALING PROTEIN, CELL ADHESION        28-JUL-11   3T6G              
TITLE     STRUCTURE OF THE COMPLEX BETWEEN NSP3 (SHEP1) AND P130CAS             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SH2 DOMAIN-CONTAINING PROTEIN 3C;                          
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 539-860;                                      
COMPND   5 SYNONYM: NOVEL SH2-CONTAINING PROTEIN 3;                             
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: BREAST CANCER ANTI-ESTROGEN RESISTANCE PROTEIN 1;          
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 FRAGMENT: UNP RESIDUES 645-870;                                      
COMPND  12 SYNONYM: CRK-ASSOCIATED SUBSTRATE, CAS SCAFFOLDING PROTEIN FAMILY    
COMPND  13 MEMBER 1, P130CAS;                                                   
COMPND  14 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: SH2D3C, NSP3, UNQ272/PRO309/PRO34088;                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: BCAR1, CAS, CASS1, CRKAS;                                      
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CDC25-HOMOLOGY DOMAIN, GTPASE EXCHANGE FACTOR, FOCAL-ADHESION         
KEYWDS   2 TARGETING DOMAIN, SIGNALING PROTEIN, CELL ADHESION                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.D.MACE,H.ROBINSON,S.J.RIEDL                                         
REVDAT   2   28-DEC-11 3T6G    1       JRNL                                     
REVDAT   1   23-NOV-11 3T6G    0                                                
JRNL        AUTH   P.D.MACE,Y.WALLEZ,M.K.DOBACZEWSKA,J.J.LEE,H.ROBINSON,        
JRNL        AUTH 2 E.B.PASQUALE,S.J.RIEDL                                       
JRNL        TITL   NSP-CAS PROTEIN STRUCTURES REVEAL A PROMISCUOUS INTERACTION  
JRNL        TITL 2 MODULE IN CELL SIGNALING.                                    
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  18  1381 2011              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   22081014                                                     
JRNL        DOI    10.1038/NSMB.2152                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.55                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 37296                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1871                            
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 29.5570 -  5.3765    0.99     3816   196  0.1835 0.2498        
REMARK   3     2  5.3765 -  4.2717    1.00     3782   191  0.1598 0.2149        
REMARK   3     3  4.2717 -  3.7329    0.99     3750   194  0.1779 0.2446        
REMARK   3     4  3.7329 -  3.3921    0.99     3709   197  0.2117 0.2571        
REMARK   3     5  3.3921 -  3.1493    0.97     3643   200  0.2290 0.3109        
REMARK   3     6  3.1493 -  2.9638    0.95     3558   188  0.2399 0.3675        
REMARK   3     7  2.9638 -  2.8155    0.93     3457   186  0.2323 0.3171        
REMARK   3     8  2.8155 -  2.6930    0.90     3395   172  0.2346 0.3103        
REMARK   3     9  2.6930 -  2.5894    0.86     3234   169  0.2649 0.3291        
REMARK   3    10  2.5894 -  2.5001    0.83     3081   178  0.2975 0.4133        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.34                                          
REMARK   3   B_SOL              : 81.97                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.930           
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) : -11.31280                                            
REMARK   3    B22 (A**2) : -11.31280                                            
REMARK   3    B33 (A**2) : 22.62550                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  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      :  0.008           6649                                  
REMARK   3   ANGLE     :  1.076           8996                                  
REMARK   3   CHIRALITY :  0.068           1070                                  
REMARK   3   PLANARITY :  0.005           1140                                  
REMARK   3   DIHEDRAL  : 16.104           2458                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 13                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (chain A and resid 543:732)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  65.1552  80.2116  17.1066              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1634 T22:   0.2837                                     
REMARK   3      T33:   0.2559 T12:   0.0090                                     
REMARK   3      T13:  -0.0686 T23:   0.1295                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2063 L22:   2.5442                                     
REMARK   3      L33:   2.7168 L12:   1.2681                                     
REMARK   3      L13:   0.6696 L23:   1.3201                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1078 S12:  -0.1157 S13:   0.1215                       
REMARK   3      S21:  -0.0059 S22:   0.0724 S23:  -0.1938                       
REMARK   3      S31:  -0.1548 S32:   0.0391 S33:  -0.1126                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (chain A and resid 733:769)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  54.2606  78.5243   6.9184              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4106 T22:   0.4937                                     
REMARK   3      T33:   0.1778 T12:   0.0313                                     
REMARK   3      T13:  -0.1180 T23:   0.0230                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6977 L22:   5.9707                                     
REMARK   3      L33:   0.4329 L12:  -0.3571                                     
REMARK   3      L13:   0.1338 L23:   1.5083                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1055 S12:   0.4592 S13:  -0.0581                       
REMARK   3      S21:  -1.4832 S22:  -0.3973 S23:   0.0541                       
REMARK   3      S31:  -0.5040 S32:   0.5770 S33:   0.3302                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (chain A and resid 770:855)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  61.3789  78.7053  18.7765              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2551 T22:   0.4045                                     
REMARK   3      T33:   0.3761 T12:  -0.0667                                     
REMARK   3      T13:  -0.0729 T23:   0.0705                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9973 L22:   2.5580                                     
REMARK   3      L33:   3.6632 L12:   0.8309                                     
REMARK   3      L13:   1.4361 L23:   0.4629                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0392 S12:  -0.2362 S13:  -0.1251                       
REMARK   3      S21:   0.0966 S22:   0.0070 S23:  -0.0617                       
REMARK   3      S31:   0.1162 S32:  -0.0473 S33:  -0.0723                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (chain C and resid 569:661)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  94.0795  57.4603 -15.0256              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8303 T22:   1.3451                                     
