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Database: PDB
Entry: 3B13
LinkDB: 3B13
Original site: 3B13 
HEADER    PROTEIN BINDING/SIGNALING PROTEIN       24-JUN-11   3B13              
TITLE     CRYSTAL STRUCTURE OF THE DHR-2 DOMAIN OF DOCK2 IN COMPLEX WITH RAC1   
TITLE    2 (T17N MUTANT)                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DEDICATOR OF CYTOKINESIS PROTEIN 2;                        
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: DHR-2 DOMAIN (UNP RESIDUES 1196-1622);                     
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1;                
COMPND   8 CHAIN: B, D;                                                         
COMPND   9 FRAGMENT: GTPASE DOMAIN (UNP RESIDUES 1-177);                        
COMPND  10 SYNONYM: CELL MIGRATION-INDUCING GENE 5 PROTEIN, RAS-LIKE PROTEIN    
COMPND  11 TC25, P21-RAC1;                                                      
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DOCK2, KIAA0209;                                               
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PE100108-03;                               
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: RAC1, TC25, MIG5;                                              
SOURCE  16 EXPRESSION_SYSTEM: CELL-FREE SYNTHESIS;                              
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PX080214-11                               
KEYWDS    PROTEIN-PTOTEIN COMPLEX, LYMPHOCYTE CHEMOTAXIS, SIGNAL TANSDUCTION,   
KEYWDS   2 GUANINE NUCLEOTIDE EXCHANGE FACTOR, GTPASE, PROTEIN BINDING-         
KEYWDS   3 SIGNALING PROTEIN COMPLEX                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.HANAWA-SUETSUGU,M.KUKIMOTO-NIINO,C.MISHIMA-TSUMAGARI,T.TERADA,      
AUTHOR   2 M.SHIROUZU,Y.FUKUI,S.YOKOYAMA                                        
REVDAT   1   14-MAR-12 3B13    0                                                
JRNL        AUTH   K.HANAWA-SUETSUGU,M.KUKIMOTO-NIINO,C.MISHIMA-TSUMAGARI,      
JRNL        AUTH 2 R.AKASAKA,N.OHSAWA,S.SEKINE,T.ITO,N.TOCHIO,S.KOSHIBA,        
JRNL        AUTH 3 T.KIGAWA,T.TERADA,M.SHIROUZU,A.NISHIKIMI,T.URUNO,T.KATAKAI,  
JRNL        AUTH 4 T.KINASHI,D.KOHDA,Y.FUKUI,S.YOKOYAMA                         
JRNL        TITL   STRUCTURAL BASIS FOR MUTUAL RELIEF OF THE RAC GUANINE        
JRNL        TITL 2 NUCLEOTIDE EXCHANGE FACTOR DOCK2 AND ITS PARTNER ELMO1 FROM  
JRNL        TITL 3 THEIR AUTOINHIBITED FORMS.                                   
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 109  3305 2012              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   22331897                                                     
JRNL        DOI    10.1073/PNAS.1113512109                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.01 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.1_743)                    
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.01                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.69                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 41565                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2091                            
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 48.6917 -  7.4062    0.97     2623   138  0.1782 0.1976        
REMARK   3     2  7.4062 -  5.8817    0.99     2625   154  0.1814 0.2069        
REMARK   3     3  5.8817 -  5.1392    0.99     2653   128  0.1754 0.2297        
REMARK   3     4  5.1392 -  4.6697    1.00     2649   148  0.1377 0.1832        
REMARK   3     5  4.6697 -  4.3352    1.00     2619   132  0.1286 0.1891        
REMARK   3     6  4.3352 -  4.0798    1.00     2649   136  0.1332 0.1800        
REMARK   3     7  4.0798 -  3.8755    1.00     2649   149  0.1508 0.2126        
REMARK   3     8  3.8755 -  3.7069    1.00     2628   152  0.1793 0.2309        
REMARK   3     9  3.7069 -  3.5642    1.00     2622   139  0.1938 0.2487        
REMARK   3    10  3.5642 -  3.4413    1.00     2602   136  0.1916 0.2296        
REMARK   3    11  3.4413 -  3.3337    1.00     2651   142  0.2090 0.2978        
REMARK   3    12  3.3337 -  3.2384    1.00     2635   137  0.2278 0.3256        
REMARK   3    13  3.2384 -  3.1532    1.00     2655   127  0.2565 0.3491        
REMARK   3    14  3.1532 -  3.0763    1.00     2598   130  0.2865 0.3554        
REMARK   3    15  3.0763 -  3.0063    0.99     2616   143  0.3332 0.3723        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
REMARK   3   K_SOL              : 0.32                                          
REMARK   3   B_SOL              : 17.71                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.860            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.580           
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) : 2.86110                                              
REMARK   3    B22 (A**2) : 2.86110                                              
REMARK   3    B33 (A**2) : -5.72230                                             
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      :  0.009          10140                                  
REMARK   3   ANGLE     :  1.239          13724                                  
REMARK   3   CHIRALITY :  0.094           1468                                  
REMARK   3   PLANARITY :  0.006           1776                                  
