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Database: PDB
Entry: 5FI0
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HEADER    PROTEIN BINDING                         22-DEC-15   5FI0              
TITLE     CRYSTAL STRUCTURE OF THE P-REX1 DH/PH TANDEM IN COMPLEX WITH RAC1     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE-DEPENDENT RAC     
COMPND   3 EXCHANGER 1 PROTEIN,PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE-        
COMPND   4 DEPENDENT RAC EXCHANGER 1 PROTEIN;                                   
COMPND   5 CHAIN: A, C, E, G;                                                   
COMPND   6 SYNONYM: PTDINS(3,4,5)-DEPENDENT RAC EXCHANGER 1,PTDINS(3,4,5)-      
COMPND   7 DEPENDENT RAC EXCHANGER 1;                                           
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1;                
COMPND  11 CHAIN: B, D, F, H;                                                   
COMPND  12 SYNONYM: CELL MIGRATION-INDUCING GENE 5 PROTEIN,RAS-LIKE PROTEIN     
COMPND  13 TC25,P21-RAC1;                                                       
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PREX1, KIAA1415;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMALC2H10T;                               
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: RAC1, TC25, MIG5;                                              
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PMALC2H10T                                
KEYWDS    DBL HOMOLOGY DOMAIN, PLECKSTRIN HOMOLOGY DOMAIN, BETA SANDWICH, SMALL 
KEYWDS   2 GTPASE, PROTEIN BINDING                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.N.CASH,J.J.G.TESMER                                                 
REVDAT   4   20-SEP-17 5FI0    1       JRNL   REMARK                            
REVDAT   3   18-MAY-16 5FI0    1       JRNL                                     
REVDAT   2   27-APR-16 5FI0    1       JRNL                                     
REVDAT   1   20-APR-16 5FI0    0                                                
JRNL        AUTH   J.N.CASH,E.M.DAVIS,J.J.TESMER                                
JRNL        TITL   STRUCTURAL AND BIOCHEMICAL CHARACTERIZATION OF THE CATALYTIC 
JRNL        TITL 2 CORE OF THE METASTATIC FACTOR P-REX1 AND ITS REGULATION BY   
JRNL        TITL 3 PTDINS(3,4,5)P3.                                             
JRNL        REF    STRUCTURE                     V.  24   730 2016              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   27150042                                                     
JRNL        DOI    10.1016/J.STR.2016.02.022                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.28 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.28                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.85                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 42775                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.920                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2104                            
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 34.8487 -  8.0636    0.99     2974   150  0.1659 0.2003        
REMARK   3     2  8.0636 -  6.4134    1.00     2877   146  0.1974 0.2422        
REMARK   3     3  6.4134 -  5.6065    1.00     2813   162  0.2057 0.2355        
REMARK   3     4  5.6065 -  5.0956    1.00     2772   163  0.1800 0.2374        
REMARK   3     5  5.0956 -  4.7313    0.99     2803   153  0.1622 0.2182        
REMARK   3     6  4.7313 -  4.4530    1.00     2781   140  0.1629 0.2094        
REMARK   3     7  4.4530 -  4.2304    0.99     2763   134  0.1650 0.2194        
REMARK   3     8  4.2304 -  4.0465    0.99     2737   150  0.1811 0.2312        
REMARK   3     9  4.0465 -  3.8909    0.99     2739   134  0.1940 0.2391        
REMARK   3    10  3.8909 -  3.7568    0.98     2720   144  0.1969 0.2488        
REMARK   3    11  3.7568 -  3.6395    0.97     2690   133  0.2143 0.2418        
REMARK   3    12  3.6395 -  3.5356    0.96     2637   130  0.2233 0.2808        
REMARK   3    13  3.5356 -  3.4426    0.95     2639   127  0.2416 0.3150        
REMARK   3    14  3.4426 -  3.3586    0.94     2587   135  0.2559 0.3165        
REMARK   3    15  3.3586 -  3.2823    0.77     2139   103  0.2521 0.2473        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.850           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 67.13                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 81.26                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005          17048                                  
REMARK   3   ANGLE     :  1.048          23056                                  
REMARK   3   CHIRALITY :  0.044           2614                                  
REMARK   3   PLANARITY :  0.006           2945                                  
REMARK   3   DIHEDRAL  : 15.568           6429                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 0 THROUGH 244 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   2.2780  28.8447  93.4674              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2416 T22:   0.2582                                     
REMARK   3      T33:   0.3441 T12:   0.0719                                     
REMARK   3      T13:  -0.0594 T23:  -0.0333                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3231 L22:   3.9842                                     
REMARK   3      L33:   4.0787 L12:   1.5659                                     
REMARK   3      L13:  -0.0300 L23:  -0.9373                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0246 S12:   0.0865 S13:   0.1548                       
REMARK   3      S21:   0.2332 S22:  -0.1231 S23:   0.1192                       
REMARK   3      S31:   0.0575 S32:  -0.3002 S33:   0.1615                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 245 THROUGH 398 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.0550  28.3927 138.6826              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2530 T22:   1.2267                                     
REMARK   3      T33:   0.5749 T12:  -0.1392                                     
REMARK   3      T13:   0.0727 T23:  -0.0131                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0740 L22:   2.8918                                     
REMARK   3      L33:   2.5007 L12:  -1.6571                                     
REMARK   3      L13:  -0.5486 L23:  -0.6120                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5060 S12:  -0.7525 S13:   0.0179                       
REMARK   3      S21:   0.9898 S22:   0.1074 S23:  -0.1047                       
REMARK   3      S31:   0.3463 S32:  -0.1914 S33:   0.3545                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 3 THROUGH 178 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  16.4051   9.4457  96.6816              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2857 T22:   0.2644                                     
REMARK   3      T33:   0.3235 T12:   0.0071                                     
REMARK   3      T13:  -0.0944 T23:   0.0028                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1107 L22:   3.6600                                     
REMARK   3      L33:   3.6397 L12:  -0.9035                                     
REMARK   3      L13:   0.7799 L23:  -0.2075                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1338 S12:   0.0554 S13:  -0.1719                       
REMARK   3      S21:   0.0249 S22:  -0.1240 S23:  -0.1954                       
REMARK   3      S31:   0.1245 S32:   0.0788 S33:  -0.0701                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 38 THROUGH 244 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):   6.1998 -25.4032  92.8411              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2636 T22:   0.3287                                     
REMARK   3      T33:   0.5537 T12:   0.0223                                     
REMARK   3      T13:  -0.1358 T23:   0.0107                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1367 L22:   5.8333                                     
REMARK   3      L33:   3.2776 L12:   1.0333                                     
REMARK   3      L13:   0.1876 L23:  -0.3523                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1301 S12:  -0.1340 S13:   0.1735                       