REMARK   3      T33:   0.9346 T12:  -0.2341                                     
REMARK   3      T13:   0.3505 T23:  -0.7669                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0759 L22:   2.4566                                     
REMARK   3      L33:   2.0671 L12:  -0.0333                                     
REMARK   3      L13:  -1.6008 L23:   0.4760                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3178 S12:   0.8798 S13:  -0.3149                       
REMARK   3      S21:  -0.8848 S22:   0.2913 S23:  -0.9386                       
REMARK   3      S31:   0.1291 S32:   0.7147 S33:  -0.3886                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (chain C and resid 662:755)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  82.2836  56.8679  -5.3411              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4187 T22:   0.7256                                     
REMARK   3      T33:   0.8789 T12:  -0.1496                                     
REMARK   3      T13:   0.1197 T23:  -0.5017                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7062 L22:   0.2694                                     
REMARK   3      L33:   3.0070 L12:  -0.2770                                     
REMARK   3      L13:   0.0782 L23:   1.0070                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0942 S12:   0.8435 S13:  -1.2671                       
REMARK   3      S21:  -0.1185 S22:   0.4657 S23:  -0.0619                       
REMARK   3      S31:   0.1826 S32:   0.3943 S33:  -0.2806                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (chain C and resid 757:785)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  96.8817  49.0852   8.2019              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5911 T22:   0.8555                                     
REMARK   3      T33:   1.5987 T12:   0.0406                                     
REMARK   3      T13:   0.1707 T23:  -0.4431                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1001 L22:   1.3299                                     
REMARK   3      L33:   0.6697 L12:  -0.5745                                     
REMARK   3      L13:   0.3591 L23:   0.6820                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2198 S12:   0.2426 S13:  -1.6091                       
REMARK   3      S21:   0.5051 S22:  -1.1069 S23:   1.2603                       
REMARK   3      S31:  -0.1064 S32:  -1.2968 S33:   0.9140                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (chain C and resid 786:855)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  92.9963  62.4737 -14.4779              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6596 T22:   1.5155                                     
REMARK   3      T33:   1.1429 T12:  -0.2139                                     
REMARK   3      T13:   0.3359 T23:  -0.7123                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1291 L22:   1.3564                                     
REMARK   3      L33:   2.0814 L12:  -0.1290                                     
REMARK   3      L13:   0.4742 L23:  -0.3083                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1849 S12:   1.1844 S13:  -0.4299                       
REMARK   3      S21:  -0.0554 S22:   0.7397 S23:  -0.8978                       
REMARK   3      S31:  -0.0848 S32:   0.5807 S33:  -0.5433                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (chain B and resid 738:755)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  39.7159  57.1243  10.5030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6902 T22:   0.4248                                     
REMARK   3      T33:   0.7961 T12:   0.1869                                     
REMARK   3      T13:  -0.0223 T23:   0.2360                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.6599 L22:   4.3746                                     
REMARK   3      L33:   9.0487 L12:   1.0748                                     
REMARK   3      L13:  -0.2910 L23:   1.2213                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3704 S12:  -0.0266 S13:  -0.6030                       
REMARK   3      S21:  -0.8047 S22:  -0.8270 S23:   1.4721                       
REMARK   3      S31:   1.7704 S32:   0.2416 S33:   0.2449                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (chain B and resid 756:857)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  32.0014  75.5141   5.3231              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2940 T22:   0.3900                                     
REMARK   3      T33:   0.5250 T12:   0.0084                                     
REMARK   3      T13:  -0.1913 T23:  -0.0543                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3483 L22:   1.2668                                     
REMARK   3      L33:   2.0297 L12:   0.1717                                     
REMARK   3      L13:  -0.0995 L23:  -0.3638                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1037 S12:  -0.0982 S13:  -0.2187                       
REMARK   3      S21:   0.0349 S22:  -0.0626 S23:   0.4693                       
REMARK   3      S31:  -0.0245 S32:  -0.0585 S33:   0.1246                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (chain B and resid 858:872)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  32.3969  55.2746   3.9824              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4478 T22:   0.4671                                     
REMARK   3      T33:   0.7302 T12:  -0.0229                                     
REMARK   3      T13:  -0.0804 T23:  -0.0567                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5700 L22:   9.9402                                     
REMARK   3      L33:   5.2965 L12:   1.1425                                     
REMARK   3      L13:   0.5694 L23:   3.1631                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1954 S12:  -0.0992 S13:  -0.3315                       
REMARK   3      S21:   0.0347 S22:  -1.1750 S23:   1.4609                       
REMARK   3      S31:   0.4964 S32:  -0.9752 S33:   0.7782                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: (chain D and resid 742:755)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 119.0207  46.2232   1.0954              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2078 T22:   1.5296                                     
REMARK   3      T33:   2.4384 T12:   0.0565                                     
REMARK   3      T13:   0.3434 T23:  -0.3273                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4650 L22:   3.6532                                     
REMARK   3      L33:   3.4027 L12:  -1.2915                                     
REMARK   3      L13:  -0.0986 L23:   0.8779                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3168 S12:   2.6159 S13:   0.1269                       
REMARK   3      S21:   0.1709 S22:  -2.4486 S23:   0.1639                       
REMARK   3      S31:   0.4928 S32:  -0.5556 S33:   2.3853                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: (chain D and resid 756:858)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 107.2781  47.2814  16.3702              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2281 T22:   0.6204                                     