REMARK   3   DIHEDRAL  : 15.691           3842                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 18                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain A and (resseq 1196:1436)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -27.7098 -56.5725  15.7428              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1151 T22:   0.2151                                     
REMARK   3      T33:   0.1865 T12:   0.0937                                     
REMARK   3      T13:  -0.0140 T23:  -0.0039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4013 L22:   0.6821                                     
REMARK   3      L33:   2.4659 L12:  -0.4688                                     
REMARK   3      L13:   0.7642 L23:  -0.2666                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0074 S12:  -0.0477 S13:  -0.0963                       
REMARK   3      S21:   0.0738 S22:   0.0517 S23:  -0.0201                       
REMARK   3      S31:  -0.0457 S32:   0.2155 S33:  -0.0526                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain A and (resseq 1437:1622)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -45.6199 -41.4511  40.3673              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3416 T22:   0.0910                                     
REMARK   3      T33:   0.1289 T12:   0.1059                                     
REMARK   3      T13:   0.0460 T23:   0.0141                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0519 L22:   0.7137                                     
REMARK   3      L33:   1.3379 L12:  -0.7974                                     
REMARK   3      L13:  -1.0601 L23:   0.0486                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1216 S12:   0.0177 S13:   0.3348                       
REMARK   3      S21:   0.1723 S22:   0.0344 S23:  -0.0948                       
REMARK   3      S31:  -0.3256 S32:  -0.0647 S33:  -0.0828                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain B and (resseq 1:39)                              
REMARK   3    ORIGIN FOR THE GROUP (A): -45.0674 -56.2298  45.0807              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1848 T22:   0.1921                                     
REMARK   3      T33:   0.2113 T12:   0.0538                                     
REMARK   3      T13:   0.0798 T23:  -0.0064                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7803 L22:   1.6652                                     
REMARK   3      L33:   1.1799 L12:   0.2820                                     
REMARK   3      L13:  -0.7947 L23:  -0.8469                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0024 S12:   0.1987 S13:  -0.1000                       
REMARK   3      S21:   0.2708 S22:  -0.0966 S23:  -0.0535                       
REMARK   3      S31:   0.1441 S32:   0.3227 S33:   0.0931                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain B and (resseq 40:61)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -49.5708 -60.0284  38.4161              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1399 T22:   0.1592                                     
REMARK   3      T33:   0.2877 T12:   0.0712                                     
REMARK   3      T13:   0.0271 T23:   0.0213                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7273 L22:   1.6805                                     
REMARK   3      L33:   8.5583 L12:   0.3685                                     
REMARK   3      L13:  -2.3733 L23:  -0.7719                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3035 S12:   0.4701 S13:  -0.4213                       
REMARK   3      S21:  -0.0046 S22:   0.1659 S23:  -0.2192                       
REMARK   3      S31:   0.8056 S32:   0.3246 S33:   0.1414                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain B and (resseq 62:115)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -57.6785 -63.9139  52.6156              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3165 T22:   0.1544                                     
REMARK   3      T33:   0.2888 T12:   0.0093                                     
REMARK   3      T13:   0.1597 T23:   0.0059                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9360 L22:   1.7919                                     
REMARK   3      L33:   2.8292 L12:  -1.1590                                     
REMARK   3      L13:   0.6892 L23:  -0.5016                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1016 S12:  -0.1409 S13:  -0.2126                       
REMARK   3      S21:   0.4440 S22:   0.0431 S23:   0.4527                       
REMARK   3      S31:   0.2986 S32:  -0.3623 S33:   0.0284                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain B and (resseq 116:131)                           
REMARK   3    ORIGIN FOR THE GROUP (A): -36.1757 -65.9482  64.9794              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5568 T22:   0.3417                                     
REMARK   3      T33:   0.3048 T12:   0.2207                                     
REMARK   3      T13:  -0.0283 T23:  -0.0102                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0084 L22:   0.9886                                     
REMARK   3      L33:   8.3403 L12:   1.7217                                     
REMARK   3      L13:  -3.3708 L23:  -1.8184                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1030 S12:  -0.6829 S13:  -0.2303                       
REMARK   3      S21:   0.5169 S22:   0.1053 S23:  -0.5178                       
