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Entry: 2YIN
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HEADER    APOPTOSIS                               16-MAY-11   2YIN              
TITLE     STRUCTURE OF THE COMPLEX BETWEEN DOCK2 AND RAC1.                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DEDICATOR OF CYTOKINESIS PROTEIN 2;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: DHR2 DOMAIN, RESIDUES 1192-1622;                           
COMPND   5 SYNONYM: DOCK2;                                                      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: CIS PEPTIDE BETWEEN 1475 AND 1476 RESIDUES OF CHAIN   
COMPND   8  A AND B.;                                                           
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1;                
COMPND  11 CHAIN: C, D;                                                         
COMPND  12 FRAGMENT: RESIDUES 1-177;                                            
COMPND  13 SYNONYM: RAC1, CELL MIGRATION-INDUCING GENE 5 PROTEIN, RAS-LIKE      
COMPND  14  PROTEIN TC25, P21-RAC1;                                             
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: B834;                                      
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: POPIN;                                    
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 EXPRESSION_SYSTEM_STRAIN: B834;                                      
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: POPIN                                     
KEYWDS    APOPTOSIS, DOCK, DOCK GUANINE NUCLEOTIDE EXCHANGE FACTORS, RHO GTPASE 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.A.KULKARNI,J.YANG,Z.ZHANG,D.BARFORD                                 
REVDAT   2   27-JUL-11 2YIN    1       JRNL   REMARK VERSN                      
REVDAT   1   25-MAY-11 2YIN    0                                                
JRNL        AUTH   K.KULKARNI,J.YANG,Z.ZHANG,D.BARFORD                          
JRNL        TITL   MULTIPLE FACTORS CONFER SPECIFIC CDC42 AND RAC PROTEIN       
JRNL        TITL 2 ACTIVATION BY DEDICATOR OF CYTOKINESIS (DOCK) NUCLEOTIDE     
JRNL        TITL 3 EXCHANGE FACTORS.                                            
JRNL        REF    J.BIOL.CHEM.                  V. 286 25341 2011              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   21613211                                                     
JRNL        DOI    10.1074/JBC.M111.236455                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.700                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 64.374                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.35                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.71                          
REMARK   3   NUMBER OF REFLECTIONS             : 43654                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.2059                          
REMARK   3   R VALUE            (WORKING SET) : 0.2033                          
REMARK   3   FREE R VALUE                     : 0.2548                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2217                            
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 64.3927 -  6.8011    0.91     2609   152  0.1807 0.1872        
REMARK   3     2  6.8011 -  5.3991    0.91     2601   115  0.2201 0.2942        
REMARK   3     3  5.3991 -  4.7168    0.93     2607   146  0.1678 0.2130        
REMARK   3     4  4.7168 -  4.2857    0.94     2585   142  0.1519 0.2047        
REMARK   3     5  4.2857 -  3.9785    0.94     2654   135  0.1669 0.2230        
REMARK   3     6  3.9785 -  3.7440    0.94     2607   149  0.1812 0.2314        
REMARK   3     7  3.7440 -  3.5565    0.94     2627   141  0.1938 0.2448        
REMARK   3     8  3.5565 -  3.4017    0.95     2619   136  0.2023 0.2706        
REMARK   3     9  3.4017 -  3.2708    0.95     2641   141  0.2175 0.2801        
REMARK   3    10  3.2708 -  3.1579    0.94     2625   128  0.2387 0.3208        
REMARK   3    11  3.1579 -  3.0592    0.94     2640   126  0.2612 0.3250        
REMARK   3    12  3.0592 -  2.9717    0.93     2573   128  0.2713 0.3166        
REMARK   3    13  2.9717 -  2.8935    0.92     2578   145  0.2838 0.3424        
REMARK   3    14  2.8935 -  2.8229    0.91     2516   150  0.3200 0.4022        
REMARK   3    15  2.8229 -  2.7587    0.91     2474   152  0.3475 0.4470        
REMARK   3    16  2.7587 -  2.7000    0.88     2481   131  0.3623 0.4495        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.72                                          
REMARK   3   K_SOL              : 0.346                                         
REMARK   3   B_SOL              : 54.961                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.47             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.86            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 63.41                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 68.9                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 9.1660                                               
REMARK   3    B22 (A**2) : 7.2882                                               
REMARK   3    B33 (A**2) : -16.4542                                             
REMARK   3    B12 (A**2) : 0.0000                                               
REMARK   3    B13 (A**2) : 2.1660                                               
REMARK   3    B23 (A**2) : 0.0000                                               
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      :  0.014           9762                                  
REMARK   3   ANGLE     :  1.439          13247                                  
REMARK   3   CHIRALITY :  0.101           1441                                  
REMARK   3   PLANARITY :  0.010           1709                                  
REMARK   3   DIHEDRAL  : 17.101           3604                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 24                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 1196:1291)                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.4761  50.9511 180.4754              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3721 T22:   0.3645                                     
REMARK   3      T33:   0.3607 T12:  -0.0460                                     
REMARK   3      T13:  -0.0199 T23:   0.0308                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5168 L22:   1.2284                                     
REMARK   3      L33:   0.3353 L12:   1.4082                                     
REMARK   3      L13:  -0.3907 L23:   0.4835                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1549 S12:  -0.2138 S13:   0.0670                       
REMARK   3      S21:   0.1318 S22:  -0.1305 S23:   0.0976                       
REMARK   3      S31:  -0.0105 S32:  -0.1303 S33:  -0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 1292:1341)                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.5231  39.5613 180.3575              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2723 T22:   0.3321                                     
REMARK   3      T33:   0.2747 T12:  -0.0242                                     
REMARK   3      T13:   0.0140 T23:   0.0149                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6640 L22:   0.3404                                     
REMARK   3      L33:   0.2107 L12:   0.1602                                     
REMARK   3      L13:  -0.8099 L23:  -0.1997                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0587 S12:   0.1223 S13:   0.0969                       
REMARK   3      S21:  -0.0201 S22:   0.0607 S23:  -0.0194                       
REMARK   3      S31:  -0.1495 S32:  -0.0532 S33:  -0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 1342:1418)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.5457  49.8528 153.5622              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3244 T22:   0.4277                                     
REMARK   3      T33:   0.3703 T12:  -0.0690                                     
REMARK   3      T13:   0.0197 T23:  -0.0773                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9426 L22:   1.4873                                     
REMARK   3      L33:   1.5377 L12:  -0.2648                                     
REMARK   3      L13:   1.2092 L23:   0.9409                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1154 S12:   0.1080 S13:  -0.1317                       
REMARK   3      S21:  -0.2425 S22:   0.2984 S23:  -0.1211                       
REMARK   3      S31:  -0.3253 S32:   0.2246 S33:  -0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 1419:1505)                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.5221  33.8182 152.9424              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3782 T22:   0.3580                                     
REMARK   3      T33:   0.3497 T12:   0.0595                                     
REMARK   3      T13:  -0.0068 T23:  -0.0434                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6525 L22:   0.6418                                     
REMARK   3      L33:  -0.0301 L12:   0.5796                                     
REMARK   3      L13:   0.5228 L23:   0.2575                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0567 S12:   0.1233 S13:  -0.1764                       
REMARK   3      S21:   0.1108 S22:  -0.0213 S23:  -0.0514                       