REMARK   3      T33:   1.7720 T12:   0.1384                                     
REMARK   3      T13:   0.0673 T23:  -0.0862                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4341 L22:   1.4235                                     
REMARK   3      L33:   1.3128 L12:  -0.4567                                     
REMARK   3      L13:  -0.3070 L23:   0.7369                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0316 S12:   0.1798 S13:  -1.9343                       
REMARK   3      S21:  -0.2087 S22:   0.0955 S23:  -1.1480                       
REMARK   3      S31:   0.2727 S32:   0.9335 S33:  -0.1434                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: (chain D and resid 859:872)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 122.9737  38.0037   6.7509              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4072 T22:   1.1130                                     
REMARK   3      T33:   3.1218 T12:  -0.0184                                     
REMARK   3      T13:   0.1783 T23:  -0.4967                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1084 L22:   0.6277                                     
REMARK   3      L33:   1.2151 L12:   0.2831                                     
REMARK   3      L13:  -0.3919 L23:  -0.8814                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4349 S12:  -0.6328 S13:  -1.0803                       
REMARK   3      S21:  -0.1638 S22:  -0.5478 S23:  -1.3258                       
REMARK   3      S31:  -0.1040 S32:   1.1923 S33:   0.9014                       
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 3T6G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-AUG-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB067096.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-SEP-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.075                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39585                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350 AND SODIUM CITRATE (PH 7.8),     
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X,-Y,Z                                                 
REMARK 290       7555   -Y+1/2,X,Z+3/4                                          
REMARK 290       8555   Y,-X+1/2,Z+1/4                                          
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       85.94150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       85.94150            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.13500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       85.94150            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       19.56750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       85.94150            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       58.70250            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       85.94150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       85.94150            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       39.13500            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       85.94150            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       58.70250            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       85.94150            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       19.56750            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
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 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: 2240 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19120 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   381                                                      
REMARK 465     GLY A   382                                                      
REMARK 465     LYS A   383                                                      
REMARK 465     THR A   384                                                      
REMARK 465     PHE A   385                                                      
REMARK 465     ASP A   599                                                      
REMARK 465     SER A   600                                                      
REMARK 465     ALA A   601                                                      
REMARK 465     PRO A   602                                                      
REMARK 465     PRO A   603                                                      
REMARK 465     GLU A   604                                                      
REMARK 465     GLY A   605                                                      
REMARK 465     PRO A   606                                                      
REMARK 465     GLU A   607                                                      
REMARK 465     PRO A   608                                                      
REMARK 465     TRP A   609                                                      
REMARK 465     GLY A   610                                                      
REMARK 465     SER A   611                                                      
REMARK 465     THR A   612                                                      
REMARK 465     ARG A   699                                                      
REMARK 465     SER A   700                                                      
REMARK 465     SER A   701                                                      
REMARK 465     GLU A   702                                                      
REMARK 465     LEU A   703                                                      
REMARK 465     LEU A   704                                                      
REMARK 465     GLU A   705                                                      
REMARK 465     HIS A   706                                                      
REMARK 465     HIS A   707                                                      
REMARK 465     HIS A   708                                                      
REMARK 465     HIS A   709                                                      
REMARK 465     HIS A   710                                                      
REMARK 465     HIS A   711                                                      
REMARK 465     MET B   644                                                      
REMARK 465     SER B   645                                                      
REMARK 465     GLN B   646                                                      
REMARK 465     ASP B   647                                                      
REMARK 465     SER B   648                                                      
REMARK 465     PRO B   649                                                      
REMARK 465     ASP B   650                                                      
REMARK 465     GLY B   651                                                      
REMARK 465     GLN B   652                                                      
REMARK 465     TYR B   653                                                      
REMARK 465     GLU B   654                                                      