REMARK   3      S31:  -0.1248 S32:   0.7963 S33:  -0.0265                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain B and (resseq 132:177)                           
REMARK   3    ORIGIN FOR THE GROUP (A): -45.6772 -70.9952  50.8124              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4489 T22:   0.1389                                     
REMARK   3      T33:   0.2623 T12:   0.0868                                     
REMARK   3      T13:   0.0819 T23:   0.0468                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6050 L22:   0.7827                                     
REMARK   3      L33:   1.8017 L12:  -0.0450                                     
REMARK   3      L13:   0.0637 L23:  -0.8212                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1524 S12:  -0.0874 S13:  -0.3299                       
REMARK   3      S21:  -0.1052 S22:   0.0935 S23:   0.0579                       
REMARK   3      S31:   0.7212 S32:   0.0922 S33:   0.0028                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain C and (resseq 1196:1449)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -55.3959 -29.8220 -16.4761              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2617 T22:   0.1058                                     
REMARK   3      T33:   0.2035 T12:   0.2636                                     
REMARK   3      T13:  -0.1276 T23:  -0.0003                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5317 L22:   1.2912                                     
REMARK   3      L33:   2.2081 L12:  -0.4462                                     
REMARK   3      L13:   0.3376 L23:  -0.6739                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0939 S12:  -0.0078 S13:   0.0871                       
REMARK   3      S21:   0.0816 S22:   0.0689 S23:   0.0742                       
REMARK   3      S31:  -0.3763 S32:  -0.1407 S33:  -0.0040                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain C and (resseq 1450:1622)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -39.5473 -48.2578 -40.5500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0921 T22:   0.2372                                     
REMARK   3      T33:   0.1242 T12:   0.0961                                     
REMARK   3      T13:  -0.0145 T23:   0.0152                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3597 L22:   2.0434                                     
REMARK   3      L33:   1.7340 L12:  -0.8985                                     
REMARK   3      L13:  -0.1454 L23:   1.3384                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0043 S12:   0.1191 S13:   0.1339                       
REMARK   3      S21:   0.0667 S22:   0.0942 S23:  -0.2772                       
REMARK   3      S31:  -0.1101 S32:   0.2580 S33:  -0.0452                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: chain D and (resseq 1:24)                              
REMARK   3    ORIGIN FOR THE GROUP (A): -58.1018 -50.8285 -44.6686              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1656 T22:   0.1458                                     
REMARK   3      T33:   0.2193 T12:   0.1014                                     
REMARK   3      T13:  -0.0191 T23:  -0.0012                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9011 L22:   4.1905                                     
REMARK   3      L33:   1.2791 L12:   0.1522                                     
REMARK   3      L13:  -0.1971 L23:   0.1721                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0047 S12:   0.1438 S13:  -0.1894                       
REMARK   3      S21:   0.2617 S22:  -0.1034 S23:  -0.4338                       
REMARK   3      S31:  -0.2779 S32:  -0.0702 S33:   0.0703                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: chain D and (resseq 25:39)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -50.7445 -41.5644 -44.6641              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4022 T22:   0.2424                                     
REMARK   3      T33:   0.2152 T12:   0.0190                                     
REMARK   3      T13:  -0.0318 T23:  -0.1079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5305 L22:   4.6044                                     
REMARK   3      L33:   0.1045 L12:  -2.4846                                     
REMARK   3      L13:  -0.3791 L23:   0.5390                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0257 S12:   0.3202 S13:  -0.1762                       
REMARK   3      S21:  -0.0381 S22:  -0.2270 S23:   0.1906                       
REMARK   3      S31:  -0.3659 S32:  -0.2474 S33:   0.1259                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: chain D and (resseq 40:61)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -58.8528 -51.7283 -38.0799              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1962 T22:   0.1826                                     
REMARK   3      T33:   0.2698 T12:   0.1464                                     
REMARK   3      T13:   0.0019 T23:  -0.0121                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3636 L22:   3.6855                                     
REMARK   3      L33:   2.4387 L12:  -0.5570                                     
REMARK   3      L13:   1.3010 L23:   0.8835                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1246 S12:  -0.2475 S13:   0.1021                       