REMARK   3      S21:  -0.0310 S22:  -0.0490 S23:   0.9058                       
REMARK   3      S31:   0.2642 S32:  -0.4239 S33:  -0.0275                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 245 THROUGH 399 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.7831 -28.1633 138.1471              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0667 T22:   1.6517                                     
REMARK   3      T33:   0.7671 T12:   0.0082                                     
REMARK   3      T13:   0.2090 T23:   0.0712                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2790 L22:   2.9761                                     
REMARK   3      L33:   3.1026 L12:  -1.6017                                     
REMARK   3      L13:  -0.7690 L23:   0.2620                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7398 S12:  -0.9929 S13:  -0.2447                       
REMARK   3      S21:   0.9076 S22:   0.6635 S23:   0.2941                       
REMARK   3      S31:  -0.1219 S32:   0.1701 S33:  -0.0570                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 2 THROUGH 179 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  23.0801 -42.7385  95.0577              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3626 T22:   0.3540                                     
REMARK   3      T33:   0.4797 T12:   0.0180                                     
REMARK   3      T13:  -0.1600 T23:   0.0509                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4866 L22:   3.5168                                     
REMARK   3      L33:   3.8241 L12:  -0.5301                                     
REMARK   3      L13:  -0.2522 L23:  -0.0350                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1175 S12:   0.0083 S13:  -0.1811                       
REMARK   3      S21:  -0.2137 S22:  -0.0864 S23:  -0.1488                       
REMARK   3      S31:   0.4070 S32:   0.3021 S33:  -0.0614                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'E' AND (RESID -2 THROUGH 244 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  36.1858  -1.1730 119.3713              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3684 T22:   0.4908                                     
REMARK   3      T33:   0.3926 T12:   0.0995                                     
REMARK   3      T13:  -0.1226 T23:  -0.0734                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8546 L22:   3.1987                                     
REMARK   3      L33:   5.5169 L12:  -0.7437                                     
REMARK   3      L13:   0.8295 L23:   0.0475                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2738 S12:  -0.3862 S13:   0.4217                       
REMARK   3      S21:   0.5806 S22:   0.0985 S23:  -0.0999                       
REMARK   3      S31:  -0.2600 S32:  -0.8734 S33:   0.1589                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 245 THROUGH 397 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  51.9606  -3.8412 161.0704              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8364 T22:   1.7931                                     
REMARK   3      T33:   0.8413 T12:  -0.2998                                     
REMARK   3      T13:  -0.5221 T23:  -0.0448                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3143 L22:   1.4769                                     
REMARK   3      L33:   2.0784 L12:   0.3545                                     
REMARK   3      L13:   1.0850 L23:  -1.1569                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4975 S12:  -1.3088 S13:  -0.0697                       
REMARK   3      S21:   1.3140 S22:  -0.7053 S23:  -0.5356                       
REMARK   3      S31:  -1.1746 S32:   0.3338 S33:   0.3071                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 1 THROUGH 181 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  40.8398 -24.9074 124.5481              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4791 T22:   0.3521                                     
REMARK   3      T33:   0.4959 T12:   0.0469                                     
REMARK   3      T13:  -0.0001 T23:   0.0242                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0823 L22:   8.0285                                     
REMARK   3      L33:   4.6660 L12:  -0.6302                                     
REMARK   3      L13:   0.2855 L23:   0.7555                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2095 S12:  -0.1673 S13:  -0.6356                       
REMARK   3      S21:   1.0388 S22:   0.1513 S23:   0.1839                       
REMARK   3      S31:   0.5135 S32:  -0.0678 S33:   0.1362                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'G' AND (RESID -2 THROUGH 244 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  38.4544 -53.3614 119.0110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5273 T22:   0.3548                                     
REMARK   3      T33:   0.4314 T12:   0.1236                                     
REMARK   3      T13:  -0.0468 T23:  -0.0609                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6665 L22:   4.1452                                     
REMARK   3      L33:   4.2419 L12:  -0.1826                                     
REMARK   3      L13:   0.3820 L23:  -0.6761                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1514 S12:  -0.0146 S13:   0.3231                       
REMARK   3      S21:   0.5083 S22:  -0.0919 S23:   0.0063                       
REMARK   3      S31:   0.1541 S32:  -0.1335 S33:   0.2340                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'G' AND (RESID 245 THROUGH 398 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  51.4466 -59.2131 161.5401              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.3939 T22:   1.4113                                     
REMARK   3      T33:   0.6523 T12:  -0.1825                                     
REMARK   3      T13:  -0.1862 T23:  -0.1257                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1032 L22:   3.5012                                     
REMARK   3      L33:   1.6947 L12:   0.3603                                     
REMARK   3      L13:  -0.5801 L23:  -0.6451                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2313 S12:  -0.8643 S13:   0.2051                       
REMARK   3      S21:   1.9308 S22:  -0.3329 S23:  -0.4381                       
REMARK   3      S31:  -1.7580 S32:   0.1878 S33:   0.3837                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 3 THROUGH 181 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  40.4859 -77.6755 122.7682              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8235 T22:   0.4300                                     
REMARK   3      T33:   0.5242 T12:   0.0026                                     
REMARK   3      T13:   0.2415 T23:  -0.0693                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8139 L22:   7.4254                                     
REMARK   3      L33:   3.7494 L12:  -1.2936                                     
REMARK   3      L13:  -0.2999 L23:   0.5519                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2788 S12:  -0.1331 S13:  -0.6107                       
REMARK   3      S21:   1.1990 S22:  -0.1497 S23:   0.9964                       
REMARK   3      S31:   0.7043 S32:  -0.3258 S33:   0.4802                       
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                                     
REMARK   3     SELECTION          : CHAIN C                                     
REMARK   3     ATOM PAIRS NUMBER  : 6761                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN E                                     
REMARK   3     ATOM PAIRS NUMBER  : 6761                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN G                                     
REMARK   3     ATOM PAIRS NUMBER  : 6761                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN B                                     
REMARK   3     SELECTION          : CHAIN D                                     
REMARK   3     ATOM PAIRS NUMBER  : 3390                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN B                                     
REMARK   3     SELECTION          : CHAIN F                                     