REMARK   3      S31:   0.2364 S32:   0.1608 S33:   0.0000                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 1506:1613)                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.9635  26.5318 142.2234              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5137 T22:   0.4506                                     
REMARK   3      T33:   0.4702 T12:  -0.0961                                     
REMARK   3      T13:  -0.0575 T23:  -0.0426                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1173 L22:   0.7616                                     
REMARK   3      L33:   0.6603 L12:   0.5212                                     
REMARK   3      L13:   0.9102 L23:   0.1408                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1614 S12:   0.0265 S13:  -0.2344                       
REMARK   3      S21:   0.0444 S22:   0.0216 S23:  -0.1802                       
REMARK   3      S31:   0.2930 S32:  -0.4196 S33:   0.0000                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 1614:1620)                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.5162  13.7239 139.6871              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9958 T22:   0.7070                                     
REMARK   3      T33:   1.2342 T12:  -0.2329                                     
REMARK   3      T13:  -0.0572 T23:  -0.1654                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0097 L22:  -0.0024                                     
REMARK   3      L33:  -0.0124 L12:   0.0236                                     
REMARK   3      L13:  -0.0022 L23:  -0.0236                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1840 S12:   0.5526 S13:  -0.4780                       
REMARK   3      S21:  -0.2509 S22:  -0.0282 S23:   0.2345                       
REMARK   3      S31:  -0.0559 S32:   0.3088 S33:  -0.0000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 1197:1291)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.7709  12.1290  60.8265              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4874 T22:   0.3857                                     
REMARK   3      T33:   0.4035 T12:  -0.0767                                     
REMARK   3      T13:   0.0053 T23:   0.0116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1978 L22:   1.1640                                     
REMARK   3      L33:   1.2728 L12:   0.6936                                     
REMARK   3      L13:   0.3850 L23:   0.2578                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0161 S12:   0.0078 S13:   0.0568                       
REMARK   3      S21:  -0.1818 S22:   0.1597 S23:   0.0609                       
REMARK   3      S31:   0.5868 S32:  -0.2292 S33:   0.0000                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 1292:1357)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.2868  24.5469  65.8898              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2368 T22:   0.1955                                     
REMARK   3      T33:   0.3023 T12:  -0.0145                                     
REMARK   3      T13:  -0.0038 T23:   0.0312                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4084 L22:   0.3064                                     
REMARK   3      L33:   0.7920 L12:   0.3458                                     
REMARK   3      L13:  -0.3781 L23:  -0.4210                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0735 S12:   0.1813 S13:  -0.1030                       
REMARK   3      S21:  -0.0455 S22:   0.0972 S23:   0.1242                       
REMARK   3      S31:  -0.1229 S32:  -0.1902 S33:   0.0000                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 1358:1418)                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.4390  13.9196  88.7113              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3184 T22:   0.4265                                     
REMARK   3      T33:   0.4979 T12:   0.0000                                     
REMARK   3      T13:  -0.0223 T23:   0.0843                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6190 L22:   1.1112                                     
REMARK   3      L33:   0.7095 L12:  -0.9125                                     
REMARK   3      L13:  -0.2939 L23:   0.0908                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0226 S12:  -0.0701 S13:  -0.2064                       
REMARK   3      S21:  -0.0042 S22:   0.0942 S23:   0.2453                       
REMARK   3      S31:  -0.0858 S32:  -0.1429 S33:   0.0000                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 1419:1444)                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.0766  27.1070  78.7215              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3474 T22:   0.4350                                     
REMARK   3      T33:   0.3964 T12:   0.0066                                     
REMARK   3      T13:   0.0218 T23:   0.0470                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.1975 L22:   0.5425                                     
REMARK   3      L33:  -0.0958 L12:   0.3400                                     
REMARK   3      L13:  -0.3810 L23:  -0.1857                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2146 S12:  -0.0317 S13:  -0.0965                       
REMARK   3      S21:  -0.1417 S22:  -0.2433 S23:  -0.0618                       
REMARK   3      S31:  -0.1838 S32:  -0.1051 S33:   0.0000                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 1445:1506)                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.2470  20.9888  95.2096              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2782 T22:   0.2861                                     
REMARK   3      T33:   0.3698 T12:   0.0415                                     
REMARK   3      T13:  -0.0011 T23:   0.0584                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4924 L22:   0.8446                                     
REMARK   3      L33:  -0.2399 L12:  -0.0206                                     
REMARK   3      L13:  -0.2501 L23:  -0.0302                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0468 S12:  -0.1125 S13:  -0.1687                       
REMARK   3      S21:  -0.0098 S22:  -0.0096 S23:  -0.0470                       
REMARK   3      S31:  -0.0612 S32:  -0.0745 S33:  -0.0000                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 1507:1620)                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.7071  44.2425  97.4096              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4721 T22:   0.3879                                     
REMARK   3      T33:   0.4390 T12:  -0.1119                                     
REMARK   3      T13:   0.0051 T23:   0.0422                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5706 L22:   0.8441                                     
REMARK   3      L33:   1.4817 L12:  -0.7131                                     
REMARK   3      L13:  -0.1256 L23:   0.8755                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1043 S12:  -0.1012 S13:   0.0586                       
REMARK   3      S21:  -0.0481 S22:  -0.0211 S23:  -0.1947                       
REMARK   3      S31:  -0.5126 S32:   0.0323 S33:   0.0000                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID -2:31)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.9572  46.3279 141.4345              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3385 T22:   0.4512                                     
REMARK   3      T33:   0.3863 T12:   0.0508                                     
REMARK   3      T13:  -0.0088 T23:  -0.0225                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0230 L22:   0.7119                                     
REMARK   3      L33:  -0.1497 L12:   0.3696                                     
REMARK   3      L13:   0.0444 L23:   0.0394                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0969 S12:  -0.2781 S13:  -0.1714                       
REMARK   3      S21:  -0.2632 S22:  -0.0874 S23:  -0.0590                       
REMARK   3      S31:  -0.1430 S32:  -0.1434 S33:  -0.0000                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 32:38)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.9303  35.7656 138.6708              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6926 T22:   0.5736                                     
REMARK   3      T33:   0.4990 T12:  -0.1769                                     
REMARK   3      T13:   0.0128 T23:  -0.1494                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0376 L22:   0.0130                                     
REMARK   3      L33:  -0.0093 L12:   0.1199                                     
REMARK   3      L13:  -0.0127 L23:   0.0941                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2619 S12:   0.0718 S13:   0.4757                       
REMARK   3      S21:  -0.6713 S22:  -0.0217 S23:   0.3131                       
REMARK   3      S31:  -0.3709 S32:  -0.0034 S33:   0.0000                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 39:55)                              
REMARK   3    ORIGIN FOR THE GROUP (A): -13.0462  48.6582 149.5749              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4622 T22:   0.4171                                     
REMARK   3      T33:   0.4852 T12:  -0.0131                                     
REMARK   3      T13:   0.0357 T23:  -0.0159                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0371 L22:  -0.0314                                     