REMARK   3      S21:   0.2360 S22:  -0.0317 S23:  -0.0489                       
REMARK   3      S31:   0.0507 S32:  -0.1254 S33:   0.1369                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: chain D and (resseq 62:71)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -51.8186 -64.5982 -53.6757              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2277 T22:   0.2758                                     
REMARK   3      T33:   0.2948 T12:   0.1086                                     
REMARK   3      T13:   0.0231 T23:  -0.1293                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8009 L22:   7.5220                                     
REMARK   3      L33:   6.1706 L12:   0.4886                                     
REMARK   3      L13:  -0.5133 L23:  -3.5050                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2106 S12:   0.7233 S13:  -0.5006                       
REMARK   3      S21:  -1.0152 S22:  -0.1397 S23:  -0.4874                       
REMARK   3      S31:   0.5093 S32:   0.6299 S33:   0.0277                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: chain D and (resseq 72:115)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -64.6557 -58.7444 -51.9284              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1524 T22:   0.2608                                     
REMARK   3      T33:   0.2639 T12:   0.0905                                     
REMARK   3      T13:  -0.0202 T23:  -0.1116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2685 L22:   2.0892                                     
REMARK   3      L33:   2.2823 L12:  -0.7326                                     
REMARK   3      L13:  -0.6365 L23:  -0.2100                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0338 S12:   0.2949 S13:  -0.4198                       
REMARK   3      S21:   0.0116 S22:  -0.0137 S23:   0.3585                       
REMARK   3      S31:   0.0029 S32:  -0.2562 S33:  -0.0033                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: chain D and (resseq 116:131)                           
REMARK   3    ORIGIN FOR THE GROUP (A): -65.0095 -38.3570 -64.4881              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4770 T22:   0.4006                                     
REMARK   3      T33:   0.3076 T12:   0.1924                                     
REMARK   3      T13:   0.0192 T23:   0.0965                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5443 L22:   1.9487                                     
REMARK   3      L33:   3.7851 L12:  -0.0896                                     
REMARK   3      L13:   0.3717 L23:   1.8505                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1560 S12:   0.7620 S13:   0.5339                       
REMARK   3      S21:  -0.5921 S22:  -0.0507 S23:   0.2395                       
REMARK   3      S31:  -1.1213 S32:  -0.3088 S33:  -0.0659                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: chain D and (resseq 132:149)                           
REMARK   3    ORIGIN FOR THE GROUP (A): -72.8146 -50.4139 -60.3089              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2099 T22:   0.3900                                     
REMARK   3      T33:   0.3461 T12:   0.1743                                     
REMARK   3      T13:   0.0087 T23:  -0.0166                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6398 L22:   0.6701                                     
REMARK   3      L33:   0.5112 L12:  -0.4399                                     
REMARK   3      L13:  -0.3590 L23:   0.0018                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1036 S12:   0.3690 S13:  -0.0163                       
REMARK   3      S21:  -0.0478 S22:  -0.0177 S23:   0.2707                       
REMARK   3      S31:  -0.1874 S32:  -0.3185 S33:  -0.2148                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: chain D and (resseq 150:164)                           
REMARK   3    ORIGIN FOR THE GROUP (A): -67.8484 -44.6659 -48.8375              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2126 T22:   0.3040                                     
REMARK   3      T33:   0.2662 T12:   0.1451                                     
REMARK   3      T13:   0.0932 T23:  -0.0072                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9926 L22:   2.6284                                     
REMARK   3      L33:   0.3995 L12:   2.0628                                     
REMARK   3      L13:  -0.4201 L23:  -0.2203                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1422 S12:   0.0150 S13:   0.4085                       
REMARK   3      S21:  -0.0600 S22:  -0.0897 S23:   0.3075                       
REMARK   3      S31:  -0.1615 S32:  -0.0711 S33:   0.0023                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: chain D and (resseq 165:177)                           
REMARK   3    ORIGIN FOR THE GROUP (A): -67.7843 -49.3983 -39.0754              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1192 T22:   0.3000                                     
REMARK   3      T33:   0.2022 T12:   0.0302                                     
REMARK   3      T13:   0.0447 T23:   0.0124                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3779 L22:   4.5964                                     
REMARK   3      L33:   4.1650 L12:  -0.4958                                     