REMARK   3     ATOM PAIRS NUMBER  : 3390                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: CHAIN B                                     
REMARK   3     SELECTION          : CHAIN H                                     
REMARK   3     ATOM PAIRS NUMBER  : 3390                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5FI0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-DEC-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000216620.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-JUL-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.127                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000, SCALEPACK                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42862                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : 0.17300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.87000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2DFK AND 5D3W                                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM DIHYDROGEN PHOSPHATE, PEG 8000,   
REMARK 280  PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       40.68650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      161.78400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       53.52650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      161.78400            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       40.68650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       53.52650            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: 2880 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25370 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3000 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2620 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25860 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
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: 2790 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25860 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
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    -2                                                      
REMARK 465     GLU A    -1                                                      
REMARK 465     SER A   305                                                      
REMARK 465     ARG A   306                                                      
REMARK 465     VAL A   307                                                      
REMARK 465     THR A   308                                                      
REMARK 465     GLY A   309                                                      
REMARK 465     SER A   310                                                      
REMARK 465     LYS A   311                                                      
REMARK 465     LYS A   312                                                      
REMARK 465     SER A   313                                                      
REMARK 465     THR A   314                                                      
REMARK 465     LYS A   315                                                      
REMARK 465     ARG A   316                                                      
REMARK 465     THR A   317                                                      
REMARK 465     LYS A   318                                                      
REMARK 465     SER A   319                                                      
REMARK 465     ILE A   320                                                      
REMARK 465     ASN A   321                                                      
REMARK 465     GLY A   322                                                      
REMARK 465     LEU A   399                                                      
REMARK 465     GLY A   400                                                      
REMARK 465     MET A   401                                                      
REMARK 465     GLU A   402                                                      
REMARK 465     ARG A   403                                                      
REMARK 465     ASP A   404                                                      
REMARK 465     ALA A   405                                                      
REMARK 465     TYR A   406                                                      
REMARK 465     VAL A   407                                                      
REMARK 465     MET A   408                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     GLU B    -1                                                      
REMARK 465     PHE B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLN B     2                                                      
REMARK 465     PRO B   179                                                      
REMARK 465     PRO B   180                                                      
REMARK 465     PRO B   181                                                      
REMARK 465     VAL B   182                                                      
REMARK 465     LYS B   183                                                      
REMARK 465     LYS B   184                                                      
REMARK 465     ARG B   185                                                      
REMARK 465     LYS B   186                                                      
REMARK 465     ARG B   187                                                      
REMARK 465     LYS B   188                                                      
REMARK 465     CYS B   189                                                      
REMARK 465     LEU B   190                                                      
REMARK 465     LEU B   191                                                      
REMARK 465     LEU B   192                                                      
REMARK 465     GLY C    35                                                      
REMARK 465     GLU C    36                                                      
REMARK 465     PHE C    37                                                      
REMARK 465     SER C   305                                                      
REMARK 465     ARG C   306                                                      
REMARK 465     VAL C   307                                                      
REMARK 465     THR C   308                                                      
REMARK 465     GLY C   309                                                      
REMARK 465     SER C   310                                                      
REMARK 465     LYS C   311                                                      
REMARK 465     LYS C   312                                                      
REMARK 465     SER C   313                                                      
REMARK 465     THR C   314                                                      
REMARK 465     LYS C   315                                                      
REMARK 465     ARG C   316                                                      
REMARK 465     THR C   317                                                      
REMARK 465     LYS C   318                                                      
REMARK 465     SER C   319                                                      
REMARK 465     ILE C   320                                                      
REMARK 465     ASN C   321                                                      
REMARK 465     GLY C   322                                                      
REMARK 465     GLY C   400                                                      
REMARK 465     MET C   401                                                      
REMARK 465     GLU C   402                                                      
REMARK 465     ARG C   403                                                      
REMARK 465     ASP C   404                                                      
REMARK 465     ALA C   405                                                      
REMARK 465     TYR C   406                                                      
REMARK 465     VAL C   407                                                      
REMARK 465     MET C   408                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     GLU D    -1                                                      
REMARK 465     PHE D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     PRO D   180                                                      