REMARK 465     ASN B   655                                                      
REMARK 465     SER B   656                                                      
REMARK 465     GLU B   657                                                      
REMARK 465     GLY B   658                                                      
REMARK 465     GLY B   659                                                      
REMARK 465     TRP B   660                                                      
REMARK 465     MET B   661                                                      
REMARK 465     GLU B   662                                                      
REMARK 465     ASP B   663                                                      
REMARK 465     TYR B   664                                                      
REMARK 465     ASP B   665                                                      
REMARK 465     TYR B   666                                                      
REMARK 465     VAL B   667                                                      
REMARK 465     HIS B   668                                                      
REMARK 465     LEU B   669                                                      
REMARK 465     GLN B   670                                                      
REMARK 465     GLY B   671                                                      
REMARK 465     LYS B   672                                                      
REMARK 465     GLU B   673                                                      
REMARK 465     GLU B   674                                                      
REMARK 465     PHE B   675                                                      
REMARK 465     GLU B   676                                                      
REMARK 465     LYS B   677                                                      
REMARK 465     THR B   678                                                      
REMARK 465     GLN B   679                                                      
REMARK 465     LYS B   680                                                      
REMARK 465     GLU B   681                                                      
REMARK 465     LEU B   682                                                      
REMARK 465     LEU B   683                                                      
REMARK 465     GLU B   684                                                      
REMARK 465     LYS B   685                                                      
REMARK 465     GLY B   686                                                      
REMARK 465     SER B   687                                                      
REMARK 465     ILE B   688                                                      
REMARK 465     THR B   689                                                      
REMARK 465     ARG B   690                                                      
REMARK 465     GLN B   691                                                      
REMARK 465     GLY B   692                                                      
REMARK 465     LYS B   693                                                      
REMARK 465     SER B   694                                                      
REMARK 465     GLN B   695                                                      
REMARK 465     LEU B   696                                                      
REMARK 465     GLU B   697                                                      
REMARK 465     LEU B   698                                                      
REMARK 465     GLN B   699                                                      
REMARK 465     GLN B   700                                                      
REMARK 465     LEU B   701                                                      
REMARK 465     LYS B   702                                                      
REMARK 465     GLN B   703                                                      
REMARK 465     PHE B   704                                                      
REMARK 465     GLU B   705                                                      
REMARK 465     ARG B   706                                                      
REMARK 465     LEU B   707                                                      
REMARK 465     GLU B   708                                                      
REMARK 465     GLN B   709                                                      
REMARK 465     GLU B   710                                                      
REMARK 465     VAL B   711                                                      
REMARK 465     SER B   712                                                      
REMARK 465     ARG B   713                                                      
REMARK 465     PRO B   714                                                      
REMARK 465     ILE B   715                                                      
REMARK 465     ASP B   716                                                      
REMARK 465     HIS B   717                                                      
REMARK 465     ASP B   718                                                      
REMARK 465     LEU B   719                                                      
REMARK 465     ALA B   720                                                      
REMARK 465     ASN B   721                                                      
REMARK 465     TRP B   722                                                      
REMARK 465     THR B   723                                                      
REMARK 465     PRO B   724                                                      
REMARK 465     ALA B   725                                                      
REMARK 465     GLN B   726                                                      
REMARK 465     PRO B   727                                                      
REMARK 465     LEU B   728                                                      
REMARK 465     ALA B   729                                                      
REMARK 465     PRO B   730                                                      
REMARK 465     GLY B   731                                                      
REMARK 465     ARG B   732                                                      
REMARK 465     THR B   733                                                      
REMARK 465     GLY B   734                                                      
REMARK 465     GLY B   735                                                      
REMARK 465     LEU B   736                                                      
REMARK 465     GLY B   737                                                      
REMARK 465     PRO B   738                                                      
REMARK 465     MET C   381                                                      
REMARK 465     GLY C   382                                                      
REMARK 465     LYS C   383                                                      
REMARK 465     THR C   384                                                      
REMARK 465     PHE C   385                                                      
REMARK 465     THR C   386                                                      