REMARK   3      L33:  -0.0114 L12:   0.1159                                     
REMARK   3      L13:  -0.1083 L23:   0.1498                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2542 S12:   0.0029 S13:  -0.0891                       
REMARK   3      S21:  -0.3583 S22:   0.6050 S23:  -0.1551                       
REMARK   3      S31:  -0.5083 S32:  -0.0692 S33:  -0.0000                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 56:76)                              
REMARK   3    ORIGIN FOR THE GROUP (A): -21.5908  41.3710 131.9070              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5095 T22:   0.5909                                     
REMARK   3      T33:   0.3777 T12:  -0.0207                                     
REMARK   3      T13:  -0.0082 T23:  -0.0680                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2880 L22:   0.2363                                     
REMARK   3      L33:   0.1498 L12:  -0.0038                                     
REMARK   3      L13:   0.0875 L23:  -0.2399                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1051 S12:   0.1263 S13:   0.1740                       
REMARK   3      S21:   0.2112 S22:  -0.0649 S23:  -0.3416                       
REMARK   3      S31:   0.2374 S32:  -0.5688 S33:  -0.0000                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 77:119)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -15.9195  53.1333 128.9203              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5332 T22:   0.4202                                     
REMARK   3      T33:   0.4180 T12:   0.0780                                     
REMARK   3      T13:  -0.0296 T23:   0.0207                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1087 L22:   0.0343                                     
REMARK   3      L33:   0.5136 L12:  -0.1594                                     
REMARK   3      L13:  -0.0771 L23:   0.2335                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0657 S12:  -0.1542 S13:   0.1600                       
REMARK   3      S21:  -0.2959 S22:   0.0288 S23:  -0.0379                       
REMARK   3      S31:  -0.6449 S32:  -0.1030 S33:  -0.0000                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 120:177)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.0282  57.6936 130.3122              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6951 T22:   0.3769                                     
REMARK   3      T33:   0.4135 T12:   0.0378                                     
REMARK   3      T13:  -0.0082 T23:   0.0274                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0006 L22:   0.2498                                     
REMARK   3      L33:   0.6147 L12:   0.6061                                     
REMARK   3      L13:   0.2839 L23:   0.2043                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0295 S12:   0.0060 S13:   0.1083                       
REMARK   3      S21:  -0.2062 S22:   0.0203 S23:   0.0230                       
REMARK   3      S31:  -0.6395 S32:   0.1038 S33:  -0.0000                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID -3:2)                               
REMARK   3    ORIGIN FOR THE GROUP (A): -12.0945  43.0114  75.0918              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0151 T22:   0.5129                                     
REMARK   3      T33:   0.4529 T12:   0.1626                                     
REMARK   3      T13:   0.1037 T23:   0.0093                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0591 L22:  -0.0569                                     
REMARK   3      L33:  -0.0056 L12:  -0.0564                                     
REMARK   3      L13:  -0.0064 L23:  -0.0071                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5236 S12:  -0.0765 S13:   0.1039                       
REMARK   3      S21:   0.4715 S22:   0.3933 S23:   0.3951                       
REMARK   3      S31:  -0.2959 S32:  -0.4060 S33:  -0.0000                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 3:30)                               
REMARK   3    ORIGIN FOR THE GROUP (A): -12.6618  34.7770  99.1324              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4232 T22:   0.4431                                     
REMARK   3      T33:   0.4190 T12:   0.0751                                     
REMARK   3      T13:  -0.0124 T23:   0.0319                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5033 L22:   0.3651                                     
REMARK   3      L33:  -0.0744 L12:   0.2193                                     
REMARK   3      L13:  -0.1046 L23:  -0.1295                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2490 S12:   0.0811 S13:  -0.0505                       
REMARK   3      S21:   0.0794 S22:  -0.1788 S23:  -0.0484                       
REMARK   3      S31:  -0.0958 S32:   0.1556 S33:  -0.0000                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 31:38)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.8746  31.5732 101.1377              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6461 T22:   0.5805                                     
REMARK   3      T33:   0.5377 T12:  -0.0603                                     
REMARK   3      T13:  -0.0136 T23:  -0.0244                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0920 L22:   0.0417                                     
REMARK   3      L33:   0.0537 L12:  -0.0594                                     
REMARK   3      L13:   0.0492 L23:  -0.0207                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0890 S12:  -0.1796 S13:   0.1383                       
REMARK   3      S21:   0.1198 S22:  -0.3432 S23:   0.7130                       
REMARK   3      S31:  -0.0624 S32:  -0.0635 S33:  -0.0000                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 39:73)                              
REMARK   3    ORIGIN FOR THE GROUP (A): -11.5837  44.2161  97.2123              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4228 T22:   0.3626                                     
REMARK   3      T33:   0.3592 T12:   0.0374                                     
REMARK   3      T13:   0.0086 T23:   0.0501                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5079 L22:   0.6665                                     
REMARK   3      L33:   0.1824 L12:   0.2534                                     
REMARK   3      L13:  -0.3191 L23:  -0.4724                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1707 S12:  -0.0294 S13:  -0.1432                       
REMARK   3      S21:   0.1974 S22:  -0.0475 S23:  -0.0650                       
REMARK   3      S31:  -0.3277 S32:  -0.0652 S33:  -0.0000                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 74:116)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -21.7609  44.9653 104.4806              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5120 T22:   0.5306                                     
REMARK   3      T33:   0.4710 T12:   0.1381                                     
REMARK   3      T13:   0.0240 T23:  -0.0636                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3307 L22:   0.0924                                     
REMARK   3      L33:   0.4698 L12:   0.4564                                     
REMARK   3      L13:  -0.5710 L23:   0.9038                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0877 S12:  -0.1906 S13:   0.0028                       
REMARK   3      S21:  -0.1969 S22:  -0.0704 S23:   0.0422                       
REMARK   3      S31:  -0.4230 S32:  -0.3906 S33:   0.0000                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 117:177)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -25.1101  32.3633 105.4195              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3260 T22:   0.5001                                     
REMARK   3      T33:   0.3822 T12:   0.0432                                     
REMARK   3      T13:   0.0588 T23:  -0.0162                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2334 L22:   0.6386                                     
REMARK   3      L33:   0.2617 L12:   0.4859                                     
REMARK   3      L13:   0.6308 L23:   0.6969                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0455 S12:   0.0121 S13:  -0.0253                       
REMARK   3      S21:  -0.0853 S22:  -0.1418 S23:   0.1086                       
REMARK   3      S31:   0.1068 S32:  -0.2844 S33:  -0.0000                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 2                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 1197:1256 OR RESSEQ     
REMARK   3                          1271:1450 OR RESSEQ 1452:1620 )             
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 1197:1256 OR RESSEQ     
REMARK   3                          1271:1450 OR RESSEQ 1452:1620 )             
REMARK   3     ATOM PAIRS NUMBER  : 3314                                        
REMARK   3     RMSD               : 0.567                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN C AND (RESSEQ 1:177 )                 
REMARK   3     SELECTION          : CHAIN D AND (RESSEQ 1:177 )                 
REMARK   3     ATOM PAIRS NUMBER  : 1378                                        
REMARK   3     RMSD               : 0.405                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: RESIDUES 1257-1270 ARE DISORDERED.        