REMARK 465     PRO D   181                                                      
REMARK 465     VAL D   182                                                      
REMARK 465     LYS D   183                                                      
REMARK 465     LYS D   184                                                      
REMARK 465     ARG D   185                                                      
REMARK 465     LYS D   186                                                      
REMARK 465     ARG D   187                                                      
REMARK 465     LYS D   188                                                      
REMARK 465     CYS D   189                                                      
REMARK 465     LEU D   190                                                      
REMARK 465     LEU D   191                                                      
REMARK 465     LEU D   192                                                      
REMARK 465     ARG E   181                                                      
REMARK 465     LYS E   182                                                      
REMARK 465     THR E   183                                                      
REMARK 465     THR E   184                                                      
REMARK 465     SER E   305                                                      
REMARK 465     ARG E   306                                                      
REMARK 465     VAL E   307                                                      
REMARK 465     THR E   308                                                      
REMARK 465     GLY E   309                                                      
REMARK 465     SER E   310                                                      
REMARK 465     LYS E   311                                                      
REMARK 465     LYS E   312                                                      
REMARK 465     SER E   313                                                      
REMARK 465     THR E   314                                                      
REMARK 465     LYS E   315                                                      
REMARK 465     ARG E   316                                                      
REMARK 465     THR E   317                                                      
REMARK 465     LYS E   318                                                      
REMARK 465     SER E   319                                                      
REMARK 465     ILE E   320                                                      
REMARK 465     ASN E   321                                                      
REMARK 465     GLY E   322                                                      
REMARK 465     LYS E   398                                                      
REMARK 465     LEU E   399                                                      
REMARK 465     GLY E   400                                                      
REMARK 465     MET E   401                                                      
REMARK 465     GLU E   402                                                      
REMARK 465     ARG E   403                                                      
REMARK 465     ASP E   404                                                      
REMARK 465     ALA E   405                                                      
REMARK 465     TYR E   406                                                      
REMARK 465     VAL E   407                                                      
REMARK 465     MET E   408                                                      
REMARK 465     GLY F    -2                                                      
REMARK 465     GLU F    -1                                                      
REMARK 465     PHE F     0                                                      
REMARK 465     VAL F   182                                                      
REMARK 465     LYS F   183                                                      
REMARK 465     LYS F   184                                                      
REMARK 465     ARG F   185                                                      
REMARK 465     LYS F   186                                                      
REMARK 465     ARG F   187                                                      
REMARK 465     LYS F   188                                                      
REMARK 465     CYS F   189                                                      
REMARK 465     LEU F   190                                                      
REMARK 465     LEU F   191                                                      
REMARK 465     LEU F   192                                                      
REMARK 465     SER G   305                                                      
REMARK 465     ARG G   306                                                      
REMARK 465     VAL G   307                                                      
REMARK 465     THR G   308                                                      
REMARK 465     GLY G   309                                                      
REMARK 465     SER G   310                                                      
REMARK 465     LYS G   311                                                      
REMARK 465     LYS G   312                                                      
REMARK 465     SER G   313                                                      
REMARK 465     THR G   314                                                      
REMARK 465     LYS G   315                                                      
REMARK 465     ARG G   316                                                      
REMARK 465     THR G   317                                                      
REMARK 465     LYS G   318                                                      
REMARK 465     SER G   319                                                      
REMARK 465     ILE G   320                                                      
REMARK 465     ASN G   321                                                      
REMARK 465     GLY G   322                                                      
REMARK 465     LEU G   399                                                      
REMARK 465     GLY G   400                                                      
REMARK 465     MET G   401                                                      
REMARK 465     GLU G   402                                                      
REMARK 465     ARG G   403                                                      
REMARK 465     ASP G   404                                                      
REMARK 465     ALA G   405                                                      
REMARK 465     TYR G   406                                                      
REMARK 465     VAL G   407                                                      
REMARK 465     MET G   408                                                      
REMARK 465     GLY H    -2                                                      
REMARK 465     GLU H    -1                                                      
REMARK 465     PHE H     0                                                      
REMARK 465     MET H     1                                                      
REMARK 465     GLN H     2                                                      
REMARK 465     VAL H   182                                                      
REMARK 465     LYS H   183                                                      
REMARK 465     LYS H   184                                                      
REMARK 465     ARG H   185                                                      
REMARK 465     LYS H   186                                                      
REMARK 465     ARG H   187                                                      
REMARK 465     LYS H   188                                                      
REMARK 465     CYS H   189                                                      
REMARK 465     LEU H   190                                                      
REMARK 465     LEU H   191                                                      
REMARK 465     LEU H   192                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH2  ARG F   102     O    THR F   108              2.11            
REMARK 500   OE1  GLU G    61     OH   TYR G   202              2.18            