REMARK 465     VAL C   387                                                      
REMARK 465     PRO C   388                                                      
REMARK 465     ILE C   389                                                      
REMARK 465     VAL C   390                                                      
REMARK 465     GLU C   391                                                      
REMARK 465     VAL C   392                                                      
REMARK 465     THR C   393                                                      
REMARK 465     SER C   394                                                      
REMARK 465     SER C   395                                                      
REMARK 465     PHE C   396                                                      
REMARK 465     ASN C   397                                                      
REMARK 465     PRO C   398                                                      
REMARK 465     ALA C   399                                                      
REMARK 465     THR C   400                                                      
REMARK 465     PHE C   401                                                      
REMARK 465     GLN C   402                                                      
REMARK 465     SER C   403                                                      
REMARK 465     LEU C   404                                                      
REMARK 465     LEU C   405                                                      
REMARK 465     ILE C   406                                                      
REMARK 465     PRO C   407                                                      
REMARK 465     ARG C   408                                                      
REMARK 465     ASP C   409                                                      
REMARK 465     ASN C   410                                                      
REMARK 465     ARG C   411                                                      
REMARK 465     ASP C   599                                                      
REMARK 465     SER C   600                                                      
REMARK 465     ALA C   601                                                      
REMARK 465     PRO C   602                                                      
REMARK 465     PRO C   603                                                      
REMARK 465     GLU C   604                                                      
REMARK 465     GLY C   605                                                      
REMARK 465     PRO C   606                                                      
REMARK 465     GLU C   607                                                      
REMARK 465     PRO C   608                                                      
REMARK 465     TRP C   609                                                      
REMARK 465     GLY C   610                                                      
REMARK 465     SER C   611                                                      
REMARK 465     THR C   612                                                      
REMARK 465     ARG C   699                                                      
REMARK 465     SER C   700                                                      
REMARK 465     SER C   701                                                      
REMARK 465     GLU C   702                                                      
REMARK 465     LEU C   703                                                      
REMARK 465     LEU C   704                                                      
REMARK 465     GLU C   705                                                      
REMARK 465     HIS C   706                                                      
REMARK 465     HIS C   707                                                      
REMARK 465     HIS C   708                                                      
REMARK 465     HIS C   709                                                      
REMARK 465     HIS C   710                                                      
REMARK 465     HIS C   711                                                      
REMARK 465     MET D   644                                                      
REMARK 465     SER D   645                                                      
REMARK 465     GLN D   646                                                      
REMARK 465     ASP D   647                                                      
REMARK 465     SER D   648                                                      
REMARK 465     PRO D   649                                                      
REMARK 465     ASP D   650                                                      
REMARK 465     GLY D   651                                                      
REMARK 465     GLN D   652                                                      
REMARK 465     TYR D   653                                                      
REMARK 465     GLU D   654                                                      
REMARK 465     ASN D   655                                                      
REMARK 465     SER D   656                                                      
REMARK 465     GLU D   657                                                      
REMARK 465     GLY D   658                                                      
REMARK 465     GLY D   659                                                      
REMARK 465     TRP D   660                                                      
REMARK 465     MET D   661                                                      
REMARK 465     GLU D   662                                                      
REMARK 465     ASP D   663                                                      
REMARK 465     TYR D   664                                                      
REMARK 465     ASP D   665                                                      
REMARK 465     TYR D   666                                                      
REMARK 465     VAL D   667                                                      
REMARK 465     HIS D   668                                                      
REMARK 465     LEU D   669                                                      
REMARK 465     GLN D   670                                                      
REMARK 465     GLY D   671                                                      
REMARK 465     LYS D   672                                                      
REMARK 465     GLU D   673                                                      
REMARK 465     GLU D   674                                                      
REMARK 465     PHE D   675                                                      
REMARK 465     GLU D   676                                                      
REMARK 465     LYS D   677                                                      
REMARK 465     THR D   678                                                      
REMARK 465     GLN D   679                                                      
REMARK 465     LYS D   680                                                      
REMARK 465     GLU D   681                                                      