REMARK   4                                                                      
REMARK   4 2YIN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-MAY-11.                  
REMARK 100 THE PDBE ID CODE IS EBI-48298.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-JAN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.90000                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43702                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.70                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 78.18                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.4                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.2                               
REMARK 200  DATA REDUNDANCY                : 2.6                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.70                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.5                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.61                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.50                               
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: CHAIN A OF PDB ENTRY 1GAF AND CHAIN A OF             
REMARK 200  PDB ENTRY 1MH1                                                      
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5, 12% (W/V) PEG          
REMARK 280  3350, 10% (V/V) GLYCEROL AND 150 MM NACL. AT 20 C                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       49.30500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
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: 3720 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3710 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.5 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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  1187                                                      
REMARK 465     GLU A  1188                                                      
REMARK 465     CYS A  1189                                                      
REMARK 465     GLY A  1190                                                      
REMARK 465     ASP A  1191                                                      
REMARK 465     MET A  1192                                                      
REMARK 465     THR A  1193                                                      
REMARK 465     ASP A  1194                                                      
REMARK 465     GLU A  1195                                                      
REMARK 465     GLN A  1257                                                      
REMARK 465     CYS A  1258                                                      
REMARK 465     ALA A  1259                                                      
REMARK 465     SER A  1260                                                      
REMARK 465     GLN A  1261                                                      
REMARK 465     VAL A  1262                                                      
REMARK 465     MET A  1263                                                      
REMARK 465     GLN A  1264                                                      
REMARK 465     THR A  1265                                                      
REMARK 465     GLY A  1266                                                      
REMARK 465     GLN A  1267                                                      
REMARK 465     GLN A  1268                                                      
REMARK 465     HIS A  1269                                                      
REMARK 465     PRO A  1270                                                      
REMARK 465     GLU A  1621                                                      
REMARK 465     MET A  1622                                                      
REMARK 465     GLY B  1187                                                      
REMARK 465     GLU B  1188                                                      
REMARK 465     CYS B  1189                                                      
REMARK 465     GLY B  1190                                                      
REMARK 465     ASP B  1191                                                      
REMARK 465     MET B  1192                                                      
REMARK 465     THR B  1193                                                      
REMARK 465     ASP B  1194                                                      
REMARK 465     GLU B  1195                                                      
REMARK 465     SER B  1196                                                      
REMARK 465     GLN B  1257                                                      
REMARK 465     CYS B  1258                                                      
REMARK 465     ALA B  1259                                                      
REMARK 465     SER B  1260                                                      
REMARK 465     GLN B  1261                                                      
REMARK 465     VAL B  1262                                                      
REMARK 465     MET B  1263                                                      
REMARK 465     GLN B  1264                                                      
REMARK 465     THR B  1265                                                      
REMARK 465     GLY B  1266                                                      
REMARK 465     GLN B  1267                                                      
REMARK 465     GLN B  1268                                                      
REMARK 465     HIS B  1269                                                      
REMARK 465     PRO B  1270                                                      
REMARK 465     GLU B  1621                                                      
REMARK 465     MET B  1622                                                      
REMARK 465     MET C   -18                                                      
REMARK 465     ALA C   -17                                                      
REMARK 465     HIS C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     HIS C   -11                                                      
REMARK 465     SER C   -10                                                      
REMARK 465     SER C    -9                                                      
REMARK 465     GLY C    -8                                                      
REMARK 465     LEU C    -7                                                      
REMARK 465     GLU C    -6                                                      
REMARK 465     VAL C    -5                                                      
REMARK 465     LEU C    -4                                                      
REMARK 465     PHE C    -3                                                      
REMARK 465     MET D   -18                                                      
REMARK 465     ALA D   -17                                                      