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    LEU E  99   CA  -  CB  -  CG  ANGL. DEV. =  14.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 101     -132.93     45.10                                   
REMARK 500    LEU A 121       69.19   -100.90                                   
REMARK 500    ASP A 185     -168.68   -101.03                                   
REMARK 500    ASN A 296       -9.35     90.26                                   
REMARK 500    ARG A 328      -30.72   -133.77                                   
REMARK 500    VAL A 335       35.09    -98.66                                   
REMARK 500    ASN A 367       18.15     57.70                                   
REMARK 500    LEU B  84       -8.76    -59.50                                   
REMARK 500    SER C 101     -133.84     45.69                                   
REMARK 500    LEU C 121       67.03   -101.28                                   
REMARK 500    ASP C 185     -167.14   -100.81                                   
REMARK 500    SER C 282     -169.65    -74.24                                   
REMARK 500    ASN C 296       -8.68     88.97                                   
REMARK 500    ARG C 328      -32.07   -131.73                                   
REMARK 500    LYS C 366       11.74   -142.27                                   
REMARK 500    ASN C 367       17.12     56.76                                   
REMARK 500    ASP D  47     -108.63     59.75                                   
REMARK 500    LYS D  96      -50.85   -122.31                                   
REMARK 500    SER E 101     -135.22     46.37                                   
REMARK 500    LEU E 121       66.97   -101.99                                   
REMARK 500    ASN E 296      -12.14     88.87                                   
REMARK 500    ARG E 328      -33.78   -134.02                                   
REMARK 500    VAL E 335       34.67    -99.59                                   
REMARK 500    ASN E 367       15.48     56.63                                   
REMARK 500    LYS F  96      -53.71   -122.39                                   
REMARK 500    SER G 101     -134.40     46.21                                   
REMARK 500    LEU G 121       69.04   -101.37                                   
REMARK 500    ASP G 185     -167.03   -105.45                                   
REMARK 500    SER G 282     -168.04    -72.42                                   
REMARK 500    ASN G 296      -11.17     88.27                                   
REMARK 500    ARG G 328      -30.92   -132.54                                   
REMARK 500    VAL G 335       33.42    -97.44                                   
REMARK 500    LYS G 366       11.50   -140.60                                   
REMARK 500    ASN G 367       17.49     57.36                                   
REMARK 500    ASP H  47       -0.54     59.41                                   
REMARK 500    LYS H  96      -52.15   -124.08                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 E 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 G 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5FI1   RELATED DB: PDB                                   
DBREF  5FI0 A   38   201  UNP    Q8TCU6   PREX1_HUMAN     38    201             
DBREF  5FI0 A  202   408  UNP    Q8TCU6   PREX1_HUMAN    202    408             
DBREF  5FI0 B    1   192  UNP    P63000   RAC1_HUMAN       1    192             
DBREF  5FI0 C   38   201  UNP    Q8TCU6   PREX1_HUMAN     38    201             
DBREF  5FI0 C  202   408  UNP    Q8TCU6   PREX1_HUMAN    202    408             
DBREF  5FI0 D    1   192  UNP    P63000   RAC1_HUMAN       1    192             
DBREF  5FI0 E   38   201  UNP    Q8TCU6   PREX1_HUMAN     38    201             
DBREF  5FI0 E  202   408  UNP    Q8TCU6   PREX1_HUMAN    202    408             
DBREF  5FI0 F    1   192  UNP    P63000   RAC1_HUMAN       1    192             
DBREF  5FI0 G   38   201  UNP    Q8TCU6   PREX1_HUMAN     38    201             
DBREF  5FI0 G  202   408  UNP    Q8TCU6   PREX1_HUMAN    202    408             
DBREF  5FI0 H    1   192  UNP    P63000   RAC1_HUMAN       1    192             
SEQADV 5FI0 GLY A   -2  UNP  Q8TCU6              EXPRESSION TAG                 
SEQADV 5FI0 GLU A   -1  UNP  Q8TCU6              EXPRESSION TAG                 
SEQADV 5FI0 PHE A    0  UNP  Q8TCU6              EXPRESSION TAG                 
SEQADV 5FI0 GLY B   -2  UNP  P63000              EXPRESSION TAG                 
SEQADV 5FI0 GLU B   -1  UNP  P63000              EXPRESSION TAG                 
SEQADV 5FI0 PHE B    0  UNP  P63000              EXPRESSION TAG                 
SEQADV 5FI0 GLY C   35  UNP  Q8TCU6              EXPRESSION TAG                 
SEQADV 5FI0 GLU C   36  UNP  Q8TCU6              EXPRESSION TAG                 
SEQADV 5FI0 PHE C   37  UNP  Q8TCU6              EXPRESSION TAG                 
SEQADV 5FI0 GLY D   -2  UNP  P63000              EXPRESSION TAG                 
SEQADV 5FI0 GLU D   -1  UNP  P63000              EXPRESSION TAG                 
SEQADV 5FI0 PHE D    0  UNP  P63000              EXPRESSION TAG                 
SEQADV 5FI0 GLY E   -2  UNP  Q8TCU6              EXPRESSION TAG                 
SEQADV 5FI0 GLU E   -1  UNP  Q8TCU6              EXPRESSION TAG                 
SEQADV 5FI0 PHE E    0  UNP  Q8TCU6              EXPRESSION TAG                 
SEQADV 5FI0 GLY F   -2  UNP  P63000              EXPRESSION TAG                 
SEQADV 5FI0 GLU F   -1  UNP  P63000              EXPRESSION TAG                 
SEQADV 5FI0 PHE F    0  UNP  P63000              EXPRESSION TAG                 
SEQADV 5FI0 GLY G   -2  UNP  Q8TCU6              EXPRESSION TAG                 
SEQADV 5FI0 GLU G   -1  UNP  Q8TCU6              EXPRESSION TAG                 
SEQADV 5FI0 PHE G    0  UNP  Q8TCU6              EXPRESSION TAG                 
SEQADV 5FI0 GLY H   -2  UNP  P63000              EXPRESSION TAG                 
SEQADV 5FI0 GLU H   -1  UNP  P63000              EXPRESSION TAG                 
SEQADV 5FI0 PHE H    0  UNP  P63000              EXPRESSION TAG                 
SEQRES   1 A  374  GLY GLU PHE ALA ALA ALA ARG GLU SER GLU ARG GLN LEU          
SEQRES   2 A  374  ARG LEU ARG LEU CYS VAL LEU ASN GLU ILE LEU GLY THR          
SEQRES   3 A  374  GLU ARG ASP TYR VAL GLY THR LEU ARG PHE LEU GLN SER          
SEQRES   4 A  374  ALA PHE LEU HIS ARG ILE ARG GLN ASN VAL ALA ASP SER          
SEQRES   5 A  374  VAL GLU LYS GLY LEU THR GLU GLU ASN VAL LYS VAL LEU          
SEQRES   6 A  374  PHE SER ASN ILE GLU ASP ILE LEU GLU VAL HIS LYS ASP          
SEQRES   7 A  374  PHE LEU ALA ALA LEU GLU TYR CYS LEU HIS PRO GLU PRO          
SEQRES   8 A  374  GLN SER GLN HIS GLU LEU GLY ASN VAL PHE LEU LYS PHE          
SEQRES   9 A  374  LYS ASP LYS PHE CYS VAL TYR GLU GLU TYR CYS SER ASN          
SEQRES  10 A  374  HIS GLU LYS ALA LEU ARG LEU LEU VAL GLU LEU ASN LYS          
SEQRES  11 A  374  ILE PRO THR VAL ARG ALA PHE LEU LEU SER CYS MET LEU          
SEQRES  12 A  374  LEU GLY GLY ARG LYS THR THR ASP ILE PRO LEU GLU GLY          
SEQRES  13 A  374  TYR LEU LEU SER PRO ILE GLN ARG ILE CYS LYS TYR PRO          
SEQRES  14 A  374  LEU LEU LEU LYS GLU LEU ALA LYS ARG THR PRO GLY LYS          
SEQRES  15 A  374  HIS PRO ASP HIS PRO ALA VAL GLN SER ALA LEU GLN ALA          
SEQRES  16 A  374  MET LYS THR VAL CYS SER ASN ILE ASN GLU THR LYS ARG          
SEQRES  17 A  374  GLN MET GLU LYS LEU GLU ALA LEU GLU GLN LEU GLN SER          
SEQRES  18 A  374  HIS ILE GLU GLY TRP GLU GLY SER ASN LEU THR ASP ILE          
SEQRES  19 A  374  CYS THR GLN LEU LEU LEU GLN GLY THR LEU LEU LYS ILE          
SEQRES  20 A  374  SER ALA GLY ASN ILE GLN GLU ARG ALA PHE PHE LEU PHE          
SEQRES  21 A  374  ASP ASN LEU LEU VAL TYR CYS LYS ARG LYS SER ARG VAL          
SEQRES  22 A  374  THR GLY SER LYS LYS SER THR LYS ARG THR LYS SER ILE          
SEQRES  23 A  374  ASN GLY SER LEU TYR ILE PHE ARG GLY ARG ILE ASN THR          
SEQRES  24 A  374  GLU VAL MET GLU VAL GLU ASN VAL GLU ASP GLY THR ALA          
SEQRES  25 A  374  ASP TYR HIS SER ASN GLY TYR THR VAL THR ASN GLY TRP          
SEQRES  26 A  374  LYS ILE HIS ASN THR ALA LYS ASN LYS TRP PHE VAL CYS          
SEQRES  27 A  374  MET ALA LYS THR ALA GLU GLU LYS GLN LYS TRP LEU ASP          
SEQRES  28 A  374  ALA ILE ILE ARG GLU ARG GLU GLN ARG GLU SER LEU LYS          
SEQRES  29 A  374  LEU GLY MET GLU ARG ASP ALA TYR VAL MET                      