REMARK   3      L13:   0.1244 L23:  -1.1436                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0069 S12:  -0.2640 S13:  -0.3183                       
REMARK   3      S21:   0.3451 S22:   0.1188 S23:   0.6952                       
REMARK   3      S31:  -0.2711 S32:  -0.6194 S33:  -0.1362                       
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 3B13 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-JUL-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB029945.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41625                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 3.210                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.12900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.0800                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.59400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.940                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2WM9, 2NZ8                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM CITRATE, 15% PEG 6000, PH   
REMARK 280  8.0, VAPOR DIFFUSION, SITTING 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       86.47867            
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       43.23933            
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       64.85900            
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       21.61967            
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      108.09833            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9720 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 55480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A  1192                                                      
REMARK 465     SER A  1193                                                      
REMARK 465     PHE A  1194                                                      
REMARK 465     THR A  1195                                                      
REMARK 465     GLY B    -6                                                      
REMARK 465     SER B    -5                                                      
REMARK 465     SER B    -4                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     GLY C  1192                                                      
REMARK 465     SER C  1193                                                      
REMARK 465     PHE C  1194                                                      
REMARK 465     THR C  1195                                                      
REMARK 465     GLY D    -6                                                      
REMARK 465     SER D    -5                                                      
REMARK 465     SER D    -4                                                      
REMARK 465     GLY D    -3                                                      
REMARK 465     SER D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     GLY D     0                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OH   TYR A  1444     OE1  GLU B    31              2.03            
REMARK 500   NH2  ARG A  1370     OE1  GLU A  1372              2.18            
REMARK 500   OD1  ASP C  1571     NH1  ARG C  1620              2.18            
REMARK 500   NH2  ARG C  1370     O    TYR D    23              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B  50   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    PRO C1427   C   -  N   -  CA  ANGL. DEV. =   9.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A1422      -73.28    -49.37                                   
REMARK 500    ASN B  39     -164.51     56.25                                   
REMARK 500    TYR B  40      156.79    175.94                                   
REMARK 500    VAL B  46      -75.25    -92.32                                   
REMARK 500    GLN B  74        1.81     83.04                                   
REMARK 500    LYS B  96      -60.76   -122.68                                   
REMARK 500    GLN B 162       -0.76     71.33                                   
REMARK 500    GLN C1267      -72.99    -56.50                                   
REMARK 500    GLU C1311      -61.41   -127.12                                   
REMARK 500    LYS C1422      -72.08    -45.50                                   
REMARK 500    VAL C1485      -63.58   -109.01                                   
REMARK 500    ASP D  11     -179.68    -68.03                                   
REMARK 500    ASN D  39     -169.51     50.43                                   
REMARK 500    TYR D  40      157.36    177.89                                   
REMARK 500    LYS D  96      -66.39   -104.59                                   
REMARK 500    GLN D 162       -2.14     74.20                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASP B  38        25.0      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3B13 A 1196  1622  UNP    Q92608   DOCK2_HUMAN   1196   1622             
DBREF  3B13 B    1   177  UNP    P63000   RAC1_HUMAN       1    177             
DBREF  3B13 C 1196  1622  UNP    Q92608   DOCK2_HUMAN   1196   1622             
DBREF  3B13 D    1   177  UNP    P63000   RAC1_HUMAN       1    177             
SEQADV 3B13 GLY A 1192  UNP  Q92608              EXPRESSION TAG                 
SEQADV 3B13 SER A 1193  UNP  Q92608              EXPRESSION TAG                 
SEQADV 3B13 PHE A 1194  UNP  Q92608              EXPRESSION TAG                 
SEQADV 3B13 THR A 1195  UNP  Q92608              EXPRESSION TAG                 