REMARK 465     HIS D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     HIS D   -11                                                      
REMARK 465     SER D   -10                                                      
REMARK 465     SER D    -9                                                      
REMARK 465     GLY D    -8                                                      
REMARK 465     LEU D    -7                                                      
REMARK 465     GLU D    -6                                                      
REMARK 465     VAL D    -5                                                      
REMARK 465     LEU D    -4                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A1420    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1422    CG   CD   CE   NZ                                   
REMARK 470     ARG A1449    NE   CZ   NH1  NH2                                  
REMARK 470     ARG A1450    NE   CZ   NH1  NH2                                  
REMARK 470     THR A1452    OG1  CG2                                            
REMARK 470     GLU A1465    CD   OE1  OE2                                       
REMARK 470     LYS A1548    CG   CD   CE   NZ                                   
REMARK 470     LYS A1570    CG   CD   CE   NZ                                   
REMARK 470     LYS A1585    CE   NZ                                             
REMARK 470     LYS A1589    CD   CE   NZ                                        
REMARK 470     ARG A1590    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A1596    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1607    CG   CD   CE   NZ                                   
REMARK 470     LYS A1615    CG   CD   CE   NZ                                   
REMARK 470     ARG A1620    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B1197    CG   CD   CE   NZ                                   
REMARK 470     ARG B1200    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B1212    CD   CE   NZ                                        
REMARK 470     ARG B1216    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B1222    NE   CZ   NH1  NH2                                  
REMARK 470     LYS B1226    CE   NZ                                             
REMARK 470     LYS B1290    CE   NZ                                             
REMARK 470     GLU B1417    CD   OE1  OE2                                       
REMARK 470     ARG B1420    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B1422    CG   CD   CE   NZ                                   
REMARK 470     ARG B1449    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B1450    NE   CZ   NH1  NH2                                  
REMARK 470     GLU B1465    CD   OE1  OE2                                       
REMARK 470     LYS B1548    CG   CD   CE   NZ                                   
REMARK 470     ARG B1557    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B1563    CG   CD   OE1  NE2                                  
REMARK 470     LYS B1570    CG   CD   CE   NZ                                   
REMARK 470     LYS B1585    CG   CD   CE   NZ                                   
REMARK 470     LYS B1589    NZ                                                  
REMARK 470     ARG B1601    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B1610    CE   NZ                                             
REMARK 470     LYS B1612    CD   CE   NZ                                        
REMARK 470     LYS B1615    CG   CD   CE   NZ                                   
REMARK 470     ARG B1620    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C  -2    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 130    NZ                                                  
REMARK 470     LYS D 133    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A1554   CB    GLU A1554   CG     -0.201                       
REMARK 500    GLU A1554   CD    GLU A1554   OE2     0.089                       
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    GLU A1554   CG  -  CD  -  OE2 ANGL. DEV. = -15.2 DEGREES          
REMARK 500    PRO B1419   CB  -  CA  -  C   ANGL. DEV. = -19.7 DEGREES          
REMARK 500    PRO B1560   C   -  N   -  CD  ANGL. DEV. = -18.3 DEGREES          
REMARK 500    ASP C  38   N   -  CA  -  C   ANGL. DEV. =  19.4 DEGREES          
REMARK 500    ASP D  38   N   -  CA  -  C   ANGL. DEV. =  17.0 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    ILE A1312        0.47   -151.84                                   
REMARK 500    TYR A1368       14.88     58.76                                   
REMARK 500    TYR A1438       32.26     70.23                                   
REMARK 500    ARG A1450      -76.23   -106.78                                   
REMARK 500    ASN B1215       97.53    -62.41                                   
REMARK 500    LYS B1292       39.06     78.38                                   
REMARK 500    MET B1293       68.40   -106.43                                   
REMARK 500    TYR B1368       14.78     58.92                                   
REMARK 500    SER B1518      -75.57    -76.98                                   
REMARK 500    ASN C  26       52.21     39.63                                   
REMARK 500    GLN C  61      170.66    -58.82                                   
REMARK 500    GLN C 162        5.33     80.07                                   
REMARK 500    GLN D  -2        6.64     87.71                                   
REMARK 500    GLN D  74        0.41     86.62                                   
REMARK 500    ARG D 120      -12.82    -48.10                                   
REMARK 500    GLN D 162       -7.98     80.62                                   
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 C  38        22.8      L          L   OUTSIDE RANGE           
REMARK 500    ASN C  39        24.7      L          L   OUTSIDE RANGE           
REMARK 500    ASP D  38        22.3      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  6-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700                                                                      
REMARK 700 THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  6-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VRW   RELATED DB: PDB                                   
REMARK 900  CRITICAL STRUCTURAL ROLE FOR THE PH AND C1 DOMAINS                  
REMARK 900  OF THE VAV1 EXCHANGE FACTOR                                         
REMARK 900 RELATED ID: 1E96   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE RAC/P67PHOX COMPLEX                                
REMARK 900 RELATED ID: 1I4D   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE ANALYSIS OF RAC1-GDP COMPLEXED                    
REMARK 900  WITHARFAPTIN (P21)                                                  
REMARK 900 RELATED ID: 1FOE   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF RAC1 IN COMPLEX WITH THE                       