SEQRES   1 B  195  GLY GLU PHE MET GLN ALA ILE LYS CYS VAL VAL VAL GLY          
SEQRES   2 B  195  ASP GLY ALA VAL GLY LYS THR CYS LEU LEU ILE SER TYR          
SEQRES   3 B  195  THR THR ASN ALA PHE PRO GLY GLU TYR ILE PRO THR VAL          
SEQRES   4 B  195  PHE ASP ASN TYR SER ALA ASN VAL MET VAL ASP GLY LYS          
SEQRES   5 B  195  PRO VAL ASN LEU GLY LEU TRP ASP THR ALA GLY GLN GLU          
SEQRES   6 B  195  ASP TYR ASP ARG LEU ARG PRO LEU SER TYR PRO GLN THR          
SEQRES   7 B  195  ASP VAL PHE LEU ILE CYS PHE SER LEU VAL SER PRO ALA          
SEQRES   8 B  195  SER PHE GLU ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL          
SEQRES   9 B  195  ARG HIS HIS CYS PRO ASN THR PRO ILE ILE LEU VAL GLY          
SEQRES  10 B  195  THR LYS LEU ASP LEU ARG ASP ASP LYS ASP THR ILE GLU          
SEQRES  11 B  195  LYS LEU LYS GLU LYS LYS LEU THR PRO ILE THR TYR PRO          
SEQRES  12 B  195  GLN GLY LEU ALA MET ALA LYS GLU ILE GLY ALA VAL LYS          
SEQRES  13 B  195  TYR LEU GLU CYS SER ALA LEU THR GLN ARG GLY LEU LYS          
SEQRES  14 B  195  THR VAL PHE ASP GLU ALA ILE ARG ALA VAL LEU CYS PRO          
SEQRES  15 B  195  PRO PRO VAL LYS LYS ARG LYS ARG LYS CYS LEU LEU LEU          
SEQRES   1 C  374  GLY GLU PHE ALA ALA ALA ARG GLU SER GLU ARG GLN LEU          
SEQRES   2 C  374  ARG LEU ARG LEU CYS VAL LEU ASN GLU ILE LEU GLY THR          
SEQRES   3 C  374  GLU ARG ASP TYR VAL GLY THR LEU ARG PHE LEU GLN SER          
SEQRES   4 C  374  ALA PHE LEU HIS ARG ILE ARG GLN ASN VAL ALA ASP SER          
SEQRES   5 C  374  VAL GLU LYS GLY LEU THR GLU GLU ASN VAL LYS VAL LEU          
SEQRES   6 C  374  PHE SER ASN ILE GLU ASP ILE LEU GLU VAL HIS LYS ASP          
SEQRES   7 C  374  PHE LEU ALA ALA LEU GLU TYR CYS LEU HIS PRO GLU PRO          
SEQRES   8 C  374  GLN SER GLN HIS GLU LEU GLY ASN VAL PHE LEU LYS PHE          
SEQRES   9 C  374  LYS ASP LYS PHE CYS VAL TYR GLU GLU TYR CYS SER ASN          
SEQRES  10 C  374  HIS GLU LYS ALA LEU ARG LEU LEU VAL GLU LEU ASN LYS          
SEQRES  11 C  374  ILE PRO THR VAL ARG ALA PHE LEU LEU SER CYS MET LEU          
SEQRES  12 C  374  LEU GLY GLY ARG LYS THR THR ASP ILE PRO LEU GLU GLY          
SEQRES  13 C  374  TYR LEU LEU SER PRO ILE GLN ARG ILE CYS LYS TYR PRO          
SEQRES  14 C  374  LEU LEU LEU LYS GLU LEU ALA LYS ARG THR PRO GLY LYS          
SEQRES  15 C  374  HIS PRO ASP HIS PRO ALA VAL GLN SER ALA LEU GLN ALA          
SEQRES  16 C  374  MET LYS THR VAL CYS SER ASN ILE ASN GLU THR LYS ARG          
SEQRES  17 C  374  GLN MET GLU LYS LEU GLU ALA LEU GLU GLN LEU GLN SER          
SEQRES  18 C  374  HIS ILE GLU GLY TRP GLU GLY SER ASN LEU THR ASP ILE          
SEQRES  19 C  374  CYS THR GLN LEU LEU LEU GLN GLY THR LEU LEU LYS ILE          
SEQRES  20 C  374  SER ALA GLY ASN ILE GLN GLU ARG ALA PHE PHE LEU PHE          
SEQRES  21 C  374  ASP ASN LEU LEU VAL TYR CYS LYS ARG LYS SER ARG VAL          
SEQRES  22 C  374  THR GLY SER LYS LYS SER THR LYS ARG THR LYS SER ILE          
SEQRES  23 C  374  ASN GLY SER LEU TYR ILE PHE ARG GLY ARG ILE ASN THR          
SEQRES  24 C  374  GLU VAL MET GLU VAL GLU ASN VAL GLU ASP GLY THR ALA          
SEQRES  25 C  374  ASP TYR HIS SER ASN GLY TYR THR VAL THR ASN GLY TRP          
SEQRES  26 C  374  LYS ILE HIS ASN THR ALA LYS ASN LYS TRP PHE VAL CYS          
SEQRES  27 C  374  MET ALA LYS THR ALA GLU GLU LYS GLN LYS TRP LEU ASP          
SEQRES  28 C  374  ALA ILE ILE ARG GLU ARG GLU GLN ARG GLU SER LEU LYS          
SEQRES  29 C  374  LEU GLY MET GLU ARG ASP ALA TYR VAL MET                      
SEQRES   1 D  195  GLY GLU PHE MET GLN ALA ILE LYS CYS VAL VAL VAL GLY          
SEQRES   2 D  195  ASP GLY ALA VAL GLY LYS THR CYS LEU LEU ILE SER TYR          
SEQRES   3 D  195  THR THR ASN ALA PHE PRO GLY GLU TYR ILE PRO THR VAL          
SEQRES   4 D  195  PHE ASP ASN TYR SER ALA ASN VAL MET VAL ASP GLY LYS          
SEQRES   5 D  195  PRO VAL ASN LEU GLY LEU TRP ASP THR ALA GLY GLN GLU          
SEQRES   6 D  195  ASP TYR ASP ARG LEU ARG PRO LEU SER TYR PRO GLN THR          
SEQRES   7 D  195  ASP VAL PHE LEU ILE CYS PHE SER LEU VAL SER PRO ALA          
SEQRES   8 D  195  SER PHE GLU ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL          
SEQRES   9 D  195  ARG HIS HIS CYS PRO ASN THR PRO ILE ILE LEU VAL GLY          
SEQRES  10 D  195  THR LYS LEU ASP LEU ARG ASP ASP LYS ASP THR ILE GLU          
SEQRES  11 D  195  LYS LEU LYS GLU LYS LYS LEU THR PRO ILE THR TYR PRO          
SEQRES  12 D  195  GLN GLY LEU ALA MET ALA LYS GLU ILE GLY ALA VAL LYS          
SEQRES  13 D  195  TYR LEU GLU CYS SER ALA LEU THR GLN ARG GLY LEU LYS          
SEQRES  14 D  195  THR VAL PHE ASP GLU ALA ILE ARG ALA VAL LEU CYS PRO          
SEQRES  15 D  195  PRO PRO VAL LYS LYS ARG LYS ARG LYS CYS LEU LEU LEU          
SEQRES   1 E  374  GLY GLU PHE ALA ALA ALA ARG GLU SER GLU ARG GLN LEU          
SEQRES   2 E  374  ARG LEU ARG LEU CYS VAL LEU ASN GLU ILE LEU GLY THR          
SEQRES   3 E  374  GLU ARG ASP TYR VAL GLY THR LEU ARG PHE LEU GLN SER          
SEQRES   4 E  374  ALA PHE LEU HIS ARG ILE ARG GLN ASN VAL ALA ASP SER          
SEQRES   5 E  374  VAL GLU LYS GLY LEU THR GLU GLU ASN VAL LYS VAL LEU          
SEQRES   6 E  374  PHE SER ASN ILE GLU ASP ILE LEU GLU VAL HIS LYS ASP          
SEQRES   7 E  374  PHE LEU ALA ALA LEU GLU TYR CYS LEU HIS PRO GLU PRO          
SEQRES   8 E  374  GLN SER GLN HIS GLU LEU GLY ASN VAL PHE LEU LYS PHE          
SEQRES   9 E  374  LYS ASP LYS PHE CYS VAL TYR GLU GLU TYR CYS SER ASN          
SEQRES  10 E  374  HIS GLU LYS ALA LEU ARG LEU LEU VAL GLU LEU ASN LYS          
SEQRES  11 E  374  ILE PRO THR VAL ARG ALA PHE LEU LEU SER CYS MET LEU          
SEQRES  12 E  374  LEU GLY GLY ARG LYS THR THR ASP ILE PRO LEU GLU GLY          
SEQRES  13 E  374  TYR LEU LEU SER PRO ILE GLN ARG ILE CYS LYS TYR PRO          
SEQRES  14 E  374  LEU LEU LEU LYS GLU LEU ALA LYS ARG THR PRO GLY LYS          
SEQRES  15 E  374  HIS PRO ASP HIS PRO ALA VAL GLN SER ALA LEU GLN ALA          
SEQRES  16 E  374  MET LYS THR VAL CYS SER ASN ILE ASN GLU THR LYS ARG          
SEQRES  17 E  374  GLN MET GLU LYS LEU GLU ALA LEU GLU GLN LEU GLN SER          
SEQRES  18 E  374  HIS ILE GLU GLY TRP GLU GLY SER ASN LEU THR ASP ILE          
SEQRES  19 E  374  CYS THR GLN LEU LEU LEU GLN GLY THR LEU LEU LYS ILE          
SEQRES  20 E  374  SER ALA GLY ASN ILE GLN GLU ARG ALA PHE PHE LEU PHE          
SEQRES  21 E  374  ASP ASN LEU LEU VAL TYR CYS LYS ARG LYS SER ARG VAL          
SEQRES  22 E  374  THR GLY SER LYS LYS SER THR LYS ARG THR LYS SER ILE          
SEQRES  23 E  374  ASN GLY SER LEU TYR ILE PHE ARG GLY ARG ILE ASN THR          
SEQRES  24 E  374  GLU VAL MET GLU VAL GLU ASN VAL GLU ASP GLY THR ALA          
SEQRES  25 E  374  ASP TYR HIS SER ASN GLY TYR THR VAL THR ASN GLY TRP          
SEQRES  26 E  374  LYS ILE HIS ASN THR ALA LYS ASN LYS TRP PHE VAL CYS          
SEQRES  27 E  374  MET ALA LYS THR ALA GLU GLU LYS GLN LYS TRP LEU ASP          
SEQRES  28 E  374  ALA ILE ILE ARG GLU ARG GLU GLN ARG GLU SER LEU LYS          
SEQRES  29 E  374  LEU GLY MET GLU ARG ASP ALA TYR VAL MET                      
SEQRES   1 F  195  GLY GLU PHE MET GLN ALA ILE LYS CYS VAL VAL VAL GLY          
SEQRES   2 F  195  ASP GLY ALA VAL GLY LYS THR CYS LEU LEU ILE SER TYR          
SEQRES   3 F  195  THR THR ASN ALA PHE PRO GLY GLU TYR ILE PRO THR VAL          
SEQRES   4 F  195  PHE ASP ASN TYR SER ALA ASN VAL MET VAL ASP GLY LYS          
SEQRES   5 F  195  PRO VAL ASN LEU GLY LEU TRP ASP THR ALA GLY GLN GLU          
SEQRES   6 F  195  ASP TYR ASP ARG LEU ARG PRO LEU SER TYR PRO GLN THR          
SEQRES   7 F  195  ASP VAL PHE LEU ILE CYS PHE SER LEU VAL SER PRO ALA          
SEQRES   8 F  195  SER PHE GLU ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL          
SEQRES   9 F  195  ARG HIS HIS CYS PRO ASN THR PRO ILE ILE LEU VAL GLY          
SEQRES  10 F  195  THR LYS LEU ASP LEU ARG ASP ASP LYS ASP THR ILE GLU          
SEQRES  11 F  195  LYS LEU LYS GLU LYS LYS LEU THR PRO ILE THR TYR PRO          
SEQRES  12 F  195  GLN GLY LEU ALA MET ALA LYS GLU ILE GLY ALA VAL LYS          
SEQRES  13 F  195  TYR LEU GLU CYS SER ALA LEU THR GLN ARG GLY LEU LYS          
SEQRES  14 F  195  THR VAL PHE ASP GLU ALA ILE ARG ALA VAL LEU CYS PRO          
SEQRES  15 F  195  PRO PRO VAL LYS LYS ARG LYS ARG LYS CYS LEU LEU LEU          
SEQRES   1 G  374  GLY GLU PHE ALA ALA ALA ARG GLU SER GLU ARG GLN LEU          
SEQRES   2 G  374  ARG LEU ARG LEU CYS VAL LEU ASN GLU ILE LEU GLY THR          