REMARK 465     LEU D   682                                                      
REMARK 465     LEU D   683                                                      
REMARK 465     GLU D   684                                                      
REMARK 465     LYS D   685                                                      
REMARK 465     GLY D   686                                                      
REMARK 465     SER D   687                                                      
REMARK 465     ILE D   688                                                      
REMARK 465     THR D   689                                                      
REMARK 465     ARG D   690                                                      
REMARK 465     GLN D   691                                                      
REMARK 465     GLY D   692                                                      
REMARK 465     LYS D   693                                                      
REMARK 465     SER D   694                                                      
REMARK 465     GLN D   695                                                      
REMARK 465     LEU D   696                                                      
REMARK 465     GLU D   697                                                      
REMARK 465     LEU D   698                                                      
REMARK 465     GLN D   699                                                      
REMARK 465     GLN D   700                                                      
REMARK 465     LEU D   701                                                      
REMARK 465     LYS D   702                                                      
REMARK 465     GLN D   703                                                      
REMARK 465     PHE D   704                                                      
REMARK 465     GLU D   705                                                      
REMARK 465     ARG D   706                                                      
REMARK 465     LEU D   707                                                      
REMARK 465     GLU D   708                                                      
REMARK 465     GLN D   709                                                      
REMARK 465     GLU D   710                                                      
REMARK 465     VAL D   711                                                      
REMARK 465     SER D   712                                                      
REMARK 465     ARG D   713                                                      
REMARK 465     PRO D   714                                                      
REMARK 465     ILE D   715                                                      
REMARK 465     ASP D   716                                                      
REMARK 465     HIS D   717                                                      
REMARK 465     ASP D   718                                                      
REMARK 465     LEU D   719                                                      
REMARK 465     ALA D   720                                                      
REMARK 465     ASN D   721                                                      
REMARK 465     TRP D   722                                                      
REMARK 465     THR D   723                                                      
REMARK 465     PRO D   724                                                      
REMARK 465     ALA D   725                                                      
REMARK 465     GLN D   726                                                      
REMARK 465     PRO D   727                                                      
REMARK 465     LEU D   728                                                      
REMARK 465     ALA D   729                                                      
REMARK 465     PRO D   730                                                      
REMARK 465     GLY D   731                                                      
REMARK 465     ARG D   732                                                      
REMARK 465     THR D   733                                                      
REMARK 465     GLY D   734                                                      
REMARK 465     GLY D   735                                                      
REMARK 465     LEU D   736                                                      
REMARK 465     GLY D   737                                                      
REMARK 465     PRO D   738                                                      
REMARK 465     SER D   739                                                      
REMARK 465     ASP D   740                                                      
REMARK 465     ARG D   741                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLN A  513   CD                                                  
REMARK 480     GLN C  513   CD                                                  
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    VAL A 387      -83.82    -40.18                                   
REMARK 500    ASP A 409       72.20   -110.73                                   
REMARK 500    LYS A 564      -59.67   -121.69                                   
REMARK 500    THR A 585      -26.69   -142.05                                   
REMARK 500    PHE A 586       99.81   -160.01                                   
REMARK 500    LEU A 596       -9.45    -55.91                                   
REMARK 500    PRO A 651      -56.92    -26.57                                   
REMARK 500    GLN A 670      -75.86     79.88                                   
REMARK 500    GLN B 802      -81.02    -62.23                                   
REMARK 500    ALA B 803      125.52     -5.44                                   
REMARK 500    LEU B 867      -70.93    -64.70                                   
REMARK 500    ALA B 868      -19.07    -41.34                                   
REMARK 500    MET C 489      -75.00    -47.13                                   
REMARK 500    THR C 498       -7.04   -144.84                                   
REMARK 500    THR C 521      -71.20    -28.33                                   
REMARK 500    LYS C 564      -66.10   -121.78                                   
REMARK 500    PRO C 580      106.53    -58.40                                   
REMARK 500    GLN C 670      -61.01     98.26                                   
REMARK 500    SER C 674      175.70    -58.40                                   
REMARK 500    GLU C 681      -70.90    -44.63                                   
REMARK 500    ALA C 697       32.38    -74.11                                   
REMARK 500    LEU D 745       -6.33    -54.57                                   
REMARK 500    LEU D 787      -79.11    -54.92                                   
REMARK 500    TYR D 815      -70.64    -53.13                                   
REMARK 500    SER D 816      -52.25    -29.53                                   
REMARK 500    GLN D 859       13.69    -67.47                                   
REMARK 500    ARG D 862      -77.97    -78.73                                   
REMARK 500    ALA D 868      -78.69    -58.83                                   