REMARK 900  GUANINENUCLEOTIDE EXCHANGE REGION OF TIAM1                          
REMARK 900 RELATED ID: 1MH1   RELATED DB: PDB                                   
REMARK 900  SMALL G-PROTEIN                                                     
REMARK 900 RELATED ID: 1I4L   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE ANALYSIS OF RAC1-GDP IN COMPLEX                   
REMARK 900  WITHARFAPTIN (P41)                                                  
REMARK 900 RELATED ID: 1HE1   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE GAP                    
REMARK 900  DOMAIN OF THE PSEUDOMONAS AERUGINOSA EXOS TOXIN AND                 
REMARK 900  HUMAN RAC                                                           
REMARK 900 RELATED ID: 1RYF   RELATED DB: PDB                                   
REMARK 900  ALTERNATIVE SPLICING OF RAC1 GENERATES RAC1B, A SELF-               
REMARK 900  ACTIVATING GTPASE                                                   
REMARK 900 RELATED ID: 2WKQ   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF A PHOTOACTIVATABLE RAC1 CONTAINING THE LOV2            
REMARK 900   C450A MUTANT                                                       
REMARK 900 RELATED ID: 1RYH   RELATED DB: PDB                                   
REMARK 900  ALTERNATIVE SPLICING OF RAC1 GENERATES RAC1B, A SELF-               
REMARK 900  ACTIVATING GTPASE                                                   
REMARK 900 RELATED ID: 1HH4   RELATED DB: PDB                                   
REMARK 900  RAC1-RHOGDI COMPLEX INVOLVED IN NADPH OXIDASE ACTIVATION            
REMARK 900 RELATED ID: 2WKR   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF A PHOTOACTIVATABLE RAC1 CONTAINING THE LOV2            
REMARK 900   C450M MUTANT                                                       
REMARK 900 RELATED ID: 2WKP   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF A PHOTOACTIVATABLE RAC1 CONTAINING LOV2                
REMARK 900  WILDTYPE                                                            
REMARK 900 RELATED ID: 2FJU   RELATED DB: PDB                                   
REMARK 900  ACTIVATED RAC1 BOUND TO ITS EFFECTOR PHOSPHOLIPASE C                
REMARK 900  BETA 2                                                              
REMARK 900 RELATED ID: 1G4U   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE SALMONELLA TYROSINE                        
REMARK 900  PHOSPHATASEAND GTPASE ACTIVATING PROTEIN SPTP BOUND TO              
REMARK 900  RAC1                                                                
REMARK 900 RELATED ID: 1I4T   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE ANALYSIS OF RAC1-GMPPNP IN COMPLEX                
REMARK 900  WITHARFAPTIN                                                        
DBREF  2YIN A 1192  1622  UNP    Q92608   DOCK2_HUMAN   1192   1622             
DBREF  2YIN B 1192  1622  UNP    Q92608   DOCK2_HUMAN   1192   1622             
DBREF  2YIN C    1   177  UNP    P63000   RAC1_HUMAN       1    177             
DBREF  2YIN D    1   177  UNP    P63000   RAC1_HUMAN       1    177             
SEQADV 2YIN GLY A 1187  UNP  Q92608              EXPRESSION TAG                 
SEQADV 2YIN GLU A 1188  UNP  Q92608              EXPRESSION TAG                 
SEQADV 2YIN CYS A 1189  UNP  Q92608              EXPRESSION TAG                 
SEQADV 2YIN GLY A 1190  UNP  Q92608              EXPRESSION TAG                 
SEQADV 2YIN ASP A 1191  UNP  Q92608              EXPRESSION TAG                 
SEQADV 2YIN GLY B 1187  UNP  Q92608              EXPRESSION TAG                 
SEQADV 2YIN GLU B 1188  UNP  Q92608              EXPRESSION TAG                 
SEQADV 2YIN CYS B 1189  UNP  Q92608              EXPRESSION TAG                 
SEQADV 2YIN GLY B 1190  UNP  Q92608              EXPRESSION TAG                 
SEQADV 2YIN ASP B 1191  UNP  Q92608              EXPRESSION TAG                 
SEQADV 2YIN MET C  -18  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN ALA C  -17  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN HIS C  -16  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN HIS C  -15  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN HIS C  -14  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN HIS C  -13  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN HIS C  -12  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN HIS C  -11  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN SER C  -10  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN SER C   -9  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN GLY C   -8  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN LEU C   -7  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN GLU C   -6  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN VAL C   -5  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN LEU C   -4  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN PHE C   -3  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN GLN C   -2  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN GLY C   -1  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN THR C    0  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN MET D  -18  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN ALA D  -17  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN HIS D  -16  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN HIS D  -15  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN HIS D  -14  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN HIS D  -13  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN HIS D  -12  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN HIS D  -11  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN SER D  -10  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN SER D   -9  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN GLY D   -8  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN LEU D   -7  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN GLU D   -6  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN VAL D   -5  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN LEU D   -4  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN PHE D   -3  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN GLN D   -2  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN GLY D   -1  UNP  P63000              EXPRESSION TAG                 
SEQADV 2YIN THR D    0  UNP  P63000              EXPRESSION TAG                 
SEQRES   1 A  436  GLY GLU CYS GLY ASP MET THR ASP GLU SER LYS ASP ASN          
SEQRES   2 A  436  ARG MET SER CYS THR VAL ASN LEU LEU ASN PHE TYR LYS          
SEQRES   3 A  436  ASP ASN ASN ARG GLU GLU MET TYR ILE ARG TYR LEU TYR          
SEQRES   4 A  436  LYS LEU ARG ASP LEU HIS LEU ASP CYS ASP ASN TYR THR          
SEQRES   5 A  436  GLU ALA ALA TYR THR LEU LEU LEU HIS THR TRP LEU LEU          
SEQRES   6 A  436  LYS TRP SER ASP GLU GLN CYS ALA SER GLN VAL MET GLN          
SEQRES   7 A  436  THR GLY GLN GLN HIS PRO GLN THR HIS ARG GLN LEU LYS          