SEQRES   3 G  374  GLU ARG ASP TYR VAL GLY THR LEU ARG PHE LEU GLN SER          
SEQRES   4 G  374  ALA PHE LEU HIS ARG ILE ARG GLN ASN VAL ALA ASP SER          
SEQRES   5 G  374  VAL GLU LYS GLY LEU THR GLU GLU ASN VAL LYS VAL LEU          
SEQRES   6 G  374  PHE SER ASN ILE GLU ASP ILE LEU GLU VAL HIS LYS ASP          
SEQRES   7 G  374  PHE LEU ALA ALA LEU GLU TYR CYS LEU HIS PRO GLU PRO          
SEQRES   8 G  374  GLN SER GLN HIS GLU LEU GLY ASN VAL PHE LEU LYS PHE          
SEQRES   9 G  374  LYS ASP LYS PHE CYS VAL TYR GLU GLU TYR CYS SER ASN          
SEQRES  10 G  374  HIS GLU LYS ALA LEU ARG LEU LEU VAL GLU LEU ASN LYS          
SEQRES  11 G  374  ILE PRO THR VAL ARG ALA PHE LEU LEU SER CYS MET LEU          
SEQRES  12 G  374  LEU GLY GLY ARG LYS THR THR ASP ILE PRO LEU GLU GLY          
SEQRES  13 G  374  TYR LEU LEU SER PRO ILE GLN ARG ILE CYS LYS TYR PRO          
SEQRES  14 G  374  LEU LEU LEU LYS GLU LEU ALA LYS ARG THR PRO GLY LYS          
SEQRES  15 G  374  HIS PRO ASP HIS PRO ALA VAL GLN SER ALA LEU GLN ALA          
SEQRES  16 G  374  MET LYS THR VAL CYS SER ASN ILE ASN GLU THR LYS ARG          
SEQRES  17 G  374  GLN MET GLU LYS LEU GLU ALA LEU GLU GLN LEU GLN SER          
SEQRES  18 G  374  HIS ILE GLU GLY TRP GLU GLY SER ASN LEU THR ASP ILE          
SEQRES  19 G  374  CYS THR GLN LEU LEU LEU GLN GLY THR LEU LEU LYS ILE          
SEQRES  20 G  374  SER ALA GLY ASN ILE GLN GLU ARG ALA PHE PHE LEU PHE          
SEQRES  21 G  374  ASP ASN LEU LEU VAL TYR CYS LYS ARG LYS SER ARG VAL          
SEQRES  22 G  374  THR GLY SER LYS LYS SER THR LYS ARG THR LYS SER ILE          
SEQRES  23 G  374  ASN GLY SER LEU TYR ILE PHE ARG GLY ARG ILE ASN THR          
SEQRES  24 G  374  GLU VAL MET GLU VAL GLU ASN VAL GLU ASP GLY THR ALA          
SEQRES  25 G  374  ASP TYR HIS SER ASN GLY TYR THR VAL THR ASN GLY TRP          
SEQRES  26 G  374  LYS ILE HIS ASN THR ALA LYS ASN LYS TRP PHE VAL CYS          
SEQRES  27 G  374  MET ALA LYS THR ALA GLU GLU LYS GLN LYS TRP LEU ASP          
SEQRES  28 G  374  ALA ILE ILE ARG GLU ARG GLU GLN ARG GLU SER LEU LYS          
SEQRES  29 G  374  LEU GLY MET GLU ARG ASP ALA TYR VAL MET                      
SEQRES   1 H  195  GLY GLU PHE MET GLN ALA ILE LYS CYS VAL VAL VAL GLY          
SEQRES   2 H  195  ASP GLY ALA VAL GLY LYS THR CYS LEU LEU ILE SER TYR          
SEQRES   3 H  195  THR THR ASN ALA PHE PRO GLY GLU TYR ILE PRO THR VAL          
SEQRES   4 H  195  PHE ASP ASN TYR SER ALA ASN VAL MET VAL ASP GLY LYS          
SEQRES   5 H  195  PRO VAL ASN LEU GLY LEU TRP ASP THR ALA GLY GLN GLU          
SEQRES   6 H  195  ASP TYR ASP ARG LEU ARG PRO LEU SER TYR PRO GLN THR          
SEQRES   7 H  195  ASP VAL PHE LEU ILE CYS PHE SER LEU VAL SER PRO ALA          
SEQRES   8 H  195  SER PHE GLU ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL          
SEQRES   9 H  195  ARG HIS HIS CYS PRO ASN THR PRO ILE ILE LEU VAL GLY          
SEQRES  10 H  195  THR LYS LEU ASP LEU ARG ASP ASP LYS ASP THR ILE GLU          
SEQRES  11 H  195  LYS LEU LYS GLU LYS LYS LEU THR PRO ILE THR TYR PRO          
SEQRES  12 H  195  GLN GLY LEU ALA MET ALA LYS GLU ILE GLY ALA VAL LYS          
SEQRES  13 H  195  TYR LEU GLU CYS SER ALA LEU THR GLN ARG GLY LEU LYS          
SEQRES  14 H  195  THR VAL PHE ASP GLU ALA ILE ARG ALA VAL LEU CYS PRO          
SEQRES  15 H  195  PRO PRO VAL LYS LYS ARG LYS ARG LYS CYS LEU LEU LEU          
HET    PO4  A 501       5                                                       
HET    PO4  C 501       5                                                       
HET    PO4  E 501       5                                                       
HET    PO4  G 501       5                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   9  PO4    4(O4 P 3-)                                                   
HELIX    1 AA1 PHE A    0  PHE A   75  1                                  39    
HELIX    2 AA2 PHE A   75  ASN A   82  1                                   8    
HELIX    3 AA3 ASN A   82  GLU A   88  1                                   7    
HELIX    4 AA4 THR A   92  SER A  101  1                                  10    
HELIX    5 AA5 ASN A  102  LEU A  121  1                                  20    
HELIX    6 AA6 LEU A  131  LYS A  139  1                                   9    
HELIX    7 AA7 ASP A  140  PHE A  142  5                                   3    
HELIX    8 AA8 CYS A  143  ASN A  163  1                                  21    
HELIX    9 AA9 ILE A  165  GLY A  179  1                                  15    
HELIX   10 AB1 PRO A  187  ARG A  212  1                                  26    
HELIX   11 AB2 ASP A  219  HIS A  256  1                                  38    
HELIX   12 AB3 ASN A  264  CYS A  269  1                                   6    
HELIX   13 AB4 ALA A  365  ASN A  367  5                                   3    
HELIX   14 AB5 THR A  376  LYS A  398  1                                  23    
HELIX   15 AB6 GLY B   15  ASN B   26  1                                  12    
HELIX   16 AB7 GLY B   60  TYR B   64  5                                   5    
HELIX   17 AB8 LEU B   67  TYR B   72  5                                   6    
HELIX   18 AB9 SER B   86  LYS B   96  1                                  11    
HELIX   19 AC1 LYS B   96  CYS B  105  1                                  10    
HELIX   20 AC2 LYS B  116  ARG B  120  5                                   5    
HELIX   21 AC3 ASP B  122  LYS B  132  1                                  11    
HELIX   22 AC4 THR B  138  ILE B  149  1                                  12    
HELIX   23 AC5 GLY B  164  CYS B  178  1                                  15    
HELIX   24 AC6 ALA C   39  PHE C   75  1                                  37    
HELIX   25 AC7 PHE C   75  ASN C   82  1                                   8    
HELIX   26 AC8 ASN C   82  GLU C   88  1                                   7    
HELIX   27 AC9 THR C   92  SER C  101  1                                  10    
HELIX   28 AD1 ASN C  102  LEU C  121  1                                  20    
HELIX   29 AD2 LEU C  131  LYS C  139  1                                   9    
HELIX   30 AD3 ASP C  140  PHE C  142  5                                   3    
HELIX   31 AD4 CYS C  143  ASN C  163  1                                  21    
HELIX   32 AD5 ILE C  165  GLY C  179  1                                  15    
HELIX   33 AD6 PRO C  187  CYS C  200  1                                  14    
HELIX   34 AD7 LYS C  201  ARG C  212  1                                  12    
HELIX   35 AD8 ASP C  219  HIS C  256  1                                  38    
HELIX   36 AD9 ASN C  264  CYS C  269  1                                   6    
HELIX   37 AE1 ALA C  365  ASN C  367  5                                   3    
HELIX   38 AE2 THR C  376  LEU C  399  1                                  24    
HELIX   39 AE3 GLY D   15  THR D   25  1                                  11    
HELIX   40 AE4 LEU D   67  TYR D   72  5                                   6    
HELIX   41 AE5 SER D   86  LYS D   96  1                                  11    
HELIX   42 AE6 LYS D   96  CYS D  105  1                                  10    
HELIX   43 AE7 LYS D  116  ARG D  120  5                                   5    
HELIX   44 AE8 ASP D  122  GLU D  131  1                                  10    
HELIX   45 AE9 THR D  138  ILE D  149  1                                  12    
HELIX   46 AF1 GLY D  164  CYS D  178  1                                  15    
HELIX   47 AF2 GLU E   -1  PHE E   75  1                                  40    
HELIX   48 AF3 PHE E   75  ASN E   82  1                                   8    
HELIX   49 AF4 ASN E   82  GLY E   90  1                                   9    
HELIX   50 AF5 THR E   92  SER E  101  1                                  10    
HELIX   51 AF6 ASN E  102  LEU E  121  1                                  20    
HELIX   52 AF7 LEU E  131  LYS E  139  1                                   9    
HELIX   53 AF8 ASP E  140  PHE E  142  5                                   3    
HELIX   54 AF9 CYS E  143  ASN E  163  1                                  21    
HELIX   55 AG1 ILE E  165  GLY E  179  1                                  15    
HELIX   56 AG2 PRO E  187  CYS E  200  1                                  14    
HELIX   57 AG3 LYS E  201  ARG E  212  1                                  12    