SEQADV 3B13 GLY B   -6  UNP  P63000              EXPRESSION TAG                 
SEQADV 3B13 SER B   -5  UNP  P63000              EXPRESSION TAG                 
SEQADV 3B13 SER B   -4  UNP  P63000              EXPRESSION TAG                 
SEQADV 3B13 GLY B   -3  UNP  P63000              EXPRESSION TAG                 
SEQADV 3B13 SER B   -2  UNP  P63000              EXPRESSION TAG                 
SEQADV 3B13 SER B   -1  UNP  P63000              EXPRESSION TAG                 
SEQADV 3B13 GLY B    0  UNP  P63000              EXPRESSION TAG                 
SEQADV 3B13 ASN B   17  UNP  P63000    THR    17 ENGINEERED MUTATION            
SEQADV 3B13 GLY C 1192  UNP  Q92608              EXPRESSION TAG                 
SEQADV 3B13 SER C 1193  UNP  Q92608              EXPRESSION TAG                 
SEQADV 3B13 PHE C 1194  UNP  Q92608              EXPRESSION TAG                 
SEQADV 3B13 THR C 1195  UNP  Q92608              EXPRESSION TAG                 
SEQADV 3B13 GLY D   -6  UNP  P63000              EXPRESSION TAG                 
SEQADV 3B13 SER D   -5  UNP  P63000              EXPRESSION TAG                 
SEQADV 3B13 SER D   -4  UNP  P63000              EXPRESSION TAG                 
SEQADV 3B13 GLY D   -3  UNP  P63000              EXPRESSION TAG                 
SEQADV 3B13 SER D   -2  UNP  P63000              EXPRESSION TAG                 
SEQADV 3B13 SER D   -1  UNP  P63000              EXPRESSION TAG                 
SEQADV 3B13 GLY D    0  UNP  P63000              EXPRESSION TAG                 
SEQADV 3B13 ASN D   17  UNP  P63000    THR    17 ENGINEERED MUTATION            
SEQRES   1 A  431  GLY SER PHE THR SER LYS ASP ASN ARG MET SER CYS THR          
SEQRES   2 A  431  VAL ASN LEU LEU ASN PHE TYR LYS ASP ASN ASN ARG GLU          
SEQRES   3 A  431  GLU MET TYR ILE ARG TYR LEU TYR LYS LEU ARG ASP LEU          
SEQRES   4 A  431  HIS LEU ASP CYS ASP ASN TYR THR GLU ALA ALA TYR THR          
SEQRES   5 A  431  LEU LEU LEU HIS THR TRP LEU LEU LYS TRP SER ASP GLU          
SEQRES   6 A  431  GLN CYS ALA SER GLN VAL MET GLN THR GLY GLN GLN HIS          
SEQRES   7 A  431  PRO GLN THR HIS ARG GLN LEU LYS GLU THR LEU TYR GLU          
SEQRES   8 A  431  THR ILE ILE GLY TYR PHE ASP LYS GLY LYS MET TRP GLU          
SEQRES   9 A  431  GLU ALA ILE SER LEU CYS LYS GLU LEU ALA GLU GLN TYR          
SEQRES  10 A  431  GLU MET GLU ILE PHE ASP TYR GLU LEU LEU SER GLN ASN          
SEQRES  11 A  431  LEU ILE GLN GLN ALA LYS PHE TYR GLU SER ILE MET LYS          
SEQRES  12 A  431  ILE LEU ARG PRO LYS PRO ASP TYR PHE ALA VAL GLY TYR          
SEQRES  13 A  431  TYR GLY GLN GLY PHE PRO SER PHE LEU ARG ASN LYS VAL          
SEQRES  14 A  431  PHE ILE TYR ARG GLY LYS GLU TYR GLU ARG ARG GLU ASP          
SEQRES  15 A  431  PHE GLN MET GLN LEU MET THR GLN PHE PRO ASN ALA GLU          
SEQRES  16 A  431  LYS MET ASN THR THR SER ALA PRO GLY ASP ASP VAL LYS          
SEQRES  17 A  431  ASN ALA PRO GLY GLN TYR ILE GLN CYS PHE THR VAL GLN          
SEQRES  18 A  431  PRO VAL LEU ASP GLU HIS PRO ARG PHE LYS ASN LYS PRO          
SEQRES  19 A  431  VAL PRO ASP GLN ILE ILE ASN PHE TYR LYS SER ASN TYR          
SEQRES  20 A  431  VAL GLN ARG PHE HIS TYR SER ARG PRO VAL ARG ARG GLY          
SEQRES  21 A  431  THR VAL ASP PRO GLU ASN GLU PHE ALA SER MET TRP ILE          
SEQRES  22 A  431  GLU ARG THR SER PHE VAL THR ALA TYR LYS LEU PRO GLY          
SEQRES  23 A  431  ILE LEU ARG TRP PHE GLU VAL VAL HIS MET SER GLN THR          
SEQRES  24 A  431  THR ILE SER PRO LEU GLU ASN ALA ILE GLU THR MET SER          
SEQRES  25 A  431  THR ALA ASN GLU LYS ILE LEU MET MET ILE ASN GLN TYR          
SEQRES  26 A  431  GLN SER ASP GLU THR LEU PRO ILE ASN PRO LEU SER MET          
SEQRES  27 A  431  LEU LEU ASN GLY ILE VAL ASP PRO ALA VAL MET GLY GLY          
SEQRES  28 A  431  PHE ALA LYS TYR GLU LYS ALA PHE PHE THR GLU GLU TYR          
SEQRES  29 A  431  VAL ARG ASP HIS PRO GLU ASP GLN ASP LYS LEU THR HIS          
SEQRES  30 A  431  LEU LYS ASP LEU ILE ALA TRP GLN ILE PRO PHE LEU GLY          
SEQRES  31 A  431  ALA GLY ILE LYS ILE HIS GLU LYS ARG VAL SER ASP ASN          
SEQRES  32 A  431  LEU ARG PRO PHE HIS ASP ARG MET GLU GLU CYS PHE LYS          
SEQRES  33 A  431  ASN LEU LYS MET LYS VAL GLU LYS GLU TYR GLY VAL ARG          
SEQRES  34 A  431  GLU MET                                                      
SEQRES   1 B  184  GLY SER SER GLY SER SER GLY MET GLN ALA ILE LYS CYS          
SEQRES   2 B  184  VAL VAL VAL GLY ASP GLY ALA VAL GLY LYS ASN CYS LEU          
SEQRES   3 B  184  LEU ILE SER TYR THR THR ASN ALA PHE PRO GLY GLU TYR          
SEQRES   4 B  184  ILE PRO THR VAL PHE ASP ASN TYR SER ALA ASN VAL MET          
SEQRES   5 B  184  VAL ASP GLY LYS PRO VAL ASN LEU GLY LEU TRP ASP THR          
SEQRES   6 B  184  ALA GLY GLN GLU ASP TYR ASP ARG LEU ARG PRO LEU SER          
SEQRES   7 B  184  TYR PRO GLN THR ASP VAL PHE LEU ILE CYS PHE SER LEU          
SEQRES   8 B  184  VAL SER PRO ALA SER PHE GLU ASN VAL ARG ALA LYS TRP          
SEQRES   9 B  184  TYR PRO GLU VAL ARG HIS HIS CYS PRO ASN THR PRO ILE          
SEQRES  10 B  184  ILE LEU VAL GLY THR LYS LEU ASP LEU ARG ASP ASP LYS          
SEQRES  11 B  184  ASP THR ILE GLU LYS LEU LYS GLU LYS LYS LEU THR PRO          
SEQRES  12 B  184  ILE THR TYR PRO GLN GLY LEU ALA MET ALA LYS GLU ILE          
SEQRES  13 B  184  GLY ALA VAL LYS TYR LEU GLU CYS SER ALA LEU THR GLN          
SEQRES  14 B  184  ARG GLY LEU LYS THR VAL PHE ASP GLU ALA ILE ARG ALA          