SEQRES   8 A  436  GLU THR LEU TYR GLU THR ILE ILE GLY TYR PHE ASP LYS          
SEQRES   9 A  436  GLY LYS MET TRP GLU GLU ALA ILE SER LEU CYS LYS GLU          
SEQRES  10 A  436  LEU ALA GLU GLN TYR GLU MET GLU ILE PHE ASP TYR GLU          
SEQRES  11 A  436  LEU LEU SER GLN ASN LEU ILE GLN GLN ALA LYS PHE TYR          
SEQRES  12 A  436  GLU SER ILE MET LYS ILE LEU ARG PRO LYS PRO ASP TYR          
SEQRES  13 A  436  PHE ALA VAL GLY TYR TYR GLY GLN GLY PHE PRO SER PHE          
SEQRES  14 A  436  LEU ARG ASN LYS VAL PHE ILE TYR ARG GLY LYS GLU TYR          
SEQRES  15 A  436  GLU ARG ARG GLU ASP PHE GLN MET GLN LEU MET THR GLN          
SEQRES  16 A  436  PHE PRO ASN ALA GLU LYS MET ASN THR THR SER ALA PRO          
SEQRES  17 A  436  GLY ASP ASP VAL LYS ASN ALA PRO GLY GLN TYR ILE GLN          
SEQRES  18 A  436  CYS PHE THR VAL GLN PRO VAL LEU ASP GLU HIS PRO ARG          
SEQRES  19 A  436  PHE LYS ASN LYS PRO VAL PRO ASP GLN ILE ILE ASN PHE          
SEQRES  20 A  436  TYR LYS SER ASN TYR VAL GLN ARG PHE HIS TYR SER ARG          
SEQRES  21 A  436  PRO VAL ARG ARG GLY THR VAL ASP PRO GLU ASN GLU PHE          
SEQRES  22 A  436  ALA SER MET TRP ILE GLU ARG THR SER PHE VAL THR ALA          
SEQRES  23 A  436  TYR LYS LEU PRO GLY ILE LEU ARG TRP PHE GLU VAL VAL          
SEQRES  24 A  436  HIS MET SER GLN THR THR ILE SER PRO LEU GLU ASN ALA          
SEQRES  25 A  436  ILE GLU THR MET SER THR ALA ASN GLU LYS ILE LEU MET          
SEQRES  26 A  436  MET ILE ASN GLN TYR GLN SER ASP GLU THR LEU PRO ILE          
SEQRES  27 A  436  ASN PRO LEU SER MET LEU LEU ASN GLY ILE VAL ASP PRO          
SEQRES  28 A  436  ALA VAL MET GLY GLY PHE ALA LYS TYR GLU LYS ALA PHE          
SEQRES  29 A  436  PHE THR GLU GLU TYR VAL ARG ASP HIS PRO GLU ASP GLN          
SEQRES  30 A  436  ASP LYS LEU THR HIS LEU LYS ASP LEU ILE ALA TRP GLN          
SEQRES  31 A  436  ILE PRO PHE LEU GLY ALA GLY ILE LYS ILE HIS GLU LYS          
SEQRES  32 A  436  ARG VAL SER ASP ASN LEU ARG PRO PHE HIS ASP ARG MET          
SEQRES  33 A  436  GLU GLU CYS PHE LYS ASN LEU LYS MET LYS VAL GLU LYS          
SEQRES  34 A  436  GLU TYR GLY VAL ARG GLU MET                                  
SEQRES   1 B  436  GLY GLU CYS GLY ASP MET THR ASP GLU SER LYS ASP ASN          
SEQRES   2 B  436  ARG MET SER CYS THR VAL ASN LEU LEU ASN PHE TYR LYS          
SEQRES   3 B  436  ASP ASN ASN ARG GLU GLU MET TYR ILE ARG TYR LEU TYR          
SEQRES   4 B  436  LYS LEU ARG ASP LEU HIS LEU ASP CYS ASP ASN TYR THR          
SEQRES   5 B  436  GLU ALA ALA TYR THR LEU LEU LEU HIS THR TRP LEU LEU          
SEQRES   6 B  436  LYS TRP SER ASP GLU GLN CYS ALA SER GLN VAL MET GLN          
SEQRES   7 B  436  THR GLY GLN GLN HIS PRO GLN THR HIS ARG GLN LEU LYS          
SEQRES   8 B  436  GLU THR LEU TYR GLU THR ILE ILE GLY TYR PHE ASP LYS          
SEQRES   9 B  436  GLY LYS MET TRP GLU GLU ALA ILE SER LEU CYS LYS GLU          
SEQRES  10 B  436  LEU ALA GLU GLN TYR GLU MET GLU ILE PHE ASP TYR GLU          
SEQRES  11 B  436  LEU LEU SER GLN ASN LEU ILE GLN GLN ALA LYS PHE TYR          
SEQRES  12 B  436  GLU SER ILE MET LYS ILE LEU ARG PRO LYS PRO ASP TYR          
SEQRES  13 B  436  PHE ALA VAL GLY TYR TYR GLY GLN GLY PHE PRO SER PHE          
SEQRES  14 B  436  LEU ARG ASN LYS VAL PHE ILE TYR ARG GLY LYS GLU TYR          
SEQRES  15 B  436  GLU ARG ARG GLU ASP PHE GLN MET GLN LEU MET THR GLN          
SEQRES  16 B  436  PHE PRO ASN ALA GLU LYS MET ASN THR THR SER ALA PRO          
SEQRES  17 B  436  GLY ASP ASP VAL LYS ASN ALA PRO GLY GLN TYR ILE GLN          
SEQRES  18 B  436  CYS PHE THR VAL GLN PRO VAL LEU ASP GLU HIS PRO ARG          
SEQRES  19 B  436  PHE LYS ASN LYS PRO VAL PRO ASP GLN ILE ILE ASN PHE          
SEQRES  20 B  436  TYR LYS SER ASN TYR VAL GLN ARG PHE HIS TYR SER ARG          
SEQRES  21 B  436  PRO VAL ARG ARG GLY THR VAL ASP PRO GLU ASN GLU PHE          
SEQRES  22 B  436  ALA SER MET TRP ILE GLU ARG THR SER PHE VAL THR ALA          
SEQRES  23 B  436  TYR LYS LEU PRO GLY ILE LEU ARG TRP PHE GLU VAL VAL          
SEQRES  24 B  436  HIS MET SER GLN THR THR ILE SER PRO LEU GLU ASN ALA          
SEQRES  25 B  436  ILE GLU THR MET SER THR ALA ASN GLU LYS ILE LEU MET          
SEQRES  26 B  436  MET ILE ASN GLN TYR GLN SER ASP GLU THR LEU PRO ILE          
SEQRES  27 B  436  ASN PRO LEU SER MET LEU LEU ASN GLY ILE VAL ASP PRO          
SEQRES  28 B  436  ALA VAL MET GLY GLY PHE ALA LYS TYR GLU LYS ALA PHE          
SEQRES  29 B  436  PHE THR GLU GLU TYR VAL ARG ASP HIS PRO GLU ASP GLN          
SEQRES  30 B  436  ASP LYS LEU THR HIS LEU LYS ASP LEU ILE ALA TRP GLN          
SEQRES  31 B  436  ILE PRO PHE LEU GLY ALA GLY ILE LYS ILE HIS GLU LYS          
SEQRES  32 B  436  ARG VAL SER ASP ASN LEU ARG PRO PHE HIS ASP ARG MET          
SEQRES  33 B  436  GLU GLU CYS PHE LYS ASN LEU LYS MET LYS VAL GLU LYS          
SEQRES  34 B  436  GLU TYR GLY VAL ARG GLU MET                                  
SEQRES   1 C  196  MET ALA HIS HIS HIS HIS HIS HIS SER SER GLY LEU GLU          
SEQRES   2 C  196  VAL LEU PHE GLN GLY THR MET GLN ALA ILE LYS CYS VAL          
SEQRES   3 C  196  VAL VAL GLY ASP GLY ALA VAL GLY LYS THR CYS LEU LEU          
SEQRES   4 C  196  ILE SER TYR THR THR ASN ALA PHE PRO GLY GLU TYR ILE          
SEQRES   5 C  196  PRO THR VAL PHE ASP ASN TYR SER ALA ASN VAL MET VAL          
SEQRES   6 C  196  ASP GLY LYS PRO VAL ASN LEU GLY LEU TRP ASP THR ALA          
SEQRES   7 C  196  GLY GLN GLU ASP TYR ASP ARG LEU ARG PRO LEU SER TYR          
SEQRES   8 C  196  PRO GLN THR ASP VAL PHE LEU ILE CYS PHE SER LEU VAL          
SEQRES   9 C  196  SER PRO ALA SER PHE GLU ASN VAL ARG ALA LYS TRP TYR          
SEQRES  10 C  196  PRO GLU VAL ARG HIS HIS CYS PRO ASN THR PRO ILE ILE          
SEQRES  11 C  196  LEU VAL GLY THR LYS LEU ASP LEU ARG ASP ASP LYS ASP          
SEQRES  12 C  196  THR ILE GLU LYS LEU LYS GLU LYS LYS LEU THR PRO ILE          
SEQRES  13 C  196  THR TYR PRO GLN GLY LEU ALA MET ALA LYS GLU ILE GLY          
SEQRES  14 C  196  ALA VAL LYS TYR LEU GLU CYS SER ALA LEU THR GLN ARG          
SEQRES  15 C  196  GLY LEU LYS THR VAL PHE ASP GLU ALA ILE ARG ALA VAL          
SEQRES  16 C  196  LEU                                                          
SEQRES   1 D  196  MET ALA HIS HIS HIS HIS HIS HIS SER SER GLY LEU GLU          
SEQRES   2 D  196  VAL LEU PHE GLN GLY THR MET GLN ALA ILE LYS CYS VAL          
SEQRES   3 D  196  VAL VAL GLY ASP GLY ALA VAL GLY LYS THR CYS LEU LEU          
SEQRES   4 D  196  ILE SER TYR THR THR ASN ALA PHE PRO GLY GLU TYR ILE          
SEQRES   5 D  196  PRO THR VAL PHE ASP ASN TYR SER ALA ASN VAL MET VAL          
SEQRES   6 D  196  ASP GLY LYS PRO VAL ASN LEU GLY LEU TRP ASP THR ALA          
SEQRES   7 D  196  GLY GLN GLU ASP TYR ASP ARG LEU ARG PRO LEU SER TYR          
SEQRES   8 D  196  PRO GLN THR ASP VAL PHE LEU ILE CYS PHE SER LEU VAL          
SEQRES   9 D  196  SER PRO ALA SER PHE GLU ASN VAL ARG ALA LYS TRP TYR          
SEQRES  10 D  196  PRO GLU VAL ARG HIS HIS CYS PRO ASN THR PRO ILE ILE          
SEQRES  11 D  196  LEU VAL GLY THR LYS LEU ASP LEU ARG ASP ASP LYS ASP          