HELIX   58 AG4 ASP E  219  HIS E  256  1                                  38    
HELIX   59 AG5 ASN E  264  CYS E  269  1                                   6    
HELIX   60 AG6 ALA E  365  ASN E  367  5                                   3    
HELIX   61 AG7 THR E  376  LEU E  397  1                                  22    
HELIX   62 AG8 GLY F   15  ASN F   26  1                                  12    
HELIX   63 AG9 GLY F   60  TYR F   64  5                                   5    
HELIX   64 AH1 LEU F   67  TYR F   72  5                                   6    
HELIX   65 AH2 SER F   86  LYS F   96  1                                  11    
HELIX   66 AH3 LYS F   96  CYS F  105  1                                  10    
HELIX   67 AH4 LYS F  116  ARG F  120  5                                   5    
HELIX   68 AH5 ASP F  122  LYS F  132  1                                  11    
HELIX   69 AH6 THR F  138  ILE F  149  1                                  12    
HELIX   70 AH7 GLY F  164  CYS F  178  1                                  15    
HELIX   71 AH8 GLU G   -1  PHE G   75  1                                  40    
HELIX   72 AH9 PHE G   75  ASN G   82  1                                   8    
HELIX   73 AI1 ASN G   82  LYS G   89  1                                   8    
HELIX   74 AI2 THR G   92  SER G  101  1                                  10    
HELIX   75 AI3 ASN G  102  LEU G  121  1                                  20    
HELIX   76 AI4 LEU G  131  LYS G  139  1                                   9    
HELIX   77 AI5 ASP G  140  CYS G  143  5                                   4    
HELIX   78 AI6 VAL G  144  ASN G  163  1                                  20    
HELIX   79 AI7 ILE G  165  GLY G  179  1                                  15    
HELIX   80 AI8 PRO G  187  CYS G  200  1                                  14    
HELIX   81 AI9 LYS G  201  ARG G  212  1                                  12    
HELIX   82 AJ1 ASP G  219  HIS G  256  1                                  38    
HELIX   83 AJ2 ASN G  264  CYS G  269  1                                   6    
HELIX   84 AJ3 ALA G  365  ASN G  367  5                                   3    
HELIX   85 AJ4 THR G  376  LEU G  397  1                                  22    
HELIX   86 AJ5 GLY H   15  THR H   25  1                                  11    
HELIX   87 AJ6 GLY H   60  TYR H   64  5                                   5    
HELIX   88 AJ7 LEU H   67  TYR H   72  5                                   6    
HELIX   89 AJ8 SER H   86  LYS H   96  1                                  11    
HELIX   90 AJ9 LYS H   96  CYS H  105  1                                  10    
HELIX   91 AK1 LYS H  116  ARG H  120  5                                   5    
HELIX   92 AK2 ASP H  122  LYS H  132  1                                  11    
HELIX   93 AK3 THR H  138  ILE H  149  1                                  12    
HELIX   94 AK4 GLY H  164  CYS H  178  1                                  15    
SHEET    1 AA1 8 ILE A 257  GLU A 258  0                                        
SHEET    2 AA1 8 TYR A 325  ASN A 332  1  O  TYR A 325   N  GLU A 258           
SHEET    3 AA1 8 LEU A 297  ARG A 303 -1  N  LYS A 302   O  ILE A 326           
SHEET    4 AA1 8 ILE A 286  PHE A 294 -1  N  PHE A 292   O  VAL A 299           
SHEET    5 AA1 8 LEU A 272  ILE A 281 -1  N  LEU A 274   O  LEU A 293           
SHEET    6 AA1 8 LYS A 368  MET A 373 -1  O  VAL A 371   N  ILE A 281           
SHEET    7 AA1 8 GLY A 358  ASN A 363 -1  N  ILE A 361   O  PHE A 370           
SHEET    8 AA1 8 MET A 336  ASN A 340 -1  N  GLU A 339   O  LYS A 360           
SHEET    1 AA2 6 TYR B  40  VAL B  46  0                                        
SHEET    2 AA2 6 LYS B  49  ASP B  57 -1  O  VAL B  51   N  VAL B  44           
SHEET    3 AA2 6 ILE B   4  GLY B  10  1  N  VAL B   8   O  TRP B  56           
SHEET    4 AA2 6 VAL B  77  SER B  83  1  O  LEU B  79   N  VAL B   7           
SHEET    5 AA2 6 ILE B 110  THR B 115  1  O  VAL B 113   N  ILE B  80           
SHEET    6 AA2 6 LYS B 153  GLU B 156  1  O  LEU B 155   N  LEU B 112           
SHEET    1 AA3 8 ILE C 257  GLU C 258  0                                        
SHEET    2 AA3 8 TYR C 325  ASN C 332  1  O  TYR C 325   N  GLU C 258           
SHEET    3 AA3 8 LEU C 297  ARG C 303 -1  N  LYS C 302   O  ILE C 326           
SHEET    4 AA3 8 ILE C 286  PHE C 294 -1  N  PHE C 292   O  VAL C 299           
SHEET    5 AA3 8 LEU C 272  ILE C 281 -1  N  LEU C 274   O  LEU C 293           
SHEET    6 AA3 8 LYS C 368  MET C 373 -1  O  VAL C 371   N  ILE C 281           
SHEET    7 AA3 8 GLY C 358  ASN C 363 -1  N  ASN C 363   O  LYS C 368           
SHEET    8 AA3 8 MET C 336  ASN C 340 -1  N  GLU C 339   O  LYS C 360           
SHEET    1 AA4 6 TYR D  40  VAL D  46  0                                        
SHEET    2 AA4 6 LYS D  49  ASP D  57 -1  O  LEU D  53   N  ALA D  42           
SHEET    3 AA4 6 ALA D   3  GLY D  10  1  N  ILE D   4   O  ASN D  52           
SHEET    4 AA4 6 VAL D  77  SER D  83  1  O  LEU D  79   N  VAL D   7           
SHEET    5 AA4 6 ILE D 110  THR D 115  1  O  VAL D 113   N  ILE D  80           
SHEET    6 AA4 6 LYS D 153  GLU D 156  1  O  LEU D 155   N  LEU D 112           
SHEET    1 AA5 8 ILE E 257  GLU E 258  0                                        
SHEET    2 AA5 8 TYR E 325  ASN E 332  1  O  PHE E 327   N  GLU E 258           
SHEET    3 AA5 8 LEU E 297  ARG E 303 -1  N  TYR E 300   O  GLY E 329           
SHEET    4 AA5 8 ILE E 286  PHE E 294 -1  N  PHE E 294   O  LEU E 297           
SHEET    5 AA5 8 LEU E 272  ILE E 281 -1  N  LEU E 274   O  LEU E 293           
SHEET    6 AA5 8 LYS E 368  MET E 373 -1  O  VAL E 371   N  ILE E 281           
SHEET    7 AA5 8 GLY E 358  ASN E 363 -1  N  ILE E 361   O  PHE E 370           
SHEET    8 AA5 8 MET E 336  ASN E 340 -1  N  GLU E 337   O  HIS E 362           
SHEET    1 AA6 6 TYR F  40  VAL F  46  0                                        
SHEET    2 AA6 6 LYS F  49  TRP F  56 -1  O  VAL F  51   N  VAL F  44           
SHEET    3 AA6 6 ALA F   3  GLY F  10  1  N  CYS F   6   O  GLY F  54           
SHEET    4 AA6 6 VAL F  77  SER F  83  1  O  LEU F  79   N  VAL F   7           
SHEET    5 AA6 6 ILE F 110  THR F 115  1  O  VAL F 113   N  ILE F  80           
SHEET    6 AA6 6 LYS F 153  GLU F 156  1  O  LEU F 155   N  LEU F 112           
SHEET    1 AA7 8 ILE G 257  GLU G 258  0                                        
SHEET    2 AA7 8 TYR G 325  ASN G 332  1  O  PHE G 327   N  GLU G 258           
SHEET    3 AA7 8 LEU G 297  ARG G 303 -1  N  LEU G 298   O  ILE G 331           
SHEET    4 AA7 8 ILE G 286  PHE G 294 -1  N  PHE G 292   O  VAL G 299           
SHEET    5 AA7 8 LEU G 272  ILE G 281 -1  N  GLY G 276   O  PHE G 291           
SHEET    6 AA7 8 LYS G 368  MET G 373 -1  O  MET G 373   N  LEU G 279           
SHEET    7 AA7 8 GLY G 358  ASN G 363 -1  N  TRP G 359   O  CYS G 372           
SHEET    8 AA7 8 MET G 336  ASN G 340 -1  N  GLU G 339   O  LYS G 360           
SHEET    1 AA8 6 TYR H  40  VAL H  46  0                                        
SHEET    2 AA8 6 LYS H  49  TRP H  56 -1  O  VAL H  51   N  VAL H  44           
SHEET    3 AA8 6 ILE H   4  GLY H  10  1  N  CYS H   6   O  GLY H  54           
SHEET    4 AA8 6 VAL H  77  SER H  83  1  O  LEU H  79   N  VAL H   9           
SHEET    5 AA8 6 ILE H 110  THR H 115  1  O  VAL H 113   N  ILE H  80           
SHEET    6 AA8 6 LYS H 153  GLU H 156  1  O  LEU H 155   N  LEU H 112           
CISPEP   1 HIS A  122    PRO A  123          0         1.99                     
CISPEP   2 HIS C  122    PRO C  123          0         3.35                     
CISPEP   3 HIS E  122    PRO E  123          0         2.42                     
CISPEP   4 HIS G  122    PRO G  123          0         1.99                     
SITE     1 AC1  3 ARG A  45  LYS A 211  ARG A 212                               
SITE     1 AC2  3 ARG C  45  LYS C 211  ARG C 212                               
SITE     1 AC3  3 ARG E  45  LYS E 211  ARG E 212                               
SITE     1 AC4  3 ARG G  45  LYS G 211  ARG G 212                               
CRYST1   81.373  107.053  323.568  90.00  90.00  90.00 P 21 21 21   16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012289  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009341  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003091        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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