REMARK 500    LEU D 871       90.57    -61.77                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3T6A   RELATED DB: PDB                                   
DBREF  3T6G A  382   703  UNP    Q8N5H7   SH2D3_HUMAN    539    860             
DBREF  3T6G B  645   870  UNP    P56945   BCAR1_HUMAN    645    870             
DBREF  3T6G C  382   703  UNP    Q8N5H7   SH2D3_HUMAN    539    860             
DBREF  3T6G D  645   870  UNP    P56945   BCAR1_HUMAN    645    870             
SEQADV 3T6G MET A  381  UNP  Q8N5H7              INITIATING METHIONINE          
SEQADV 3T6G SER A  497  UNP  Q8N5H7    CYS   654 ENGINEERED MUTATION            
SEQADV 3T6G SER A  598  UNP  Q8N5H7    CYS   755 ENGINEERED MUTATION            
SEQADV 3T6G LEU A  704  UNP  Q8N5H7              EXPRESSION TAG                 
SEQADV 3T6G GLU A  705  UNP  Q8N5H7              EXPRESSION TAG                 
SEQADV 3T6G HIS A  706  UNP  Q8N5H7              EXPRESSION TAG                 
SEQADV 3T6G HIS A  707  UNP  Q8N5H7              EXPRESSION TAG                 
SEQADV 3T6G HIS A  708  UNP  Q8N5H7              EXPRESSION TAG                 
SEQADV 3T6G HIS A  709  UNP  Q8N5H7              EXPRESSION TAG                 
SEQADV 3T6G HIS A  710  UNP  Q8N5H7              EXPRESSION TAG                 
SEQADV 3T6G HIS A  711  UNP  Q8N5H7              EXPRESSION TAG                 
SEQADV 3T6G MET B  644  UNP  P56945              INITIATING METHIONINE          
SEQADV 3T6G LEU B  871  UNP  P56945              EXPRESSION TAG                 
SEQADV 3T6G GLU B  872  UNP  P56945              EXPRESSION TAG                 
SEQADV 3T6G MET C  381  UNP  Q8N5H7              INITIATING METHIONINE          
SEQADV 3T6G SER C  497  UNP  Q8N5H7    CYS   654 ENGINEERED MUTATION            
SEQADV 3T6G SER C  598  UNP  Q8N5H7    CYS   755 ENGINEERED MUTATION            
SEQADV 3T6G LEU C  704  UNP  Q8N5H7              EXPRESSION TAG                 
SEQADV 3T6G GLU C  705  UNP  Q8N5H7              EXPRESSION TAG                 
SEQADV 3T6G HIS C  706  UNP  Q8N5H7              EXPRESSION TAG                 
SEQADV 3T6G HIS C  707  UNP  Q8N5H7              EXPRESSION TAG                 
SEQADV 3T6G HIS C  708  UNP  Q8N5H7              EXPRESSION TAG                 
SEQADV 3T6G HIS C  709  UNP  Q8N5H7              EXPRESSION TAG                 
SEQADV 3T6G HIS C  710  UNP  Q8N5H7              EXPRESSION TAG                 
SEQADV 3T6G HIS C  711  UNP  Q8N5H7              EXPRESSION TAG                 
SEQADV 3T6G MET D  644  UNP  P56945              INITIATING METHIONINE          
SEQADV 3T6G LEU D  871  UNP  P56945              EXPRESSION TAG                 
SEQADV 3T6G GLU D  872  UNP  P56945              EXPRESSION TAG                 
SEQRES   1 A  331  MET GLY LYS THR PHE THR VAL PRO ILE VAL GLU VAL THR          
SEQRES   2 A  331  SER SER PHE ASN PRO ALA THR PHE GLN SER LEU LEU ILE          
SEQRES   3 A  331  PRO ARG ASP ASN ARG PRO LEU GLU VAL GLY LEU LEU ARG          
SEQRES   4 A  331  LYS VAL LYS GLU LEU LEU ALA GLU VAL ASP ALA ARG THR          
SEQRES   5 A  331  LEU ALA ARG HIS VAL THR LYS VAL ASP CYS LEU VAL ALA          
SEQRES   6 A  331  ARG ILE LEU GLY VAL THR LYS GLU MET GLN THR LEU MET          
SEQRES   7 A  331  GLY VAL ARG TRP GLY MET GLU LEU LEU THR LEU PRO HIS          
SEQRES   8 A  331  GLY ARG GLN LEU ARG LEU ASP LEU LEU GLU ARG PHE HIS          
SEQRES   9 A  331  THR MET SER ILE MET LEU ALA VAL ASP ILE LEU GLY SER          
SEQRES  10 A  331  THR GLY SER ALA GLU GLU ARG ALA ALA LEU LEU HIS LYS          
SEQRES  11 A  331  THR ILE GLN LEU ALA ALA GLU LEU ARG GLY THR MET GLY          
SEQRES  12 A  331  ASN MET PHE SER PHE ALA ALA VAL MET GLY ALA LEU ASP          
SEQRES  13 A  331  MET ALA GLN ILE SER ARG LEU GLU GLN THR TRP VAL THR          
SEQRES  14 A  331  LEU ARG GLN ARG HIS THR GLU GLY ALA ILE LEU TYR GLU          
SEQRES  15 A  331  LYS LYS LEU LYS PRO PHE LEU LYS SER LEU ASN GLU GLY          
SEQRES  16 A  331  LYS GLU GLY PRO PRO LEU SER ASN THR THR PHE PRO HIS          
SEQRES  17 A  331  VAL LEU PRO LEU ILE THR LEU LEU GLU SER ASP SER ALA          
SEQRES  18 A  331  PRO PRO GLU GLY PRO GLU PRO TRP GLY SER THR GLU HIS          
SEQRES  19 A  331  GLY VAL GLU VAL VAL LEU ALA HIS LEU GLU ALA ALA ARG          
SEQRES  20 A  331  THR VAL ALA HIS HIS GLY GLY LEU TYR HIS THR ASN ALA          
SEQRES  21 A  331  GLU VAL LYS LEU GLN GLY PHE GLN ALA ARG PRO GLU LEU          
SEQRES  22 A  331  LEU GLU VAL PHE SER THR GLU PHE GLN MET ARG LEU LEU          
SEQRES  23 A  331  TRP GLY SER GLN GLY ALA SER SER SER GLN ALA ARG ARG          
SEQRES  24 A  331  TYR GLU LYS PHE ASP LYS VAL LEU THR ALA LEU SER HIS          
SEQRES  25 A  331  LYS LEU GLU PRO ALA VAL ARG SER SER GLU LEU LEU GLU          
SEQRES  26 A  331  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 B  229  MET SER GLN ASP SER PRO ASP GLY GLN TYR GLU ASN SER          
SEQRES   2 B  229  GLU GLY GLY TRP MET GLU ASP TYR ASP TYR VAL HIS LEU          
SEQRES   3 B  229  GLN GLY LYS GLU GLU PHE GLU LYS THR GLN LYS GLU LEU          
SEQRES   4 B  229  LEU GLU LYS GLY SER ILE THR ARG GLN GLY LYS SER GLN          
SEQRES   5 B  229  LEU GLU LEU GLN GLN LEU LYS GLN PHE GLU ARG LEU GLU          
SEQRES   6 B  229  GLN GLU VAL SER ARG PRO ILE ASP HIS ASP LEU ALA ASN          
SEQRES   7 B  229  TRP THR PRO ALA GLN PRO LEU ALA PRO GLY ARG THR GLY          
SEQRES   8 B  229  GLY LEU GLY PRO SER ASP ARG GLN LEU LEU LEU PHE TYR          
SEQRES   9 B  229  LEU GLU GLN CYS GLU ALA ASN LEU THR THR LEU THR ASN          
SEQRES  10 B  229  ALA VAL ASP ALA PHE PHE THR ALA VAL ALA THR ASN GLN          
SEQRES  11 B  229  PRO PRO LYS ILE PHE VAL ALA HIS SER LYS PHE VAL ILE          
SEQRES  12 B  229  LEU SER ALA HIS LYS LEU VAL PHE ILE GLY ASP THR LEU          
SEQRES  13 B  229  SER ARG GLN ALA LYS ALA ALA ASP VAL ARG SER GLN VAL          
SEQRES  14 B  229  THR HIS TYR SER ASN LEU LEU CYS ASP LEU LEU ARG GLY          
SEQRES  15 B  229  ILE VAL ALA THR THR LYS ALA ALA ALA LEU GLN TYR PRO          
SEQRES  16 B  229  SER PRO SER ALA ALA GLN ASP MET VAL GLU ARG VAL LYS          
SEQRES  17 B  229  GLU LEU GLY HIS SER THR GLN GLN PHE ARG ARG VAL LEU          
SEQRES  18 B  229  GLY GLN LEU ALA ALA ALA LEU GLU                              
SEQRES   1 C  331  MET GLY LYS THR PHE THR VAL PRO ILE VAL GLU VAL THR          
SEQRES   2 C  331  SER SER PHE ASN PRO ALA THR PHE GLN SER LEU LEU ILE          
SEQRES   3 C  331  PRO ARG ASP ASN ARG PRO LEU GLU VAL GLY LEU LEU ARG          
SEQRES   4 C  331  LYS VAL LYS GLU LEU LEU ALA GLU VAL ASP ALA ARG THR          
SEQRES   5 C  331  LEU ALA ARG HIS VAL THR LYS VAL ASP CYS LEU VAL ALA          
SEQRES   6 C  331  ARG ILE LEU GLY VAL THR LYS GLU MET GLN THR LEU MET          
SEQRES   7 C  331  GLY VAL ARG TRP GLY MET GLU LEU LEU THR LEU PRO HIS          
SEQRES   8 C  331  GLY ARG GLN LEU ARG LEU ASP LEU LEU GLU ARG PHE HIS          
SEQRES   9 C  331  THR MET SER ILE MET LEU ALA VAL ASP ILE LEU GLY SER          
SEQRES  10 C  331  THR GLY SER ALA GLU GLU ARG ALA ALA LEU LEU HIS LYS          
SEQRES  11 C  331  THR ILE GLN LEU ALA ALA GLU LEU ARG GLY THR MET GLY          
SEQRES  12 C  331  ASN MET PHE SER PHE ALA ALA VAL MET GLY ALA LEU ASP          
SEQRES  13 C  331  MET ALA GLN ILE SER ARG LEU GLU GLN THR TRP VAL THR          