SEQRES  15 B  184  VAL LEU                                                      
SEQRES   1 C  431  GLY SER PHE THR SER LYS ASP ASN ARG MET SER CYS THR          
SEQRES   2 C  431  VAL ASN LEU LEU ASN PHE TYR LYS ASP ASN ASN ARG GLU          
SEQRES   3 C  431  GLU MET TYR ILE ARG TYR LEU TYR LYS LEU ARG ASP LEU          
SEQRES   4 C  431  HIS LEU ASP CYS ASP ASN TYR THR GLU ALA ALA TYR THR          
SEQRES   5 C  431  LEU LEU LEU HIS THR TRP LEU LEU LYS TRP SER ASP GLU          
SEQRES   6 C  431  GLN CYS ALA SER GLN VAL MET GLN THR GLY GLN GLN HIS          
SEQRES   7 C  431  PRO GLN THR HIS ARG GLN LEU LYS GLU THR LEU TYR GLU          
SEQRES   8 C  431  THR ILE ILE GLY TYR PHE ASP LYS GLY LYS MET TRP GLU          
SEQRES   9 C  431  GLU ALA ILE SER LEU CYS LYS GLU LEU ALA GLU GLN TYR          
SEQRES  10 C  431  GLU MET GLU ILE PHE ASP TYR GLU LEU LEU SER GLN ASN          
SEQRES  11 C  431  LEU ILE GLN GLN ALA LYS PHE TYR GLU SER ILE MET LYS          
SEQRES  12 C  431  ILE LEU ARG PRO LYS PRO ASP TYR PHE ALA VAL GLY TYR          
SEQRES  13 C  431  TYR GLY GLN GLY PHE PRO SER PHE LEU ARG ASN LYS VAL          
SEQRES  14 C  431  PHE ILE TYR ARG GLY LYS GLU TYR GLU ARG ARG GLU ASP          
SEQRES  15 C  431  PHE GLN MET GLN LEU MET THR GLN PHE PRO ASN ALA GLU          
SEQRES  16 C  431  LYS MET ASN THR THR SER ALA PRO GLY ASP ASP VAL LYS          
SEQRES  17 C  431  ASN ALA PRO GLY GLN TYR ILE GLN CYS PHE THR VAL GLN          
SEQRES  18 C  431  PRO VAL LEU ASP GLU HIS PRO ARG PHE LYS ASN LYS PRO          
SEQRES  19 C  431  VAL PRO ASP GLN ILE ILE ASN PHE TYR LYS SER ASN TYR          
SEQRES  20 C  431  VAL GLN ARG PHE HIS TYR SER ARG PRO VAL ARG ARG GLY          
SEQRES  21 C  431  THR VAL ASP PRO GLU ASN GLU PHE ALA SER MET TRP ILE          
SEQRES  22 C  431  GLU ARG THR SER PHE VAL THR ALA TYR LYS LEU PRO GLY          
SEQRES  23 C  431  ILE LEU ARG TRP PHE GLU VAL VAL HIS MET SER GLN THR          
SEQRES  24 C  431  THR ILE SER PRO LEU GLU ASN ALA ILE GLU THR MET SER          
SEQRES  25 C  431  THR ALA ASN GLU LYS ILE LEU MET MET ILE ASN GLN TYR          
SEQRES  26 C  431  GLN SER ASP GLU THR LEU PRO ILE ASN PRO LEU SER MET          
SEQRES  27 C  431  LEU LEU ASN GLY ILE VAL ASP PRO ALA VAL MET GLY GLY          
SEQRES  28 C  431  PHE ALA LYS TYR GLU LYS ALA PHE PHE THR GLU GLU TYR          
SEQRES  29 C  431  VAL ARG ASP HIS PRO GLU ASP GLN ASP LYS LEU THR HIS          
SEQRES  30 C  431  LEU LYS ASP LEU ILE ALA TRP GLN ILE PRO PHE LEU GLY          
SEQRES  31 C  431  ALA GLY ILE LYS ILE HIS GLU LYS ARG VAL SER ASP ASN          
SEQRES  32 C  431  LEU ARG PRO PHE HIS ASP ARG MET GLU GLU CYS PHE LYS          
SEQRES  33 C  431  ASN LEU LYS MET LYS VAL GLU LYS GLU TYR GLY VAL ARG          
SEQRES  34 C  431  GLU MET                                                      
SEQRES   1 D  184  GLY SER SER GLY SER SER GLY MET GLN ALA ILE LYS CYS          
SEQRES   2 D  184  VAL VAL VAL GLY ASP GLY ALA VAL GLY LYS ASN CYS LEU          
SEQRES   3 D  184  LEU ILE SER TYR THR THR ASN ALA PHE PRO GLY GLU TYR          
SEQRES   4 D  184  ILE PRO THR VAL PHE ASP ASN TYR SER ALA ASN VAL MET          
SEQRES   5 D  184  VAL ASP GLY LYS PRO VAL ASN LEU GLY LEU TRP ASP THR          
SEQRES   6 D  184  ALA GLY GLN GLU ASP TYR ASP ARG LEU ARG PRO LEU SER          
SEQRES   7 D  184  TYR PRO GLN THR ASP VAL PHE LEU ILE CYS PHE SER LEU          
SEQRES   8 D  184  VAL SER PRO ALA SER PHE GLU ASN VAL ARG ALA LYS TRP          
SEQRES   9 D  184  TYR PRO GLU VAL ARG HIS HIS CYS PRO ASN THR PRO ILE          
SEQRES  10 D  184  ILE LEU VAL GLY THR LYS LEU ASP LEU ARG ASP ASP LYS          
SEQRES  11 D  184  ASP THR ILE GLU LYS LEU LYS GLU LYS LYS LEU THR PRO          
SEQRES  12 D  184  ILE THR TYR PRO GLN GLY LEU ALA MET ALA LYS GLU ILE          
SEQRES  13 D  184  GLY ALA VAL LYS TYR LEU GLU CYS SER ALA LEU THR GLN          
SEQRES  14 D  184  ARG GLY LEU LYS THR VAL PHE ASP GLU ALA ILE ARG ALA          
SEQRES  15 D  184  VAL LEU                                                      
FORMUL   5  HOH   *10(H2 O)                                                     
HELIX    1   1 SER A 1196  ASN A 1214  1                                  19    
HELIX    2   2 ARG A 1216  CYS A 1234  1                                  19    
HELIX    3   3 ASN A 1236  TRP A 1249  1                                  14    
HELIX    4   4 THR A 1272  GLY A 1291  1                                  20    
HELIX    5   5 MET A 1293  GLU A 1311  1                                  19    
HELIX    6   6 ASP A 1314  ILE A 1335  1                                  22    
HELIX    7   7 ARG A 1370  PHE A 1382  1                                  13    
HELIX    8   8 GLY A 1395  ASN A 1400  1                                   6    
HELIX    9   9 HIS A 1418  LYS A 1422  5                                   5    
HELIX   10  10 PRO A 1427  ASN A 1437  1                                  11    
HELIX   11  11 SER A 1493  ASP A 1519  1                                  27    
HELIX   12  12 ILE A 1524  ASP A 1536  1                                  13    
HELIX   13  13 PHE A 1543  PHE A 1551  1                                   9    
HELIX   14  14 THR A 1552  HIS A 1559  1                                   8    
HELIX   15  15 ASP A 1562  VAL A 1591  1                                  30    
HELIX   16  16 SER A 1592  ASN A 1594  5                                   3    
HELIX   17  17 LEU A 1595  GLY A 1618  1                                  24    