SEQRES  12 D  196  THR ILE GLU LYS LEU LYS GLU LYS LYS LEU THR PRO ILE          
SEQRES  13 D  196  THR TYR PRO GLN GLY LEU ALA MET ALA LYS GLU ILE GLY          
SEQRES  14 D  196  ALA VAL LYS TYR LEU GLU CYS SER ALA LEU THR GLN ARG          
SEQRES  15 D  196  GLY LEU LYS THR VAL PHE ASP GLU ALA ILE ARG ALA VAL          
SEQRES  16 D  196  LEU                                                          
FORMUL   5  HOH   *91(H2 O)                                                     
HELIX    1   1 SER A 1196  ASN A 1215  1                                  20    
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  LYS A 1292  1                                  21    
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  ALA A 1401  1                                   7    
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 ASN A 1457  SER A 1461  1                                   5    
HELIX   12  12 SER A 1493  ASP A 1519  1                                  27    
HELIX   13  13 ILE A 1524  ASP A 1536  1                                  13    
HELIX   14  14 PHE A 1543  PHE A 1551  1                                   9    
HELIX   15  15 THR A 1552  HIS A 1559  1                                   8    
HELIX   16  16 ASP A 1562  ARG A 1590  1                                  29    
HELIX   17  17 SER A 1592  ASN A 1594  5                                   3    
HELIX   18  18 LEU A 1595  GLY A 1618  1                                  24    
HELIX   19  19 LYS B 1197  ASN B 1214  1                                  18    
HELIX   20  20 ARG B 1216  ASP B 1235  1                                  20    
HELIX   21  21 ASN B 1236  TRP B 1249  1                                  14    
HELIX   22  22 THR B 1272  LYS B 1292  1                                  21    
HELIX   23  23 MET B 1293  GLU B 1311  1                                  19    
HELIX   24  24 ASP B 1314  ILE B 1335  1                                  22    
HELIX   25  25 ARG B 1370  PHE B 1382  1                                  13    
HELIX   26  26 GLY B 1395  ASN B 1400  1                                   6    
HELIX   27  27 PRO B 1427  SER B 1436  1                                  10    
HELIX   28  28 ASN B 1457  ALA B 1460  5                                   4    
HELIX   29  29 SER B 1493  ASP B 1519  1                                  27    
HELIX   30  30 ILE B 1524  ASP B 1536  1                                  13    
HELIX   31  31 PHE B 1543  PHE B 1551  1                                   9    
HELIX   32  32 THR B 1552  HIS B 1559  1                                   8    
HELIX   33  33 ASP B 1562  ARG B 1590  1                                  29    
HELIX   34  34 SER B 1592  ASN B 1594  5                                   3    
HELIX   35  35 LEU B 1595  TYR B 1617  1                                  23    
HELIX   36  36 ASP C   11  GLY C   15  5                                   5    
HELIX   37  37 LYS C   16  THR C   25  1                                  10    
HELIX   38  38 GLU C   62  ARG C   66  5                                   5    
HELIX   39  39 LEU C   67  TYR C   72  5                                   6    
HELIX   40  40 SER C   86  LYS C   96  1                                  11    
HELIX   41  41 LYS C   96  CYS C  105  1                                  10    
HELIX   42  42 ASP C  122  LYS C  132  1                                  11    
HELIX   43  43 THR C  138  GLY C  150  1                                  13    
HELIX   44  44 GLY C  164  ALA C  175  1                                  12    
HELIX   45  45 ASP D   11  VAL D   14  5                                   4    
HELIX   46  46 GLY D   15  THR D   25  1                                  11    
HELIX   47  47 GLN D   61  ARG D   66  5                                   6    
HELIX   48  48 LEU D   67  TYR D   72  5                                   6    
HELIX   49  49 SER D   86  LYS D   96  1                                  11    
HELIX   50  50 LYS D   96  CYS D  105  1                                  10    
HELIX   51  51 ASP D  118  ASP D  121  5                                   4    
HELIX   52  52 ASP D  122  LYS D  132  1                                  11    
HELIX   53  53 THR D  138  GLY D  150  1                                  13    
HELIX   54  54 GLY D  164  LEU D  177  1                                  14    
SHEET    1  AA 8 TYR A1342  TYR A1348  0                                        
SHEET    2  AA 8 TYR A1405  VAL A1414 -1  O  TYR A1405   N  TYR A1348           
SHEET    3  AA 8 VAL A1439  ARG A1449 -1  O  ARG A1441   N  VAL A1414           
SHEET    4  AA 8 MET A1462  LEU A1475 -1  O  TRP A1463   N  VAL A1448           
SHEET    5  AA 8 TRP A1481  ILE A1492 -1  O  GLU A1483   N  ALA A1472           
SHEET    6  AA 8 LYS A1359  ARG A1364 -1  O  VAL A1360   N  VAL A1484           
SHEET    7  AA 8 TYR A1342  TYR A1348  0                                        
SHEET    1  BA 8 TYR B1342  TYR B1347  0                                        
SHEET    2  BA 8 TYR B1405  PRO B1413 -1  O  GLN B1407   N  GLY B1346           
SHEET    3  BA 8 VAL B1439  ARG B1449 -1  O  HIS B1443   N  GLN B1412           
SHEET    4  BA 8 MET B1462  LEU B1475 -1  O  TRP B1463   N  VAL B1448           
SHEET    5  BA 8 TRP B1481  ILE B1492 -1  O  GLU B1483   N  ALA B1472           
SHEET    6  BA 8 LYS B1359  ARG B1364 -1  O  VAL B1360   N  VAL B1484           
SHEET    7  BA 8 TYR B1342  TYR B1347  0                                        
SHEET    1  CA 6 TYR C  40  VAL C  46  0                                        
SHEET    2  CA 6 LYS C  49  ASP C  57 -1  O  LYS C  49   N  VAL C  46           
SHEET    3  CA 6 GLN C   2  VAL C   9  1  O  GLN C   2   N  ASN C  52           
SHEET    4  CA 6 VAL C  77  SER C  83  1  O  VAL C  77   N  VAL C   7           
SHEET    5  CA 6 ILE C 110  THR C 115  1  O  ILE C 111   N  ILE C  80           
SHEET    6  CA 6 LYS C 153  GLU C 156  1  O  LYS C 153   N  LEU C 112           
SHEET    1  DA 6 TYR D  40  VAL D  46  0                                        
SHEET    2  DA 6 LYS D  49  ASP D  57 -1  O  LYS D  49   N  VAL D  46           
SHEET    3  DA 6 GLN D   2  VAL D   9  1  O  GLN D   2   N  ASN D  52           
SHEET    4  DA 6 VAL D  77  SER D  83  1  O  VAL D  77   N  VAL D   7           
SHEET    5  DA 6 ILE D 110  THR D 115  1  O  ILE D 111   N  ILE D  80           
SHEET    6  DA 6 LYS D 153  GLU D 156  1  O  LYS D 153   N  LEU D 112           
CISPEP   1 LEU A 1475    PRO A 1476          0         3.74                     
CISPEP   2 LEU B 1475    PRO B 1476          0         7.11                     
CRYST1   68.510   98.610  130.130  90.00  99.64  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014596  0.000000  0.002479        0.00000                         
SCALE2      0.000000  0.010141  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007795        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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