SEQRES  14 C  331  LEU ARG GLN ARG HIS THR GLU GLY ALA ILE LEU TYR GLU          
SEQRES  15 C  331  LYS LYS LEU LYS PRO PHE LEU LYS SER LEU ASN GLU GLY          
SEQRES  16 C  331  LYS GLU GLY PRO PRO LEU SER ASN THR THR PHE PRO HIS          
SEQRES  17 C  331  VAL LEU PRO LEU ILE THR LEU LEU GLU SER ASP SER ALA          
SEQRES  18 C  331  PRO PRO GLU GLY PRO GLU PRO TRP GLY SER THR GLU HIS          
SEQRES  19 C  331  GLY VAL GLU VAL VAL LEU ALA HIS LEU GLU ALA ALA ARG          
SEQRES  20 C  331  THR VAL ALA HIS HIS GLY GLY LEU TYR HIS THR ASN ALA          
SEQRES  21 C  331  GLU VAL LYS LEU GLN GLY PHE GLN ALA ARG PRO GLU LEU          
SEQRES  22 C  331  LEU GLU VAL PHE SER THR GLU PHE GLN MET ARG LEU LEU          
SEQRES  23 C  331  TRP GLY SER GLN GLY ALA SER SER SER GLN ALA ARG ARG          
SEQRES  24 C  331  TYR GLU LYS PHE ASP LYS VAL LEU THR ALA LEU SER HIS          
SEQRES  25 C  331  LYS LEU GLU PRO ALA VAL ARG SER SER GLU LEU LEU GLU          
SEQRES  26 C  331  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 D  229  MET SER GLN ASP SER PRO ASP GLY GLN TYR GLU ASN SER          
SEQRES   2 D  229  GLU GLY GLY TRP MET GLU ASP TYR ASP TYR VAL HIS LEU          
SEQRES   3 D  229  GLN GLY LYS GLU GLU PHE GLU LYS THR GLN LYS GLU LEU          
SEQRES   4 D  229  LEU GLU LYS GLY SER ILE THR ARG GLN GLY LYS SER GLN          
SEQRES   5 D  229  LEU GLU LEU GLN GLN LEU LYS GLN PHE GLU ARG LEU GLU          
SEQRES   6 D  229  GLN GLU VAL SER ARG PRO ILE ASP HIS ASP LEU ALA ASN          
SEQRES   7 D  229  TRP THR PRO ALA GLN PRO LEU ALA PRO GLY ARG THR GLY          
SEQRES   8 D  229  GLY LEU GLY PRO SER ASP ARG GLN LEU LEU LEU PHE TYR          
SEQRES   9 D  229  LEU GLU GLN CYS GLU ALA ASN LEU THR THR LEU THR ASN          
SEQRES  10 D  229  ALA VAL ASP ALA PHE PHE THR ALA VAL ALA THR ASN GLN          
SEQRES  11 D  229  PRO PRO LYS ILE PHE VAL ALA HIS SER LYS PHE VAL ILE          
SEQRES  12 D  229  LEU SER ALA HIS LYS LEU VAL PHE ILE GLY ASP THR LEU          
SEQRES  13 D  229  SER ARG GLN ALA LYS ALA ALA ASP VAL ARG SER GLN VAL          
SEQRES  14 D  229  THR HIS TYR SER ASN LEU LEU CYS ASP LEU LEU ARG GLY          
SEQRES  15 D  229  ILE VAL ALA THR THR LYS ALA ALA ALA LEU GLN TYR PRO          
SEQRES  16 D  229  SER PRO SER ALA ALA GLN ASP MET VAL GLU ARG VAL LYS          
SEQRES  17 D  229  GLU LEU GLY HIS SER THR GLN GLN PHE ARG ARG VAL LEU          
SEQRES  18 D  229  GLY GLN LEU ALA ALA ALA LEU GLU                              
HET    ACT  C   1       7                                                       
HETNAM     ACT ACETATE ION                                                      
FORMUL   5  ACT    C2 H3 O2 1-                                                  
FORMUL   6  HOH   *59(H2 O)                                                     
HELIX    1   1 ASN A  397  PHE A  401  5                                   5    
HELIX    2   2 GLU A  414  GLU A  427  1                                  14    
HELIX    3   3 ASP A  429  ALA A  445  1                                  17    
HELIX    4   4 THR A  451  GLY A  459  1                                   9    
HELIX    5   5 TRP A  462  LEU A  467  1                                   6    
HELIX    6   6 THR A  468  HIS A  471  5                                   4    
HELIX    7   7 GLY A  472  GLY A  496  1                                  25    
HELIX    8   8 SER A  500  THR A  521  1                                  22    
HELIX    9   9 ASN A  524  ASP A  536  1                                  13    
HELIX   10  10 MET A  537  ARG A  542  1                                   6    
HELIX   11  11 LEU A  543  HIS A  554  1                                  12    
HELIX   12  12 HIS A  554  LYS A  564  1                                  11    
HELIX   13  13 LYS A  564  GLU A  574  1                                  11    
HELIX   14  14 PRO A  580  THR A  584  5                                   5    
HELIX   15  15 VAL A  589  LEU A  596  1                                   8    
HELIX   16  16 GLY A  615  HIS A  631  1                                  17    
HELIX   17  17 HIS A  632  LEU A  644  1                                  13    
HELIX   18  18 ARG A  650  PHE A  657  1                                   8    
HELIX   19  19 SER A  658  GLY A  668  1                                  11    
HELIX   20  20 GLN A  670  SER A  674  5                                   5    
HELIX   21  21 SER A  675  GLU A  695  1                                  21    
HELIX   22  22 ASP B  740  THR B  771  1                                  32    
HELIX   23  23 PRO B  774  GLN B  802  1                                  29    
HELIX   24  24 ALA B  805  GLN B  836  1                                  32    
HELIX   25  25 SER B  839  LEU B  871  1                                  33    
HELIX   26  26 GLU C  414  ALA C  426  1                                  13    
HELIX   27  27 ASP C  429  ALA C  445  1                                  17    
HELIX   28  28 THR C  451  GLY C  459  1                                   9    
HELIX   29  29 TRP C  462  LEU C  467  1                                   6    
HELIX   30  30 LEU C  469  HIS C  471  5                                   3    
HELIX   31  31 GLY C  472  LEU C  495  1                                  24    
HELIX   32  32 SER C  500  GLY C  520  1                                  21    
HELIX   33  33 ASN C  524  ASP C  536  1                                  13    
HELIX   34  34 MET C  537  ARG C  542  1                                   6    
HELIX   35  35 LEU C  543  HIS C  554  1                                  12    
HELIX   36  36 HIS C  554  LYS C  564  1                                  11    
HELIX   37  37 LYS C  564  GLU C  574  1                                  11    
HELIX   38  38 VAL C  589  GLU C  597  1                                   9    
HELIX   39  39 GLY C  615  HIS C  632  1                                  18    
HELIX   40  40 HIS C  632  LEU C  644  1                                  13    
HELIX   41  41 ARG C  650  GLU C  655  1                                   6    
HELIX   42  42 SER C  658  ALA C  672  1                                  15    
HELIX   43  43 SER C  675  GLU C  695  1                                  21    
HELIX   44  44 LEU D  743  THR D  771  1                                  29    
HELIX   45  45 PRO D  774  ALA D  803  1                                  30    
HELIX   46  46 ALA D  805  GLN D  836  1                                  32    
HELIX   47  47 SER D  839  LEU D  871  1                                  33    
CISPEP   1 TYR B  837    PRO B  838          0        -2.37                     
CISPEP   2 TYR D  837    PRO D  838          0        -2.44                     
SITE     1 AC1  7 LEU C 535  ASP C 536  SER C 541  TRP C 547                    
SITE     2 AC1  7 TYR C 561  GLU C 562  LYS C 566                               
CRYST1  171.883  171.883   78.270  90.00  90.00  90.00 I 41         16          
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      0.005818  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005818  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012776        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system