HELIX   18  18 GLY B   15  THR B   25  1                                  11    
HELIX   19  19 GLN B   61  ASP B   65  5                                   5    
HELIX   20  20 LEU B   67  TYR B   72  5                                   6    
HELIX   21  21 SER B   86  LYS B   96  1                                  11    
HELIX   22  22 LYS B   96  CYS B  105  1                                  10    
HELIX   23  23 LYS B  116  ARG B  120  5                                   5    
HELIX   24  24 ASP B  122  LYS B  132  1                                  11    
HELIX   25  25 THR B  138  ILE B  149  1                                  12    
HELIX   26  26 GLY B  164  LEU B  177  1                                  14    
HELIX   27  27 SER C 1196  ASN C 1214  1                                  19    
HELIX   28  28 ARG C 1216  CYS C 1234  1                                  19    
HELIX   29  29 ASN C 1236  TRP C 1249  1                                  14    
HELIX   30  30 THR C 1272  GLY C 1291  1                                  20    
HELIX   31  31 MET C 1293  GLU C 1311  1                                  19    
HELIX   32  32 ASP C 1314  ILE C 1335  1                                  22    
HELIX   33  33 ARG C 1370  THR C 1380  1                                  11    
HELIX   34  34 GLY C 1395  ASN C 1400  1                                   6    
HELIX   35  35 HIS C 1418  LYS C 1422  5                                   5    
HELIX   36  36 PRO C 1427  ASN C 1437  1                                  11    
HELIX   37  37 SER C 1493  ASP C 1519  1                                  27    
HELIX   38  38 ILE C 1524  ASP C 1536  1                                  13    
HELIX   39  39 PHE C 1543  PHE C 1551  1                                   9    
HELIX   40  40 THR C 1552  HIS C 1559  1                                   8    
HELIX   41  41 ASP C 1562  VAL C 1591  1                                  30    
HELIX   42  42 LEU C 1595  GLY C 1618  1                                  24    
HELIX   43  43 GLY D   15  THR D   25  1                                  11    
HELIX   44  44 GLN D   61  ASP D   65  5                                   5    
HELIX   45  45 LEU D   67  TYR D   72  5                                   6    
HELIX   46  46 SER D   86  LYS D   96  1                                  11    
HELIX   47  47 LYS D   96  CYS D  105  1                                  10    
HELIX   48  48 LYS D  116  ARG D  120  5                                   5    
HELIX   49  49 ASP D  122  LYS D  132  1                                  11    
HELIX   50  50 THR D  138  GLY D  150  1                                  13    
HELIX   51  51 GLY D  164  LEU D  177  1                                  14    
SHEET    1   A 8 ALA A1385  LYS A1387  0                                        
SHEET    2   A 8 GLN A1404  PRO A1413  1  O  ILE A1406   N  GLU A1386           
SHEET    3   A 8 VAL A1439  ARG A1449 -1  O  HIS A1443   N  GLN A1412           
SHEET    4   A 8 MET A1462  LEU A1475 -1  O  GLU A1465   N  ARG A1446           
SHEET    5   A 8 TRP A1481  ILE A1492 -1  O  VAL A1485   N  VAL A1470           
SHEET    6   A 8 LYS A1359  GLU A1367 -1  N  VAL A1360   O  VAL A1484           
SHEET    7   A 8 PRO A1340  TYR A1348 -1  N  PHE A1343   O  TYR A1363           
SHEET    8   A 8 GLN A1404  PRO A1413 -1  O  VAL A1411   N  TYR A1342           
SHEET    1   B 6 TYR B  40  MET B  45  0                                        
SHEET    2   B 6 PRO B  50  ASP B  57 -1  O  LEU B  55   N  TYR B  40           
SHEET    3   B 6 GLN B   2  GLY B  10  1  N  ILE B   4   O  ASN B  52           
SHEET    4   B 6 VAL B  77  SER B  83  1  O  LEU B  79   N  VAL B   9           
SHEET    5   B 6 ILE B 110  THR B 115  1  O  VAL B 113   N  ILE B  80           
SHEET    6   B 6 LYS B 153  GLU B 156  1  O  LEU B 155   N  LEU B 112           
SHEET    1   C 8 GLU C1386  LYS C1387  0                                        
SHEET    2   C 8 TYR C1405  VAL C1414  1  O  ILE C1406   N  GLU C1386           
SHEET    3   C 8 VAL C1439  ARG C1449 -1  O  HIS C1443   N  GLN C1412           
SHEET    4   C 8 MET C1462  LEU C1475 -1  O  PHE C1469   N  PHE C1442           
SHEET    5   C 8 TRP C1481  ILE C1492 -1  O  VAL C1485   N  VAL C1470           
SHEET    6   C 8 LYS C1359  ARG C1364 -1  N  VAL C1360   O  VAL C1484           
SHEET    7   C 8 TYR C1342  TYR C1348 -1  N  PHE C1343   O  TYR C1363           
SHEET    8   C 8 TYR C1405  VAL C1414 -1  O  VAL C1411   N  TYR C1342           
SHEET    1   D 6 TYR D  40  VAL D  46  0                                        
SHEET    2   D 6 LYS D  49  ASP D  57 -1  O  LEU D  55   N  TYR D  40           
SHEET    3   D 6 GLN D   2  GLY D  10  1  N  VAL D   8   O  TRP D  56           
SHEET    4   D 6 VAL D  77  SER D  83  1  O  CYS D  81   N  VAL D   9           
SHEET    5   D 6 ILE D 110  THR D 115  1  O  ILE D 111   N  PHE D  78           
SHEET    6   D 6 LYS D 153  GLU D 156  1  O  LEU D 155   N  GLY D 114           
CISPEP   1 LEU A 1475    PRO A 1476          0        -4.84                     
CISPEP   2 LEU C 1475    PRO C 1476          0         1.87                     
CRYST1  168.651  168.651  129.718  90.00  90.00 120.00 P 65         12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005929  0.003423  0.000000        0.00000                         
SCALE2      0.000000  0.006847  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007709        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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